Patent Publication Number: US-2004053258-A1

Title: Transporters and ion channels

Description:
TECHNICAL FIELD  
       [0001] This invention relates to nucleic acid and amino acid sequences of transporters and ion channels and to the use of these sequences in the diagnosis, treatment, and prevention of transport, neurological, muscle, immunological, and cell proliferative disorders, and in the assessment of the effects of exogenous compounds on the expression of nucleic acid and amino acid sequences of transporters and ion channels.  
       BACKGROUND OF THE INVENTION  
       [0002] Eukaryotic cells are surrounded and subdivided into functionally distinct organelles by hydrophobic lipid bilayer membranes which are highly impermeable to most polar molecules. Cells and organelles require transport proteins to import and export essential nutrients and metal ions including K + , NH 4   + , P i , SO 4   2− , sugars, and vitamins, as well as various metabolic waste products. Transport proteins also play roles in antibiotic resistance, toxin secretion, ion balance, synaptic neurotransmission, kidney function, intestinal absorption, tumor growth, and other diverse cell functions (Griffith, J. and C. Sansom (1998)  The Transporter Pacts Book,  Academic Press, San Diego Calif., pp. 3-29). Transport can occur by a passive concentration-dependent mechanism, or can be linked to an energy source such as ATP hydrolysis or an ion gradient Proteins that function in transport include carrier proteins, which bind to a specific solute and undergo a conformational change that translocates the bound solute across the membrane, and channel proteins, which form hydrophilic pores that allow specific solutes to diffuse through the membrane down an electrochemical solute gradient.  
       [0003] Carrier proteins which transport a single solute from one side of the membrane to the other are called uniporters. In contrast, coupled transporters link the transfer of one solute with simultaneous or sequential transfer of a second solute, either in the same direction (symport) or in the opposite direction (antiport). For example, intestinal and kidney epithelium contains a variety of symporter systems driven by the sodium gradient that exists across the plasma membrane. Sodium moves into the cell down its electrochemical gradient and brings the solute into the cell with it. The sodium gradient that provides the driving force for solute uptake is maintained by the ubiquitous Na + /K +  ATPase system. Sodium-coupled transporters include the mammalian glucose transporter (SGLT1), iodide transporter (NIS), and multivitamin transporter (SMVT). All three transporters have twelve putative transmembrane segments, extracellular glycosylation sites, and cytoplasmically-oriented N- and C-termini. NIS plays a crucial role in the evaluation, diagnosis, and treatment of various thyroid pathologies because it is the molecular basis for radioiodide thyroid-imaging techniques and for specific targeting of radioisotopes to the thyroid gland (Levy, O. et al. (1997) Proc. Natl. Acad. Sci. USA 94:5568-5573). SMVT is expressed in the intestinal mucosa, kidney, and placenta, and is implicated in the transport of the water-soluble vitamins, e.g., biotin and pantothenate (Prasad, P. D. et al. (1998) J. Biol. Chem. 273:7501-7506).  
       [0004] One of the largest families of transporters is the major facilitator superfamily (MFS), also called the uniporter-symporter-antiporter family. MFS transporters are single polypeptide carriers that transport small solutes in response to ion gradients. Members of the MFS are found in all classes of living organisms, and include transporters for sugars, oligosaccharides, phosphates, nitrates, nucleosides, monocarboxylates, and drugs. MFS transporters found in eukaryotes all have a structure comprising 12 transmembrane segments (Pao, S. S. et al. (1998) Microbiol. Molec. Biol. Rev. 62:1-34). The largest family of MFS transporters is the sugar transporter family, which includes the seven glucose transporters (GLUT1-GLUT7) found in humans that are required for the transport of glucose and other hexose sugars. These glucose transport proteins have unique tissue distributions and physiological functions. GLUT1 provides many cell types with their basal glucose requirements and transports glucose across epithelial and endothelial barrier tissues; GLUT2 facilitates glucose uptake or efflux from the liver; GLUT3 regulates glucose supply to neurons; GLUT4 is responsible for insulin-regulated glucose disposal; and GLUT5 regulates fructose uptake into skeletal muscle. Defects in glucose transporters are involved in a recently identified neurological syndrome causing infantile seizures and developmental delay, as well as glycogen storage disease, Fanconi-Bickel syndrome, and non-insulin-dependent diabetes mellitus (Mueckler, M. (1994) Eur. J. Biochem. 219:713-725; Longo, N. and L. J. Elsas (1998) Adv. Pediatr. 45:293-313).  
       [0005] Monocarboxylate anion transporters are proton-coupled symporters with a broad substrate specificity that includes L-lactate, pyruvate, and the ketone bodies acetate, acetoacetate, and beta-hydroxybutyrate. At least seven isoforms have been identified to date. The isoforms are predicted to have twelve transmembrane (TM) helical domains with a large intracellular loop between TM6 and TM7, and play a critical role in maintaining intracellular pH by removing the protons that are produced stoichiometrically with lactate during glycolysis. The best characterized H + -monocarboxylate transporter is that of the erthrocyte membrane, which transports L-lactate and a wide range of other aliphatic monocarboxylates. Other cells possess H + -linked monocarboxylate transporters with differing substrate and inhibitor selectivities. In particular, cardiac muscle and tumor cells have transporters that differ in their K m  values for certain substrates, including stereoselectivity for L- over D-lactate, and in their sensitivity to inhibitors. There are Na + -monocarboxylate cotransporters on the luminal surface of intestinal and kidney epithelia, which allow the uptake of lactate, pyruvate, and ketone bodies in these tissues. In addition, there are specific and selective transporters for organic cations and organic anions in organs including the kidiney, intestine and liver. Organic anion transporters are selective for hydrophobic, charged molecules with electron-attracting side groups. Organic cation transporters, such as the ammonium transporter, mediate the secretion of a variety of drugs and endogenous metabolites, and contribute to the maintenance of intercellular pH (Poole, R. C. and A. P. Halestrap (1993) Am J. Physiol. 264:C761-C782; Price, N. T. et al. (1998) Biochem. J. 329:321-328; and Martinelle, K and I. Haggstrom (1993) J. Biotechnol. 30:339-350).  
       [0006] ATP-binding cassette (ABC) transporters are members of a superfamily of membrane proteins that transport substances ranging from small molecules such as ions, sugars, amino acids, peptides, and phospholipids, to lipopeptides, large proteins, and complex hydrophobic drugs. ABC transporters consist of four modules: two nucleotide-binding domains (NBD), which hydrolyze ATP to supply the energy required for transport, and two membrane-spanning domains (MSD), each containing six putative transmembrane segments. These four modules may be encoded by a single gene, as is the case for the cystic fibrosis transmembrane regulator (CFTR), or by separate genes. When encoded by separate genes, each gene product contains a single NBD and MSD. These “half-molecules” form homo- and heterodimers, such as Tap1 and Tap2, the endoplasmic reticulum-based major histocompatibility (MHC) peptide transport system. Several genetic diseases are attributed to defects in ABC transporters, such as the following diseases and their corresponding proteins: cystic fibrosis (CFTR, an ion channel), adrenoleukodystrophy (adrenoleukodystrophy protein, ALDP), Zellweger syndrome (peroxisomal membrane protein-70, PMP70), and hyperinsulinemic hypoglycemia (sulfonylurea receptor, SUR). Overexpression of the multidrug resistance (MDR) protein, another ABC transporter, in human cancer cells makes the cells resistant to a variety of cytotoxic drugs used in chemotherapy Taglicht, D. and S. Michaelis (1998) Meth Enzymol. 292:130-162).  
       [0007] A number of metal ions such as iron, zinc, copper, cobalt, manganese, molybdenum, selenium, nickel, and chromium are important as cofactors for a number of enzymes. For example, copper is involved in hemoglobin synthesis, connective tissue metabolism, and bone development, by acting as a cofactor in oxidoreductases such as superoxide dismutase, ferroxidase (ceruloplasmin), and lysyl oxidase. Copper and other metal ions must be provided in the diet, and are absorbed by transporters in the gastrointestinal tract Plasma proteins transport the metal ions to the liver and other target organs, where specific transporters move the ions into cells and cellular organelles as needed. Imbalances in metal ion metabolism have been associated with a number of disease states (Danks, D. M. (1986) J. Med. Genet. 23:99-106).  
       [0008] Transport of fatty acids across the plasma membrane can occur by diffusion, a high capacity, low affinity process. However, under normal physiological conditions a significant fraction of fatty acid transport appears to occur via a high affinity, low capacity protein-mediated transport process. Fatty acid transport protein (FATP), an integral membrane protein with four transmembrane segments, is expressed in tissues exhibiting high levels of plasma membrane fatty acid flux, such as muscle, heart, and adipose. Expression of FATP is upregulated in 3T3-L1 cells during adipose conversion, and expression in COS7 fibroblasts elevates uptake of long-chain fatty acids (Hui, T. Y. et al. (1998) J. Biol. Chem. 273:27420-27429).  
       [0009] Mitochondrial carrier proteins are transmembrane-spanning proteins which transport ions and charged metabolites between the cytosol and the mitochondrial matrix. Examples include the ADP, ATP carrier protein; the 2-oxoglutarate/malate carrier; the phosphate carrier protein; the pyruvate carrier; the dicarboxylate carrier which transports malate, succinate, fumarate, and phosphate; the tricarboxylate carrier which transports citrate and malate; and the Grave&#39;s disease carrier protein, a protein recognized by IgG in patients with active Grave&#39;s disease, an autoimmune disorder resulting in hyperthyroidism. Proteins in this family consist of three tandem repeats of an approximately 100 amino acid domain, each of which contains two transmembrane regions (Stryer, L. (1995)  Biochemistry,  W. H. Freeman and Company, New York N.Y., p. 551; PROSITE PDOC00189 Mitochondrial energy transfer proteins signature; Online Mendelian Inheritance in Man (OMIM) *275000 Graves Disease).  
       [0010] This class of transporters also includes the mitochondrial uncoupling proteins, which create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation from ATP synthesis. The result is energy dissipation in the form of heat. Mitochondrial uncoupling proteins have been implicated as modulators of thermoregulation and metabolic rate, and have been proposed as potential targets for drugs against metabolic diseases such as obesity (Ricquier, D. et al. (1999) J. Int. Med. 245:637-642).  
       [0011] Ion Channels  
       [0012] The electrical potential of a cell is generated and maintained by controlling the movement of ions across the plasma membrane. The movement of ions requires ion channels, which form ion-selective pores within the membrane. There are two basic types of ion channels, ion transporters and gated ion channels. Ion transporters utilize the energy obtained from ATP hydrolysis to actively transport an ion against the ion&#39;s concentration gradient. Gated ion channels allow passive flow of an ion down the ion&#39;s electrochemical gradient under restricted conditions. Together, these types of ion channels generate, maintain, and utilize an electrochemical gradient that is used in 1) electrical impulse conduction down the axon of a nerve cell, 2) transport of molecules into cells against concentration gradients, 3) initiation of muscle contraction, and 4) endocrine cell secretion.  
       [0013] Ion Transporters  
       [0014] Ion transporters generate and maintain the resting electrical potential of a cell. Utilizing the energy derived from ATP hydrolysis, they transport ions against the ion&#39;s concentration gradient. These transmembrane ATPases are divided into three families. The phosphorylated (P) class ion transporters, including Na + -K +  ATPase, Ca 2+ -ATPase, and H + -ATPase, are activated by a phosphorylation event. P-class ion transporters are responsible for maintaining resting potential distributions such that cytosolic concentrations of Na +  and Ca 2+  are low and cytosolic concentration of K +  is high. The vacuolar (V) class of ion transporters includes H +  pumps on intracellular organelles, such as lysosomes and Golgi. V-class ion transporters are responsible for generating the low pH within the lumen of these organelles that is required for function. The coupling factor (F) class consists of H +  pumps in the mitochondria. F-class ion transporters utilize a proton gradient to generate AT? from ADP and inorganic phosphate (P i ).  
       [0015] The P-ATPases are hexamers of a 100 kD subunit with ten transmembrane domains and several large cytoplasmic regions that may play a role in ion binding (Scarborough, G. A. (1999) Curr. Opin. Cell Biol. 11:517-522). The V-ATPases are composed of two functional domains: the V 1  domain, a peripheral complex responsible for ATP hydrolysis; and the V 0  domain, an integral complex responsible for proton translocation across the membrane. The F-ATPases are structurally and evolutionarily related to the V-ATPases. The F-ATPase F 0  domain contains 12 copies of the c subunit, a highly hydrophobic protein composed of two transmembrane domains and containing a single buried carboxyl group in TM2 that is essential for proton transport. The V-ATPase V 0  domain contains three types of homologous c subunits with four or five transmembrane domains and the essential carboxyl group in TM4 or TM3. Both types of complex also contain a single a subunit that may be involved in regulating the pH dependence of activity (Forgac, M. (1999) J. Biol. Chem. 274:12951-12954).  
       [0016] The resting potential of the cell is utilized in many processes involving carrier proteins and gated ion channels. Carrier proteins utilize the resting potential to transport molecules into and out of the cell. Amino acid and glucose transport into many cells is linked to sodium ion co-transport (symport) so that the movement of Na +  down an electrochemical gradient drives transport of the other molecule up a concentration gradient Similarly, cardiac muscle links transfer of Ca 2+  out of the cell with transport of Na +  into the cell (antiport).  
       [0017] Gated Ion Channels  
       [0018] Gated ion channels control ion flow by regulating the opening and closing of pores. The ability to control ion flux through various gating mechanisms allows ion channels to mediate such diverse signaling and homeostatic functions as neuronal and endocrine signaling, muscle contraction, fertilization, and regulation of ion and pH balance. Gated ion channels are categorized according to the manner of regulating the gating function. Mechanically-gated channels open their pores in response to mechanical stress; voltage-gated channels (e.g., Na + , K + , Ca 2+ , and Cl −  channels) open their pores in response to changes in membrane potential; and ligand-gated channels (e.g., acetylcholine-, serotonin-, and glutamate-gated cation channels, and GABA- and glycine-gated chloride channels) open their pores in the presence of a specific ion, nucleotide, or neurotransmitter. The gating properties of a particular ion channel (i.e., its threshold for and duration of opening and closing) are sometimes modulated by association with auxiliary channel proteins and/or post translational modifications, such as phosphorylation.  
       [0019] Mechanically-gated or mechanosensitive ion channels act as transducers for the senses of touch, hearing, and balance, and also play important roles in cell volume regulation, smooth muscle contraction, and cardiac rhythm generation. A stretch-inactivated channel (SIC) was recently cloned from rat kidney. The SIC channel belongs to a group of channels which are activated by pressure or stress on the cell membrane and conduct both Ca 2+  and Na +  (Suzuki, M. et al. (1999) J. Biol. Chem. 274:6330-6335).  
       [0020] The pore-forming subunits of the voltage-gated cation channels form a superfamily of ion channel proteins. The characteristic domain of these channel proteins comprises six transmembrane domains (S1-S6), a pore-forming region (P) located between S5 and S6, and intracellular amino and carboxy termini. In the Na +  and Ca 2+  subfamilies, this domain is repeated four times, while in the K +  channel subfamily, each channel is formed from a tetramer of either identical or dissimilar subunits. The P region contains information specifying the ion selectivity for the channel. In the case of K +  channels, a GYG tripeptide is involved in this selectivity (Ishii, T. M. et al. (1997) Proc. Natl. Acad. Sci. USA 94:11651-11656).  
       [0021] Voltage-gated Na +  and K +  channels are necessary for the function of electrically excitable cells, such as nerve and muscle cells. Action potentials, which lead to neurotransmitter release and muscle contraction, arise from large, transient changes in the permeability of the membrane to Na +  and K +  ions. Depolarization of the membrane beyond the threshold level opens voltage-gated Na +  channels. Sodium ions flow into the cell, further depolarizing the membrane and opening more voltage-gated Na +  channels, which propagates the depolarization down the length of the cell. Depolarization also opens voltage-gated potassium channels. Consequently, potassium ions flow outward, which leads to repolarization of the membrane. Voltage-gated channels utilize charged residues in the fourth transmembrane segment (S4) to sense voltage change. The open state lasts only about 1 millisecond, at which time the channel spontaneously converts into an inactive state that cannot be opened irrespective of the membrane potential. Inactivation is mediated by the channel&#39;s N-terminus, which acts as a plug that closes the pore. The transition from an inactive to a closed state requires a return to resting potential.  
       [0022] Voltage-gated Na +  channels are heterotrimeric complexes composed of a 260 kDa pore-forming a subunit that associates with two smaller auxiliary subunits, β1 and β2. The β2 subunit is a integral membrane glycoprotein that contains an extracellular Ig domain, and its association with α and β1 subunits correlates with increased functional expression of the channel, a change in its gating properties, as well as an increase in whole cell capacitance due to an increase in membrane surface area (Isom, L. L. et al. (1995) Cell 83:433-442).  
       [0023] Non voltage-gated Na +  channels include the members of the amiloride-sensitive Na +  channel/degenerin (NaC/DEG) family. Channel subunits of this family are thought to consist of two transmembrane domains flanking a long extracellular loop, with the amino and carboxyl termini located within the cell. The NaC/DEG family includes the epithelial Na +  channel (ENaC) involved in Na +  reabsorption in epithelia including the airway, distal colon, cortical collecting duct of the kidney, and exocrine duct glands. Mutations in ENaC result in pseudohypoaldosteronism type 1 and Liddle&#39;s syndrome (pseudohyperaldosteronism). The NaC/DEG family also includes the recently characterized H + -gated cation channels or acid-sensing ion channels (ASIC). ASIC subunits are expressed in the brain and form heteromultimeric Na + -permeable channels. These channels require acid pH fluctuations for activation. ASIC subunits show homology to the degenerins, a family of mechanically-gated channels originally isolated from  C. elegans.  Mutations in the degenerins cause neurodegeneration. ASIC subunits may also have a role in neuronal function, or in pain perception, since tissue acidosis causes pain (Waldmann, R. and M. Lazdunski (1998) Curr. Opine Neurobiol. 8:418424; Eglen, R. M. et al. (1999) Trends Pharmacol. Sci. 20:337-342).  
       [0024] K +  channels are located in all cell types, and may be regulated by voltage, ATP concentration, or second messengers such as Ca 2+  and cAMP. In non-excitable tissue, K +  channels are involved in protein synthesis, control of endocrine secretions, and the maintenance of osmotic equilibrium across membranes. In neurons and other excitable cells, in addition to regulating action potentials and repolarizing membranes, K +  channels are responsible for setting resting membrane potential. The cytosol contains non-diffusible anions and, to balance this net negative charge, the cell contains a Na + -K +  pump and ion channels that provide the redistribution of Na + , K + , and Cl − . The pump actively transports Na +  out of the cell and K +  into the cell in a 3:2 ratio. Ion channels in the plasma membrane allow K +  and Cl −  to flow by passive diffusion. Because of the high negative charge within the cytosol, Cl −  flows out of the cell. The flow of K +  is balanced by an electromotive force pulling K +  into the cell, and a K +  concentration gradient pushing K +  out of the cell. Thus, the resting membrane potential is primarily regulated by K + flow (Salkoff, L. and T. Jegla (1995) Neuron 15:489-492).  
       [0025] Potassium channel subunits of the Shaker-like superfamily all have the characteristic six transmembrane/1 pore domain structure. Four subunits combine as homo- or heterotetramers to form functional K channels. These pore-forming subunits also associate with various cytoplasmic β subunits that alter channel inactivation kinetics. The Shaker-like channel family includes the voltage-gated K +  channels as well as the delayed rectifier type channels such as the human ether-a-go-go related gene (HERG) associated with long QT, a cardiac dysrythmia syndrome (Curran, M. E. (1998) Curr. Opin. Biotechnol. 9:565-572; Kaczorowski, G. J. and M. L. Garcia (1999) Curr. Opin. Chem. Biol. 3:448-458).  
       [0026] A second superfamily of K +  channels is composed of the inward rectifying channels (Kir). Kir channels have the property of preferentially conducting K +  currents in the inward direction. These proteins consist of a single potassium selective pore domain and two transmembrane domains, which correspond to the fifth and sixth transmembrane domains of voltage-gated K +  channels. Kir subunits also associate as tetramers. The Kir family includes ROMK1, mutations in which lead to Bartter syndrome, a renal tubular disorder. Kir channels are also involved in regulation of cardiac pacemaker activity, seizures and epilepsy, and insulin regulation (Doupnik, C. A. et al. (1995) Curr. Opin. Neurobiol. 5:268-277; Curran, supra).  
       [0027] The recently recognized TWIK K +  channel family includes the mammalian TWIK-1, TREK-1 and TASK proteins. Members of this family possess an overall structure with four transmembrane domains and two P domains. These proteins are probably involved in controlling the resting potential in a large set of cell types (Duprat, F. et al. (1997) EMBO J 16:5464-5471).  
       [0028] The voltage-gated Ca 2+  channels have been classified into several subtypes based upon their electrophysiological and pharmacological characteristics. L-type Ca 2+  channels are predominantly expressed in heart and skeletal muscle where they play an essential role in excitation-contraction coupling. T-type channels are important for cardiac pacemaker activity, while N-type and P/Q-type channels are involved in the control of neurotransmitter release in the central and peripheral nervous system. The L-type and N-type voltage-gated Ca 2+  channels have been purified and, though their functions differ dramatically, they have similar subunit compositions. The channels are composed of three subunits. The α 1  subunit forms the membrane pore and voltage sensor, while the α 2 δ and β subunits modulate the voltage-dependence, gating properties, and the current amplitude of the channel. These subunits are encoded by at least six α 1 , one α 2 δ, and four β genes. A fourth subunit, γ, has been identified in skeletal muscle (Walker, D. et al. (1998) J. Biol. Chem. 273:2361-2367; McCleskey, E. W. (1994) Curr. Opin Neurobiol. 4:304-312).  
       [0029] The transient receptor family (Trp) of calcium ion channels are thought to mediate capacitative calcium entry (CCE). CCE is the Ca 2+  influx into cells to resupply Ca 2+  stores depleted by the action of inositol triphosphate (IP3) and other agents in response to numerous hormones and growth factors. Trp and Trp-like were first cloned from Drosophila and have similarity to voltage gated Ca2+ channels in the S3 through S6 regions. This suggests that Trp and/or related proteins may form mammalian CCC entry channels (Zhu, X. et al. (1996) Cell 85:661-671; Boulay, G. et al. (1997) J. Biol. Chem. 272:29672-29680). Melastatin is a gene isolated in both the mouse and human, and whose expression in melanoma cells is inversely correlated with melanoma aggressiveness in vivo. The human cDNA transcript corresponds to a 1533-amino acid protein having homology to members of the Trp family. It has been proposed that the combined use of malastatin mRNA expression status and tumor thickness might allow for the determination of subgroups of patients at both low and high risk for developing metastatic disease (Duncan, L. M. et al (2001) J. Clin. Oncol. 19:568-576).  
       [0030] Chloride channels are necessary in endocrine secretion and in regulation of cytosolic and organelle pH. In secretory epithelial cells, Cl −  enters the cell across a basolateral membrane through an Na + , K + /Cl −  cotransporter, accumulating in the cell above its electrochemical equilibrium concentration. Secretion of Cl −  from the apical surface, in response to hormonal stimulation, leads to flow of Na +  and water into the secretory lumen. The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride channel encoded by the gene for cystic fibrosis, a common fatal genetic disorder in humans. CFTR is a member of the ABC transporter family, and is composed of two domains each consisting of six transmembrane domains followed by a nucleotide-binding site. Loss of CFTR function decreases transepithelial water secretion and, as a result, the layers of mucus that coat the respiratory tree, pancreatic ducts, and intestine are dehydrated and difficult to clear. The resulting blockage of these sites leads to pancreatic insufficiency, “meconium ileus”, and devastating “chronic obstructive pulmonary disease” (Al-Awqati, Q. et al. (1992) J. Exp. Biol. 172:245-266).  
       [0031] The voltage-gated chloride channels (CLC) are characterized by 10-12 transmembrane domains, as well as two small globular domains known as CBS domains. The CLC subunits probably function as homotetramers. CLC proteins are involved in regulation of cell volume, membrane potential stabilization, signal transduction, and transepithelial transport. Mutations in CLC-1, expressed predominantly in skeletal muscle, are responsible for autosomal recessive generalized myotonia and autosomal dominant myotonia congenita, while mutations in the kidney channel CLC-5 lead to kidney stones (Jentsch, T. J. (1996) Curr. Opin. Neurobiol. 6:303-310).  
       [0032] Ligand-gated channels open their pores when an extracellular or intracellular mediator binds to the channel. Neurotransmitter-gated channels are channels that open when a neurotransmitter binds to their extracellular domain. These channels exist in the postsynaptic membrane of nerve or muscle cells. There are two types of neurotransmitter-gated channels. Sodium channels open in response to excitatory neurotransmitters, such as acetylcholine, glutamate, and serotonin. This opening causes an influx of Na +  and produces the initial localized depolarization that activates the voltage-gated channels and starts the action potential. Chloride channels open in response to inhibitory neurotransmitters, such as y-aminobutyric acid (GABA) and glycine, leading to hyperpolarization of the membrane and the subsequent generation of an action potential. Neurotransmitter-gated ion channels have four transmembrane domains and probably function as pentamers (Jentsch, supra). Amino acids in the second transmembrane domain appear to be important in determining channel permeation and selectivity (Sather, W. A. et al. (1994) Curr. Opin. Neurobiol. 4:313-323).  
       [0033] Ligand-gated channels can be regulated by intracellular second messengers. For example, calcium-activated K +  channels are gated by internal calcium ions. In nerve cells, an influx of calcium during depolarization opens K +  channels to modulate the magnitude of the action potential (Ishi et al., supra). The large conductance (BK) channel has been purified from brain and its subunit composition determined. The a subunit of the BK channel has seven rather than six transmembrane domains in contrast to voltage-gated K +  channels. The extra transmembrane domain is located at the subunit N-terminus. A 28-amino-acid stretch in the C-terminal region of the subunit (the “calcium bowl” region) contains many negatively charged residues and is thought to be the region responsible for calcium binding. The β subunit consists of two transmembrane domains connected by a glycosylated extracellular loop, with intracellular N- and C-termini (Kaczorowski, supra; Vergara, C. et al. (1998) Curr. Opin. Neurobiol. 8:321-329).  
       [0034] Cyclic nucleotide-gated (CNG) channels are gated by cytosolic cyclic nucleotides. The best examples of these are the cAMP-gated Na +  channels involved in olfaction and the cGMP-gated cation channels involved in vision. Both systems involve ligand-mediated activation of a G-protein coupled receptor which then alters the level of cyclic nucleotide within the cell. CNG channels also represent a major pathway for Ca 2+  entry into neurons, and play roles in neuronal development and plasticity. CNG channels are tetramers containing at least two types of subunits, an α subunit which can form functional homomeric channels, and a β subunit, which modulates the channel properties. All CNG subunits have six transmembrane domains and a pore forming region between the fifth and sixth transmembrane domains, similar to voltage-gated K +  channels. A large C-terminal domain contains a cyclic nucleotide binding domain, while the N-terminal domain confers variation among channel subtypes (Zufall, F. et al. (1997) Curr. Opin. Neurobiol. 7:404-412).  
       [0035] The activity of other types of ion channel proteins may also be modulated by a variety of intracellular signalling proteins. Many channels have sites for phosphorylation by one or more protein kinases including protein kinase A, protein kinase C, tyrosine kinase, and casein kinase II, all of which regulate ion channel activity in cells. Kir channels are activated by the binding of the Gβγ subunits of heterotrimeric G-proteins (Reimann, F. and F. M. Ashcroft (1999) Curr. Opin. Cell. Biol. 11:503-508). Other proteins are involved in the localization of ion channels to specific sites in the cell membrane. Such proteins include the PDZ domain proteins known as MAGUKs (membrane-associated guanylate kinases) which regulate the clustering of ion channels at neuronal synapses (Craven, S. E. and D. S. Bredt (1998) Cell 93:495-498).  
       [0036] Disease Correlation  
       [0037] The etiology of numerous human diseases and disorders can be attributed to defects in the transport of molecules across membranes. Defects in the trafficking of membrane-bound transporters and ion channels are associated with several disorders, e.g., cystic fibrosis, glucose-galactose malabsorption syndrome, hypercholesterolemia, von Gierke disease, and certain forms of diabetes mellitus. Single-gene defect diseases resulting in an inability to transport small molecules across membranes include, e.g., cystinuria, iminoglycinuria, Hartup disease, and Fanconi disease (van&#39;t Hoff, W. G. (1996) Exp. Nephrol. 4:253-262; Talente, G. M. et al. (1994) Ann. Intern. Med. 120:218-226; and Chillon, M. et al. (1995) New Engl. J. Med 332:1475-1480).  
       [0038] Human diseases caused by mutations in ion channel genes include disorders of skeletal muscle, cardiac muscle, and the central nervous system. Mutations in the pore-forming subunits of sodium and chloride channels cause myotonia, a muscle disorder in which relaxation after voluntary contraction is delayed Sodium channel myotonias have been treated with channel blockers. Mutations in muscle sodium and calcium channels cause forms of periodic paralysis, while mutations in the sarcoplasmic calcium release channel, T-tubule calcium channel, and muscle sodium channel cause malignant hyperthermia Cardiac arrythmia disorders such as the long QT syndromes and idiopathic ventricular fibrillation are caused by mutations in potassium and sodium channels (Cooper, E. C. and L. Y. Jan (1998) Proc. Natl. Acad. Sci. USA 96:4759-4766). All four known human idiopathic epilepsy genes code for ion channel proteins (Berkovic, S. F. and I. E. Scheffer (1999) Curr. Opin. Neurology 12:177-182). Other neurological disorders such as ataxias, hemiplegic migraine and hereditary deafness can also result from mutations in ion channel genes (Jen, J. (1999) Curr. Opin. Neurobiol. 9:274-280; Cooper, supra).  
       [0039] Ion channels have been the target for many drug therapies. Neurotransmitter-gated channels have been targeted in therapies for treatment of insomnia, anxiety, depression, and schizophrenia. Voltage-gated channels have been targeted in therapies for arrhythmia, ischemic stroke, head trauma, and neurodegenerative disease (Taylor, C. P. and L. S. Narasimhan (1997) Adv. Pharmacol. 39:47-98). Various classes of ion channels also play an important role in the perception of pain, and thus are potential targets for new analgesics. These include the vanilloid-gated ion channels, which are activated by the vanilloid capsaicin, as well as by noxious heat. Local anesthetics such as lidocaine and mexiletine which blockade voltage-gated Na +  channels have been useful in the treatment of neuropathic pain (Eglen, supra).  
       [0040] Ion channels in the immune system have recently been suggested as targets for immunomodulation. Tell activation depends upon calcium signaling, and a diverse set of T-cell specific ion channels has been characterized that affect this signaling process. Channel blocking agents can inhibit secretion of lymphokines, cell proliferation, and killing of target cells. A peptide antagonist of the T-cell potassium channel Kv1.3 was found to suppress delayed-type hypersensitivity and allogenic responses in pigs, validating the idea of channel blockers as safe and efficacious immunosuppressants (Cahalan, M. D. and K. G. Chandy (1997) Curr. Opin. Biotechnol. 8:749-756).  
       [0041] The discovery of new transporters and ion channels, and the polynucleotides encoding them, satisfies a need in the art by providing new compositions which are useful in the diagnosis, prevention, and treatment of transport, neurological, muscle, immunological, and cell proliferative disorders, and in the assessment of the effects of exogenous compounds on the expression of nucleic acid and amino acid sequences of transporters and ion channels.  
       SUMMARY OF THE INVENTION  
       [0042] The invention features purified polypeptides, transporters and ion channels, referred to collectively as “TRICH” and individually as “TRICH-1,” “TRICH-2,” “TRICH-3,” “TRICH-4,” “TRICH-5,” “TRICH-6,” “TRICH-7,” “TRICH-8,” “TRICH-9,” “TRICH-10,” “TRICH-11,” “TRICH-12,” “TRICH-13,” “TRICH-14,” “TRICH-15,” “TRICH-16,” “TRICH-17,” “TRICH-18,” “TRICH-19,” “TRICH-20,” “TRICH-21,” “TRICH-22,” “TRICH-23,” “TRICH-24,” “TRICH-25,” “TRICH-26,” “TRICH-27,” “TRICH-28,” “TRICH-29,” “TRICH-30,” “TRICH-31,” and “TRICH-32.” In one aspect, the invention provides an isolated polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32. In one alternative, the invention provides an isolated polypeptide comprising the amino acid sequence of SEQ ID NOS: 1-32.  
       [0043] The invention further provides an isolated polynucleotide encoding a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32. In one alternative, the polynucleotide encodes a polypeptide selected from the group consisting of SEQ ID NOS: 1-32. In another alternative, the polynucleotide is selected from the group consisting of SEQ ID NOS: 33-64.  
       [0044] Additionally, the invention provides a recombinant polynucleotide comprising a promoter sequence operably linked to a polynucleotide encoding a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32. In one alternative, the invention provides a cell transformed with the recombinant polynucleotide. In another alternative, the invention provides a transgenic organism comprising the recombinant polynucleotide.  
       [0045] The invention also provides a method for producing a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32. The method comprises a) culturing a cell under conditions suitable for expression of the polypeptide, wherein said cell is transformed with a recombinant polynucleotide comprising a promoter sequence operably linked to a polynucleotide encoding the polypeptide, and b) recovering the polypeptide so expressed.  
       [0046] Additionally, the invention provides an isolated antibody which specifically binds to a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32.  
       [0047] The invention further provides an isolated polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NOS: 33-64, b) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NOS: 33-64, c) a polynucleotide complementary to the polynucleotide of a), d) a polynucleotide complementary to the polynucleotide of b), and e) an RNA equivalent of a)-d). In one alternative, the polynucleotide comprises at least 60 contiguous nucleotides.  
       [0048] Additionally, the invention provides a method for detecting a target polynucleotide in a sample, said target polynucleotide having a sequence of a polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NOS: 33-64, b) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NOS: 33-64, c) a polynucleotide complementary to the polynucleotide of a), d) a polynucleotide complementary to the polynucleotide of b), and e) an RNA equivalent of a)-d). The method comprises a) hybridizing the sample with a probe comprising at least 20 contiguous nucleotides comprising a sequence complementary to said target polynucleotide in the sample, and which probe specifically hybridizes to said target polynucleotide, under conditions whereby a hybridization complex is formed between said probe and said target polynucleotide or fragments thereof, and b) detecting the presence or absence of said hybridization complex, and optionally, if present, the amount thereof. In one alternative, the probe comprises at least 60 contiguous nucleotides.  
       [0049] The invention further provides a method for detecting a target polynucleotide in a sample, said target polynucleotide having a sequence of a polynucleotide selected from the group consisting of a) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NOS: 33-64, b) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NOS: 33-64, c) a polynucleotide complementary to the polynucleotide of a), d) a polynucleotide complementary to the polynucleotide of b), and e) an RNA equivalent of a)-d). The method comprises a) amplifying said target polynucleotide or fragment thereof using polymerase chain reaction amplification, and b) detecting the presence or absence of said amplified target polynucleotide or fragment thereof, and, optionally, if present, the amount thereof.  
       [0050] The invention further provides a composition comprising an effective amount of a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, and a pharmaceutically acceptable excipient In one embodiment, the composition comprises an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32. The invention additionally provides a method of treating a disease or condition associated with decreased expression of functional TRICH, comprising administering to a patient in need of such treatment the composition.  
       [0051] The invention also provides a method for screening a compound for effectiveness as an agonist of a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32. The method comprises a) exposing a sample comprising the polypeptide to a compound, and b) detecting agonist activity in the sample. In one alternative, the invention provides a composition comprising an agonist compound identified by the method and a pharmaceutically acceptable excipient. In another alternative, the invention provides a method of treating a disease or condition associated with decreased expression of functional TRICH, comprising administering to a patient in need of such treatment the composition.  
       [0052] Additionally, the invention provides a method for screening a compound for effectiveness as an antagonist of a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32. The method comprises a) exposing a sample comprising the polypeptide to a compound, and b) detecting antagonist activity in the sample. In one alternative, the invention provides a composition comprising an antagonist compound identified by the method and a pharmaceutically acceptable excipient In another alternative, the invention provides a method of treating a disease or condition associated with overexpression of functional TRICH, comprising administering to a patient in need of such treatment the composition.  
       [0053] The invention further provides a method of screening for a compound that specifically binds to a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32. The method comprises a) combining the polypeptide with at least one test compound under suitable conditions, and b) detecting binding of the polypeptide to the test compound, thereby identifying a compound that specifically binds to the polypeptide.  
       [0054] The invention further provides a method of screening for a compound that modulates the activity of a polypeptide selected from the group consisting of a) a polypeptide comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, b) a polypeptide comprising a naturally occurring amino acid sequence at least 90% identical to an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, c) a biologically active fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32, and d) an immunogenic fragment of a polypeptide having an amino acid sequence selected from the group consisting of SEQ ID NOS: 1-32. The method comprises a) combining the polypeptide with at least one test compound under conditions permissive for the activity of the polypeptide, b) assessing the activity of the polypeptide in the presence of the test compound, and c) comparing the activity of the polypeptide in the presence of the test compound with the activity of the polypeptide in the absence of the test compound, wherein a change in the activity of the polypeptide in the presence of the test compound is indicative of a compound that modulates the activity of the polypeptide.  
       [0055] The invention further provides a method for screening a compound for effectiveness in altering expression of a target polynucleotide, wherein said target polynucleotide comprises a sequence selected from the group consisting of SEQ ID NOS: 33-64, the method comprising a) exposing a sample comprising the target polynucleotide to a compound, and b) detecting altered expression of the target polynucleotide.  
       [0056] The invention further provides a method for assessing toxicity of a test compound, said method comprising a) treating a biological sample containing nucleic acids with the test compound; b) hybridizing the nucleic acids of the treated biological sample with a probe comprising at least 20 contiguous nucleotides of a polynucleotide selected from the group consisting of i) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NOS: 33-64, ii) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NOS: 33-64, iii) a polynucleotide having a sequence complementary to i), iv) a polynucleotide complementary to the polynucleotide of ii), and v) an RNA equivalent of i)-iv). Hybridization occurs under conditions whereby a specific hybridization complex is formed between said probe and a target polynucleotide in the biological sample, said target polynucleotide selected from the group consisting of i) a polynucleotide comprising a polynucleotide sequence selected from the group consisting of SEQ ID NOS: 33-64, ii) a polynucleotide comprising a naturally occurring polynucleotide sequence at least 90% identical to a polynucleotide sequence selected from the group consisting of SEQ ID NOS: 33-64, iii) a polynucleotide complementary to the polynucleotide of i), iv) a polynucleotide complementary to the polynucleotide of ii), and v) an RNA equivalent of i)-iv). Alternatively, the target polynucleotide comprises a fragment of a polynucleotide sequence selected from the group consisting of i)-v) above; c) quantifying the amount of hybridization complex; and d) comparing the amount of hybridization complex in the treated biological sample with the amount of hybridization complex in an untreated biological sample, wherein a difference in the amount of hybridization complex in the treated biological sample is indicative of toxicity of the test compound.  
       BRIEF DESCRIPTION OF THE TABLES  
       [0057] Table 1 summarizes the nomenclature for the full length polynucleotide and polypeptide sequences of the present invention.  
       [0058] Table 2 shows the GenBank identification number and annotation of the nearest GenBank homolog for polypeptides of the invention. The probability score for the match between each polypeptide and its GenBank homolog is also shown.  
       [0059] Table 3 shows structural features of polypeptide sequences of the invention, including predicted motifs and domains, along with the methods, algorithms, and searchable databases used for analysis of the polypeptides.  
       [0060] Table 4 lists the cDNA and/or genomic DNA fragments which were used to assemble polynucleotide sequences of the invention, along with selected fragments of the polynucleotide sequences.  
       [0061] Table 5 shows the representative cDNA library for polynucleotides of the invention.  
       [0062] Table 6 provides an appendix which describes the tissues and vectors used for construction of the cDNA libraries shown in Table 5.  
       [0063] Table 7 shows the tools, programs, and algorithms used to analyze the polynucleotides and polypeptides of the invention, along with applicable descriptions, references, and threshold parameters.  
       DESCRIPTION OF THE INVENTION  
       [0064] Before the present proteins, nucleotide sequences, and methods are described, it is understood that this invention is not limited to the particular machines, materials and methods described, as these may vary. It is also to be understood that the terminology used herein is for the purpose of describing particular embodiments only, and is not intended to limit the scope of the present invention which will be limited only by the appended claims.  
       [0065] It must be noted that as used herein and in the appended claims, the singular forms “a,” “an,” and “the” include plural reference unless the context clearly dictates otherwise. Thus, for example, a reference to “a host cell” includes a plurality of such host cells, and a reference to “an antibody” is a reference to one or more antibodies and equivalents thereof known to those skilled in the art, and so forth.  
       [0066] Unless defined otherwise, all technical and scientific terms used herein have the same meanings as commonly understood by one of ordinary skill in the art to which this invention belongs. Although any machines, materials, and methods similar or equivalent to those described herein can be used to practice or test the present invention, the preferred machines, materials and methods are now described. All publications mentioned herein are cited for the purpose of describing and disclosing the cell lines, protocols, reagents and vectors which are reported in the publications and which might be used in connection with the invention. Nothing herein is to be construed as an admission that the invention is not entitled to antedate such disclosure by virtue of prior invention.  
       [0067] Definitions  
       [0068] “TRICH” refers to the amino acid sequences of substantially purified TRICH obtained from any species, particularly a mammalian species, including bovine, ovine, porcine, murine, equine, and human, and from any source, whether natural, synthetic, semi-synthetic, or recombinant.  
       [0069] The term “agonist” refers to a molecule which intensifies or mimics the biological activity of TRICH. Agonists may include proteins, nucleic acids, carbohydrates, small molecules, or any other compound or composition which modulates the activity of TRICH either by directly interacting with TRICH or by acting on components of the biological pathway in which TRICH participates.  
       [0070] An “allelic variant” is an alternative form of the gene encoding TRICH. Allelic variants may result from at least one mutation in the nucleic acid sequence and may result in altered mRNAs or in polypeptides whose structure or function may or may not be altered. A gene may have none, one, or many allelic variants of its naturally occurring form. Common mutational changes which give rise to allelic variants are generally ascribed to natural deletions, additions, or substitutions of nucleotides. Each of these types of changes may occur alone, or in combination with the others, one or more times in a given sequence.  
       [0071] “Altered” nucleic acid sequences encoding TRICH include those sequences with deletions, insertions, or substitutions of different nucleotides, resulting in a polypeptide the same as TRICH or a polypeptide with at least one functional characteristic of TRICH. Included within this definition are polymorphisms which may or may not be readily detectable using a particular oligonucleotide probe of the polynucleotide encoding TRICH, and improper or unexpected hybridization to allelic variants, with a locus other than the normal chromosomal locus for the polynucleotide sequence encoding TRICH. The encoded protein may also be “altered,” and may contain deletions, insertions, or substitutions of amino acid residues which produce a silent change and result in a functionary equivalent TRICH. Deliberate amino acid substitutions may be made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity, and/or the amphipathic nature of the residues, as long as the biological or immunological activity of TRICH is retained. For example, negatively charged amino acids may include aspartic acid and glutamic acid, and positively charged amino acids may include lysine and arginine. Amino acids with uncharged polar side chains having similar hydrophilicity values may include: asparagine and glutamine; and serine and threonine. Amino acids with uncharged side chains having similar hydrophilicity values may include: leucine, isoleucine, and valine; glycine and alanine; and phenylalanine and tyrosine.  
       [0072] The terms “amino acid” and “amino acid sequence” refer to an oligopeptide, peptide, polypeptide, or protein sequence, or a fragment of any of these, and to naturally occurring or synthetic molecules. Where “amino acid sequence” is recited to refer to a sequence of a naturally occurring protein molecule, “amino acid sequence” and like terms are not meant to limit the amino acid sequence to the complete native amino acid sequence associated with the recited protein molecule.  
       [0073] “Amplification” relates to the production of additional copies of a nucleic acid sequence. Amplification is generally carried out using polymerase chain reaction (PCR) technologies well known in the art.  
       [0074] The term “antagonist” refers to a molecule which inhibits or attenuates the biological activity of TRICH. Antagonists may include proteins such as antibodies, nucleic acids, carbohydrates, small molecules, or any other compound or composition which modulates the activity of TRICH either by directly interacting with TRICH or by acting on components of the biological pathway in which TRICH participates.  
       [0075] The term “antibody” refers to intact immunoglobulin molecules as well as to fragments thereof, such as Fab, F(ab′) 2 , and Fv fragments, which are capable of binding an epitopic determinant. Antibodies that bind TRICH polypeptides can be prepared using intact polypeptides or using fragments containing small peptides of interest as the immunizing antigen. The polypeptide or oligopeptide used to immunize an animal (e.g., a mouse, a rat, or a rabbit) can be derived from the translation of RNA, or synthesized chemically, and can be conjugated to a carrier protein if desired. Commonly used carriers that are chemically coupled to peptides include bovine serum albumin, thyroglobulin, and keyhole limpet hemocyanin (KLH). The coupled peptide is then used to immunize the animal.  
       [0076] The term “antigenic determinant” refers to that region of a molecule (i.e., an epitope) that makes contact with a particular antibody. When a protein or a fragment of a protein is used to immunize a host animal, numerous regions of the protein may induce the production of antibodies which bind specifically to antigenic determinants (particular regions or three-dimensional structures on the protein). An antigenic determinant may compete with the intact antigen (i.e., the immunogen used to elicit the immune response) for binding to an antibody.  
       [0077] The term “antisense” refers to any composition capable of base-pairing with the “sense” (coding) strand of a specific nucleic acid sequence. Antisense compositions may include DNA; RNA; peptide nucleic acid (PNA); oligonucleotides having modified backbone linkages such as phosphorothioates, methylphosphonates, or benzylphosphonates; oligonucleotides having modified sugar groups such as 2′-methoxyethyl sugars or 2′-methoxyethoxy sugars; or oligonucleotides having modified bases such as 5-methyl cytosine, 2′-deoxyuracil, or 7-deaza-2′-deoxyguanosine. Antisense molecules may be produced by any method including chemical synthesis or transcription. Once introduced into a cell, the complementary antisense molecule base-pairs with a naturally occurring nucleic acid sequence produced by the cell to form duplexes which block either transcription or translation. The designation “negative” or “minus” can refer to the antisense strand, and the designation “positive” or “plus” can refer to the sense strand of a reference DNA molecule.  
       [0078] The term “biologically active” refers to a protein having structural, regulatory, or biochemical functions of a naturally occurring molecule. Likewise, “immunologically active” or “immunogenic” refers to the capability of the natural, recombinant, or synthetic TRICH, or of any oligopeptide thereof, to induce a specific immune response in appropriate animals or cells and to bind with specific antibodies.  
       [0079] “Complementary” describes the relationship between two single-stranded nucleic acid sequences that anneal by base-pairing. For example, 5′-AGT-3′ pairs with its complement, 3′-TCA-5′.  
       [0080] A “composition comprising a given polynucleotide sequence” and a “composition comprising a given amino acid sequence” refer broadly to any composition containing the given polynucleotide or amino acid sequence. The composition may comprise a dry formulation or an aqueous solution. Compositions comprising polynucleotide sequences encoding TRICH or fragments of TRICH may be employed as hybridization probes. The probes may be stored in freeze-dried form and may be associated with a stabilizing agent such as a carbohydrate. In hybridizations, the probe may be deployed in an aqueous solution containing salts (e.g., NaCl), detergents (e.g., sodium dodecyl sulfate; SDS), and other components (e.g., Denhardt&#39;s solution, dry milk, salmon sperm DNA, etc.).  
       [0081] “Consensus sequence” refers to a nucleic acid sequence which has been subjected to repeated DNA sequence analysis to resolve uncalled bases, extended using the XL-PCR kit (Applied Biosystems, Foster City Calif.) in the 5′ and/or the 3′ direction, and resequenced, or which has been assembled from one or more overlapping cDNA, EST, or genomic DNA fragments using a computer program for fragment assembly, such as the GELVIEW fragment assembly system (GCG, Madison Wis.) or Phrap (University of Washington, Seattle Wash.). Some sequences have been both extended and assembled to produce the consensus sequence.  
       [0082] “Conservative amino acid substitutions” are those substitutions that are predicted to least interfere with the properties of the original protein, i.e., the structure and especially the function of the protein is conserved and not significantly changed by such substitutions. The table below shows amino acids which may be substituted for an original amino acid in a protein and which are regarded as conservative amino acid substitutions.  
                                                   Original Residue   Conservative Substitution                          Ala   Gly, Ser           Arg   His, Lys           Asn   Asp, Gln, His           Asp   Asn, Glu           Cys   Ala, Ser           Gln   Asn, Glu, His           Glu   Asp, Gln, His           Gly   Ala           His   Asn, Arg, Gln, Glu           Ile   Leu, Val           Leu   Ile, Val           Lys   Arg, Gln, Glu           Met   Leu, Ile           Phe   His, Met, Leu, Trp, Tyr           Ser   Cys, Thr           Thr   Ser, Val           Trp   Phe, Tyr           Tyr   His, Phe, Trp           Val   Ile, Leu, Thr                      
 
       [0083] Conservative amino acid substitutions generally maintain (a) the structure of the polypeptide backbone in the area of the substitution, for example, as a beta sheet or alpha helical conformation, (b) the charge or hydrophobicity of the molecule at the site of the substitution, and/or (c) the bulk of the side chain.  
       [0084] A “deletion” refers to a change in the amino acid or nucleotide sequence that results in the absence of one or more amino acid residues or nucleotides.  
       [0085] The term “derivative” refers to a chemically modified polynucleotide or polypeptide. Chemical modifications of a polynucleotide can include, for example, replacement of hydrogen by an alkyl, acyl, hydroxyl, or amino group. A derivative polynucleotide encodes a polypeptide which retains at least one biological or immunological function of the natural molecule. A derivative polypeptide is one modified by glycosylation, pegylation, or any similar process that retains at least one biological or immunological function of the polypeptide from which it was derived.  
       [0086] A “detectable label” refers to a reporter molecule or enzyme that is capable of generating a measurable signal and is covalently or noncovalently joined to a polynucleotide or polypeptide.  
       [0087] “Differential expression” refers to increased or upregulated; or decreased, downregulated, or absent gene or protein expression, determined by comparing at least two different samples. Such comparisons may be carried out between, for example, a treated and an untreated sample, or a diseased and a normal sample.  
       [0088] A “fragment” is a unique portion of TRICH or the polynucleotide encoding TRICH which is identical in sequence to but shorter in length than the parent sequence. A fragment may comprise up to the entire length of the defined sequence, minus one nucleotide/amino acid residue. For example, a fragment may comprise from 5 to 1000 contiguous nucleotides or amino acid residues. A fragment used as a probe, primer, antigen, therapeutic molecule, or for other purposes, may be at least 5, 10, 15, 16, 20, 25, 30, 40, 50, 60,75, 100, 150, 250 or at least 500 contiguous nucleotides or amino acid residues in length. Fragments may be preferentially selected from certain regions of a molecule. For example, a polypeptide fragment may comprise a certain length of contiguous amino acids selected from the first 250 or 500 amino acids (or first 25% or 50%) of a polypeptide as shown in a certain defined sequence. Clearly these lengths are exemplary, and any length that is supported by the specification, including the Sequence Listing, tables, and figures, may be encompassed by the present embodiments.  
       [0089] A fragment of SEQ ID NOS: 33-64 comprises a region of unique polynucleotide sequence that specifically identifies SEQ ID NOS: 33-64, for example, as distinct from any other sequence in the genome from which the fragment was obtained. A fragment of SEQ ID NOS: 33-64 is useful, for example, in hybridization and amplification technologies and in analogous methods that distinguish SEQ ID NOS: 33-64 from related polynucleotide sequences. The precise length of a fragment of SEQ ID NOS: 33-64 and the region of SEQ ID NOS: 33-64 to which the fragment corresponds are routinely determinable by one of ordinary skill in the art based on the intended purpose for the fragment.  
       [0090] A fragment of SEQ ID NOS: 1-32 is encoded by a fragment of SEQ ID NOS: 33-64. A fragment of SEQ ID NOS: 1-32 comprises a region of unique amino acid sequence that specifically identifies SEQ ID NOS: 1-32. For example, a fragment of SEQ ID NOS: 1-32 is useful as an immunogenic peptide for the development of antibodies that specifically recognize SEQ ID NOS: 1-32. The precise length of a fragment of SEQ ID NOS: 1-32 and the region of SEQ ID NOS: 1-32 to which the fragment corresponds are routinely determinable by one of ordinary skill in the art based on the intended purpose for the fragment.  
       [0091] A “full length” polynucleotide sequence is one containing at least a translation initiation codon (e.g., methionine) followed by an open reading frame and a translation termination codon. A “full length” polynucleotide sequence encodes a “full length” polypeptide sequence.  
       [0092] “Homology” refers to sequence similarity or, interchangeably, sequence identity, between two or more polynucleotide sequences or two or more polypeptide sequences.  
       [0093] The terms “percent identity” and “% identity,” as applied to polynucleotide sequences, refer to the percentage of residue matches between at least two polynucleotide sequences aligned using a standardized algorithm. Such an algorithm may insert, in a standardized and reproducible way, gaps in the sequences being compared in order to opt alignment between two sequences, and therefore achieve a more meaningful comparison of the two sequences.  
       [0094] Percent identity between polynucleotide sequences may be determined using the default parameters of the CLUSTAL V algorithm as incorporated into the MEGALIGN version 3.12e sequence alignment program. This program is part of the LASERGENE software package, a suite of molecular biological analysis programs (DNASTAR, Madison Wis.). CLUSTAL V is described in Higgins, D. G. and P. M. Sharp (1989) CABIOS 5:151-153 and in Higgins, D. G. et al. (1992) CABIOS 8:189-191. For pairwise alignments of polynucleotide sequences, the default parameters are set as follows: Ktuple=2, gap penalty=5, window=4, and “diagonals saved”=4. The “weighted” residue weight table is selected as the default. Percent identity is reported by CLUSTAL V as the “percent similarity” between aligned polynucleotide sequences.  
       [0095] Alternatively, a suite of commonly used and freely available sequence comparison algorithms is provided by the National Center for Biotechnology Information (NCBI) Basic Local Alignment Search Tool (BLAST) (Altschul, S. F. et al. (1990) J. Mol. Biol. 215:403-410), which is available from several sources, including the NCBI, Bethesda, Md., and on the Internet at http://www.ncbi.nlm.nih.gov/BLAST/. The BLAST software suite includes various sequence analysis programs including “blastn,” that is used to align a known polynucleotide sequence with other polynucleotide sequences from a variety of databases. Also available is a tool called “BLAST 2 Sequences” that is used for direct pairwise comparison of two nucleotide sequences. “BLAST 2 Sequences” can be accessed and used interactively at http://www.ncbi.nlm.nih.gov/gorf/b12.html. The “BLAST 2 Sequences” tool can be used for both blastn and blastp (discussed below). BLAST programs are commonly used with gap and other parameters set to default settings. For example, to compare two nucleotide sequences, one may use blastn with the “BLAST 2 Sequences” tool Version 2.0.12 (Apr. 21, 2000) set at default parameters. Such default parameters may be, for example:  
       [0096] Matrix: BLOSUM62  
       [0097] Reward for match: 1  
       [0098] Penalty for mismatch: −2  
       [0099] Open Gap: 5 and Extension Gap: 2 penalties  
       [0100] Gap x drop-off: 50  
       [0101] Expect: 10  
       [0102] Word Size: 11  
       [0103] Filter: on  
       [0104] Percent identity may be measured over the length of an entire defined sequence, for example, as defined by a particular SEQ ID number, or may be measured over a shorter length, for example, over the length of a fragment taken from a larger, defined sequence, for instance, a fragment of at least 20, at least 30, at least 40, at least 50, at least 70, at least 100, or at least 200 contiguous nucleotides. Such lengths are exemplary only, and it is understood that any fragment length supported by the sequences shown herein, in the tables, figures, or Sequence Listing, may be used to describe a length over which percentage identity may be measured.  
       [0105] Nucleic acid sequences that do not show a high degree of identity may nevertheless encode similar amino acid sequences due to the degeneracy of the genetic code. It is understood that changes in a nucleic acid sequence can be made using this degeneracy to produce multiple nucleic acid sequences that all encode substantially the same protein.  
       [0106] The phrases “percent identity” and “% identity,” as applied to polypeptide sequences, refer to the percentage of residue matches between at least two polypeptide sequences aligned using a standardized algorithm. Methods of polypeptide sequence alignment are well-known. Some alignment methods take into account conservative amino acid substitutions. Such conservative substitutions, explained in more detail above, generally preserve the charge and_hydrophobicity at the site of substitution, thus preserving the structure (and therefore function) of the polypeptide.  
       [0107] Percent identity between polypeptide sequences may be determined using the default parameters of the CLUSTAL V algorithm as incorporated into the MEGALIGN version 3.12e sequence alignment program (described and referenced above). For pairwise alignments of polypeptide sequences using CLUSTAL V, the default parameters are set as follows: Ktuple=1, gap penalty=3, window=5, and “diagonals saved”=5. The PAM250 matrix is selected as the default residue weight table. As with polynucleotide alignments, the percent identity is reported by CLUSTAL V as the “percent similarity” between aligned polypeptide sequence pairs.  
       [0108] Alternatively the NCBI BLAST software suite may be used. For example, for a pairwise comparison of two polypeptide sequences, one may use the “BLAST 2 Sequences” tool Version 2.0.12 (Apr. 21, 2000) with blastp set at default parameters. Such default parameters may be, for example:  
       [0109] Matrix: BLOSUM62  
       [0110] Open Gap: 11 and Extension Gap: 1 penalties  
       [0111] Gap x drop-off: 50  
       [0112] Expect: 10  
       [0113] Word Size: 3  
       [0114] Filter: on  
       [0115] Percent identity may be measured over the length of an entire defined polypeptide sequence, for example, as defined by a particular SEQ ID number, or may be measured over a shorter length, for example, over the length of a fragment taken from a larger, defined polypeptide sequence, for instance, a fragment of at least 15, at least 20, at least 30, at least 40, at least 50, at least 70 or at least 150 contiguous residues. Such lengths are exemplary only, and it is understood that any fragment length supported by the sequences shown herein, in the tables, figures or Sequence Listing, may be used to describe a length over which percentage identity may be measured.  
       [0116] “Human artificial chromosomes” (HACs) are linear microchromosomes which may contain DNA sequences of about 6 kb to 10 Mb in size and which contain all of the elements required for chromosome replication, segregation and maintenance.  
       [0117] The term “humanized antibody” refers to an antibody molecule in which the amino acid sequence in the non-antigen binding regions has been altered so that the antibody more closely resembles a human antibody, and still retains its original binding ability.  
       [0118] “Hybridization” refers to the process by which a polynucleotide strand anneals with a complementary strand through base pairing under defined hybridization conditions. Specific hybridization is an indication that two nucleic acid sequences share a high degree of complementarity. Specific hybridization complexes form under permissive annealing conditions and remain hybridized after the “washing” step(s). The washing step(s) is particularly important in determining the stringency of the hybridization process, with more stringent conditions allowing less non-specific binding, i.e., binding between pairs of nucleic acid strands that are not perfectly matched Permissive conditions for annealing of nucleic acid sequences are routinely determinable by one of ordinary skill in the art and may be consistent among hybridization experiments, whereas wash conditions may be varied among experiments to achieve the desired stringency, and therefore hybridization specificity. Permissive annealing conditions occur, for example, at 68° C. in the presence of about 6×SSC, about 1% (w/v) SDS, and about 100 μg/ml sheared, denatured salmon sperm DNA.  
       [0119] Generally, stringency of hybridization is expressed, in part, with reference to the temperature under which the wash step is carried out. Such wash temperatures are typically selected to be about 5° C. to 20° C. lower than the thermal melting point (T m ) for the specific sequence at a defined ionic strength and pH. The T m  is the temperature (under defined ionic strength and pH) at which 50% of the target sequence hybridizes to a perfectly matched probe. An equation for calculating T m  and conditions for nucleic acid hybridization are well known and can be found in Sambrook, J. et al. (1989)  Molecular Cloning: A Laboratory Manual,  2 nd  ed., vol. 1-3, Cold Spring Harbor Press, Plainview N.Y.; specifically see volume 2, chapter 9.  
       [0120] High stringency conditions for hybridization between polynucleotides of the present invention include wash conditions of 68° C. in the presence of about 0.2×SSC and about 0.1% SDS, for 1 hour. Alternatively, temperatures of about 65° C., 60° C., 55° C., or 42° C. may be used. SSC concentration may be varied from about 0.1 to 2×SSC, with SDS being present at about 0.1%. Typically, blocking reagents are used to block non-specific hybridization. Such blocking reagents include, for instance, sheared and denatured salmon sperm DNA at about 100-200 μg/ml. Organic solvent, such as formamide at a concentration of about 35-50% v/v, may also be used under particular circumstances, such as for RNA:DNA hybridizations. Useful variations on these wash conditions will be readily apparent to those of ordinary skill in the art. Hybridization, particularly under high stringency conditions, may be suggestive of evolutionary similarity between the nucleotides. Such similarity is strongly indicative of a similar role for the nucleotides and their encoded polypeptides.  
       [0121] The term “hybridization complex” refers to a complex formed between two nucleic acid sequences by virtue of the formation of hydrogen bonds between complementary bases. A hybridization complex may be formed in solution (e.g., C 0 t or R 0 t analysis) or formed between one nucleic acid sequence present in solution and another nucleic acid sequence immobilized on a solid support (e.g., paper, membranes, filters, chips, pins or glass slides, or any other appropriate substrate to which cells or their nucleic acids have been fixed).  
       [0122] The words “insertion” and “addition” refer to changes in an amino acid or nucleotide sequence resulting in the addition of one or more amino acid residues or nucleotides, respectively.  
       [0123] “Immune response” can refer to conditions associated with inflammation, trauma, immune disorders, or infectious or genetic disease, etc. These conditions can be characterized by expression of various factors, e.g., cytokines, chemokines, and other signaling molecules, which may affect cellular and systemic defense systems.  
       [0124] An “immunogenic fragment” is a polypeptide or oligopeptide fragment of TRICH which is capable of eliciting an immune response when introduced into a living organism, for example, a mammal. The term “immunogenic fragment” also includes any polypeptide or oligopeptide fragment of TRICH which is useful in any of the antibody production methods disclosed herein or known in the art.  
       [0125] The term “microarray” refers to an arrangement of a plurality of polynucleotides, polypeptides, or other chemical compounds on a substrate.  
       [0126] The terms “element” and “array element” refer to a polynucleotide, polypeptide, or other chemical compound having a unique and defined position on a microarray.  
       [0127] The term “modulate” refers to a change in the activity of TRICH. For example, modulation may cause an increase or a decrease in protein activity, binding characteristics, or any other biological, functional, or immunological properties of TRICH.  
       [0128] The phrases “nucleic acid” and “nucleic acid sequence” refer to a nucleotide, oligonucleotide, polynucleotide, or any fragment thereof. These phrases also refer to DNA or RNA of genomic or synthetic origin which may be single-stranded or double-stranded and may represent the sense or the antisense strand, to peptide nucleic acid (PNA), or to any DNA-like or RNA-like material.  
       [0129] “Operably linked” refers to the situation in which a first nucleic acid sequence is placed in a functional relationship with a second nucleic acid sequence. For instance, a promoter is operably linked to a coding sequence if the promoter affects the transcription or expression of the coding sequence. Operably linked DNA sequences may be in close proximity or contiguous and, where necessary to join two protein coding regions, in the same reading frame.  
       [0130] “Peptide nucleic acid” (PNA) refers to an antisense molecule or anti-gene agent which comprises an oligonucleotide of at least about 5 nucleotides in length linked to a peptide backbone of amino acid residues ending in lysine. The terminal lysine confers solubility to the composition. PNAs preferentially bind complementary single stranded DNA or RNA and stop transcript elongation, and may be pegylated to extend their lifespan in the cell.  
       [0131] “Post-translational modification” of an TRICH may involve lipidation, glycosylation, phosphorylation, acetylation, racemization, proteolytic cleavage, and other modifications known in the art. These processes may occur synthetically or biochemically. Biochemical modifications will vary by cell type depending on the enzymatic milieu of TRICH.  
       [0132] “Probe” refers to nucleic acid sequences encoding TRICH, their complements, or fragments thereof, which are used to detect identical, allelic or related nucleic acid sequences. Probes are isolated oligonucleotides or polynucleotides attached to a detectable label or reporter molecule. Typical labels include radioactive isotopes, ligands, chemiluminescent agents, and enzymes. “Primers” are short nucleic acids, usually DNA oligonucleotides, which may be annealed to a target polynucleotide by complementary base-pairing. The primer may then be extended along the target DNA strand by a DNA polymerase enzyme. Primer pairs can be used for amplification (and identification) of a nucleic acid sequence, e.g., by the polymerase chain reaction PCR).  
       [0133] Probes and primers as used in the present invention typically comprise at least 15 contiguous nucleotides of a known sequence. In order to enhance specificity, longer probes and primers may also be employed, such as probes and primers that comprise at least 20, 25, 30, 40, 50, 60, 70, 80, 90, 100, or at least 150 consecutive nucleotides of the disclosed nucleic acid sequences. Probes and primers may be considerably longer than these examples, and it is understood that any length supported by the specification, including the tables, figures, and Sequence Listing, may be used Methods for preparing and using probes and primers are described in the references, for example Sambrook, J. et al. (1989)  Molecular Cloning: A Laboratory Manual,  2 nd  ed., vol. 1-3, Cold Spring Harbor Press, Plainview N.Y.; Ausubel, F. M. et al. (1987)  Current Protocols in Molecular Biology,  Greene Publ. Assoc. &amp; Wiley-Intersciences, New York N.Y.; Innis, M. et al. (1990)  PCR Protocols, A Guide to Methods and Applications,  Academic Press, San Diego Calif. PCR primer pairs can be derived from a known sequence, for example, by using computer programs intended for that purpose such as Primer (Version 0.5, 1991, Whitehead Institute for Biomedical Research, Cambridge Mass.).  
       [0134] Oligonucleotides for use as primers are selected using software known in the art for such purpose. For example, OLIGO 4.06 software is useful for the selection of PCR primer pairs of up to 100 nucleotides each, and for the analysis of oligonucleotides and larger polynucleotides of up to 5,000 nucleotides from an input polynucleotide sequence of up to 32 kilobases. Similar primer selection programs have incorporated additional features for expanded capabilities. For example, the PrimOU primer selection program (available to the public from the Genome Center at University of Texas South West Medical Center, Dallas Tex.) is capable of choosing specific primers from megabase sequences and is thus useful for designing primers on a genome-wide scope. The Primer3 primer selection program (available to the public from the Whitehead Institute/MIT Center for Genome Research, Cambridge Mass.) allows the user to input a “mispriming library,” in which sequences to avoid as primer binding sites are user-specified. Primer 3 is useful, in particular, for the selection of oligonucleotides for microarrays. (The source code for the latter two primer selection programs may also be obtained from their respective sources and modified to meet the user&#39;s specific needs.) The PrimeGen program (available to the public from the UK Human Genome Mapping Project Resource Centre, Cambridge UK) designs primers based on multiple sequence alignments, thereby allowing selection of primers that hybridize to either the most conserved or least conserved regions of aligned nucleic acid sequences. Hence, this program is useful for identification of both unique and conserved oligonucleotides and polynucleotide fragments. The oligonucleotides and polynucleotide fragments identified by any of the above selection methods are useful in hybridization technologies, for example, as PCR or sequencing primers, microarray elements, or specific probes to identify fully or partially complementary polynucleotides in a sample of nucleic acids. Methods of oligonucleotide selection are not limited to those described above.  
       [0135] A “recombinant nucleic acid” is a sequence that is not naturally occurring or has a sequence that is made by an artificial combination of two or more otherwise separated segments of sequence. This artificial combination is often accomplished by chemical synthesis or, more commonly, by the artificial manipulation of isolated segments of nucleic acids, e.g., by genetic engineering techniques such as those described in Sambrook, supra. The term recombinant includes nucleic acids that have been altered solely by addition, substitution, or deletion of a portion of the nucleic acid. Frequently, a recombinant nucleic acid may include a nucleic acid sequence operably linked to a promoter sequence. Such a recombinant nucleic acid may be part of a vector that is used, for example, to transform a cell.  
       [0136] Alternatively, such recombinant nucleic acids may be part of a viral vector, e.g., based on a vaccinia virus, that could be use to vaccinate a mammal wherein the recombinant nucleic acid is expressed, inducing a protective immunological response in the mammal.  
       [0137] A “regulatory element” refers to a nucleic acid sequence usually derived from untranslated regions of a gene and includes enhancers, promoters, introns, and 5′ and 3′ untranslated regions (UTRs). Regulatory elements interact with host or viral proteins which control transcription, translation, or RNA stability.  
       [0138] “Reporter molecules” are chemical or biochemical moieties used for labeling a nucleic acid, amino acid, or antibody. Reporter molecules include radionuclides; enzymes; fluorescent, chemiluminescent, or chromogenic agents; substrates; cofactors; inhibitors; magnetic particles; and other moieties known in the art.  
       [0139] An “RNA equivalent,” in reference to a DNA sequence, is composed of the same linear sequence of nucleotides as the reference DNA sequence with the exception that all occurrences of the nitrogenous base thymine are replaced with uracil, and the sugar backbone is composed of ribose instead of deoxyribose.  
       [0140] The term “sample” is used in its broadest sense. A sample suspected of containing TRICH, nucleic acids encoding TRICH, or fragments thereof may comprise a bodily fluid; an extract from a cell, chromosome, organelle, or membrane isolated from a cell; a cell; genomic DNA, RNA, or cDNA, in solution or bound to a substrate; a tissue; a tissue print; etc.  
       [0141] The terms “specific binding” and “specifically binding” refer to that interaction between a protein or peptide and an agonist, an antibody, an antagonist, a small molecule, or any natural or synthetic binding composition. The interaction is dependent upon the presence of a particular structure of the protein, e.g., the antigenic determinant or epitope, recognized by the binding molecule. For example, if an antibody is specific for epitope “A,” the presence of a polypeptide comprising the epitope A, or the presence of free unlabeled A, in a reaction containing free labeled A and the antibody will reduce the amount of labeled A that binds to the antibody.  
       [0142] The term “substantially purified” refers to nucleic acid or amino acid sequences that are removed from their natural environment and are isolated or separated, and are at least 60% free, preferably at least 75% free, and most preferably at least 90% free from other components with which they are naturally associated.  
       [0143] A “substitution” refers to the replacement of one or more amino acid residues or nucleotides by different amino acid residues or nucleotides, respectively.  
       [0144] “Substrate” refers to any suitable rigid or semi-rigid support including membranes, filters, chips, slides, wafers, fibers, magnetic or nonmagnetic beads, gels, tubing, plates, polymers, microparticles and capillaries. The substrate can have a variety of surface forms, such as wells, trenches, pins, channels and pores, to which polynucleotides or polypeptides are bound.  
       [0145] A “transcript image” refers to the collective pattern of gene expression by a particular cell type or tissue under given conditions at a given time.  
       [0146] “Transformation” describes a process by which exogenous DNA is introduced into a recipient cell. Transformation may occur under natural or artificial conditions according to various methods well known in the art, and may rely on any known method for the insertion of foreign nucleic acid sequences into a prokaryotic or eukaryotic host cell. The method for transformation is selected based on the type of host cell being transformed and may include, but is not limited to, bacteriophage or viral infection, electroporation, heat shock, lipofection, and particle bombardment. The term “transformed cells” includes stably transformed cells in which the inserted DNA is capable of replication either as an autonomously replicating plasmid or as part of the host chromosome, as well as transiently transformed cells which express the inserted DNA or RNA for limited periods of time.  
       [0147] A “transgenic organism,” as used herein, is any organism, including but not limited to animals and plants, in which one or more of the cells of the organism contains heterologous nucleic acid introduced by way of human intervention, such as by transgenic techniques well known in the art. The nucleic acid is introduced into the cell, directly or indirectly by introduction into a precursor of the cell, by way of deliberate genetic manipulation, such as by microinjection or by infection with a recombinant virus. The term genetic manipulation does not include classical cross-breeding, or in vitro fertilization, but rather is directed to the introduction of a recombinant DNA molecule. The transgenic organisms contemplated in accordance with the present invention include bacteria, cyanobacteria, fungi, plants and animals. The isolated DNA of the present invention can be introduced into the host by methods known in the art, for example infection, transfection, transformation or transconjugation. Techniques for transferring the DNA of the present invention into such organisms are widely known and provided in references such as Sambrook et al. (1989), supra.  
       [0148] A “variant” of a particular nucleic acid sequence is defined as a nucleic acid sequence having at least 40% sequence identity to the particular nucleic acid sequence over a cerain length of one of the nucleic acid sequences using blastn with the “BLAST 2 Sequences” tool Version 2.0.9 (May 07, 1999) set at default parameters. Such a pair of nucleic acids may show, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% or greater sequence identity over a certain defined length. A variant may be described as, for example, an “allelic” (as defined above), “splice,” “species,” or “polymorphic” variant. A splice variant may have significant identity to a reference molecule, but will generally have a greater or lesser number of polynucleotides due to alternative splicing of exons during mRNA processing. The corresponding polypeptide may possess additional functional domains or lack domains that are present in the reference molecule. Species variants are polynucleotide sequences that vary from one species to another. The resulting polypeptides will generally have significant amino acid identity relative to each other. A polymorphic variant is a variation in the polynucleotide sequence of a particular gene between individuals of a given species. Polymorphic variants also may encompass “single nucleotide polymorphisms” (SNPs) in which the polynucleotide sequence varies by one nucleotide base. The presence of SNPs may be indicative of, for example, a certain population, a disease state, or a propensity for a disease state.  
       [0149] A “variant” of a particular polypeptide sequence is defined as a polypeptide sequence having at least 40% sequence identity to the particular polypeptide sequence over a certain length of one of the polypeptide sequences using blastp with the “BLAST 2 Sequences” tool Version 2.0.9 (May 07, 1999) set at default parameters. Such a pair of polypeptides may show, for example, at least 50%, at least 60%, at least 70%, at least 80%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% or greater sequence identity over a certain defined length of one of the polypeptides.  
       [0150] The Invention  
       [0151] The invention is based on the discovery of new human transporters and ion channels (TRICH), the polynucleotides encoding TRICH, and the use of these compositions for the diagnosis, treatment, or prevention of transport, neurological, muscle, immunological, and cell proliferative disorders.  
       [0152] Table 1 snarizes the nomenclature for the full length polynucleotide and polypeptide sequences of the invention. Each polynucleotide and its corresponding polypeptide are correlated to a single Incyte project identification number (Incyte Project ID). Each polypeptide sequence is denoted by both a polypeptide sequence identification number (Polypeptide SEQ ID NO:) and an Incyte polypeptide sequence number (Incyte Polypeptide ID) as shown. Each polynucleotide sequence is denoted by both a polynucleotide sequence identification number (Polynucleotide SEQ ID NO:) and an Incyte polynucleotide consensus sequence number (Incyte Polynucleotide ID) as shown.  
       [0153] Table 2 shows sequences with homology to the polypeptides of the invention as identified by BLAST analysis against the GenBank protein (genpept) database. Columns 1 and 2 show the polypeptide sequence identification number (Polypeptide SEQ ID NO:) and the corresponding Incyte polypeptide sequence number (Incyte Polypeptide ID) for polypeptides of the invention. Column 3 shows the GenBank identification number (Genbank ID NO:) of the nearest GenBank homolog. Column 4 shows the probability score for the match between each polypeptide and its GenBank homolog. Column 5 shows the annotation of the GenBank homolog along with relevant citations where applicable, all of which are expressly incorporated by reference herein.  
       [0154] Table 3 shows various structural features of the polypeptides of the invention. Columns 1 and 2 show the polypeptide sequence identification number (SEQ ID NO:) and the corresponding Incyte polypeptide sequence number (Incyte Polypeptide ID) for each polypeptide of the invention. Column 3 shows the number of amino acid residues in each polypeptide. Column 4 shows potential phosphorylation sites, and column 5 shows potential glycosylation sites, as determined by the MOTIFS program of the GCG sequence analysis software package (Genetics Computer Group, Madison Wis.). Column 6 shows amino acid residues comprising signature sequences, domains, and motifs. Column 7 shows analytical methods for protein structure/function analysis and in some cases, searchable databases to which the analytical methods were applied.  
       [0155] Together, Tables 2 and 3 summarize the properties of polypeptides of the invention, and these properties establish that the claimed polypeptides are transporters and ion channels. For example, SEQ ID NO: 5 is 83% identical to rat GABA receptor rho-3 subunit precursor (GenBank ID g1060975) as determined by the Basic Local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 1.7e-206, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO: 5 also contains a neurotransmitter-gated ion channel domain as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) Data from BLIMPS, MOTIFS, and PROFILESCAN analyses provide further corroborative evidence that SEQ ID NO: 5 is a neurotransmitter-gated ion channel. In an alternate example, SEQ ID NO: 16 is 57% identical to human Na+/glucose cotransporter (GenBank ID g338055) as determined by the Basic Local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 2.4e-181, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO: 16 also contains a sodium:solute symporter family domain as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) Data from BLIMPS, MOTIFS, and PROFILESCAN analyses provide further corroborative evidence that SEQ ID NO: 16 is a Na+/glucose cotransporter. In an alternate example, SEQ ID NO: 27 is 53% identical to human ATP-binding cassette transporter-1 (ABC-1) (GenBank ID g4128033) as determined by the Basic Local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 0.0, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO: 27 also contains an ABC transporter domain as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) Data from BLIMPS, MOTIFS, and PROFILESCAN analyses provide further corroborative evidence that SEQ ID NO: 27 is an ABC transporter. In an alternate example, SEQ ID NO: 12 is 45% identical to rat thyroid sodium/iodide symporter NIS (GenBank ID g1399954) as determined by the Basic Local Alignment Search Tool (BLAST). (See Table 2.) The BLAST probability score is 3.0e-143, which indicates the probability of obtaining the observed polypeptide sequence alignment by chance. SEQ ID NO: 12 also contains a sodium:solute symporter family domain as determined by searching for statistically significant matches in the hidden Markov model (HMM)-based PFAM database of conserved protein family domains. (See Table 3.) Data from BLIMPS and PROFILESCAN analyses provide further corroborative evidence that SEQ ID NO: 12 is a sodium:solute symporter. SEQ ID NOS: 1-4, SEQ ID NOS: 6-11, SEQ ID NOS: 13-15, SEQ ID NOS: 17-26and SEQ ID NOS: 28-32 were analyzed and annotated in a similar manner. The algorithms and parameters for the analysis of SEQ ID NOS: 1-32 are described in Table 7.  
       [0156] As shown in Table 4, the full length polynucleotide sequences of the present invention were assembled using cDNA sequences or coding (exon) sequences derived from genomic DNA, or any combination of these two types of sequences. Columns 1 and 2 list the polynucleotide sequence identification number (Polynucleotide SEQ ID NO:) and the corresponding Incyte polynucleotide consensus sequence number (Incyte Polynucleotide ID) for each polynucleotide of the invention. Column 3 shows the length of each polynucleotide sequence in basepairs. Column 4 lists fragments of the polynucleotide sequences which are useful, for example, in hybridization or amplification technologies that identify SEQ ID NOS: 33-64 or that distinguish between SEQ ID NOS: 33-64 and related polynucleotide sequences. Column 5 shows identification numbers corresponding to cDNA sequences, coding sequences (exons) predicted from genomic DNA, and/or sequence assemblages comprised of both cDNA and genomic DNA. These sequences were used to assemble the full length polynucleotide sequences of the invention. Columns 6 and 7 of Table 4 show the nucleotide start (5′) and stop (3′) positions of the cDNA and/or genomic sequences in column 5 relative to their respective full length sequences.  
       [0157] The identification numbers in Column 5 of Table 4 may refer specifically, for example, to Incyte cDNAs along with their corresponding cDNA libraries. For example, 6724643H1 is the identification number of an Incyte cDNA sequence, and LUNLTMT01 is the cDNA library from which it is derived. Incyte cDNAs for which cDNA libraries are not indicated were derived from pooled cDNA libraries (e.g., 71495515V1). Alternatively, the identification numbers in column 5 may refer to GenBank cDNAs or ESTs (e.g., g5746200) which contributed to the assembly of the full length polynucleotide sequences. In addition, the identification numbers in column 5 may identify sequences derived from the ENSEMBL (The Sanger Centre, Cambridge, UK) database (i.e., those sequences including the designation “ENST”). Alternatively, the identification numbers in column 5 may be derived from the NCBI RefSeq Nucleotide Sequence Records Database (i.e., those sequences including the designation “NM” or “NT”) or the NCBI RefSeq Protein Sequence Records (i.e., those sequences including the designation “NP”). Alternatively, the identification numbers in column 5 may refer to assemblages of both cDNA and Genscan-predicted exons brought together by an “exon stitching” algorithm For example, FL_XXXXXX_N 1— N 2— YYYYY_N 3— N 4  represents a “stitched” sequence in which XXXXXX is the identification number of the cluster of sequences to which the algorithm was applied, and YYYYY is the number of the prediction generated by the algorithm, and N 1,2,3 . . .  , if present, represent specific exons that may have been manually edited during analysis (See Example V). Alternatively, the identification numbers in column 5 may refer to assemblages of exons brought together by an “exon-stretching” algorithm. For example, FLXXXXXX_gAAAAA_gBBBBB — 1_N is the identification number of a “stretched” sequence, with XXXXXX being the Incyte project identification number, gAAAAA being the GenBank identification number of the human genomic sequence to which the “exon-stretching” algorithm was applied, gBBBBB being the GenBank identification number or NCBI RefSeq identification number of the nearest GenBank protein homolog, and N referring to specific exons (See Example V). In instances where a RefSeq sequence was used as a protein homolog for the “exon-stretching” algorithm, a RefSeq identifier (denoted by “NM,” “NP,” or “NT”) may be used in place of the GenBank identifier (i.e., gBBBBB).  
       [0158] Alternatively, a prefix identifies component sequences that were hand-edited, predicted from genomic DNA sequences, or derived from a combination of sequence analysis methods. The following Table lists examples of component sequence prefixes and corresponding sequence analysis methods associated with the prefixes (see Example IV and Example V).  
                                   Prefix   Type of analysis and/or examples of programs                  GNN, GFG,   Exon prediction from genomic sequences using, for       ENST   example, GENSCAN (Stanford University, CA,           U.S.A.) or FGENES (Computer Genomics Group,           The Sanger Centre, Cambridge, UK).       GBI   Hand-edited analysis of genomic sequences.       FL   Stitched or stretched genomic sequences (see Example V).                  
 
       [0159] In some cases, Incyte cDNA coverage redundant with the sequence coverage shown in column 5 was obtained to confirm the final consensus polynucleotide sequence, but the relevant Incyte cDNA identification numbers are not shown.  
       [0160] Table 5 shows the representative cDNA libraries for those full length polynucleotide sequences which were assembled using Incyte cDNA sequences. The representative cDNA library is the Incyte cDNA library which is most frequently represented by the Incyte cDNA sequences which were used to assemble and confirm the above polynucleotide sequences. The tissues and vectors which were used to construct the cDNA libraries shown in Table 5 are described in Table 6.  
       [0161] The invention also encompasses TRICH variants. A preferred TRICH variant is one which has at least about 80%, or alternatively at least about 90%, or even at least about 95% amino acid sequence identity to the TRICH amino acid sequence, and which contains at least one functional or structural characteristic of TRICH.  
       [0162] The invention also encompasses polynucleotides which encode TRICH. In a particular embodiment, the invention encompasses a polynucleotide sequence comprising a sequence selected from the group consisting of SEQ ID NOS: 33-64, which encodes TRICH. The polynucleotide sequences of SEQ ID NOS: 33-64, as presented in the Sequence Listing, embrace the equivalent RNA sequences, wherein occurrences of the nitrogenous base thymine are replaced with uracil, and the sugar backbone is composed of ribose instead of deoxyribose.  
       [0163] The invention also encompasses a variant of a polynucleotide sequence encoding TRICH. In particular, such a variant polynucleotide sequence will have at least about 70%, or alternatively at least about 85%, or even at least about 95% polynucleotide sequence identity to the polynucleotide sequence encoding TRICH. A particular aspect of the invention encompasses a variant of a polynucleotide sequence comprising a sequence selected from the group consisting of SEQ ID NOS: 33-64 which has at least about 70%, or alternatively at least about 85%, or even at least about 95% polynucleotide sequence identity to a nucleic acid sequence selected from the group consisting of SEQ ID NOS: 33-64. Any one of the polynucleotide variants described above can encode an amino acid sequence which contains at least one functional or structural characteristic of TRICH.  
       [0164] It will be appreciated by those skilled in the art that as a result of the degeneracy of the genetic code, a multitude of polynucleotide sequences encoding TRICH, some bearing minimal similarity to the polynucleotide sequences of any known and naturally occurring gene, may be produced. Thus, the invention contemplates each and every possible variation of polynucleotide sequence that could be made by selecting combinations based on possible codon choices. These combinations are made in accordance with the standard triplet genetic code as applied to the polynucleotide sequence of naturally occurring TRICH, and all such variations are to be considered as being specifically disclosed.  
       [0165] Although nucleotide sequences which encode TRICH and its variants are generally capable of hybridizing to the nucleotide sequence of the naturally occurring TRICH under appropriately selected conditions of stringency, it may be advantageous to produce nucleotide sequences encoding TRICH or its derivatives possessing a substantially different codon usage, e.g., inclusion of non-naturally occurring codons. Codons may be selected to increase the rate at which expression of the peptide occurs in a particular prokaryotic or eukaryotic host in accordance with the frequency with which particular codons are utilized by the host. Other reasons for substantially altering the nucleotide sequence encoding TRICH and its derivatives without altering the encoded amino acid sequences include the production of RNA transcripts having more desirable properties, such as a greater half-life, than transcripts produced from the naturally occurring sequence.  
       [0166] The invention also encompasses production of DNA sequences which encode TRICH and TRICH derivatives, or fragments thereof, entirely by synthetic chemistry. After production, the synthetic sequence may be inserted into any of the many available expression vectors and cell systems using reagents well known in the art. Moreover, synthetic chemistry may be used to introduce mutations into a sequence encoding TRICH or any fragment thereof.  
       [0167] Also encompassed by the invention are polynucleotide sequences that are capable of hybridizing to the claimed polynucleotide sequences, and, in particular, to those shown in SEQ ID NOS: 33-64 and fragments thereof under various conditions of stringency. (See, e.g., Wahl, G. M. and S. L. Berger (1987) Methods Enzymol. 152:399407; Kimmel, A. R. (1987) Methods Enzymol. 152:507-511.) Hybridization conditions, including annealing and wash conditions, are described in “Definitions.” 
       [0168] Methods for DNA sequencing are well known in the art and may be used to practice any of the embodiments of the invention. The methods may employ such enzymes as the Klenow fragment of DNA polymerase I, SEQUENASE (US Biochemical, Cleveland Ohio), Taq polymerase (Applied Biosystems), thermostable T7 polymerase (Amersham Pharmacia Biotech, Piscataway N.J.), or combinations of polymerases and proofreading exonucleases such as those found in the ELONGASE amplification system (Life Technologies, Gaithersburg Md.). Preferably, sequence preparation is automated with machines such as the MICROLAB 2200 liquid transfer system (Hamilton, Reno Nev.), PTC200 thermal cycler (MJ Research, Watertown Mass.) and ABI CATALYST 800 thermal cycler (Applied Biosystems). Sequencing is then carried out using either the ABI 373 or 377 DNA sequencing system (Applied Biosystems), the MEGABACE 1000 DNA sequencing system (Molecular Dynamics, Sunnyvale Calif.), or other systems known in the art. The resulting sequences are analyzed using a variety of algorithms which are well known in the art. (See, e.g., Ausubel, F. M. (1997)  Short Protocols in Molecular Biology,  John Wiley &amp; Sons, New York N.Y., unit 7.7; Meyers, R. A. (1995)  Molecular Biology and Biotechnology,  Wiley VCH, New York N.Y., pp. 856-853.)  
       [0169] The nucleic acid sequences encoding TRICH may be extended utilizing a partial nucleotide sequence and employing various PCR-based methods known in the art to detect upstream sequences, such as promoters and regulatory elements. For example, one method which may be employed, restriction-site PCR, uses universal and nested primers to amplify unknown sequence from genomic DNA within a cloning vector. (See, e.g., Sarkar, G. (1993) PCR Methods Applic. 2:318-322.) Another method, inverse PCR, uses primers that extend in divergent directions to amplify unknown sequence from a circularized template. The template is derived from restriction fragments comprising a known genomic locus and surrounding sequences. (See, e.g., Triglia, T. et al. (1988) Nucleic Acids Res. 16:8186.) A third method, capture PCR, involves PCR amplification of DNA fragments adjacent to known sequences in human and yeast artificial chromosome DNA. (See, e.g., Lagerstrom, M. et al. (1991) PCR Methods Applic. 1:111-119.) In this method, multiple restriction enzyme digestions and ligations may be used to insert an engineered double-stranded sequence into a region of unknown sequence before performing PCR. Other methods which may be used to retrieve unknown sequences are known in the art. (See, e.g., Parker, J. D. et al. (1991) Nucleic Acids Res. 19:3055-3060). Additionally, one may use PCR, nested primers, and PROMOTERFINDER libraries (Clontech, Palo Alto Calif.) to walk genomic DNA. This procedure avoids the need to screen libraries and is useful in finding intron/exon junctions. For all PCR-based methods, primers may be designed using commercially available software, such as OLIGO 4.06 primer analysis software (National Biosciences, Plymouth Minn.) or another appropriate program, to be about 22 to 30 nucleotides in length, to have a GC content of about 50% or more, and to anneal to the template at temperatures of about 68° C. to 72° C.  
       [0170] When screening for full length cDNAs, it is preferable to use libraries that have been size-selected to include larger cDNAs. In addition, random-primed libraries, which often include sequences containing the 5′ regions of genes, are preferable for situations in which an oligo d(T) library does not yield a full-length cDNA Genomic libraries may be useful for extension of sequence into 5′ non-transcribed regulatory regions.  
       [0171] Capillary electrophoresis systems which are commercially available may be used to analyze the size or confirm the nucleotide sequence of sequencing or PCR products. In particular, capillary sequencing may employ flowable polymers for electrophoretic separation, four different nucleotide-specific, laser-stimulated fluorescent dyes, and a charge coupled device camera for detection of the emitted wavelengths. Output/light intensity may be converted to electrical signal using appropriate software (e.g., GENOTYPER and SEQUENCE NAVIGATOR, Applied Biosystems), and the entire process from loading of samples to computer analysis and electronic data display may be computer controlled. Capillary electrophoresis is especially preferable for sequencing small DNA fragments which may be present in limited amounts in a particular sample.  
       [0172] In another embodiment of the invention, polynucleotide sequences or fragments thereof which encode TRICH may be cloned in recombinant DNA molecules that direct expression of TRICH, or fragments or functional equivalents thereof, in appropriate host cells. Due to the inherent degeneracy of the genetic code, other DNA sequences which encode substantially the same or a functionally equivalent amino acid sequence may be produced and used to express TRICH.  
       [0173] The nucleotide sequences of the present invention can be engineered using methods generally known in the art in order to alter TRICH-encoding sequences for a variety of purposes including, but not limited to, modification of the cloning, processing, and/or expression of the gene product. DNA shuffling by random fragmentation and PCR reassembly of gene fragments and synthetic oligonucleotides may be used to engineer the nucleotide sequences. For example, oligonucleotide-mediated site-directed mutagenesis may be used to introduce mutations that create new restriction sites, alter glycosylation patterns, change codon preference, produce splice variants, and so forth.  
       [0174] The nucleotides of the present invention may be subjected to DNA shuffling techniques such as MOLECULARBREEDING (Maxygen Inc., Santa Clara Calif.; described in U.S. Pat. No. 5,837,458; Chang, C. -C. et al. (1999) Nat. Biotechnol. 17:793-797; Christians, F. C. et al. (1999) Nat. Biotechnol. 17:259-264; and Crameri, A. et al. (1996) Nat. Biotechnol. 14:315-319) to alter or improve the biological properties of TRICH, such as its biological or enzymatic activity or its ability to bind to other molecules or compounds. DNA shuffling is a process by which a library of gene variants is produced using PCR-mediated recombination of gene fragments. The library is then subjected to selection or screening procedures that identify those gene variants with the desired properties. These preferred variants may then be pooled and further subjected to recursive rounds of DNA shuffling and selection/screening. Thus, genetic diversity is created through “artificial” breeding and rapid molecular evolution. For example, fragments of a single gene containing random point mutations may be recombined, screened, and then reshuffled until the desired properties are optimized. Alternatively, fragments of a given gene may be recombined with fragments of homologous genes in the same gene family, either from the same or different species, thereby maximizing the genetic diversity of multiple naturally occurring genes in a directed and controllable manner.  
       [0175] In another embodiment, sequences encoding TRICH may be synthesized, in whole or in part, using chemical methods well known in the art. (See, e.g., Caruthers, M. H. et al. (1980) Nucleic Acids Symp. Ser. 7:215-223; and Horn, T. et al. (1980) Nucleic Acids Symp. Ser. 7:225-232.) Alternatively, TRICH itself or a fragment thereof may be synthesized using chemical methods. For example, peptide synthesis can be performed using various solution-phase or solid-phase techniques. (See, e.g., Creighton, T. (1984)  Proteins, Structures and Molecular Properties,  W H Freeman, New York N.Y., pp. 55-60; and Roberge, J. Y. et al. (1995) Science 269:202-204.) Automated synthesis may be achieved using the ABI 431A peptide synthesizer (Applied Biosystems). Additionally, the amino acid sequence of TRICH, or any part thereof, may be altered during direct synthesis and/or combined with sequences from other proteins, or any part thereof, to produce a variant polypeptide or a polypeptide having a sequence of a naturally occurring polypeptide.  
       [0176] The peptide may be substantially purified by preparative high performance liquid chromatography. (See, e.g., Chiez, R. M. and F. Z. Regnier (1990) Methods Enzymol. 182:392-421.) The composition of the synthetic peptides may be confirmed by amino acid analysis or by sequencing. (See, e.g., Creighton, supra, pp. 28-53.)  
       [0177] In order to express a biologically active TRICH, the nucleotide sequences encoding TRICH or derivatives thereof may be inserted into an appropriate expression vector, i.e., a vector which contains the necessary elements for transcriptional and translational control of the inserted coding sequence in a suitable host. These elements include regulatory sequences, such as enhancers, constitutive and inducible promoters, and 5′ and 3′ untranslated regions in the vector and in polynucleotide sequences encoding TRICH. Such elements may vary in their strength and specificity. Specific initiation signals may also be used to achieve more efficient translation of sequences encoding TRICH. Such signals include the ATG initiation codon and adjacent sequences, e.g. the Kozak sequence. In cases where sequences encoding TRICH and its initiation codon and upstream regulatory sequences are inserted into the appropriate expression vector, no additional transcriptional or translational control signals may be needed. However, in cases where only coding sequence, or a fragment thereof, is inserted, exogenous translational control signals including an in-frame ATG initiation codon should be provided by the vector. Exogenous translational elements and initiation codons may be of various origins, both natural and synthetic. The efficiency of expression may be enhanced by the inclusion of enhancers appropriate for the particular host cell system used. (See, e.g., Scharf, D. et al. (1994) Results Probl. Cell Differ. 20:125-162.)  
       [0178] Methods which are well known to those skilled in the art may be used to construct expression vectors containing sequences encoding TRICH and appropriate transcriptional and translational control elements. These methods include in vitro recombinant DNA techniques, synthetic techniques, and in vivo genetic recombination (See, e.g., Sambrook, J. et al. (1989)  Molecular Cloning, A Laboratory Manual,  Cold Spring Harbor Press, Plainview N.Y., ch. 4, 8, and 16-17; Ausubel, F. M. et al. (1995)  Current Protocols in Molecular Biology,  John Wiley &amp; Sons, New York N.Y., ch. 9, 13, and 16.)  
       [0179] A variety of expression vector/host systems may be utilized to contain and express sequences encoding TRICH. These include, but are not limited to, microorganisms such as bacteria transformed with recombinant bacteriophage, plasmid, or cosmid DNA expression vectors; yeast transformed with yeast expression vectors; insect cell systems infected with viral expression vectors (e.g., baculovirus); plant cell systems transformed with viral expression vectors (e.g., cauliflower mosaic virus, CaMV, or tobacco mosaic virus, TMV) or with bacterial expression vectors (e.g., Ti or pBR322 plasmids); or animal cell systems. (See, e.g., Sambrook, supra; Ausubel, supra; Van Heeke, G. and S. M. Schuster (1989) J. Biol. Chem. 264:5503-5509; Engelhard, E. K. et al. (1994) Proc. Natl. Acad. Sci. USA 91:3224-3227; Sandig, V. et al. (1996) Hum. Gene Ther. 7:1937-1945; Takamatsu, N. (1987) EMBO J. 6:307-311;  The McGraw Hill Yearbook of Science and Technology  (1992) McGraw Hill, New York N.Y., pp. 191-196; Logan, J. and T. Shenk (1984) Proc. Natl. Acad. Sci. USA 81:3655-3659; and Harrington, J. J. et al. (1997) Nat. Genet. 15:345-355.) Expression vectors derived from retroviruses, adenoviruses, or herpes or vaccinia viruses, or from various bacterial plasmids, may be used for delivery of nucleotide sequences to the targeted organ, tissue, or cell population. (See, e.g., Di Nicola, M. et al. (1998) Cancer Gen. Ther. 5(6):350-356; Yu, M. et al. (1993) Proc. Natl. Acad. Sci. USA 90(13):6340-6344; Buller, R. M. et al. (1985) Nature 317(6040):813-815; McGregor, D. P. et al. (1994) Mol. Immunol. 31(3):219-226; and Verma, I. M. and N. Somia (1997) Nature 389:239-242.) The invention is not limited by the host cell employed.  
       [0180] In bacterial systems, a number of cloning and expression vectors may be selected depending upon the use intended for polynucleotide sequences encoding TRICH. For example, routine cloning, subcloning, and propagation of polynucleotide sequences encoding TRICH can be achieved using a multifunctional  E. coli  vector such as PBLUESCRIPT (Stratagene, La Jolla Calif.) or PSPORT1 plasmid (Life Technologies). Ligation of sequences encoding TRICH into the vector&#39;s multiple cloning site disrupts the lacZ gene, allowing a colorimetric screening procedure for identification of transformed bacteria containing recombinant molecules. In addition, these vectors may be useful for in vitro transcription, dideoxy sequencing, single strand rescue with helper phage, and creation of nested deletions in the cloned sequence. (See, e.g., Van Heeke, G. and S. M. Schuster (1989) J. Biol. Chem. 264:5503-5509.) When large quantities of TRICH are needed, e.g. for the production of antibodies, vectors which direct high level expression of TRICH may be used. For example, vectors containing the strong, inducible SP6 or T7 bacteriophage promoter may be used.  
       [0181] Yeast expression systems may be used for production of TRICH. A number of vectors containing constitutive or inducible promoters, such as alpha factor, alcohol oxidase, and PGH promoters, may be used in the yeast  Saccharomyces cerevisiae  or  Pichia pastoris.  In addition, such vectors direct either the secretion or intracellular retention of expressed proteins and enable integration of foreign sequences into the host genome for stable propagation (See, e.g., Ausubel, 1995, supra; Bitter, G. A. et al. (1987) Methods Enzymol. 153:516-544; and Scorer, C. A. et al. (1994) Bio/Technology 12:181-184.)  
       [0182] Plant systems may also be used for expression of TRICH. Transcription of sequences encoding TRICH may be driven by viral promoters, e.g., the 35S and 19S promoters of CaMV used alone or in combination with the omega leader sequence from TMV (Takamatsu, N. (1987) EMBO J. 6:307-311). Alternatively, plant promoters such as the small subunit of RUBISCO or heat shock promoters may be used. (See, e.g., Coruzzi, G. et al. (1984) EMBO J. 3:1671-1680; Broglie, R. et al. (1984) Science 224:838-843; and Winter, J. et al. (1991) Results Probl. Cell Differ. 17:85-105.) These constructs can be introduced into plant cells by direct DNA transformation or pathogen-mediated transfection. (See, e.g.,  The McGraw Hill Yearbook of Science and Technology  (1992) McGraw Hill, New York N.Y., pp. 191-196.)  
       [0183] In mammalian cells, a number of viral-based expression systems may be utilized. In cases where an adenovirus is used as an expression vector, sequences encoding TRICH may be ligated into an adenovirus transcription/translation complex consisting of the late promoter and tripartite leader sequence. Insertion in a non-essential E1 or E3 region of the viral genome may be used to obtain infective virus which expresses TRICH in host cells. (See, e.g., Logan, J. and T. Shenk (1984) Proc. Natl. Acad Sci. USA 81:3655-3659.) In addition, transcription enhancers, such as the Rous sarcoma virus (RSV) enhancer, may be used to increase expression in mammalian host cells. SV40 or EBV-based vectors may also be used for high-level protein expression.  
       [0184] Human artificial chromosomes (HACs) may also be employed to deliver larger fragments of DNA than can be contained in and expressed from a plasmid. HACs of about 6 kb to 10 Mb are constructed and delivered via conventional delivery methods (liposomes, polycationic amino polymers, or vesicles) for therapeutic purposes. (See, e.g., Harrington, J. J. et al. (1997) Nat. Genet. 15:345-355.)  
       [0185] For long term production of recombinant proteins in mammalian systems, stable expression of TRICH in cell lines is preferred. For example, sequences encoding TRICH can be transformed into cell lines using expression vectors which may contain viral origins of replication and/or endogenous expression elements and a selectable marker gene on the same or on a separate vector. Following the introduction of the vector, cells may be allowed to grow for about 1 to 2 days in enriched media before being switched to selective media. The purpose of the selectable marker is to confer resistance to a selective agent, and its presence allows growth and recovery of cells which successfully express the introduced sequences. Resistant clones of stably transformed cells may be propagated using tissue culture techniques appropriate to the cell type.  
       [0186] Any number of selection systems may be used to recover transformed cell lines. These include, but are not limited to, the herpes simplex virus thymidine kinase and adenine phosphoribosyltransferase genes, for use in tk −  and apr −  cells, respectively. (See, e.g., Wigler, M. et al. (1977) Cell 11:223-232; Lowy, I. et al. (1980) Cell 22:817-823.) Also, antimetabolite, antibiotic, or herbicide resistance can be used as the basis for selection. For example, dlifr confers resistance to methotrexate; neo confers resistance to the aminoglycosides neomycin and G-418; and als and pat confer resistance to chlorsulfuron and phosphinotricin acetyltransferase, respectively. (See, e.g., Wigler, M. et al. (1980) Proc. Natl. Acad. Sci. USA 77:3567-3570; Colbere-Garapin, F. et al. (1981) J. Mol. Biol. 150:1-14.) Additional selectable genes have been described, e.g., trpB and hisD, which alter cellular requirements for metabolites. (See, e.g., Hartman, S. C. and R. C. Mulligan (1988) Proc. Natl. Acad. Sci. USA 85:8047-8051.) Visible markers, e.g., anthocyanins, green fluorescent proteins (GFP; Clontech), β glucuronidase and its substrate β-glucuronide, or luciferase and its substrate luciferin may be used. These markers can be used not only to identify transformants, but also to quantify the amount of transient or stable protein expression attributable to a specific vector system. (See, e.g., Rhodes, C. A. (1995) Methods Mol. Biol. 55:121-131.)  
       [0187] Although the presence/absence of marker gene expression suggests that the gene of interest is also present, the presence and expression of the gene may need to be confirmed. For example, if the sequence encoding TRICH is inserted within a marker gene sequence, transformed cells containing sequences encoding TRICH can be identified by the absence of marker gene function. Alternatively, a marker gene can be placed in tandem with a sequence encoding TRICH under the control of a single promoter. Expression of the marker gene in response to induction or selection usually indicates expression of the tandem gene as well.  
       [0188] In general, host cells that contain the nucleic acid sequence encoding TRICH and that express TRICH may be identified by a variety of procedures known to those of skill in the art. These procedures include, but are not limited to, DNA-DNA or DNA-RNA hybridizations, PCR amplification, and protein bioassay or immunoassay techniques which include membrane, solution, or chip based technologies for the detection and/or quantification of nucleic acid or protein sequences.  
       [0189] Immunological methods for detecting and measuring the expression of TRICH using either specific polyclonal or monoclonal antibodies are known in the art. Examples of such techniques include enzyme-linked immunosorbent assays (ELISAs), radioimmunoassays (RIAs), and fluorescence activated cell sorting (FACS). A two-site, monoclonal-based immunoassay utilizing monoclonal antibodies reactive to two non-interfering epitopes on TRICH is preferred, but a competitive binding assay may be employed. These and other assays are well known in the art. (See, e.g., Hampton, R. et al. (1990)  Serological Methods, a Laboratory Manual,  APS Press, St. Paul Minn., Sect. IV; Coligan, J. E. et al. (1997)  Current Protocols in Immunology,  Greene Pub. Associates and Wiley-Interscience, New York N.Y.; and Pound, J. D. (1998)  Immunochemical Protocols,  Humana Press, Totowa N.J.)  
       [0190] A wide variety of labels and conjugation techniques are known by those skilled in the art and may be used in various nucleic acid and amino acid assays. Means for producing labeled hybridization or PCR probes for detecting sequences related to polynucleotides encoding TRICH include oligolabeling, nick translation, end-labeling, or PCR amplification using a labeled nucleotide. Alternatively, the sequences encoding TRICH, or any fragments thereof, may be cloned into a vector for the production of an mRNA probe. Such vectors are known in the art, are commercially available, and may be used to synthesize RNA probes in vitro by addition of an appropriate RNA polymerase such as T7, T3, or SP6 and labeled nucleotides. These procedures may be conducted using a variety of commercially available kits, such as those provided by Amersham Pharmacia Biotech, Promega (Madison Wis.), and US Biochemical. Suitable reporter molecules or labels which may be used for ease of detection include radionuclides, enzymes, fluorescent, chemiluminescent, or chromogenic agents, as well as substrates, cofactors, inhibitors, magnetic particles, and the like.  
       [0191] Host cells transformed with nucleotide sequences encoding TRICH may be cultured under conditions suitable for the expression and recovery of the protein from cell culture. The protein produced by a transformed cell may be secreted or retained intracellularly depending on the sequence and/or the vector used. As will be understood by those of skill in the art, expression vectors containing polynucleotides which encode TRICH may be designed to contain signal sequences which direct secretion of TRICH through a prokaryotic or eukaryotic cell membrane.  
       [0192] In addition, a host cell strain may be chosen for its ability to modulate expression of the inserted sequences or to process the expressed protein in the desired fashion. Such modifications of the polypeptide include, but are not limited to, acetylation, carboxylation, glycosylation, phosphorylation, lipidation, and acylation. Post-translational processing which cleaves a “prepro” or “pro” form of the protein may also be used to specify protein targeting, folding, and/or activity. Different host cells which have specific cellular machinery and characteristic mechanisms for post-translational activities (e.g., CHO, HeLa, MDCK, HEK293, and WI38) are available from the American Type Culture Collection (ATCC, Manassas Va.) and may be chosen to ensure the correct modification and processing of the foreign protein.  
       [0193] In another embodiment of the invention, natural, modified, or recombinant nucleic acid sequences encoding TRICH may be ligated to a heterologous sequence resulting in translation of a fusion protein in any of the aforementioned host systems. For example, a chimeric TRICH protein containing a heterologous moiety that can be recognized by a commercially available antibody may facilitate the screening of peptide libraries for inhibitors of TRICH activity. Heterologous protein and peptide moieties may also facilitate purification of fusion proteins using commercially available affinity matrices. Such moieties include, but are not limited to, glutathione S-transferase (GST), maltose binding protein (MBP), thioredoxin (Trx), calmodulin binding peptide (CBP), 6-His, FLAG, c-myc, and hemagglutinin (HA). GST, MBP, Trx, CBP, and 6-His enable purification of their cognate fusion proteins on immobilized glutathione, maltose, phenylarsine oxide, calmodulin, and metal-chelate resins, respectively. FLAG, c-myc, and hemagglutinin (HA) enable immunoaffinity purification of fusion proteins using commercially available monoclonal and polyclonal antibodies that specifically recognize these epitope tags. A fusion protein may also be engineered to contain a proteolytic cleavage site located between the TRICH encoding sequence and the heterologous protein sequence, so that TRICH may be cleaved away from the heterologous moiety following purification. Methods for fusion protein expression and purification are discussed in Ausubel (1995, supra, ch. 10). A variety of commercially available kits may also be used to facilitate expression and purification of fusion proteins.  
       [0194] In a further embodiment of the invention, synthesis of radiolabeled TRICH may be achieved in vitro using the TNT rabbit reticulocyte lysate or wheat germ extract system (Promega). These systems couple transcription and translation of protein-coding sequences operably associated with the T7, T3, or SP6 promoters. Translation takes place in the presence of a radiolabeled amino acid precursor, for example,  35 S-methionine.  
       [0195] TRICH of the present invention or fragments thereof may be used to screen for compounds that specifically bind to TRICH. At least one and up to a plurality of test compounds may be screened for specific binding to TRICH. Examples of test compounds include antibodies, oligonucleotides, proteins (e.g., receptors), or small molecules.  
       [0196] In one embodiment, the compound thus identified is closely related to the natural ligand of TRICH, e.g., a ligand or fragment thereof, a natural substrate, a structural or functional mimetic, or a natural binding partner. (See, e.g., Coligan, J. E. et al. (1991)  Current Protocols in Immunology  1(2): Chapter 5.) Similarly, the compound can be closely related to the natural receptor to which TRICH binds, or to at least a fragment of the receptor, e.g., the ligand binding site. In either case, the compound can be rationally designed using known techniques. In one embodiment, screening for these compounds involves producing appropriate cells which express TRICH, either as a secreted protein or on the cell membrane. Preferred cells include cells from mammals, yeast, Drosophila, or  E. coli.  Cells expressing TRICH or cell membrane fractions which contain TRICH are then contacted with a test compound and binding, stimulation, or inhibition of activity of either TRICH or the compound is analyzed.  
       [0197] An assay may simply test binding of a test compound to the polypeptide, wherein binding is detected by a fluorophore, radioisotope, enzyme conjugate, or other detectable label. For example, the assay may comprise the steps of combining at least one test compound with TRICH, either in solution or affixed to a solid support, and detecting the binding of TRICH to the compound. Alternatively, the assay may detect or measure binding of a test compound in the presence of a labeled competitor. Additionally, the assay may be carried out using cell-free preparations, chemical libraries, or natural product mixtures, and the test compound(s) may be free in solution or affixed to a solid support.  
       [0198] TRICH of the present invention or fragments thereof may be used to screen for compounds that modulate the activity of TRICH. Such compounds may include agonists, antagonists, or partial or inverse agonists. In one embodiment, an assay is performed under conditions permissive for TRICH activity, wherein TRICH is combined with at least one test compound, and the activity of TRICH in the presence of a test compound is compared with the activity of TRICH in the absence of the test compound. A change in the activity of TRICH in the presence of the test compound is indicative of a compound that modulates the activity of TRICH. Alternatively, a test compound is combined with an in vitro or cell-free system comprising TRICH under conditions suitable for TRICH activity, and the assay is performed. In either of these assays, a test compound which modulates the activity of TRICH may do so indirectly and need not come in direct contact with the test compound. At least one and up to a plurality of test compounds may be screened.  
       [0199] In another embodiment, polynucleotides encoding TRICH or their mammalian homologs may be “knocked out” in an animal model system using homologous recombination in embryonic stem (ES) cells. Such techniques are well known in the art and are useful for the generation of animal models of human disease. (See, e.g., U.S. Pat. No. 5,175,383 and U.S. Pat. No. 5,767,337.) For example, mouse ES cells, such as the mouse 129/SvJ cell line, are derived from the early mouse embryo and grown in culture. The ES cells are transformed with a vector containing the gene of interest disrupted by a marker gene, e.g., the neomycin phosphotransferase gene (neo; Capecchi, M. R. (1989) Science 244:1288-1292). The vector integrates into the corresponding region of the host genome by homologous recombination. Alternatively, homologous recombination takes place using the Cre-loxP system to knockout a gene of interest in a tissue- or developmental stage-specific manner (Marth, J. D. (1996) Clin. Invest. 97:1999-2002; Wagner, K. U. et al. (1997) Nucleic Acids Res. 25:4323-4330). Transformed ES cells are identified and microinjected into mouse cell blastocysts such as those from the C57BL/6 mouse strain. The blastocysts are surgically transferred to pseudopregnant dams, and the resulting chimeric progeny are genotyped and bred to produce heterozygous or homozygous strains. Transgemic animals thus generated may be tested with potential therapeutic or toxic agents.  
       [0200] Polynucleotides encoding TRICH may also be manipulated in vitro in ES cells derived from human blastocysts. Human ES cells have the potential to differentiate into at least eight separate cell lineages including endoderm, mesoderm, and ectodermal cell types. These cell lineages differentiate into, for example, neural cells, hematopoietic lineages, and cardiomyocytes (Thomson, J. A. et al. (1998) Science 282:1145-1147).  
       [0201] Polynucleotides encoding TRICH can also be used to create “knockin” humanized animals (pigs) or transgenic animals (mice or rats) to model human disease. With knockin technology, a region of a polynucleotide encoding TRICH is injected into animal ES cells, and the injected sequence integrates into the animal cell genome. Transformed cells are injected into blastulae, and the blastulae are implanted as described above. Transgenic progeny or inbred lines are studied and treated with potential pharmaceutical agents to obtain information on treatment of a human disease. Alternatively, a mammal inbred to overexpress TRICH, e.g., by secreting TRICH in its milk, may also serve as a convenient source of that protein (Janne, J. et al. (1998) Biotechnol. Annu. Rev. 4:55-74).  
       [0202] Therapeutics  
       [0203] Chemical and structural similarity, e.g., in the context of sequences and motifs, exists between regions of TRICH and transporters and ion channels. In addition, the expression of TRICH is closely associated with adrenal, testicular, and prostate tumors, Crohn&#39;s disease, teratocarcinoma and dendritic cells, brain, lung, ileum, small intestine, uterine myometrial, colon, and pancreatic tissues. Therefore, TRICH appears to play a role in transport, neurological, muscle, immunological, and cell proliferative disorders. In the treatment of disorders associated with increased TRICH expression or activity, it is desirable to decrease the expression or activity of TRICH. In the treatment of disorders associated with decreased TRICH expression or activity, it is desirable to increase the expression or activity of TRICH.  
       [0204] Therefore, in one embodiment TRICH or a fragment or derivative thereof may be administered to a subject to treat or prevent a disorder associated with decreased expression or activity of TRICH. Examples of such disorders include, but are not limited to, a transport disorder such as akinesia, amyotrophic lateral sclerosis, ataxia telangiectasia, cystic fibrosis, Becker&#39;s muscular dystrophy, Bell&#39;s palsy, Charcot-Marie Tooth disease, diabetes mellitus, diabetes insipidus, diabetic neuropathy, Duchenne muscular dystrophy, hyperkalemic periodic paralysis, normokalemic periodic paralysis, Parkinson&#39;s disease, malignant hyperthermia, multidrug resistance, myasthenia gravis, myotonic dystrophy, catatonia, tardive dyskinesia, dystonias, peripheral neuropathy, cerebral neoplasms, prostate cancer, cardiac disorders associated with transport, e.g., angina, bradyarrythmia, tachyarrthmia, hypertension, Long QT syndrome, myocarditis, cardiomyopathy, nemaline myopathy, centronuclear myopathy, lipid myopathy, mitochondrial myopathy, thyrotoxic myopathy, ethanol myopathy, dermatomyositis, inclusion body myositis, infectious myositis, polymyositis, neurological disorders associated with transport, e.g., Alzheimer&#39;s disease, amnesia, bipolar disorder, dementia, depression, epilepsy, Tourette&#39;s disorder, paranoid psychoses, and schizophrenia, and other disorders associated with transport, e.g., neurofibromatosis, postherpetic neuralgia, trigeminal neuropathy, sarcoidosis, sickle cell anemia, Wilson&#39;s disease, cataracts, infertility, pulmonary artery stenosis, sensorineural autosomal deafness, hyperglycemia, hypoglycemia, Grave&#39;s disease, goiter, Cushing&#39;s disease, Addison&#39;s disease, glucose-galactose malabsorption syndrome, hypercholesterolemia, adrenoleukodystrophy, Zellweger syndrome, Menkes disease, occipital horn syndrome, von Gierke disease, cystinuria, iminoglycinuria, Hartup disease, and Fanconi disease; a neurological disorder such as epilepsy, ischemic cerebrovascular disease, stroke, cerebral neoplasms, Alzheimer&#39;s disease, Pick&#39;s disease, Huntington&#39;s disease, dementia, Parkinson&#39;s disease and other extrapyramidal disorders, amyotrophic lateral sclerosis and other motor neuron disorders, progressive neural muscular atrophy, retinitis pigmentosa, hereditary ataxias, multiple sclerosis and other demyelinating diseases, bacterial and viral meningitis, brain abscess, subdural empyema, epidural abscess, suppurative intracranial thrombophlebitis, myelitis and radiculitis, viral central nervous system disease, prion diseases including kuru, Creutzfeldt-Jakob disease, and Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia, nutritional and metabolic diseases of the nervous system, neurofibromatosis, tuberous sclerosis, cerebelloretinal hemangioblastomatosis, encephalotrigeminal syndrome, mental retardation and other developmental disorders of the central nervous system including Down syndrome, cerebral palsy, neuroskeletal disorders, autonomic nervous system disorders, cranial nerve disorders, spinal cord diseases, muscular dystrophy and other neuromuscular disorders, peripheral nervous system disorders, dermatomyositis and polymyositis, inherited, metabolic, endocrine, and toxic myopathies, myasthenia gravis, periodic paralysis, mental disorders including mood, anxiety, and schizophrenic disorders, seasonal affective disorder (SAD), akathesia, amnesia, catatonia, diabetic neuropathy, tardive dyskinesia, dystonias, paranoid psychoses, postherpetic neuralgia, Tourette&#39;s disorder, progressive supranuclear palsy, corticobasal degeneration, and familial frontotemporal dementia; a muscle disorder such as cardiomyopathy, myocarditis, Duchenne&#39;s muscular dystrophy, Becker&#39;s muscular dystrophy, myotonic dystrophy, central core disease, nemaline myopathy, centronuclear myopathy, lipid myopathy, mitochondrial myopathy, infectious myositis, polymyositis, dermatomyositis, inclusion body myositis, thyrotoxic myopathy, ethanol myopathy, angina, anaphylactic shock, arrhythmias, asthma, cardiovascular shock, Cushing&#39;s syndrome, hypertension, hypoglycemia, myocardial infarction, migraine, pheochromocytoma, and myopathies including encephalopathy, epilepsy, Kearns-Sayre syndrome, lactic acidosis, myoclonic disorder, ophthalmoplegia, and acid maltase deficiency (AMD, also known as Pompe&#39;s disease); an immunological disorder such as acquired immunodeficiency syndrome (AIDS), Addison&#39;s disease, adult respiratory distress syndrome, allergies, ankylosing spondylitis, amyloidosis, anemia, asthma, atherosclerosis, autoimmune hemolytic anemia, autoimmune thyroiditis, autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED), bronchitis, cholecystitis, contact dermatitis, Crohn&#39;s disease, atopic dermatitis, dermatomyositis, diabetes mellitus, emphysema, episodic lymphopenia with lymphocytotoxins, erythroblastosis fetalis, erythema nodosum, atrophic gastritis, glomerulonephritis, Goodpasture&#39;s syndrome, gout, Graves&#39; disease, Hashimoto&#39;s thyroiditis, hypereosinophilia, irritable bowel syndrome, multiple sclerosis, myasthenia gravis, myocardial or pericardial inflammation, osteoarthritis, osteoporosis, pancreatitis, polymyositis, psoriasis, Reiter&#39;s syndrome, rheumatoid arthritis, scleroderma, Sjögren&#39;s syndrome, systemic anaphylaxis, systemic lupus erythematosus, systemic sclerosis, thrombocytopenic purpura, ulcerative colitis, uveitis, Werner syndrome, complications of cancer, hemodialysis, and extracorporeal circulation, viral, bacterial, fungal, parasitic, protozoal, and helminthic infections, and trauma; and a cell proliferative disorder such as actinic keratosis, arteriosclerosis, atherosclerosis, bursitis, cirrhosis, hepatitis, mixed connective tissue disease (MCTD), myelofibrosis, paroxysmal nocturnal hemoglobinuria, polycythemia vera, psoriasis, primary thrombocythemia, and cancers including adenocarcinoma, leukemia, lymphoma, melanoma, myeloma, sarcoma, teratocarcinoma, and, in particular, cancers of the adrenal gland, bladder, bone, bone marrow, brain, breast, cervix, gall bladder, ganglia, gastrointestinal tract, heart, kidney, liver, lung, muscle, ovary, pancreas, parathyroid, penis, prostate, salivary glands, skin, spleen, testis, thymus, thyroid, and uterus.  
       [0205] In another embodiment, a vector capable of expressing TRICH or a fragment or derivative thereof may be administered to a subject to treat or prevent a disorder associated with decreased expression or activity of TRICH including, but not limited to, those described above.  
       [0206] In a further embodiment, a composition comprising a substantially purified TRICH in conjunction with a suitable pharmaceutical carrier may be administered to a subject to treat or prevent a disorder associated with decreased expression or activity of TRICH including, but not limited to, those provided above.  
       [0207] In still another embodiment, an agonist which modulates the activity of TRICH may be administered to a subject to treat or prevent a disorder associated with decreased expression or activity of TRICH including, but not limited to, those listed above.  
       [0208] In a further embodiment, an antagonist of TRICH may be administered to a subject to treat or prevent a disorder associated with increased expression or activity of TRICH. Examples of such disorders include, but are not limited to, those transport, neurological, muscle, immunological, and cell proliferative disorders described above. In one aspect, an antibody which specifically binds TRICH may be used directly as an antagonist or indirectly as a targeting or delivery mechanism for bringing a pharmaceutical agent to cells or tissues which express TRICH.  
       [0209] In an additional embodiment, a vector expressing the complement of the polynucleotide encoding TRICH may be administered to a subject to treat or prevent a disorder associated with increased expression or activity of TRICH including, but not limited to, those described above.  
       [0210] In other embodiments, any of the proteins, antagonists, antibodies, agonists, complementary sequences, or vectors of the invention may be administered in combination with other appropriate therapeutic agents. Selection of the appropriate agents for use in combination therapy may be made by one of ordinary skill in the art, according to conventional pharmaceutical principles. The combination of therapeutic agents may act synergistically to effect the treatment or prevention of the various disorders described above. Using this approach, one may be able to achieve therapeutic efficacy with lower dosages of each agent, thus reducing the potential for adverse side effects.  
       [0211] An antagonist of TRICH may be produced using methods which are generally known in the art In particular, purified TRICH may be used to produce antibodies or to screen libraries of pharmaceutical agents to identify those which specifically bind TRICH. Antibodies to TRICH may also be generated using methods that are well known in the art. Such antibodies may include, but are not limited to, polyclonal, monoclonal, chimeric, and single chain antibodies, Fab fragments, and fragments produced by a Fab expression library. Neutralizing antibodies (i.e., those which inhibit dimer formation) are generally preferred for therapeutic use.  
       [0212] For the production of antibodies, various hosts including goats, rabbits, rats, mice, humans, and others may be immunized by injection with TRICH or with any fragment or oligopeptide thereof which has immunogenic properties. Depending on the host species, various adjuvants may be used to increase immunological response. Such adjuvants include, but are not limited to, Freund&#39;s, mineral gels such as aluminum hydroxide, and surface active substances such as lysolecithin, pluronic polyols, polyanions, peptides, oil emulsions, KLH, and dinitrophenol. Among adjuvants used in humans, BCG (bacilli Calmette-Guerin) and  Corynebacterium parvum  are especially preferable.  
       [0213] It is preferred that the oligopeptides, peptides, or fragments used to induce antibodies to TRICH have an amino acid sequence consisting of at least about 5 amino acids, and generally will consist of at least about 10 amino acids. It is also preferable that these oligopeptides, peptides, or fragments are identical to a portion of the amino acid sequence of the natural protein. Short stretches of TRICH amino acids may be fused with those of another protein, such as KLH, and antibodies to the chimeric molecule may be produced.  
       [0214] Monoclonal antibodies to TRICH may be prepared using any technique which provides for the production of antibody molecules by continuous cell lines in culture. These include, but are not limited to, the hybridoma technique, the human Bell hybridoma technique, and the EBV-hybridoma technique. (See, e.g., Kohler, G. et al. (1975) Nature 256:495497; Kozbor, D. et al. (1985) J. Immunol. Methods 81:31-42; Cote, R. J. et al. (1983) Proc. Natl. Acad. Sci. USA 80:2026-2030; and Cole, S. P. et al. (1984) Mol. Cell Biol. 62:109-120.)  
       [0215] In addition, techniques developed for the production of “chimeric antibodies,” such as the splicing of mouse antibody genes to human antibody genes to obtain a molecule with appropriate antigen specificity and biological activity, can be used. (See, e g., Morrison, S. L. et al. (1984) Proc. Natl. Acad. Sci. USA 81:6851-6855; Neuberger, M. S. et al. (1984) Nature 312:604-608; and Takeda, S. et al. (1985) Nature 314:452454.) Alternatively, techniques described for the production of single chain antibodies may be adapted, using methods known in the art, to produce TRICH-specific single chain antibodies. Antibodies with related specificity, but of distinct idiotypic composition, may be generated by chain shuffling from random combinatorial immunoglobulin libraries. (See, e.g., Burton, D. R. (1991) Proc. Natl. Acad. Sci. USA 88:10134-10137.)  
       [0216] Antibodies may also be produced by inducing in vivo production in the lymphocyte population or by screening immunoglobulin libraries or panels of highly specific binding reagents as disclosed in the literature. (See, e.g., Orlandi, R. et al. (1989) Proc. Natl. Acad. Sci. USA 86:3833-3837; Winter, G. et al. (1991) Nature 349:293-299.)  
       [0217] Antibody fragments which contain specific binding sites for TRICH may also be generated. For example, such fragments include, but are not limited to, F(ab′) 2  fragments produced by pepsin digestion of the antibody molecule and Fab fragments generated by reducing the disulfide bridges of the F(ab′)2 fragments. Alternatively, Fab expression libraries may be constructed to allow rapid and easy identification of monoclonal Fab fragments with the desired specificity. (See, e.g., Huse, W. D. et al. (1989) Science 246:1275-1281.)  
       [0218] Various immunoassays may be used for screening to identify antibodies having the desired specificity. Numerous protocols for competitive binding or immunoradiometric assays using either polyclonal or monoclonal antibodies with established specificities are well known in the art. Such immunoassays typically involve the measurement of complex formation between TRICH and its specific antibody. A two-site, monoclonal-based immunoassay utilizing monoclonal antibodies reactive to two non-interfering TRICH epitopes is generally used, but a competitive binding assay may also be employed (Pound, supra).  
       [0219] Various methods such as Scatchard analysis in conjunction with radioimmunoassay techniques may be used to assess the affinity of antibodies for TRICH. Affinity is expressed as an association constant, K a , which is defined as the molar concentration of TRICH-antibody complex divided by the molar concentrations of free antigen and free antibody under equilibrium conditions. The K a  determined for a preparation of polyclonal antibodies, which are heterogeneous in their affinities for multiple TRICH epitopes, represents the average affinity, or avidity, of the antibodies for TRICH. The K a  determined for a preparation of monoclonal antibodies, which are monospecific for a particular TRICH epitope, represents a true measure of affinity. High-affinity antibody preparations with K a  ranging from about 10 9  to 10 12  L/mole are preferred for use in immunoassays in which the TRICH-antibody complex must withstand rigorous manipulations. Low-affinity antibody preparations with K a  ranging from about 10 6  to 10 7  L/mole are preferred for use in immunopurification and similar procedures which ultimately require dissociation of TRICH, preferably in active form, from the antibody (Catty, D. (1988)  Antibodies, Volume l: A Practical Approach,  IRL: Press, Washington D.C.; Liddell, J. E. and A. Cryer (1991)  A Practical Guide to Monoclonal Antibodies,  John Wiley &amp; Sons, New York N.Y.).  
       [0220] The titer and avidity of polyclonal antibody preparations may be further evaluated to determine the quality and suitability of such preparations for certain downstream applications. For example, a polyclonal antibody preparation containing at least 1-2 mg specific antibody/ml, preferably 5-10 mg specific antibody/ml, is generally employed in procedures requiring precipitation of TRICH-antibody complexes. Procedures for evaluating antibody specificity, titer, and avidity, and guidelines for antibody quality and usage in various applications, are generally available. (See, e.g., Catty, supra, and Coligan et al. supra.)  
       [0221] In another embodiment of the invention, the polynucleotides encoding TRICH, or any fragment or complement thereof, may be used for therapeutic purposes. In one aspect, modifications of gene expression can be achieved by designing complementary sequences or antisense molecules (DNA, RNA, PNA, or modified oligonucleotides) to the coding or regulatory regions of the gene encoding TRICH. Such technology is well known in the art, and antisense oligonucleotides or larger fragments can be designed from various locations along the coding or control regions of sequences encoding TRICH. (See, e.g., Agrawal, S., ed. (1996)  Antisense Therapeutics,  Humana Press Inc., Totawa N.J.)  
       [0222] In therapeutic use, any gene delivery system suitable for introduction of the antisense sequences into appropriate target cells can be used. Antisense sequences can be delivered intracellularly in the form of an expression plasmid which, upon transcription, produces a sequence complementary to at least a portion of the cellular sequence encoding the target protein. (See, e.g., Slater, J. E. et al. (1998) J. Allergy Clin. Immunol. 102(3):469475; and Scanlon, K. J. et al. (1995) 9(13):1288-1296.) Antisense sequences can also be introduced intracellularly through the use of viral vectors, such as retrovirus and adeno-associated virus vectors. (See, e.g., Miler, A. D. (1990) Blood 76:271; Ausubel, supra; Uckert, W. and W. Walther (1994) Pharmacol. Ther. 63(3):323-347.) Other gene delivery mechanisms include liposome-derived systems, artificial viral envelopes, and other systems known in the art. (See, e.g., Rossi, J. J. (1995) Br. Med. Bull. 51(1):217-225; Boado, R. J. et al. (1998) J. Pharm. Sci. 87(11):1308-1315; and Morris, M. C. et al. (1997) Nucleic Acids Res. 25(14):2730-2736.)  
       [0223] In another embodiment of the invention, polynucleotides encoding TRICH may be used for somatic or germline gene therapy. Gene therapy may be performed to (i) correct a genetic deficiency (e.g., in the cases of severe combined immunodeficiency (SCID)-X1 disease characterized by X-linked inheritance (Cavazzana-Calvo, M. et al. (2000) Science 288:669-672), severe combined immunodeficiency syndrome associated with an inherited adenosine deaminase (ADA) deficiency (Blaese, R. M. et al. (1995) Science 270:475-480; Bordignon, C. et al. (1995) Science 270:470-475), cystic fibrosis (Zabner, J. et al. (1993) Cell 75:207-216; Crystal, R. G. et al. (1995) Hum. Gene Therapy 6:643-666; Crystal, R. G. et al. (1995) Hum. Gene Therapy 6:667-703), thalassamias, familial hypercholesterolemia, and hemophilia resulting from Factor VIII or Factor IX deficiencies (Crystal, R. G. (1995) Science 270:404-410; Verma, I. M. and N. Somia (1997) Nature 389:239-242)), (ii) express a conditionally lethal gene product (e.g., in the case of cancers which result from unregulated cell proliferation), or (iii) express a protein which affords protection against intracellular parasites (e.g., against human retroviruses, such as human immunodeficiency virus (HIV) (Baltimore, D. (1988) Nature 335:395-396; Poeschla, E. et al. (1996) Proc. Natl. Acad. Sci. USA. 93:11395-11399), hepatitis B or C virus (HBV, HCV); fungal parasites, such as  Candida albicans  and  Paracoccidioides brasiliensis;  and protozoan parasites such as  Plasmodium falciparum  and  Trypanosoma cruzi ). In the case where a genetic deficiency in TRICH expression or regulation causes disease, the expression of TRICH from an appropriate population of transduced cells may alleviate the clinical manifestations caused by the genetic deficiency.  
       [0224] In a further embodiment of the invention, diseases or disorders caused by deficiencies in TRICH are treated by constructing mammalian expression vectors encoding TRICH and introducing these vectors by mechanical means into TRICH-deficient cells. Mechanical transfer technologies for use with cells in vivo or ex vitro include (i) direct DNA microinjection into individual cells, (ii) ballistic gold particle delivery, (iii) liposome-mediated transfection, (iv) receptor-mediated gene transfer, and (v) the use of DNA transposons (Morgan, R. A. and W. F. Anderson (1993) Annu. Rev. Biochem. 62:191-217; Ivics, Z. (1997) Cell 91:501-510; Boulay, J-L. and H. Récipon (1998) Curr. Opin. Biotechnol. 9:445-450).  
       [0225] Expression vectors that may be effective for the expression of TRICH include, but are not limited to, the PCDNA 3.1, EPITAG, PRCCMV2, PREP, PVAX vectors (Invitrogen, Carlsbad Calif.), PCMV-SCRIPT, PCMV-TAG, PEGSH/PERV (Stratagene, La Jolla Calif.), and PTET-OFF, PTET-ON, PTRE2, PTRE2-LUC, PTK-HYG (Clontech, Palo Alto Calif.). TRICH may be expressed using (i) a constitutively active promoter, (e.g., from cytomegalovirus (CMV), Rous sarcoma virus (RSV), SV40 virus, thymidine kinase (TK), or β-actin genes), (ii) an inducible promoter (e.g., the tetracycline-regulated promoter (Gossen, M. and H. Bujard (1992) Proc. Natl. Acad. Sci. USA 89:5547-5551; Gossen, M. et al. (1995) Science 268:1766-1769; Rossi, F. M. V. and H. M. Blau (1998) Curr. Opin. Biotechnol. 9:451-456), commercially available in the T-REX plasmid (Invitrogen)); the ecdysone-inducible promoter (available in the plasmids PVGRXR and PIND; Invitrogen); the FK506/rapamycin inducible promoter; or the RU486/mifepristone inducible promoter (Rossi, F. M. V. and Blau, H. M. supra)), or (iii) a tissue-specific promoter or the native promoter of the endogenous gene encoding TRICH from a normal individual.  
       [0226] Commercially available liposome transformation kits (e.g., the PERFECT LIPID TRANSFECTION KIT, available from Invitrogen) allow one with ordinary skill in the art to deliver polynucleotides to target cells in culture and require minimal effort to optimize experimental parameters. In the alternative, transformation is performed using the calcium phosphate method (Graham, F. L. and A. J. Eb (1973) Virology 52:456-467), or by electroporation (Neumann, E. et al. (1982) EMBO J. 1:841-845). The introduction of DNA to primary cells requires modification of these standardized mammalian transfection protocols.  
       [0227] In another embodiment of the invention, diseases or disorders caused by genetic defects with respect to TRICH expression are treated by constructing a retrovirus vector consisting of (i) the polynucleotide encoding TRICH under the control of an independent promoter or the retrovirus long terminal repeat (LTR) promoter, (ii) appropriate RNA packaging signals, and (iii) a Rev-responsive element (RRE) along with additional retrovirus cis-acting RNA sequences and coding sequences required for efficient vector propagation. Retrovirus vectors (e.g., PFB and PFBNEO) are commercially available (Stratagene) and are based on published data (Riviere, I. et al. (1995) Proc. Natl. Acad. Sci. USA 92:6733-6737), incorporated by reference herein. The vector is propagated in an appropriate vector producing cell line (VPCL) that expresses an envelope gene with a tropism for receptors on the target cells or a promiscuous envelope protein such as VSVg (Armentano, D. et al. (1987) J. Virol. 61:1647-1650; Bender, M. A. et al. (1987) J. Virol. 61:1639-1646; Adam, M. A. and A. D. Miller (1988) J. Virol. 62:3802-3806; Dull, T. et al. (1998) J. Virol. 72:8463-8471; Zufferey, R. et al. (1998) J. Virol. 72:9873-9880). U.S. Pat. No. 5,910,434 to Rigg (“Method for obtaining retrovirus packaging cell lines producing high transducing efficiency retroviral supernatant”) discloses a method for obtaining retrovirus packaging cell lines and is hereby incorporated by reference. Propagation of retrovirus vectors, transduction of a population of cells (e.g., CD4 +  T-cells), and the return of transduced cells to a patient are procedures well known to persons skilled in the art of gene therapy and have been well documented (Ranga, U. et al. (1997) J. Virol. 71:7020-7029; Bauer, G. et al. (1997) Blood 89:2259-2267; Bonyhadi M. L. (1997) J. Virol. 71:4707-4716; Ranga, U. et al. (1998) Proc. Natl. Acad. Sci. USA 95:1201-1206; Su, L. (1997) Blood 89:2283-2290).  
       [0228] In the alternative, an adenovirus-based gene therapy delivery system is used to deliver polynucleotides encoding TRICH to cells which have one or more genetic abnormalities with respect to the expression of TRICH. The construction and packaging of adenovirus-based vectors are well known to those with ordinary skill in the art. Replication defective adenovirus vectors have proven to be versatile for importing genes encoding immunoregulatory proteins into intact islets in the pancreas (Csete, M. E. et al. (1995) Transplantation 27:263-268). Potentially useful adenoviral vectors are described in U.S. Pat. No. 5,707,618 to Armentano (“Adenovirus vectors for gene therapy”), hereby incorporated by reference. For adenoviral vectors, see also Antinozzi, P. A. et al. (1999) Annu. Rev. Nutr. 19:511-544 and Verma, I. M. and N. Somia (1997) Nature 18:389:239-242, both incorporated by reference herein.  
       [0229] In another alternative, a herpes-based, gene therapy delivery system is used to deliver polynucleotides encoding TRICH to target cells which have one or more genetic abnormalities with respect to the expression of TRICH. The use of herpes simplex virus (HSV)-based vectors may be especially valuable for introducing TRICH to cells of the central nervous system, for which HSV has a tropism. The construction and packaging of herpes-based vectors are well known to those with ordinary skill in the art. A replication-competent herpes simplex virus (HSV) type 1-based vector has been used to deliver a reporter gene to the eyes of primates (Liu, X. et al. (1999) Exp. Eye Res. 169:385-395). The construction of a HSV-1 virus vector has also been disclosed in detail in U.S. Pat. No. 5,804,413 to DeLuca (“Herpes simplex virus strains for gene transfer”), which is hereby incorporated by reference. U.S. Pat. No. 5,804,413 teaches the use of recombinant HSV d92 which consists of a genome containing at least one exogenous gene to be transferred to a cell under the control of the appropriate promoter for purposes including human gene therapy. Also taught by this patent are the construction and use of recombinant HSV strains deleted for ICP4, ICP27 and ICP22. For HSV vectors, see also Goins, W. F. et al. (1999) J. Virol. 73:519-532 and Xu, H. et al. (1994) Dev. Biol. 163:152-161, hereby incorporated by reference. The manipulation of cloned herpesvirus sequences, the generation of recombinant virus following the transfection of multiple plasmids containing different segments of the large herpesvirus genomes, the growth and propagation of herpesvirus, and the infection of cells with herpesvirus are techniques well known to those of ordinary skill in the art.  
       [0230] In another alternative, an alphavirus (positive, single-stranded RNA virus) vector is used to deliver polynucleotides encoding TRICH to target cells. The biology of the prototypic alphavirus, Semliki Forest Virus (SFV), has been studied extensively and gene transfer vectors have been based on the SFV genome (Garoff, H. and K. -J. Li (1998) Curr. Opin. Biotechnol. 9:464-469). During alphavirus RNA replication, a subgenomic RNA is generated that normally encodes the viral capsid proteins. This subgenomic RNA replicates to higher levels than the full length genomic RNA, resulting in the overproduction of capsid proteins relative to the viral proteins with enzymatic activity (e.g., protease and polymerase). Similarly, inserting the coding sequence for TRICH into the alphavirus genome in place of the capsid-coding region results in the production of a large number of TRICH-coding RNAs and the synthesis of high levels of TRICH in vector transduced cells. While alphavirus infection is typically associated with cell lysis within a few days, the ability to establish a persistent infection in hamster normal kidney cells (BHK-21) with a variant of Sindbis virus (SIN) indicates that the lytic replication of alphaviruses can be altered to suit the needs of the gene therapy application (Dryga, S. A. et al. (1997) Virology 228:74-83). The wide host range of alphaviruses will allow the introduction of TRICH into a variety of cell types. The specific transduction of a subset of cells in a population may require the sorting of cells prior to transduction. The methods of manipulating infectious cDNA clones of alphaviruses, performing alphavirus cDNA and RNA transfections, and performing alphavirus infections, are well known to those with ordinary skill in the art.  
       [0231] Oligonucleotides derived from the transcription initiation site, e.g., between about positions −10 and +10 from the start site, may also be employed to inhibit gene expression. Similarly, inhibition can be achieved using triple helix base-pairing methodology. Triple helix pairing is useful because it causes inhibition of the ability of the double helix to open sufficiently for the binding of polymerases, transcription factors, or regulatory molecules. Recent therapeutic advances using triplex DNA have been described in the literature. (See, e.g., Gee, J. E. et al. (1994) in Huber, B. E. and B. I. Carr,  Molecular and Immunologic Approaches,  Futura Publishing, Mt. Kisco N.Y., pp. 163-177.) A complementary sequence or antisense molecule may also be designed to block translation of mRNA by preventing the transcript from binding to ribosomes.  
       [0232] Ribozymes, enzymatic RNA molecules, may also be used to catalyze the specific cleavage of RNA. The mechanism of ribozyme action involves sequence-specific hybridization of the ribozyme molecule to complementary target RNA, followed by endonucleolytic cleavage. For example, engineered hammerhead motif ribozyme molecules may specifically and efficiently catalyze endonucleolytic cleavage of sequences encoding TRICH.  
       [0233] Specific ribozyme cleavage sites within any potential RNA target are initially identified by scanning the target molecule for ribozyme cleavage sites, including the following sequences: GUA, GUU, and GUC. Once identified, short RNA sequences of between 15 and 20 ribonucleotides, corresponding to the region of the target gene containing the cleavage site, may be evaluated for secondary structural features which may render the oligonucleotide inoperable. The suitability of candidate targets may also be evaluated by testing accessibility to hybridization with complementary oligonucleotides using ribonuclease protection assays.  
       [0234] Complementary ribonucleic acid molecules and ribozymes of the invention may be prepared by any method known in the art for the synthesis of nucleic acid molecules. These include techniques for chemically synthesizing oligonucleotides such as solid phase phosphoramidite chemical synthesis. Alternatively, RNA molecules may be generated by in vitro and in vivo transcription of DNA sequences encoding TRICH. Such DNA sequences may be incorporated into a wide variety of vectors with suitable RNA polymerase promoters such as T7 or SP6. Alternatively, these cDNA constructs that synthesize complementary RNA, constitutively or inducibly, can be introduced into cell lines, cells, or tissues.  
       [0235] RNA molecules may be modified to increase intracellular stability and half-life. Possible modifications include, but are not limited to, the addition of flanking sequences at the 5′ and/or 3′ ends of the molecule, or the use of phosphorothioate or 2′ O-methyl rather than phosphodiesterase linkages within the backbone of the molecule. This concept is inherent in the production of PNAs and can be extended in al of these molecules by the inclusion of nontraditional bases such as inosine, queosine, and wybutosine, as well as acetyl-, methyl-, thio-, and similarly modified forms of adenine, cytidine, guanine, thymine, and uridine which are not as easily recognized by endogenous endonucleases.  
       [0236] An additional embodiment of the invention encompasses a method for screening for a compound which is effective in altering expression of a polynucleotide encoding TRICH. Compounds which may be effective in altering expression of a specific polynucleotide may include, but are not limited to, oligonucleotides, antisense oligonucleotides, triple helix-forming oligonucleotides, transcription factors and other polypeptide transcriptional regulators, and non-macromolecular chemical entities which are capable of interacting with specific polynucleotide sequences. Effective compounds may alter polynucleotide expression by acting as either inhibitors or promoters of polynucleotide expression. Thus, in the treatment of disorders associated with increased TRICH expression or activity, a compound which specifically inhibits expression of the polynucleotide encoding TRICH may be therapeutically useful, and in the treatment of disorders associated with decreased TRICH expression or activity, a compound which specifically promotes expression of the polynucleotide encoding TRICH may be therapeutically useful.  
       [0237] At least one, and up to a plurality, of test compounds may be screened for effectiveness in altering expression of a specific polynucleotide. A test compound may be obtained by any method commonly known in the art, including chemical modification of a compound known to be effective in altering polynucleotide expression; selection from an existing, commercially-available or proprietary library of naturally-occurring or non-natural chemical compounds; rational design of a compound based on chemical and/or structural properties of the target polynucleotide; and selection from a library of chemical compounds created combinatorially or randomly. A sample comprising a polynucleotide encoding TRICH is exposed to at least one test compound thus obtained. The sample may comprise, for example, an intact or permeabilized cell, or an in vitro cell-free or reconstituted biochemical system. Alterations in the expression of a polynucleotide encoding TRICH are assayed by any method commonly known in the art. Typically, the expression of a specific nucleotide is detected by hybridization with a probe having a nucleotide sequence complementary to the sequence of the polynucleotide encoding TRICH. The amount of hybridization may be quantified, thus forming the basis for a comparison of the expression of the polynucleotide both with and without exposure to one or more test compounds. Detection of a change in the expression of a polynucleotide exposed to a test compound indicates that the test compound is effective in altering the expression of the polynucleotide. A screen for a compound effective in altering expression of a specific polynucleotide can be carried out, for example, using a  Schizosaccharomyces pombe  gene expression system (Atkins, D. et al. (1999) U.S. Pat. No. 5,932,435; Arndt, G. M. et al. (2000) Nucleic Acids Res. 28:E15) or a human cell line such as HeLa cell (Clarke, M. L. et al. (2000) Biochem. Biophys. Res. Commun. 268:8-13). A particular embodiment of the present invention involves screening a combinatorial library of oligonucleotides (such as deoxyribonucleotides, ribonucleotides, peptide nucleic acids, and modified oligonucleotides) for antisense activity against a specific polynucleotide sequence (Bruice, T. W. et al. (1997) U.S. Pat. No. 5,686,242; Bruice, T. W. et al. (2000) U.S. Pat. No. 6,022,691).  
       [0238] Many methods for introducing vectors into cells or tissues are available and equally suitable for use in vivo, in vitro, and ex vivo. For ex vivo therapy, vectors may be introduced into stem cells taken from the patient and clonally propagated for autologous transplant back into that same patient. Delivery by transfection, by liposome injections, or by polycationic amino polymers may be achieved using methods which are well known in the art. (See, e.g., Goldman, C. K. et al. (1997) Nat. Biotechnol. 15:462-466.)  
       [0239] Any of the therapeutic methods described above may be applied to any subject in need of such therapy, including, for example, mammals such as humans, dogs, cats, cows, horses, rabbits, and monkeys.  
       [0240] An additional embodiment of the invention relates to the administration of a composition which generally comprises an active ingredient formulated with a pharmaceutically acceptable excipient. Excipients may include, for example, sugars, starches, celluloses, gums, and proteins. Various formulations are commonly known and are thoroughly discussed in the latest edition of  Remington&#39;s Pharmaceutical Sciences  (Maack Publishing, Easton Pa.). Such compositions may consist of TRICH, antibodies to TRICH, and mimetics, agonists, antagonists, or inhibitors of TRICH.  
       [0241] The compositions utilized in this invention may be administered by any number of routes including, but not limited to, oral, intravenous, intramuscular, intra-arterial, intramedullary, intrathecal, intraventricular, pulmonary, transdermal, subcutaneous, intraperitoneal, intranasal, enteral, topical, sublingual, or rectal means.  
       [0242] Compositions for pulmonary administration may be prepared in liquid or dry powder form. These compositions are generally aerosolized immediately prior to inhalation by the patient. In the case of small molecules (e.g. traditional low molecular weight organic drugs), aerosol delivery of fast-acting formulations is well-known in the art. In the case of macromolecules (e.g. larger peptides and proteins), recent developments in the field of pulmonary delivery via the alveolar region of the lung have enabled the practical delivery of drugs such as insulin to blood circulation (see, e.g., Patton, J. S. et al., U.S. Pat. No. 5,997,848). Pulmonary delivery has the advantage of administration without needle injection, and obviates the need for potentially toxic penetration enhancers.  
       [0243] Compositions suitable for use in the invention include compositions wherein the active ingredients are contained in an effective amount to achieve the intended purpose. The determination of an effective dose is well within the capability of those skilled in the art.  
       [0244] Specialized forms of compositions may be prepared for direct intracellular delivery of macromolecules comprising TRICH or fragments thereof. For example, liposome preparations containing a cell-impermeable macromolecule may promote cell fusion and intracellular delivery of the macromolecule. Alternatively, TRICH or a fragment thereof may be joined to a short cationic N-terminal portion from the HIV Tat-1 protein. Fusion proteins thus generated have been found to transduce into the cells of all tissues, including the brain, in a mouse model system (Schwarze, S. R. et al. (1999) Science 285:1569-1572).  
       [0245] For any compound, the therapeutically effective dose can be estimated initially either in cell culture assays, e.g., of neoplastic cells, or in animal models such as mice, rats, rabbits, dogs, monkeys, or pigs. An animal model may also be used to determine the appropriate concentration range and route of administration. Such information can then be used to determine useful doses and routes for administration in humans.  
       [0246] A therapeutically effective dose refers to that amount of active ingredient, for example TRICH or fragments thereof, antibodies of TRICH, and agonists, antagonists or inhibitors of TRICH, which ameliorates the symptoms or condition. Therapeutic efficacy and toxicity may be determined by standard pharmaceutical procedures in cell cultures or with experimental animals, such as by calculating the ED 50  (the dose therapeutically effective in 50% of the population) or LD 50  (the dose lethal to 50% of the population) statistics. The dose ratio of toxic to therapeutic effects is the therapeutic index, which can be expressed as the LD50/ED 50  ratio. Compositions which exhibit large therapeutic indices are preferred. The data obtained from cell culture assays and animal studies are used to formulate a range of dosage for human use. The dosage contained in such compositions is preferably within a range of circulating concentrations that includes the ED 50  with little or no toxicity. The dosage varies within this range depending upon the dosage form employed, the sensitivity of the patient, and the route of administration.  
       [0247] The exact dosage will be determined by the practitioner, in light of factors related to the subject requiring treatment. Dosage and administration are adjusted to provide sufficient levels of the active moiety or to maintain the desired effect. Factors which may be taken into account include the severity of the disease state, the general health of the subject, the age, weight, and gender of the subject, time and frequency of administration, drug combination(s), reaction sensitivities, and response to therapy. Long-acting compositions may be administered every 3 to 4 days, every week, or biweekly depending on the half-life and clearance rate of the particular formulation.  
       [0248] Normal dosage amounts may vary from about 0.1 μg to 100,000 μg, up to a total dose of about 1 gram, depending upon the route of administration. Guidance as to particular dosages and methods of delivery is provided in the literature and generally available to practitioners in the art. Those skilled in the art will employ different formulations for nucleotides than for proteins or their inhibitors. Similarly, delivery of polynucleotides or polypeptides will be specific to particular cells, conditions, locations, etc.  
       [0249] Diagnostics  
       [0250] In another embodiment, antibodies which specifically bind TRICH may be used for the diagnosis of disorders characterized by expression of TRICH, or in assays to monitor patients being treated with TRICH or agonists, antagonists, or inhibitors of TRICH. Antibodies useful for diagnostic purposes may be prepared in the same manner as described above for therapeutics. Diagnostic assays for TRICH include methods which utilize the antibody and a label to detect TRICH in human body fluids or in extracts of cells or tissues. The antibodies may be used with or without modification, and may be labeled by covalent or non-covalent attachment of a reporter molecule. A wide variety of reporter molecules, several of which are described above, are known in the art and may be used.  
       [0251] A variety of protocols for measuring TRICH, including ELISAs, RIAs, and FACS, are known in the art and provide a basis for diagnosing altered or abnormal levels of TRICH expression. Normal or standard values for TRICH expression are established by combining body fluids or cell extracts taken from normal mammalian subjects, for example, human subjects, with antibodies to TRICH under conditions suitable for complex formation. The amount of standard complex formation may be quantitated by various methods, such as photometric means. Quantities of TRICH expressed in subject, control, and disease samples from biopsied tissues are compared with the standard values. Deviation between standard and subject values establishes the parameters for diagnosing disease.  
       [0252] In another embodiment of the invention, the polynucleotides encoding TRICH may be used for diagnostic purposes. The polynucleotides which may be used include oligonucleotide sequences, complementary RNA and DNA molecules, and PNAs. The polynucleotides may be used to detect and quantify gene expression in biopsied tissues in which expression of TRICH may be correlated with disease. The diagnostic assay may be used to determine absence, presence, and excess expression of TRICH, and to monitor regulation of TRICH levels during therapeutic intervention.  
       [0253] In one aspect, hybridization with PCR probes which are capable of detecting polynucleotide sequences, including genomic sequences, encoding TRICH or closely related molecules may be used to identify nucleic acid sequences which encode TRICH. The specificity of the probe, whether it is made from a highly specific region, e.g., the 5′ regulatory region, or from a less specific region, e.g., a conserved motif, and the stringency of the hybridization or amplification will determine whether the probe identifies only naturally occurring sequences encoding TRICH, allelic variants, or related sequences.  
       [0254] Probes may also be used for the detection of related sequences, and may have at least 50% sequence identity to any of the TRICH encoding sequences. The hybridization probes of the subject invention may be DNA or RNA and may be derived from the sequence of SEQ ID NOS: 33-64 or from genomic sequences including promoters, enhancers, and introns of the TRICH gene.  
       [0255] Means for producing specific hybridization probes for DNAs encoding TRICH include the cloning of polynucleotide sequences encoding TRICH or TRICH derivatives into vectors for the production of mRNA probes. Such vectors are known in the art, are commercially available, and may be used to synthesize RNA probes in vitro by means of the addition of the appropriate RNA polymerases and the appropriate labeled nucleotides. Hybridization probes may be labeled by a variety of reporter groups, for example, by radionuclides such as  32 P or  35 S, or by enzymatic labels, such as alkaline phosphatase coupled to the probe via avidin/biotin coupling systems, and the like.  
       [0256] Polynucleotide sequences encoding TRICH may be used for the diagnosis of disorders associated with expression of TRICH. Examples of such disorders include, but are not limited to, a transport disorder such as akinesia, amyotrophic lateral sclerosis, ataxia telangiectasia, cystic fibrosis, Becker&#39;s muscular dystrophy, Bell&#39;s palsy, Charcot-Marie Tooth disease, diabetes mellitus, diabetes insipidus, diabetic neuropathy, Duchenne muscular dystrophy, hyperkalemic periodic paralysis, normokalemic periodic paralysis, Parkinson&#39;s disease, malignant hyperthermia, multidrug resistance, myasthenia gravis, myotonic dystrophy, catatonia, tardive dyskinesia, dystonias, peripheral neuropathy, cerebral neoplasms, prostate cancer, cardiac disorders associated with transport, e.g., angina, bradyarrythmia, tachyarrythmia, hypertension, Long QT syndrome, myocarditis, cardiomyopathy, nemaline myopathy, centronuclear myopathy, lipid myopathy, mitochondrial myopathy, thyrotoxic myopathy, ethanol myopathy, dermatomyositis, inclusion body myositis, infectious myositis, polymyositis, neurological disorders associated with transport, e.g., Alzheimer&#39;s disease, amnesia, bipolar disorder, dementia, depression, epilepsy, Tourette&#39;s disorder, paranoid psychoses, and schizophrenia, and other disorders associated with transport, e.g., neurofibromatosis, postherpetic neuralgia, trigeminal neuropathy, sarcoidosis, sickle cell anemia, Wilson&#39;s disease, cataracts, infertility, pulmonary artery stenosis, sensorineural autosomal deafness, hyperglycemia, hypoglycemia, Grave&#39;s disease, goiter, Cushing&#39;s disease, Addison&#39;s disease, glucose-galactose malabsorption syndrome, hypercholesterolemia, adrenoleukodystrophy, Zellweger syndrome, Menkes disease, occipital horn syndrome, von Gierke disease, cystinuria, iminoglycinuria, Hartup disease, and Fanconi disease; a neurological disorder such as epilepsy, ischemic cerebrovascular disease, stroke, cerebral neoplasms, Alzheimer&#39;s disease, Pick&#39;s disease, Huntington&#39;s disease, dementia, Parkinson&#39;s disease and other extrapyramidal disorders, amyotrophic lateral sclerosis and other motor neuron disorders, progressive neural muscular atrophy, retinitis pigmentosa, hereditary ataxias, multiple sclerosis and other demyelinating diseases, bacterial and viral meningitis, brain abscess, subdural empyema, epidural abscess, suppurative intracranial thrombophlebitis, myelitis and radiculitis, viral central nervous system disease, prion diseases including kuru, Creutzfeldt-Jakob disease, and Gerstmann-Straussler-Scheinker syndrome, fatal familial insomnia, nutritional and metabolic diseases of the nervous system, neurofibromatosis, tuberous sclerosis, cerebelloretinal hemangioblastomatosis, encephalotrigeminal syndrome, mental retardation and other developmental disorders of the central nervous system including Down syndrome, cerebral palsy, neuroskeletal disorders, autonomic nervous system disorders, cranial nerve disorders, spinal cord diseases, muscular dystrophy and other neuromuscular disorders, peripheral nervous system disorders, dermatomyositis and polymyositis, inherited, metabolic, endocrine, and toxic myopathies, myasthenia gravis, periodic paralysis, mental disorders including mood, anxiety, and schizophrenic disorders, seasonal affective disorder (SAD), akathesia, amnesia, catatonia, diabetic neuropathy, tardive dyskinesia, dystonias, paranoid psychoses, postherpetic neuralgia, Tourette&#39;s disorder, progressive supranuclear palsy, corticobasal degeneration, and familial frontotemporal dementia; a muscle disorder such as cardiomyopathy, myocarditis, Duchenne&#39;s muscular dystrophy, Becker&#39;s muscular dystrophy, myotonic dystrophy, central core disease, nemaline myopathy, centronuclear myopathy, lipid myopathy, mitochondrial myopathy, infectious myositis, polymyositis, dermatomyositis, inclusion body myositis, thyrotoxic myopathy, ethanol myopathy, angina, anaphylactic shock, arrhythmias, asthma, cardiovascular shock, Cushing&#39;s syndrome, hypertension, hypoglycemia, myocardial infarction, migraine, pheochromocytoma, and myopathies including encephalopathy, epilepsy, Kearns-Sayre syndrome, lactic acidosis, myoclonic disorder, ophthalmoplegia, and acid maltase deficiency (AMD, also known as Pompe&#39;s disease); an immunological disorder such as acquired immunodeficiency syndrome (AIDS), Addison&#39;s disease, adult respiratory distress syndrome, allergies, ankylosing spondylitis, amyloidosis, anemia, asthma, atherosclerosis, autoimmune hemolytic anemia, autoimmune thyroiditis, autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED), bronchitis, cholecystitis, contact dermatitis, Crohn&#39;s disease, atopic dermatitis, dermatomyositis, diabetes mellitus, emphysema, episodic lymphopenia with lymphocytotoxins, erythroblastosis fetalis, erythema nodosum, atrophic gastritis, glomerulonephritis, Goodpasture&#39;s syndrome, gout, Graves&#39; disease, Hashimoto&#39;s thyroiditis, hypereosinophilia, irritable bowel syndrome, multiple sclerosis, myasthenia gravis, myocardial or pericardial inflammation, osteoarthritis, osteoporosis, pancreatitis, polymyositis, psoriasis, Reiter&#39;s syndrome, rheumatoid arthritis, scleroderma, Sjögren&#39;s syndrome, systemic anaphylaxis, systemic lupus erythematosus, systemic sclerosis, thrombocytopenic purpura, ulcerative colitis, uveitis, Werner syndrome, complications of cancer, hemodialysis, and extracorporeal circulation, viral, bacterial, fungal, parasitic, protozoal, and helminthic infections, and trauma; and a cell proliferative disorder such as actinic keratosis, arteriosclerosis, atherosclerosis, bursitis, cirrhosis, hepatitis, mixed connective tissue disease (MCTD), myelofibrosis, paroxysmal nocturnal hemoglobinuria, polycythemia vera, psoriasis, primary thrombocythemia, and cancers including adenocarcinoma, leukemia, lymphoma, melanoma, myeloma, sarcoma, teratocarcinoma, and, in particular, cancers of the adrenal gland, bladder, bone, bone marrow, brain, breast, cervix, gall bladder, ganglia, gastrointestinal tract, heart, kidney, liver, lung, muscle, ovary, pancreas, parathyroid, penis, prostate, salivary glands, skin, spleen, testis, thymus, thyroid, and uterus. The polynucleotide sequences encoding TRICH may be used in Southern or northern analysis, dot blot, or other membrane-based technologies; in PCR technologies; in dipstick, pin, and multiformat ELISA-like assays; and in microarrays utilizing fluids or tissues from patients to detect altered TRICH expression. Such qualitative or quantitative methods are well known in the art.  
       [0257] In a particular aspect, the nucleotide sequences encoding TRICH may be useful in assays that detect the presence of associated disorders, particularly those mentioned above. The nucleotide sequences encoding TRICH may be labeled by standard methods and added to a fluid or tissue sample from a patient under conditions suitable for the formation of hybridization complexes. After a suitable incubation period, the sample is washed and the signal is quantified and compared with a standard value. If the amount of signal in the patient sample is significantly altered in comparison to a control sample then the presence of altered levels of nucleotide sequences encoding TRICH in the sample indicates the presence of the associated disorder. Such assays may also be used to evaluate the efficacy of a particular therapeutic treatment regimen in animal studies, in clinical trials, or to monitor the treatment of an individual patient.  
       [0258] In order to provide a basis for the diagnosis of a disorder associated with expression of TRICH, a normal or standard profile for expression is established. This may be accomplished by combining body fluids or cell extracts taken from normal subjects, either animal or human, with a sequence, or a fragment thereof, encoding TRICH, under conditions suitable for hybridization or amplification. Standard hybridization may be quantified by comparing the values obtained from normal subjects with values from an experiment in which a known amount of a substantially purified polynucleotide is used. Standard values obtained in this manner may be compared with values obtained from samples from patients who are symptomatic for a disorder. Deviation from standard values is used to establish the presence of a disorder.  
       [0259] Once the presence of a disorder is established and a treatment protocol is initiated, hybridization assays may be repeated on a regular basis to determine if the level of expression in the patient begins to approximate that which is observed in the normal subject The results obtained from successive assays may be used to show the efficacy of treatment over a period ranging from several days to months.  
       [0260] With respect to cancer, the presence of an abnormal amount of transcript (either under- or overexpressed) in biopsied tissue from an individual may indicate a predisposition for the development of the disease, or may provide a means for detecting the disease prior to the appearance of actual clinical symptoms. A more definitive diagnosis of this type may allow health professionals to employ preventative measures or aggressive treatment earlier thereby preventing the development or further progression of the cancer.  
       [0261] Additional diagnostic uses for oligonucleotides designed from the sequences encoding TRICH may involve the use of PCR. These oligomers may be chemically synthesized, generated enzymatically, or produced in vitro. Oligomers will preferably contain a fragment of a polynucleotide encoding TRICH, or a fragment of a polynucleotide complementary to the polynucleotide encoding TRICH, and will be employed under optimized conditions for identification of a specific gene or condition. Oligomers may also be employed under less stringent conditions for detection or quantification of closely related DNA or RNA sequences.  
       [0262] In a particular aspect, oligonucleotide primers derived from the polynucleotide sequences encoding TRICH may be used to detect single nucleotide polymorphisms (SNPs). SNPs are substitutions, insertions and deletions that are a frequent cause of inherited or acquired genetic disease in humans. Methods of SNP detection include, but are not limited to, single-stranded conformation polymorphism (SSCP) and fluorescent SSCP (fSSCP) methods. In SSCP, oligonucleotide primers derived from the polynucleotide sequences encoding TRICH are used to amplify DNA using the polymerase chain reaction (PCR). The DNA may be derived, for example, from diseased or normal tissue, biopsy samples, bodily fluids, and the like. SNPs in the DNA cause differences in the secondary and tertiary structures of PCR products in single-stranded form, and these differences are detectable using gel electrophoresis in non-denaturing gels. In fSCCP, the oligonucleotide primers are fluorescently labeled, which allows detection of the amplimers in high-throughput equipment such as DNA sequencing machines. Additionally, sequence database analysis methods, termed in silico SNP (isSNP), are capable of identifying polymorphisms by comparing the sequence of individual overlapping DNA fragments which assemble into a common consensus sequence. These computer-based methods filter out sequence variations due to laboratory preparation of DNA and sequencing errors using statistical models and automated analyses of DNA sequence chromatograms. In the alternative, SNPs may be detected and characterized by mass spectrometry using, for example, the high throughput MASSARRAY system (Sequenom, Inc., San Diego Calif.).  
       [0263] Methods which may also be used to quantify the expression of TRICH include radiolabeling or biotinylating nucleotides, coamplification of a control nucleic acid, and interpolating results from standard curves. (See, e.g., Melby, P. C. et al. (1993) J. Immunol. Methods 159:235-244; Duplaa, C. et al. (1993) Anal. Biochem. 212:229-236.) The speed of quantitation of multiple samples may be accelerated by running the assay in a high-throughput format where the oligomer or polynucleotide of interest is presented in various dilutions and a spectrophotometric or colorimetric response gives rapid quantitation.  
       [0264] In further embodiments, oligonucleotides or longer fragments derived from any of the polynucleotide sequences described herein may be used as elements on a microarray. The microarray can be used in transcript imaging techniques which monitor the relative expression levels of large numbers of genes simultaneously as described below. The microarray may also be used to identify genetic variants, mutations, and polymorphisms. This information may be used to determine gene function, to understand the genetic basis of a disorder, to diagnose a disorder, to monitor progression/regression of disease as a function of gene expression, and to develop and monitor the activities of therapeutic agents in the treatment of disease. In particular, this information may be used to develop a pharmacogenomic profile of a patient in order to select the most appropriate and effective treatment regimen for that patient. For example, therapeutic agents which are highly effective and display the fewest side effects may be selected for a patient based on his/her pharmacogenomic profile.  
       [0265] In another embodiment, TRICH, fragments of TRICH, or antibodies specific for TRICH may be used as elements on a microarray. The microarray may be used to monitor or measure protein-protein interactions, drug-target interactions, and gene expression profiles, as described above.  
       [0266] A particular embodiment relates to the use of the polynucleotides of the present invention to generate a transcript image of a tissue or cell type. A transcript image represents the global pattern of gene expression by a particular tissue or cell type. Global gene expression patterns are analyzed by quantifying the number of expressed genes and their relative abundance under given conditions and at a given time. (See Seilhamer et al., “Comparative Gene Transcript Analysis,” U.S. Pat. No. 5,840,484, expressly incorporated by reference herein.) Thus a transcript image may be generated by hybridizing the polynucleotides of the present invention or their complements to the totality of transcripts or reverse transcripts of a particular tissue or cell type. In one embodiment, the hybridization takes place in high-throughput format, wherein the polynucleotides of the present invention or their complements comprise a subset of a plurality of elements on a microarray. The resultant transcript image would provide a profile of gene activity.  
       [0267] Transcript images may be generated using transcripts isolated from tissues, cell lines, biopsies, or other biological samples. The transcript image may thus reflect gene expression in vivo, as in the case of a tissue or biopsy sample, or in vitro, as in the case of a cell line.  
       [0268] Transcript images which profile the expression of the polynucleotides of the present invention may also be used in conjunction with in vitro model systems and preclinical evaluation of pharmaceuticals, as well as toxicological testing of industrial and naturally-occurring environmental compounds. All compounds induce characteristic gene expression patterns, frequently termed molecular fingerprints or toxicant signatures, which are indicative of mechanisms of action and toxicity (Nuwaysir, E. F. et al. (1999) Mol. Carcinog. 24:153-159; Steiner, S. and N. L. Anderson (2000) Toxicol. Lett. 112-113:467-471, expressly incorporated by reference herein). If a test compound has a signature similar to that of a compound with known toxicity, it is likely to share those toxic properties. These fingerprints or signatures are most useful and refined when they contain expression information from a large number of genes and gene families. Ideally, a genome-wide measurement of expression provides the highest quality signature. Even genes whose expression is not altered by any tested compounds are important as well, as the levels of expression of these genes are used to normalize the rest of the expression data. The normalization procedure is useful for comparison of expression data after treatment with different compounds. While the assignment of gene function to elements of a toxicant signature aids in interpretation of toxicity mechanisms, knowledge of gene function is not necessary for the statistical matching of signatures which leads to prediction of toxicity. (See, for example, Press Release 00-02 from the National Institute of Environmental Health Sciences, released Feb. 29, 2000, available at http://www.niehs.nih.gov/oc/news/toxchip.htm.) Therefore, it is important and desirable in toxicological screening using toxicant signatures to include all expressed gene sequences.  
       [0269] In one embodiment, the toxicity of a test compound is assessed by treating a biological sample containing nucleic acids with the test compound. Nucleic acids that are expressed in the treated biological sample are hybridized with one or more probes specific to the polynucleotides of the present invention, so that transcript levels corresponding to the polynucleotides of the present invention may be quantified. The transcript levels in the treated biological sample are compared with levels in an untreated biological sample. Differences in the transcript levels between the two samples are indicative of a toxic response caused by the test compound in the treated sample.  
       [0270] Another particular embodiment relates to the use of the polypeptide sequences of the present invention to analyze the proteome of a tissue or cell type. The term proteome refers to the global pattern of protein expression in a particular tissue or cell type. Each protein component of a proteome can be subjected individually to further analysis. Proteome expression patterns, or profiles, are analyzed by quantifying the number of expressed proteins and their relative abundance under given conditions and at a given time, A profile of a cell&#39;s proteome may thus be generated by separating and analyzing the polypeptides of a particular tissue or cell type. In one embodiment, the separation is achieved using two-dimensional gel electrophoresis, in which proteins from a sample are separated by isoelectric focusing in the first dimension, and then according to molecular weight by sodium dodecyl sulfate slab gel electrophoresis in the second dimension (Steiner and Anderson, supra). The proteins are visualized in the gel as discrete and uniquely positioned spots, typically by staining the gel with an agent such as Coomassie Blue or silver or fluorescent stains. The optical density of each protein spot is generally proportional to the level of the protein in the sample. The optical densities of equivalently positioned protein spots from different samples, for example, from biological samples either treated or untreated with a test compound or therapeutic agent, are compared to identify any changes in protein spot density related to the treatment. The proteins in the spots are partially sequenced using, for example, standard methods employing chemical or enzymatic cleavage followed by mass spectrometry. The identity of the protein in a spot may be determined by comparing its partial sequence, preferably of at least 5 contiguous amino acid residues, to the polypeptide sequences of the present invention. In some cases, further sequence data may be obtained for definitive protein identification.  
       [0271] A proteomic profile may also be generated using antibodies specific for TRICH to quantify the levels of TRICH expression. In one embodiment, the antibodies are used as elements on a microarray, and protein expression levels are quantified by exposing the microarray to the sample and detecting the levels of protein bound to each array element (Lueking, A. et al. (1999) Anal. Biochem 270:103-111; Mendoze, L. G. et al. (1999) Biotechniques 27:778-788). Detection may be performed by a variety of methods known in the art, for example, by reacting the proteins in the sample with a thiol- or amino-reactive fluorescent compound and detecting the amount of fluorescence bound at each array element.  
       [0272] Toxicant signatures at the proteome level are also useful for toxicological screening, and should be analyzed in parallel with toxicant signatures at the transcript level. There is a poor correlation between transcript and protein abundances for some proteins in some tissues (Anderson, N. L. and J. Seilhamer (1997) Electrophoresis 18:533-537), so proteome toxicant signatures may be useful in the analysis of compounds which do not significantly affect the transcript image, but which alter the proteomic profile. In addition, the analysis of transcripts in body fluids is difficult, due to rapid degradation of mRNA, so proteomic profiling may be more reliable and informative in such cases.  
       [0273] In another embodiment, the toxicity of a test compound is assessed by treating a biological sample containing proteins with the test compound. Proteins that are expressed in the treated biological sample are separated so that the amount of each protein can be quantified. The amount of each protein is compared to the amount of the corresponding protein in an untreated biological sample. A difference in the amount of protein between the two samples is indicative of a toxic response to the test compound in the treated sample. Individual proteins are identified by sequencing the amino acid residues of the individual proteins and comparing these partial sequences to the polypeptides of the present invention.  
       [0274] In another embodiment, the toxicity of a test compound is assessed by treating a biological sample containing proteins with the test compound. Proteins from the biological sample are incubated with antibodies specific to the polypeptides of the present invention. The amount of protein recognized by the antibodies is quantified. The amount of protein in the treated biological sample is compared with the amount in an untreated biological sample. A difference in the amount of protein between the two samples is indicative of a toxic response to the test compound in the treated sample.  
       [0275] Microarrays may be prepared, used, and analyzed using methods known in the art. (See, e.g., Brennan, T. M. et al. (1995) U.S. Pat. No. 5,474,796; Schena, M. et al. (1996) Proc. Natl. Acad. Sci. USA 93:10614-10619; Baldeschweiler et al. (1995) PCT application WO95/251116; Shalon, D. et al. (1995) PCT application WO95/35505; Heller, R. A. et al. (1997) Proc. Natl. Acad. Sci. USA 94:2150-2155; and Heller, M. J. et al. (1997) U.S. Pat. No. 5,605,662.) Various types of microarrays are well known and thoroughly described in  DNA Microarrays: A Practical Approach,  M. Schena, ed. (1999) Oxford University Press, London, hereby expressly incorporated by reference.  
       [0276] In another embodiment of the invention, nucleic acid sequences encoding TRICH may be used to generate hybridization probes useful in mapping the naturally occurring genomic sequence. Either coding or noncoding sequences may be used, and in some instances, noncoding sequences may be preferable over coding sequences. For example, conservation of a coding sequence among members of a multi-gene family may potentially cause undesired cross hybridization during chromosomal mapping. The sequences may be mapped to a particular chromosome, to a specific region of a chromosome, or to artificial chromosome constructions, e.g., human artificial chromosomes (HACs), yeast artificial chromosomes (YACs), bacterial artificial chromosomes (BACs), bacterial P1 constructions, or single chromosome cDNA libraries. (See, e.g., Harrington, J. J. et al. (1997) Nat. Genet. 15:345-355; Price, C. M. (1993) Blood Rev. 7:127-134; and Trask, B. J. (1991) Trends Genet. 7:149-154.) Once mapped, the nucleic acid sequences of the invention may be used to develop genetic linkage maps, for example, which correlate the inheritance of a disease state with the inheritance of a particular chromosome region or restriction fragment length polymorphism (RFLP). (See, for example, Lander, E. S. and D. Botstein (1986) Proc. Natl. Acad. Sci. USA 83:7353-7357.) Fluorescent in situ hybridization (FISH) may be correlated with other physical and genetic map data. (See, e.g., Heinz-Ulrich, et al. (1995) in Meyers, supra, pp. 965-968.) Examples of genetic map data can be found in various scientific journals or at the Online Mendelian Inheritance in Man (OMIM) World Wide Web site. Correlation between the location of the gene encoding TRICH on a physical map and a specific disorder, or a predisposition to a specific disorder, may help define the region of DNA associated with that disorder and thus may further positional cloning efforts.  
       [0277] In situ hybridization of chromosomal preparations and physical mapping techniques, such as linkage analysis using established chromosomal markers, may be used for extending genetic maps. Often the placement of a gene on the chromosome of another mammalian species, such as mouse, may reveal associated markers even if the exact chromosomal locus is not known. This information is valuable to investigators searching for disease genes using positional cloning or other gene discovery techniques. Once the gene or genes responsible for a disease or syndrome have been crudely localized by genetic linkage to a particular genomic region, e.g., ataxia-telangiectasia to 11q22-23, any sequences mapping to that area may represent associated or regulatory genes for further investigation. (See, e.g., Gatti, R. A. et al. (1988) Nature 336:577-580.) The nucleotide sequence of the instant invention may also be used to detect differences in the chromosomal location due to translocation, inversion, etc., among normal, carrier, or affected individuals.  
       [0278] In another embodiment of the invention, TRICH, its catalytic or immunogenic fragments, or oligopeptides thereof can be used for screening libraries of compounds in any of a variety of drug screening techniques. The fragment employed in such screening may be free in solution, affixed to a solid support, borne on a cell surface, or located intracellularly. The formation of binding complexes between TRICH and the agent being tested may be measured.  
       [0279] Another technique for drug screening provides for high throughput screening of compounds having suitable binding affinity to the protein of interest. (See, e.g., Geysen, et al. (1984) PCT application WO84/03564.) In this method, large numbers of different small test compounds are synthesized on a solid substrate. The test compounds are reacted with TRICH, or fragments thereof, and washed. Bound TRICH is then detected by methods well known in the art. Purified TRICH can also be coated direly onto plates for use in the aforementioned drug screening techniques. Alternatively, non-neutralizing antibodies can be used to capture the peptide and immobilize it on a solid support.  
       [0280] In another embodiment, one may use competitive drug screening assays in which neutralizing antibodies capable of binding TRICH specifically compete with a test compound for binding TRICH. In this manner, antibodies can be used to detect the presence of any peptide which shares one or more antigenic determinants with TRICH.  
       [0281] In additional embodiments, the nucleotide sequences which encode TRICH may be used in any molecular biology techniques that have yet to be developed, provided the new techniques rely on properties of nucleotide sequences that are currently known, including, but not limited to, such properties as the triplet genetic code and specific base pair interactions.  
       [0282] Without further elaboration, it is believed that one skilled in the art can, using the preceding description, utilize the present invention to its fullest extent. The following embodiments are, therefore, to be construed as merely illustrative, and not limitative of the remainder of the disclosure in any way whatsoever.  
       [0283] The disclosures of all patents, applications and publications, mentioned above and below including U.S. Ser. No. 60/216,547, U.S. Ser. No. 60/218,232, U.S. Ser. No. 60/220,112, and U.S. Ser. No. 60/221,839 are expressly incorporated by reference herein, are expressly incorporated by reference herein. 
     
    
    
     EXAMPLES  
     [0284] I. Construction of cDNA Libraries  
     [0285] Incyte cDNAs were derived from cDNA libraries described in the LIFESEQ GOLD database (Incyte Genomics, Palo Alto Calif.) and shown in Table 4, column 5. Some tissues were homogenized and lysed in guanidinium isothiocyanate, while others were homogenized and lysed in phenol or in a suitable mixture of denaturants, such as TRIZOL (Life Technologies), a monophasic solution of phenol and guanidine isothiocyanate. The resulting lysates were centrifuged over CsCl cushions or extracted with chloroform. RNA was precipitated from the lysates with either isopropanol or sodium acetate and ethanol, or by other routine methods.  
     [0286] Phenol extraction and precipitation of RNA were repeated as necessary to increase RNA purity. In some cases, RNA was treated with DNase. For most libraries, poly(A)+ RNA was isolated using oligo d(T)-coupled paramagnetic particles (Promega), OLIGOTEX latex particles (QIAGEN, Chatsworth Calif.), or an OLIGOTEX mRNA purification kit (QIAGEN). Alternatively, RNA was isolated directly from tissue lysates using other RNA isolation kits, e.g. the POLY(A)PURE mRNA purification kit (Ambion, Austin Tex.).  
     [0287] In some cases, Stratagene was provided with RNA and constructed the corresponding cDNA libraries. Otherwise, cDNA was synthesized and cDNA libraries were constructed with the UNIZAP vector system (Stratagene) or SUPERSCRIPT plasmid system (Life Technologies), using the recommended procedures or similar methods known in the art (See, e.g., Ausubel, 1997, supra, units 5.1-6.6.) Reverse transcription was initiated using oligo d(T) or random primers. Synthetic oligonucleotide adapters were ligated to double stranded cDNA, and the cDNA was digested with the appropriate restriction enzyme or enzymes. For most libraries, the cDNA was size-selected (300-1000 bp) using SEPHACRYL S1000, SEPHAROSE CL2B, or SEPHAROSE CL4B column chromatography (Amersham Pharmacia Biotech) or preparative agarose gel electrophoresis. cDNAs were ligated into compatible restriction enzyme sites of the polylinker of a suitable plasmid, e.g., PBLUESCRIPT plasmid (Stratagene), PSPORT1 plasmid (Life Technologies), PCDNA2.1 plasmid (Invitrogen, Carlsbad Calif.), PBK-CMV plasmid (Stratagene), or pINCY (Incyte Genomics, Palo Alto Calif.), or derivatives thereof. Recombinant plasmids were transformed into competent  E. coli  cells including XL1-Blue, XL1-BlueMRF, or SOLR from Stratagene or DH5α, DH10B, or ElectroMAX DH10B from Life Technologies.  
     [0288] II. Isolation of cDNA Clones  
     [0289] Plasmids obtained as described in Example I were recovered from host cells by in vivo excision using the UNIZAP vector system (Stratagene) or by cell lysis. Plasmids were purified using at least one of the following: a Magic or WIZARD Minipreps DNA purification system (Promega); an AGTC Miniprep purification kit (Edge Biosystems, Gaithersburg Md.); and QIAWELL 8 Plasmid, QIAWELL 8 Plus Plasmid, QIAWELL 8 Ultra Plasmid purification systems or the R.E.A.L. PREP 96 plasmid purification kit from QIAGEN. Following precipitation, plasmids were resuspended in 0.1 ml of distilled water and stored, with or without lyophilization, at 4° C.  
     [0290] Alternatively, plasmid DNA was amplified from host cell lysates using direct link PCR in a high-throughput format (Rao, V. B. (1994) Anal. Biochem. 216:1-14). Host cell lysis and thermal cycling steps were carried out in a single reaction mixture. Samples were processed and stored in 384-well plates, and the concentration of amplified plasmid DNA was quantified fluorometrically using PICOGREEN dye (Molecular Probes, Eugene Oreg.) and a FLUOROSKAN II fluorescence scanner (Labsystems Oy, Helsinki, Finland).  
     [0291] III. Sequencing and Analysis  
     [0292] Incyte cDNA recovered in plasmids as described in Example II were sequenced as follows. Sequencing reactions were processed using standard methods or high-throughput instrumentation such as the ABI CATALYST 800 (Applied Biosystems) thermal cycler or the PTC-200 thermal cycler (MJ Research) in conjunction with the HYDRA microdispenser (Robbins Scientific) or the MICROLAB 2200 (Hamilton) liquid transfer system. cDNA sequencing reactions were prepared using reagents provided by Amersham Pharmacia Biotech or supplied in ABI sequencing kits such as the ABI PRISM BIGDYE Terminator cycle sequencing ready reaction kit (Applied Biosystems). Electrophoretic separation of cDNA sequencing reactions and detection of labeled polynucleotides were carried out using the MEGABACE 1000 DNA sequencing system (Molecular Dynamics); the ABI PRISM 373 or 377 sequencing system (Applied Biosystems) in conjunction with standard ABI protocols and base calling software; or other sequence analysis systems known in the art. Reading frames within the cDNA sequences were identified using standard methods (reviewed in Ausubel, 1997, supra, unit 7.7). Some of the cDNA sequences were selected for extension using the techniques disclosed in Example VIII.  
     [0293] The polynucleotide sequences derived from Incyte cDNAs were validated by removing vector, linker, and poly(A) sequences and by masking ambiguous bases, using algorithms and programs based on BLAST, dynamic programming, and dinucleotide nearest neighbor analysis. The Incyte cDNA sequences or translations thereof were then queried against a selection of public databases such as the GenBank primate, rodent, mammalian, vertebrate, and eukaryote databases, and BLOCKS, PRINTS, DOMO, PRODOM, and hidden Markov model (HMM)-based protein family databases such as PFAM. (HMM is a probabilistic approach which analyzes consensus primary structures of gene families. See, for example, Eddy, S. R. (1996) Curr. Opin. Struct. Biol. 6:361-365.) The queries were performed using programs based on BLAST, FASTA, BLIMPS, and HMMER. The Incyte cDNA sequences were assembled to produce fill length polynucleotide sequences. Alternatively, GenBank cDNAs, GenBank ESTs, stitched sequences, stretched sequences, or Genscan-predicted coding sequences (see Examples IV and V) were used to extend Incyte cDNA assemblages to full length. Assembly was performed using programs based on Phred, Phrap, and Consed, and cDNA assemblages were screened for open reading frames using programs based on GeneMark, BLAST, and FASTA. The full length polynucleotide sequences were translated to derive the corresponding full length polypeptide sequences. Alternatively, a polypeptide of the invention may begin at any of the methionine residues of the full length translated polypeptide. Full length polypeptide sequences were subsequently analyzed by querying against databases such as the GenBank protein databases (genpept), SwissProt, BLOCKS, PRINTS, DOMO, PRODOM, Prosite, and hidden Markov model (HMM)-based protein family databases such as PFAM. Full length polynucleotide sequences are also analyzed using MACDNASIS PRO software (Hitachi Software Engineering, South San Francisco Calif.) and LASERGENE software (DNASTAR). Polynucleotide and polypeptide sequence alignments are generated using default parameters specified by the CLUSTAL algorithm as incorporated into the MEGALIGN multisequence alignment program (DNASTAR), which also calculates the percent identity between aligned sequences.  
     [0294] Table 7 summarizes the tools, programs, and algorithms used for the analysis and assembly of Incyte cDNA and full length sequences and provides applicable descriptions, references, and threshold parameters. The first column of Table 7 shows the tools, programs, and algorithms used, the second column provides brief descriptions thereof, the third column presents appropriate references, all of which are incorporated by reference herein in their entirety, and the fourth column presents, where applicable, the scores, probability values, and other parameters used to evaluate the strength of a match between two sequences (the higher the score or the lower the probability value, the greater the identity between two sequences).  
     [0295] The programs described above for the assembly and analysis of full length polynucleotide and polypeptide sequences were also used to identify polynucleotide sequence fragments from SEQ ID NOS: 33-64. Fragments from about 20 to about 4000 nucleotides which are useful in hybridization and amplification technologies are described in Table 4, column 4.  
     [0296] IV. Identification and Editing of Coding Sequences from Genomic DNA  
     [0297] Putative transporters and ion channels were initially identified by running the Genscan gene identification program against public genomic sequence databases (e.g., gbpri and gbhtg). Genscan is a general-purpose gene identification program which analyzes genomic DNA sequences from a variety of organisms (See Burge, C. and S. Karlin (1997) J. Mol. Biol. 268:78-94, and Burge, C. and S. Karlin (1998) Curr. Opin. Struct. Biol. 8:346-354). The program concatenates predicted exons to form an assembled cDNA sequence extending from a methionine to a stop codon. The output of Genscan is a FASTA database of polynucleotide and polypeptide sequences. The maximum range of sequence for Genscan to analyze at once was set to 30 kb. To determine which of these Genscan predicted cDNA sequences encode transporters and ion channels, the encoded polypeptides were analyzed by querying against PFAM models for transporters and ion channels. Potential transporters and ion channels were also identified by homology to Incyte cDNA sequences that had been annotated as transporters and ion channels. These selected Genscan-predicted sequences were then compared by BLAST analysis to the genpept and gbpri public databases. Where necessary, the Genscan-predicted sequences were then edited by comparison to the top BLAST hit from genpept to correct errors in the sequence predicted by Genscan, such as extra or omitted exons. BLAST analysis was also used to find any Incyte cDNA or public cDNA coverage of the Genscan-predicted sequences, thus providing evidence for transcription. When Incyte cDNA coverage was available, this information was used to correct or confirm the Genscan predicted sequence. Full length polynucleotide sequences were obtained by assembling Genscan-predicted coding sequences with Incyte cDNA sequences and/or public cDNA sequences using the assembly process described in Example III. Alternatively, fill length polynucleotide sequences were derived entirely from edited or unedited Genscan-predicted coding sequences.  
     [0298] V. Assembly of Genomic Sequence Data with cDNA Sequence Data  
     [0299] “Stitched” Sequences  
     [0300] Partial cDNA sequences were extended with exons predicted by the Genscan gene identification program described in Example IV. Partial cDNAs assembled as described in Example III were mapped to genomic DNA and parsed into clusters containing related cDNAs and Genscan exon predictions from one or more genomic sequences. Each cluster was analyzed using an algorithm based on graph theory and dynamic programming to integrate cDNA and genomic information, generating possible splice variants that were subsequently confirmed, edited, or extended to create a full length sequence. Sequence intervals in which the entire length of the interval was present on more than one sequence in the cluster were identified, and intervals thus identified were considered to be equivalent by transitivity. For example, if an interval was present on a cDNA and two genomic sequences, then all three intervals were considered to be equivalent. This process allows unrelated but consecutive genomic sequences to be brought together, bridged by cDNA sequence. Intervals thus identified were then “stitched” together by the stitching algorithm in the order that they appear along their parent sequences to generate the longest possible sequence, as well as sequence variants. Linkages between intervals which proceed along one type of parent sequence (cDNA to cDNA or genomic sequence to genomic sequence) were given preference over linkages which change parent type (cDNA to genomic sequence). The resultant stitched sequences were translated and compared by BLAST analysis to the genpept and gbpri public databases. Incorrect exons predicted by Genscan were corrected by comparison to the top BLAST hit from genpept. Sequences were further extended with additional cDNA sequences, or by inspection of genomic DNA, when necessary.  
     [0301] “Stretched” Sequences  
     [0302] Partial DNA sequences were extended to full length with an algorithm based on BLAST analysis. First, partial cDNAs assembled as described in Example III were queried against public databases such as the GenBank primate, rodent, mammalian, vertebrate, and eukaryote databases using the BLAST program. The nearest GenBank protein homolog was then compared by BLAST analysis to either Incyte cDNA sequences or GenScan exon predicted sequences described in Example IV. A chimeric protein was generated by using the resultant high-scoring segment pairs (HSPs) to map the translated sequences onto the GenBank protein homolog. Insertions or deletions may occur in the chimeric protein with respect to the original GenBank protein homolog. The GenBank protein homolog, the chimeric protein, or both were used as probes to search for homologous genomic sequences from the public human genome databases. Partial DNA sequences were therefore “stretched” or extended by the addition of homologous genomic sequences. The resultant stretched sequences were examined to determine whether it contained a complete gene.  
     [0303] VI. Chromosomal Mapping of TRICH Encoding Polynucleotides  
     [0304] The sequences which were used to assemble SEQ ID NOS: 33-64 were compared with sequences from the Incyte LIFESEQ database and public domain databases using BLAST and other implementations of the Smith-Waterman algorithm. Sequences from these databases that matched SEQ ID NOS: 33-64 were assembled into clusters of contiguous and overlapping sequences using assembly algorithms such as Phrap (Table 7). Radiation hybrid and genetic mapping data available from public resources such as the Stanford Human Genome Center (SHGC), Whitehead Institute for Genome Research (WIGR), and Généthon were used to determine if any of the clustered sequences had been previously mapped. Inclusion of a mapped sequence in a cluster resulted in the assignment of all sequences of that cluster, including its particular SEQ ID NO:, to that map location.  
     [0305] Map locations are represented by ranges, or intervals, of human chromosomes. The map position of an interval, in centiMorgans, is measured relative to the terminus of the chromosome&#39;s p-arm. (The centiMorgan (cM) is a unit of measurement based on recombination frequencies between chromosomal markers. On average, 1 cM is roughly equivalent to 1 megabase (Mb) of DNA in humans, although this can vary widely due to hot and cold spots of recombination.) The cM distances are based on genetic markers mapped by Généthon which provide boundaries for radiation hybrid markers whose sequences were included in each of the clusters. Human genome maps and other resources available to the public, such as the NCBI “GeneMap &#39;99” World Wide Web site (http://www.ncbi.nlm.nih.gov/genemap/), can be employed to determine if previously identified disease genes map within or in proximity to the intervals indicated above.  
     [0306] VII. Analysis of Polynucleotide Expression  
     [0307] Northern analysis is a laboratory technique used to detect the presence of a transcript of a gene and involves the hybridization of a labeled nucleotide sequence to a membrane on which RNAs from a particular cell type or tissue have been bound. (See, e.g., Sambrook, supra, ch. 7; Ausubel (1995) supra, ch. 4 and 16.)  
     [0308] Analogous computer techniques applying BLAST were used to search for identical or related molecules in cDNA databases such as GenBank or LIFESEQ (Incyte Genomics). This analysis is much faster than multiple membrane-based hybridizations. In addition, the sensitivity of the computer search can be modified to determine whether any particular match is categorized as exact or similar. The basis of the search is the product score, which is defined as:  
         BLAST                 Score   ×   Percent                 Identity       5   ×   minimum        {       length                   (     Seq   .              1     )       ,     length        (     Seq   .              2     )         }                     
 
     [0309] The product score takes into account both the degree of similarity between two sequences and the length of the sequence match. The product score is a normalized value between 0 and 100, and is calculated as follows: the BLAST score is multiplied by the percent nucleotide identity and the product is divided by (5 times the length of the shorter of the two sequences). The BLAST score is calculated by assigning a score of +5 for every base that matches in a high-scoring segment pair (HSP), and −4 for every mismatch. Two sequences may share more than one HSP (separated by gaps). If there is more than one HSP, then the pair with the highest BLAST score is used to calculate the product score. The product score represents a balance between fractional overlap and quality in a BLAST alignment. For example, a product score of 100 is produced only for 100% identity over the entire length of the shorter of the two sequences being compared. A product score of 70 is produced either by 100% identity and 70% overlap at one end, or by 88% identity and 100% overlap at the other. A product score of 50 is produced either by 100% identity and 50% overlap at one end, or 79% identity and 100% overlap.  
     [0310] Alternatively, polynucleotide sequences encoding TRICH are analyzed with respect to the tissue sources from which they were derived. For example, some full length sequences are assembled, at least in part, with overlapping Incyte cDNA sequences (see Example III). Each cDNA sequence is derived from a cDNA library constructed from a human tissue. Each human tissue is classified into one of the following organ/tissue categories: cardiovascular system; connective tissue; digestive system; embryonic structures; endocrine system; exocrine glands; genitalia, female; genitalia, male; germ cells; hemic and immune system; liver; musculoskeletal system; nervous system; pancreas; respiratory system; sense organs; skin; stomatognathic system; unclassified/mixed; or urinary tract. The number of libraries in each category is counted and divided by the total number of libraries across all categories. Similarly, each human tissue is classified into one of the following disease/condition categories: cancer, cell line, developmental, inflammation, neurological, trauma, cardiovascular, pooled, and other, and the number of libraries in each category is counted and divided by the total number of libraries across all categories. The resulting percentages reflect the tissue- and disease-specific expression of cDNA encoding TRICH. cDNA sequences and cDNA library/tissue information are found in the LIFESEQ GOLD database (Incyte Genomics, Palo Alto Calif.).  
     [0311] VIII. Extension of TRICH Encoding Polynucleotides  
     [0312] Full length polynucleotide sequences were also produced by extension of an appropriate fragment of the full length molecule using oligonucleotide primers designed from this fragment. One primer was synthesized to initiate 5′ extension of the known fragment, and the other primer was synthesized to initiate 3′ extension of the known fragment. The initial primers were designed using OLIGO 4.06 software (National Biosciences), or another appropriate program, to be about 22 to 30 nucleotides in length, to have a GC content of about 50% or more, and to anneal to the target sequence at temperatures of about 68° C. to about 72° C. Any stretch of nucleotides which would result in hairpin structures and primer-primer dimerizations was avoided.  
     [0313] Selected human cDNA libraries were used to extend the sequence. If more than one extension was necessary or desired, additional or nested sets of primers were designed.  
     [0314] High fidelity amplification was obtained by PCR using methods well known in the art. PCR was performed in 96-well plates using the PTC-200 thermal cycler (MJ Research, Inc.). The reaction mix contained DNA template, 200 nmol of each primer, reaction buffer containing Mg 2+ , (NH 4 ) 2 SO 4 , and 2-mercaptoethanol, Taq DNA polymerase (Amersham Pharmacia Biotech), ELONGASE enzyme (Life Technologies), and Pfu DNA polymerase (Stratagene), with the following parameters for primer pair PCI A and PCI B: Step 1: 94° C., 3 min; Step 2: 94° C., 15 sec; Step 3: 60° C., 1 min; Step 4: 68° C., 2 min; Step 5: Steps 2, 3, and 4 repeated 20 times; Step 6: 68° C., 5 min; Step 7: storage at 4° C. In the alternative, the parameters for primer pair T7 and SK+ were as follows: Step 1: 94° C., 3 min; Step 2: 94° C., 15 sec; Step 3: 57° C., 1 min; Step 4: 68° C., 2 min; Step 5: Steps 2, 3, and 4 repeated 20 times; Step 6: 68° C., 5 min; Step 7: storage at 4° C.  
     [0315] The concentration of DNA in each well was determined by dispensing 100 μl PICOGREEN quantitation reagent (0.25% (v/v) PICOGREEN; Molecular Probes, Eugene Oreg.) dissolved in 1× TE and 0.5 μl of undiluted PCR product into each well of an opaque fluorimeter plate (Corning Costar, Acton Mass.), allowing the DNA to bind to the reagent. The plate was scanned in a Fluoroskan II (Labsystems Oy, Helsinki, Finland) to measure the fluorescence of the sample and to quantify the concentration of DNA. A 5 μl to 10 μl aliquot of the reaction mixture was analyzed by electrophoresis on a 1% agarose gel to determine which reactions were successful in extending the sequence.  
     [0316] The extended nucleotides were desalted and concentrated, transferred to 384-well plates, digested with CviJI cholera virus endonuclease (Molecular Biology Research, Madison Wis.), and sonicated or sheared prior to religation into pUC 18 vector (Amersham Pharmacia Biotech). For shotgun sequencing, the digested nucleotides were separated on low concentration (0.6 to 0.8%) agarose gels, fragments were excised, and agar digested with Agar ACE (Promega). Extended clones were religated using T4 ligase (New England Biolabs, Beverly Mass.) into pUC 18 vector (Amersham Pharmacia Biotech), treated with Pfu DNA polymerase (Stratagene) to fill-in restriction site overhangs, and transfected into competent  E. coli  cells. Transformed cells were selected on antibiotic-containing media, and individual colonies were picked and cultured overnight at 37° C. in 384-well plates in LB/2× carb liquid media.  
     [0317] The cells were lysed, and DNA was amplified by PCR using Taq DNA polymerase (Amersham Pharmacia Biotech) and Pfu DNA polymerase (Stratagene) with the following parameters: Step 1: 94° C., 3 min; Step 2: 94° C., 15 sec; Step 3: 60° C., 1 min; Step 4: 72° C., 2 min; Step 5: steps 2, 3, and 4 repeated 29 times; Step 6: 72° C., 5 min; Step 7: storage at 4° C. DNA was quantified by PICOGREEN reagent (Molecular Probes) as described above. Samples with low DNA recoveries were reamplified using the same conditions as described above. Samples were diluted with 20% dimethysulfoxide (1:2, v/v), and sequenced using DYENAMIC energy transfer sequencing primers and the DYENAMIC DIRECT kit (Amersham Pharmacia Biotech) or the ABI PRISM BIGDYE Terminator cycle sequencing ready reaction kit (Applied Biosystems).  
     [0318] In like manner, full length polynucleotide sequences are verified using the above procedure or are used to obtain 5′ regulatory sequences using the above procedure along with oligonucleotides designed for such extension, and an appropriate genomic library.  
     [0319] IX. Labeling and Use of Individual Hybridization Probes  
     [0320] Hybridization probes derived from SEQ ID NOS: 33-64 are employed to screen cDNAs, genomic DNAs, or mRNAs. Although the labeling of oligonucleotides, consisting of about 20 base pairs, is specifically described, essentially the same procedure is used with larger nucleotide fragments. Oligonucleotides are designed using state-of-the-art software such as OLIGO 4.06 software (National Biosciences) and labeled by combining 50 pmol of each oligomer, 250 μCi of [γ- 32 P] adenosine triphosphate (Amersham Pharmacia Biotech), and T4 polynucleotide kinase (DuPont NEN, Boston Mass.). The labeled oligonucleotides are substantially purified using a SEPHADEX G-25 superfine size exclusion dextran bead column (Amersham Pharmacia Biotech). An aliquot containing 10 7  counts per minute of the labeled probe is used in a typical membrane-based hybridization analysis of human genomic DNA digested with one of the following endonucleases: Ase I, Bgl II, Eco RI, Pst I, Xba I, or Pvu II (DuPont NEN).  
     [0321] The DNA from each digest is fractionated on a 0.7% agarose gel and transferred to nylon membranes (Nytran Plus, Schleicher &amp; Schuell, Durham N.H.). Hybridization is carried out for 16 hours at 40° C. To remove nonspecific signals, blots are sequentially washed at room temperature under conditions of up to, for example, 0.1× saline sodium citrate and 0.5% sodium dodecyl sulfate. Hybridization patterns are visualized using autoradiography or an alternative imaging means and compared.  
     [0322] X. Microarrays  
     [0323] The linkage or synthesis of array elements upon a microarray can be achieved utilizing photolithography, piezoelectric printing (ink-jet printing, See, e.g., Baldeschweiler, supra.), mechanical microspotting technologies, and derivatives thereof. The substrate in each of the aforementioned technologies should be uniform and solid with a non-porous surface (Schena (1999), supra). Suggested substrates include silicon, silica, glass slides, glass chips, and silicon wafers. Alternatively, a procedure analogous to a dot or slot blot may also be used to arrange and link elements to the surface of a substrate using thermal, UV, chemical, or mechanical bonding procedures. A typical array may be produced using available methods and machines well known to those of ordinary skill in the art and may contain any appropriate number of elements. (See, e.g., Schena, M. et al. (1995) Science 270:467-470; Shalon, D. et al. (1996) Genome Res. 6:639-645; Marshall, A. and J. Hodgson (1998) Nat Biotechnol. 16:27-31.)  
     [0324] Full length cDNAs, Expressed Sequence Tags (ESTs), or fragments or oligomers thereof may comprise the elements of the microarray. Fragments or oligomers suitable for hybridization can be selected using software well known in the art such as LASERGENE software (DNASTAR). The array elements are hybridized with polynucleotides in a biological sample. The polynucleotides in the biological sample are conjugated to a fluorescent label or other molecular tag for ease of detection. After hybridization, nonhybridized nucleotides from the biological sample are removed, and a fluorescence scanner is used to detect hybridization at each array element. Alternatively, laser desorbtion and mass spectrometry may be used for detection of hybridization. The degree of complementarity and the relative abundance of each polynucleotide which hybridizes to an element on the microarray may be assessed. In one embodiment, microarray preparation and usage is described in detail below.  
     [0325] Tissue or Cell Sample Preparation  
     [0326] Total RNA is isolated from tissue samples using the guanidinium thiocyanate method and poly(A) +  RNA is purified using the oligo-(dT) cellulose method. Each poly(A) +  RNA sample is reverse transcribed using MMLV reverse-transcriptase, 0.05 pg/o oligo-(dT) primer (21 mer), 1× first strand buffer, 0.03 units/μl RNase inhibitor, 500 μM dATP, 500 μM dGTP, 500 μM dTTP, 40 μM dCTP, 40 μM dCTP-Cy3 (BDS) or dCTP-Cy5 (Amersham Pharmacia Biotech). The reverse transcription reaction is performed in a 25 ml volume containing 200 ng poly(A) +  RNA with GEMBRIGHT kits (Incyte). Specific control poly(A) +  RNAs are synthesized by in vitro transcription from non-coding yeast genomic DNA. After incubation at 37° C. for 2 hr, each reaction sample (one with Cy3 and another with Cy5 labeling) is treated with 2.5 ml of 0.5M sodium hydroxide and incubated for 20 minutes at 85° C. to the stop the reaction and degrade the RNA. Samples are purified using two successive CHROMA SPIN 30 gel filtration spin columns (CLONTECH Laboratories, Inc. (CLONTECH), Palo Alto Calif.) and after combining, both reaction samples are ethanol precipitated using 1 ml of glycogen (1 mg/ml), 60 ml sodium acetate, and 300 ml of 100% ethanol. The sample is then dried to completion using a SpeedVAC (Savant Instruments Inc., Holbrook N.Y.) and resuspended in 14 μl 5×SSC/0.2% SDS.  
     [0327] Microarray Preparation  
     [0328] Sequences of the present invention are used to generate array elements. Each array element is amplified from bacterial cells containing vectors with cloned cDNA inserts. PCR amplification uses primers complementary to the vector sequences flanking the cDNA insert. Array elements are amplified in thirty cycles of PCR from an initial quantity of 1-2 ng to a final quantity greater than 5 μg. Amplified array elements are then purified using SEPHACRYL-400 (Amersham Pharmacia Biotech).  
     [0329] Purified array elements are immobilized on polymer-coated glass slides. Glass microscope slides (Corning) are cleaned by ultrasound in 0.1% SDS and acetone, with extensive distilled water washes between and after treatments. Glass slides are etched in 4% hydrofluoric acid (VWR Scientific Products Corporation (VWR), West Chester Pa.), washed extensively in distilled water, and coated with 0.05% aminopropyl silane (Sigma) in 95% ethanol. Coated slides are cured in a 110° C. oven.  
     [0330] Array elements are applied to the coated glass substrate using a procedure described in U.S. Pat. No. 5,807,522, incorporated herein by reference. 1 μl of the array element DNA, at an average concentration of 100 ng/μl, is loaded into the open capillary printing element by a high-speed robotic apparatus. The apparatus then deposits about 5 nl of array element sample per slide.  
     [0331] Microarrays are UV-crosslinked using a STRATALINKER UV-crosslinker (Stratagene). Microarrays are washed at room temperature once in 0.2% SDS and three times in distilled water. Non-specific binding sites are blocked by incubation of microarrays in 0.2% casein in phosphate buffered saline (PBS) (Tropix, Inc., Bedford Mass.) for 30 minutes at 60° C. followed by washes in 0.2% SDS and distilled water as before.  
     [0332] Hybridization  
     [0333] Hybridization reactions contain 9 μl of sample mixture consisting of 0.2 μg each of Cy3 and Cy5 labeled cDNA synthesis products in 5×SSC, 0.2% SDS hybridization buffer. The sample mixture is heated to 65° C. for 5 minutes and is aliquoted onto the microarray surface and covered with an 1.8 cm 2  coverslip. The arrays are transferred to a waterproof chamber having a cavity just slightly larger than a microscope slide. The chamber is kept at 100% humidity internally by the addition of 140 μl of 5×SSC in a corner of the chamber. The chamber containing the arrays is incubated for about 6.5 hours at 60° C. The arrays are washed for 10 min at 45° C. in a first wash buffer (1×SSC, 0.1% SDS), three times for 1 minutes each at 45° C. in a second wash buffer (0.1× SSC), and dried.  
     [0334] Detection  
     [0335] Reporter-labeled hybridization complexes are detected with a microscope equipped with an Innova 70 mixed gas 10 W laser (Coherent, Inc., Santa Clara Calif.) capable of generating spectral lines at 488 nm for excitation of Cy3 and at 632 nm for excitation of Cy5. The excitation laser light is focused on the array using a 20× microscope objective (Nikon, Inc., Melville N.Y.). The slide containing the array is placed on a computer-controlled X-Y stage on the microscope and raster-scanned past the objective. The 1.8 cm×1.8 cm array used in the present example is scanned with a resolution of 20 micrometers.  
     [0336] In two separate scans, a mixed gas multiline laser excites the two fluorophores sequentially. Emitted light is split, based on wavelength, into two photomultiplier tube detectors PMT R1477, Hamamatsu Photonics Systems, Bridgewater N.J.) corresponding to the two fluorophores. Appropriate filters positioned between the array and the photomultiplier tubes are used to filter the signals. The emission maxima of the fluorophores used are 565 nm for Cy3 and 650 nm for Cy5. Each array is typically scanned twice, one scan per fluorophore using the appropriate filters at the laser source, although the apparatus is capable of recording the spectra from both fluorophores simultaneously.  
     [0337] The sensitivity of the scans is typically calibrated using the signal intensity generated by a cDNA control species added to the sample mixture at a known concentration. A specific location on the array contains a complementary DNA sequence, allowing the intensity of the signal at that location to be correlated with a weight ratio of hybridizing species of 1:100,000. When two samples from different sources (e.g., representing test and control cells), each labeled with a different fluorophore, are hybridized to a single array for the purpose of identifying genes that are differentially expressed, the calibration is done by labeling samples of the calibrating cDNA with the two fluorophores and adding identical amounts of each to the hybridization mixture.  
     [0338] The output of the photomultiplier tube is digitized using a 12-bit RTI-835H analog-to-digital (A/D) conversion board (Analog Devices, Inc., Norwood Mass.) installed in an IBM-compatible PC computer. The digitized data are displayed as an image where the signal intensity is mapped using a linear 20-color transformation to a pseudocolor scale ranging from blue (low signal) to red (high signal). The data is also analyzed quantitatively. Where two different fluorophores are excited and measured simultaneously, the data are first corrected for optical crosstalk (due to overlapping emission spectra) between the fluorophores using each fluorophore&#39;s emission spectrum.  
     [0339] A grid is superimposed over the fluorescence signal image such that the signal from each spot is centered in each element of the grid. The fluorescence signal within each element is then integrated to obtain a numerical value corresponding to the average intensity of the signal. The software used for signal analysis is the GEMTOOLS gene expression analysis program (Incyte).  
     [0340] XI. Complementary Polynucleotides  
     [0341] Sequences complementary to the TRICH-encoding sequences, or any parts thereof, are used to detect, decrease, or inhibit expression of naturally occurring TRICH. Although use of oligonucleotides comprising from about 15 to 30 base pairs is described, essentially the same procedure is used with smaller or with larger sequence fragments. Appropriate oligonucleotides are designed using OLIGO 4.06 software (National Biosciences) and the coding sequence of TRICH. To inhibit transcription, a complementary oligonucleotide is designed from the most unique 5′ sequence and used to prevent promoter binding to the coding sequence. To inhibit translation, a complementary oligonucleotide is designed to prevent ribosomal binding to the TRICH-encoding transcript.  
     [0342] XII. Expression of TRICH  
     [0343] Expression and purification of TRICH is achieved using bacterial or virus-based expression systems. For expression of TRICH in bacteria, cDNA is subcloned into an appropriate vector containing an antibiotic resistance gene and an inducible promoter that directs high levels of cDNA transcription. Examples of such promoters include, but are not limited to, the trp-lac (tac) hybrid promoter and the T5 or T7 bacteriophage promoter in conjunction with the lac operator regulatory element. Recombinant vectors are transformed into suitable bacterial hosts, e.g., BL21(DE3). Antibiotic resistant bacteria express TRICH upon induction with isopropyl beta-D-thiogalactopyranoside (IPTG). Expression of TRICH in eukaryotic cells is achieved by infecting insect or mammalian cell lines with recombinant  Autographica californica  nuclear polyhedrosis virus (AcMNPV), commonly known as baculovinus. The nonessential polyhedrin gene of baculovirus is replaced with cDNA encoding TRICH by either homologous recombination or bacterial-mediated transposition involving transfer plasmid intermediates. Viral infectivity is maintained and the strong polyhedrin promoter drives high levels of cDNA transcription. Recombinant baculovirus is used to infect  Spodoptera frugiperda  (Sf9) insect cells in most cases, or human hepatocytes, in some cases. Infection of the latter requires additional genetic modifications to baculovirus. (See Engelhard, E. K. et al. (1994) Proc. Natl. Acad Sci. USA 91:3224-3227; Sandig, V. et al. (1996) Hum. Gene Ther. 7:1937-1945.)  
     [0344] In most expression systems, TRICH is synthesized as a fusion protein with, e.g., glutathione S-transferase (GST) or a peptide epitope tag, such as FLAG or 6-His, permitting rapid, single-step, affinity-based purification of recombinant fusion protein from crude cell lysates. GST, a 26-kilodalton enzyme from  Schistosoma japonicum,  enables the purification of fusion proteins on immobilized glutathione under conditions that maintain protein activity and antigenicity (Amersham Pharmacia Biotech). Following purification, the GST moiety can be proteolytically cleaved from TRICH at specifically engineered sites. FLAG, an 8-amino acid peptide, enables immunoaffinity purification using commercially available monoclonal and polyclonal anti-FLAG antibodies (Eastman Kodak). 6-His, a stretch of six consecutive histidine residues, enables purification on metal-chelate resins (QIAGEN). Methods for protein expression and purification are discussed in Ausubel (1995, supra, ch. 10 and 16). Purified TRICH obtained by these methods can be used directly in the assays shown in Examples XVI, XVII, and XVIII where applicable.  
     [0345] XIII. Functional Assays  
     [0346] TRICH function is assessed by expressing the sequences encoding TRICH at physiologically elevated levels in mammalian cell culture systems. cDNA is subcloned into a mammalian expression vector containing a strong promoter that drives high levels of cDNA expression. Vectors of choice include PCMV SPORT (Life Technologies) and PCR3.1 (Invitrogen, Carlsbad Calif.), both of which contain the cytomegalovirus promoter. 5-10 μg of recombinant vector are transiently transfected into a human cell line, for example, an endothelial or hematopoietic cell line, using either liposome formulations or electroporation. 1-2 μg of an additional plasmid containing sequences encoding a marker protein are co-transfected. Expression of a marker protein provides a means to distinguish transfected cells from nontransfected cells and is a reliable predictor of cDNA expression from the recombinant vector. Marker proteins of choice include, e.g., Green Fluorescent Protein (GFP; Clontech), CD64, or a CD64-GFP fusion protein. Flow cytometry (FCM), an automated, laser optics-based technique, is used to identify transfected cells expressing GFP or CD64-GFP and to evaluate the apoptotic state of the cells and other cellular properties. FCM detects and quantifies the uptake of fluorescent molecules that diagnose events preceding or coincident with cell death. These events include changes in nuclear DNA content as measured by staining of DNA with propidium iodide; changes in cell size and granularity as measured by forward light scatter and 90 degree side light scatter; down-regulation of DNA synthesis as measured by decrease in bromodeoxyuridine uptake; alterations in expression of cell surface and intracellular proteins as measured by reactivity with specific antibodies; and alterations in plasma membrane composition as measured by the binding of fluorescein-conjugated Annexin V protein to the cell surface. Methods in flow cytometry are discussed in Ormerod, M. G. (1994)  Flow Cytometry,  Oxford, New York N.Y.  
     [0347] The influence of TRICH on gene expression can be assessed using highly purified populations of cells transfected with sequences encoding TRICH and either CD64 or CD64-GFP. CD64 and CD64-GFP are expressed on the surface of transfected cells and bind to conserved regions of human immunoglobulin G (IgG). Transfected cells are efficiently separated from nontransfected cells using magnetic beads coated with either human IgG or antibody against CD64 (DYNAL, Lake Success N.Y.). mRNA can be purified from the cells using methods well known by those of skill in the art. Expression of mRNA encoding TRICH and other genes of interest can be analyzed by northern analysis or microarray techniques.  
     [0348] XIV. Production of TRICH Specific Antibodies  
     [0349] TRICH substantially purified using polyacrylamide gel electrophoresis (PAGE; see, e.g., Harrington, M. G. (1990) Methods Enzymol. 182:488495), or other purification techniques, is used to immnunize rabbits and to produce antibodies using standard protocols.  
     [0350] Alternatively, the TRICH amino acid sequence is analyzed using LASERGENE software (DNASTAR) to determine regions of high immunogenicity, and a corresponding oligopeptide is synthesized and used to raise antibodies by means known to those of skill in the art. Methods for selection of appropriate epitopes, such as those near the C-terminus or in hydrophilic regions are well described in the art. (See, e.g., Ausubel, 1995, supra, ch. 11.)  
     [0351] Typically, oligopeptides of about 15 residues in length are synthesized using an ABI 431A peptide synthesizer (Applied Biosystems) using FMOC chemistry and coupled to KLH (Sigma-Aldrich, St. Louis Mo.) by reaction with N-maleimidobenzoyl-N-hydroxysuccinimide ester (MBS) to increase immunogenicity. (See, e.g., Ausubel, 1995, supra.) Rabbits are immunized with the oligopeptide-KLH complex in complete Freund&#39;s adjuvant. Resulting antisera are tested for antipeptide and anti-TRICH activity by, for example, binding the peptide or TRICH to a substrate, blocking with 1% BSA, reacting with rabbit antisera, washing, and reacting with radio-iodinated goat anti-rabbit IgG.  
     [0352] XV. Purification of Naturally Occurring TRICH Using Specific Antibodies  
     [0353] Naturally occurring or recombinant TRICH is substantially purified by immunoaffinity chromatography using antibodies specific for TRICH. An immunoaffinity column is constructed by covalently coupling anti-TRICH antibody to an activated chromatographic resin, such as CNBr-activated SEPHAROSE (Amersham Pharmacia Biotech). After the coupling, the resin is blocked and washed according to the manufacturer&#39;s instructions.  
     [0354] Media containing TRICH are passed over the immunoaffinity column, and the column is washed under conditions that allow the preferential absorbance of TRICH (e.g., high ionic strength buffers in the presence of detergent). The column is eluted under conditions that disrupt antibody/TRICH binding (e.g., a buffer of pH 2 to pH 3, or a high concentration of a chaotrope, such as urea or thiocyanate ion), and TRICH is collected.  
     [0355] XVI. Identification of Molecules which Interact with TRICH  
     [0356] Molecules which interact with TRICH may include transporter substrates, agonists or antagonists, modulatory proteins such as Gβγ proteins (Reimann, supra) or proteins involved in TRICH localization or clustering such as MAGUKs (Craven, supra). TRICH, or biologically active fragments thereof, are labeled with 125I Bolton-Hunter reagent (See, e.g., Bolton A. E. and W. M. Hunter (1973) Biochem J. 133:529-539.) Candidate molecules previously arrayed in the wells of a multi-well plate are incubated with the labeled TRICH, washed, and any wells with labeled TRICH complex are assayed. Data obtained using different concentrations of TRICH are used to calculate values for the number, affinity, and association of TRICH with the candidate molecules.  
     [0357] Alternatively, proteins that interact with TRICH are isolated using the yeast 2-hybrid system (Fields, S. and O. Song (1989) Nature 340:245-246). TRICH, or fragments thereof, are expressed as fusion proteins with the DNA binding domain of Gal4 or lexA, and potential interacting proteins are expressed as fusion proteins with an activation domain. Interactions between the TRICH fusion protein and the TRICH interacting proteins (fusion proteins with an activation domain) reconstitute a transactivation function that is observed by expression of a reporter gene. Yeast 2-hybrid systems are commercially available, and methods for use of the yeast 2-hybrid system with ion channel proteins are discussed in Niethammer, M. and M. Sheng (1998, Meth. Enzymol. 293:104-122).  
     [0358] TRICH may also be used in the PATHCALLING process (CuraGen Corp., New Haven Conn.) which employs the yeast two-hybrid system in a high-throughput manner to determine all interactions between the proteins encoded by two large libraries of genes (Nandabalan, K. et al. (2000) U.S. Pat. No. 6,057,101).  
     [0359] Potential TRICH agonists or antagonists may be tested for activation or inhibition of TRICH ion channel activity using the assays described in section XVIII.  
     [0360] XVII. Demonstration of TRICH Activity  
     [0361] Ion channel activity of TRICH is demonstrated using an electrophysiological assay for ion conductance. TRICH can be expressed by transforming a mammalian cell line such as COS7, HeLa or CHO with a eukaryotic expression vector encoding TRICH. Eukaryotic expression vectors are commercially available, and the techniques to introduce them into cells are well known to those skilled in the art. A second plasmid which expresses any one of a number of marker genes, such as β-galactosidase, is co-transformed into the cells to allow rapid identification of those cells which have taken up and expressed the foreign DNA. The cells are incubated for 48-72 hours after transformation under conditions appropriate for the cell line to allow expression and accumulation of TRICH and β-galactosidase.  
     [0362] Transformed cells expressing β-galactosidase are stained blue when a suitable colorimetric substrate is added to the culture media under conditions that are well known in the art. Stained cells are tested for differences in membrane conductance by electrophysiological techniques that are well known in the art. Untransformed cells, and/or cells transformed with either vector sequences alone or β-galactosidase sequences alone, are used as controls and tested in parallel. Cells expressing TRICH will have higher anion or cation conductance relative to control cells. The contribution of TRICH to conductance can be confirmed by incubating the cells using antibodies specific for TRICH. The antibodies will bind to the extracellular side of TRICH, thereby blocking the pore in the ion channel, and the associated conductance.  
     [0363] Alternatively, ion channel activity of TRICH is measured as current flow across a TRICH-containing  Xenopus laevis  oocyte membrane using the two-electrode voltage-clamp technique (Ishi et al., supra; Jegla, T. and L. Salkoff (1997) J. Neurosci. 17:32-44). TRICH is subcloned into an appropriate Xenopus oocyte expression vector, such as pBF, and 0.5-5 ng of mRNA is injected into mature stage IV oocytes. Injected oocytes are incubated at 18° C. for 1-5 days. Inside-out macropatches are excised into an intracellular solution containing 116 mM K-gluconate, 4 mM KCl, and 10 mM Hepes (pH 7.2). The intracellular solution is supplemented with varying concentrations of the TRICH mediator, such as cAMP, cGMP, or Ca +2  (in the form of CaCl 2 ), where appropriate. Electrode resistance is set at 2-5 MΩ and electrodes are filled with the intracellular solution lacking mediator. Experiments are performed at room temperature from a holding potential of 0 mV. Voltage ramps (2.5 s) from −100 to 100 mV are acquired at a sampling frequency of 500 Hz. Current measured is proportional to the activity of TRICH in the assay.  
     [0364] In particular, the activities of TRICH-1, TRICH-2, and TRICH-10, are measured as K +  conductance, the activities of TRICH-6 and TRICH-9 are measured as K +  conductance in the presence of membrane stretch or free fatty acids, the activities of TRICH-18, TRICH-25 and TRICH-31 are measured as voltage-gated K +  conductance, TRICH-5 activity is measured as Cl −  conductance in the presence of GABA, TRICH-11 activity is measured as cation conductance in the presence of heat, and the activity of TRICH-9, TRICH-28 is measured as Ca 2+  conductance.  
     [0365] Transport activity of TRICH is assayed by measuring uptake of labeled substrates into  Xenopus laevis  oocytes. Oocytes at stages V and VI are injected with TRICH mRNA (10 ng per oocyte) and incubated for 3 days at 18° C. in OR2 medium (82.5 mM NaCl, 2.5 mM KCl, 1 mM CaCl 2 , 1 mM MgCl 2 , 1 mM Na 2 HPO 4 , 5 mM Hepes, 3.8 mM NaOH, 50 μg/ml gentamycin, pH 7.8) to allow expression of TRICH. Oocytes are then transferred to standard uptake medium (100 mM NaCl, 2 mM KCl, 1 mM CaCl 2 , 1 mM MgCl 2 , 10 mM Hepes/Tris pH 7.5). Uptake of various substrates (e.g., amino acids, sugars, drugs, ions, and neurotransmitters) is initiated by adding labeled substrate (e.g. radiolabeled with  3 H, fluorescently labeled with rhodamine, etc.) to the oocytes. After incubating for 30 minutes, uptake is terminated by washing the oocytes three times in Na + -free medium, measuring the incorporated label, and comparing with controls. TRICH activity is proportional to the level of internalized labeled substrate. In particular, test substrates include pigment precursors and related molecules for TRICH-3, aminophospholipids for TRICH-4, fructose and glucose for TRICH-7 and TRICH-15, amino acids for TRICH-8, Na +  and iodide for TRICH-12, Na +  and H +  for TRICH-13 and TRICH-21, Na +  and glucose for TRICH-16 and TRICH-19, and glucose for TRICH-23, TRICH-26, TRICH-29, TRICH-30, and TRICH-32.  
     [0366] ATPase activity associated with TRICH can be measured by hydrolysis of radiolabeled ATP-[γ- 32 P], separation of the hydrolysis products by chromatographic methods, and quantitation of the recovered  32 P using a scintillation counter. The reaction mixture contains ATP-[γ- 32 P] and varying amounts of TRICH in a suitable buffer incubated at 37° C. for a suitable period of time. The reaction is terminated by acid precipitation with trichloroacetic acid and then neutralized with base, and an aliquot of the reaction mixture is subjected to membrane or filter paper-based chromatography to separate the reaction products. The amount of  32 P liberated is counted in a scintillation counter. The amount of radioactivity recovered is proportional to the ATPase activity of TRICH in the assay.  
     [0367] XVIII. Identification of TRICH Agonists and Antagonists  
     [0368] TRICH is expressed in a eukaryotic cell line such as CHO (Chinese Hamster Ovary) or HEK (Human Embryonic Kidney) 293. Ion channel activity of the transformed cells is measured in the presence and absence of candidate agonists or antagonists. Ion channel activity is assayed using patch clamp methods well known in the art or as described in Example XVII. Alternatively, ion channel activity is assayed using fluorescent techniques that measure ion flux across the cell membrane (Velicelebi, G. et al. (1999) Meth. Enzymol. 294:20-47; West, M. R. and C. R. Molloy (1996) Anal. Biochem. 241:51-58). These assays may be adapted for high-throughput screening using microplates. Changes in internal ion concentration are measured using fluorescent dyes such as the Ca 2+  indicator Fluo4 AM, sodium-sensitive dyes such as SBFI and sodium green, or the Cl −  indicator MQAE (all available from Molecular Probes) in combination with the FLIPR fluorimetric plate reading system (Molecular Devices). In a more generic version of this assay, changes in membrane potential caused by ionic flux across the plasma membrane are measured using oxonyl dyes such as DiBAC 4  (Molecular Probes). DiBAC 4  equilibrates between the extracellular solution and cellular sites according to the cellular membrane potential. The dye&#39;s fluorescence intensity is 20-fold greater when bound to hydrophobic intracellular sites, allowing detection of DiBAC 4  entry into the cell (Gonzalez, J. E. and P. A. Negulescu (1998) Curr. Opin. Biotechnol. 9:624-631). Candidate agonists or antagonists may be selected from known ion channel agonists or antagonists, peptide libraries, or combinatorial chemical libraries.  
     [0369] Various modifications and variations of the described methods and systems of the invention will be apparent to those skilled in the art without departing from the scope and spirit of the invention. Although the invention has been described in connection with certain embodiments, it should be understood that the invention as claimed should not be unduly limited to such specific embodiments. Indeed, various modifications of the described modes for carrying out the invention which are obvious to those skilled in molecular biology or related fields are intended to be within the scope of the following claims.  
                               TABLE 1                               Incyte       Incyte       Incyte   Polypeptide   Polypeptide   Polynucleotide   Polynucleotide       Project ID   SEQ ID NO:   ID   SEQ ID NO:   ID                                                    3474673   1   3474673CD1   33   3474673CB1       4588877   2   4588877CD1   34   4588877CB1       7472214   3   7472214CD1   35   7472214CB1       7473053   4   7473053CD1   36   7473053CB1       7473347   5   7473347CD1   37   7473347CB1       7474240   6   7474240CD1   38   7474240CB1       7475338   7   7475338CD1   39   7475338CB1       7476747   8   7476747CD1   40   7476747CB1       7477898   9   7477898CD1   41   7477898CB1       7472728   10   7472728CD1   42   7472728CB1       7474322   11   7474322CD1   43   7474322CB1       5455621   12   5455621CD1   44   5455621CB1       7477248   13   7477248CD1   45   7477248CB1       2944004   14   2944004CD1   46   2944004CB1       3046849   15   3046849CD1   47   3046849CB1       4538363   16   4538363CD1   48   4538363CB1       6427460   17   6427460CD1   49   6427460CB1       7474127   18   7474127CD1   50   7474127CB1       7476949   19   7476949CD1   51   7476949CB1       7477249   20   7477249CD1   52   7477249CB1       7477720   21   7477720CD1   53   7477720CB1       7477852   22   7477852CD1   54   7477852CB1       1471717   23   1471717CD1   55   1471717CB1       3874406   24   3874406CD1   56   3874406CB1       4599654   25   4599654CD1   57   4599654CB1       5047435   26   5047435CD1   58   5047435CB1       7475603   27   7475603CD1   59   7475603CB1       7477845   28   7477845CD1   60   7477845CB1       168827   29   168827CD1   61   168827CB1       7472734   30   7472734CD1   62   7472734CB1       7473473   31   7473473CD1   63   7473473CB1       7477725   32   7477725CD1   64   7477725CB1                  
 
     [0370]                               TABLE 2                           Incyte                   Polypeptide   Polypeptide   GenBank ID   Probability       SEQ ID NO:   ID   NO:   score   GenBank Homolog                                                    1   3474673CD1   g13507377   1.00E−151   [f1] [ Homo sapiens ] potassium channel TASK-4                       (Decher, N. et al. (2001) FEBS Lett. 492 (1-2), 84-89)       2   4588877CD1   g13926111   3.00E−96   [f1] [ Homo sapiens ] (AF358910) 2P domain potassium                       channel Talk-2       3   7472214CD1   g1107730   1.70E−243   [ Mus musculus ] ABC8                       (Savary, S. et al. (1996) Mamm. Genome 7 (9), 673-676)               g11342541   0   [f1] [ Homo sapiens ] putative white family ATP-binding                       cassette transporter       4   7473053CD1   g3850108   9.00E−209   [ Schizosaccharomyces pombe ] putative calcium-                       transporting atpase               g3628757   0   [ Homo sapiens ] FIC1                       (Bull, L. N. et al. (1998) Nat. Genet. 18 (3), 219-224)       5   7473347CD1   g1060975   1.70E−206   [ Rattus norvegicus ] GABA receptor rho-3 subunit                       precursor                       (Ogurusu, T. et al. (1996) Biochim. Biophys. Acta 1305                       (1-2), 15-18)       6   7474240CD1   g2745727   0   [ Rattus norvegicus ] potassium channel                       (Shi, W. et al. (1997) J. Neurosci. 17 (24), 9423-9432)       7   7475338CD1   g183298   2.10E−158   [ Homo sapiens ] GLUT5 protein                       (Kayano, T. et al. (1990) J. Biol. Chem. 265 (22),                       13276-13282)       9   7477898CD1   g2745729   0   [ Rattus norvegicus ] potassium channel                       (Shi, W. et al. (1997) J. Neurosci. 17 (24), 9423-9432)       10   7472728CD1   g8452900   3.50E−261   [ Rattus norvegicus ] potassium channel TREK-2                       (Bang, H. et al. (2000) J. Biol. Chem. 275 (23), 17412-17419)       11   7474322CD1   g12003146   0   [f1] [ Homo sapiens ] capsaicin receptor       12   5455621CD1   g1399954   3.00E−143   [ Rattus norvegicus ] thyroid sodium/iodide symporter NIS                       (Dai, G. et al. (1996) Nature 379 (6564), 458-460)       13   7477248CD1   g2944233   3.10E−195   [ Homo sapiens ] sodium-hydrogen exchanger 6                       (Numata, M. et al. (1998) J. Biol. Chem. 273 (12), 6951-6959)       14   2944004CD1   g3451312   1.40E−188   [ Schizosaccharomyces pombe ] membrane atpase       15   3046849CD1   g12802047   0   [f1] [ Homo sapiens ] (AJ271290) facilitative glucose                       transporter GLUT11       16   4538363CD1   g338055   7.40E−181   [ Homo sapiens ] Na+/glucose cotransporter                       (Hediger, M. A. et al. (1989) Proc. Natl. Acad. Sci.                       U.S.A. 86 (15), 5748-5752)       17   6427460CD1   g6457274   0   [ Mus musculus ] putative E1-E2 ATPase                       (Halleck, M. S. et al. (1999) Physiol. Genomics (Online)                       1 (3), 139-150)       18   7474127CD1   g206044   0   [ Rattus norvegicus ] potassium channel Kv3.2b                       (Wiedmann, R. et al. (1991) FEBS Lett. 288, 163-167)       19   7476949CD1   g9588428   0   [5′ incom] [ Homo sapiens ] dJ1024N4.1 (novel                       Sodium: solute symporter family member similar to SLC5A1                       (SGLT1))               g338055   3.70E−202   [ Homo sapiens ] Na+/glucose cotransporter                       (Hediger, M. A. et al. (1989) Proc. Natl. Acad. Sci.                       U.S.A. 86 (15), 5748-5752)       20   7477249CD1   g7715417   0   [ Oryctolagus cuniculus ] RING-finger binding protein                       (Mansharamani, M. et al. (2001) J. Biol. Chem. 276 (5),                       3641-3649)       21   7477720CD1   g205709   0   [ Rattus norvegicus ] sodium-hydrogen exchange protein-                       isoform 4                       [Orlowski, J. et al. (1992) J. Biol. Chem. 267, 9331-9339)       22   7477852CD1   g8920219   0   [f1] [ Homo sapiens ] epithelial calcium channel                       (Muller, D. et al. (2000) Genomics 67 (1), 48-53)       23   1471717CD1   g529590   5.00E−36   [ Rattus norvegicus ] liver-specific transport protein                       (Simonson, G. D. et al. (1994) J. Cell. Sci 107, 1065-1072)       24   3874406CD1   g1514530   1.90E−117   [ Homo sapiens ) ABC-C transporter                       (Klugbauer, N. et al. (1996) FEBS Lett. 391 (1-2), 61-65)       25   4599654CD1   g3242244   0   [ Mus musculus ] hyperpolarization-activated cation                       channel, HAC3                       (Ludwig, A. et al. (1998) Nature 393 (6685), 587-591)       26   5047435CD1   g13445575   0   [f1] [ Homo sapiens ] facilitative glucose transporter                       GLUT10                       (McVie-Wylie, A. J. et al. (2001) Genomics 72 (1), 113-117)       27   7475603CD1   g9211112   0   [f1] [ Homo sapiens ] macrophage ABC transporter                       (Kaminski, W. E. et al. (2000) Biochem. Biophys. Res.                       Commun. 273 (2), 532-538)       28   7477845CD1   g3800830   0   [ Rattus norvegicus ] putative four repeat ion channel                       (Lee, J. H. et al. (1999) FEBS Lett. 445 (2-3), 231-236)       29   168827CD1   g7707622   1.20E−116   [ Homo sapiens ] organic anion transporter 4                       (Cha, S. H. et al. (2000) J. Biol. Chem. 275 (6), 4507-4512)               g3004482   0   [f1] [ Rattus norvegicus ] putative integral membrane                       transport protein                       (Schomig, E. et al. (1998) FEBS Lett. 425 (1), 79-86)       30   7472734CD1   g7707622   4.50E−117   [ Homo sapiens ] organic anion transporter 4                       (Cha, S. H. et al. (2000) J. Biol. Chem. 275 (6), 4507-4512)               g3004482   0   [f1] [ Rattus norvegicus ] putative integral membrane                       transport protein                       (Schomig, E. et al. (1998) FEBS Lett. 425 (1), 79-86)       31   7473473CD1   g6625694   0   [ Rattus norvegicus ] potasium channel Eag2                       (Saganich, M. J. et al. (1999) J. Neurosci. 19 (24),                       10789-10802)       32   7477725CD1   g3004482   1.00E−177   [f1] [ Rattus norvegicus ] putative integral membrane                       transport protein                       (Schomig, E. et al. (1998) FEBS Lett. 425 (1), 79-86)               g7707622   4.20E−130   [ Homo sapiens ] organic anion transporter 4                       (Cha, S. H. et al. (2000) J. Biol. Chem. 275 (6), 4507-4512)                    
     [0371]                           TABLE 3                                      Potential                                             SEQ   Incyte   Amino   Potential    Glyco-       Analytical       ID   Polypeptide   Acid   Phosphorylation   sylation   Signature Sequences,   Methods and       NO:   ID   Residues   Sites   Sites   Domains and Motifs   Databases                                                 1   3474673CD1   332   S201 S207 S234   N65 N94   Transmembrane domains:   HMMER                   S265 S280 S281       R130-M155, V245-L264                   S289 S51 T169       TASK K+ channel domain:   HMMER_PFAM                   T67       V14-S332       2   4588877CD1   226   S101 S128 S159       Transmembrane domain:   HMMER                   S174 S175 S183       V139-L158                   S95       CHANNEL PROTEIN IONIC POTASSIUM SUBUNIT   BLAST_PRODOM                           K+ PUTATIVE SUBFAMILY K MEMBER                           PD021430: A78-E162       3   7472214CD1   646   S143 S229 S261   N169 N422   Transmembrane domains:   HMMER                   S340 S341 S463       S430-M450, W564-D589, M618-V637                   S554 S57 S644       ABC transporter domain:   HMMER_PFAM                   S69 S89 T138       R95-G277                   T157 T23 T472       ABC transporters family signature   BLIMPS_BLOCKS                   T500 T591       BL00211: I100-F111, L201-D232                           ABC transporters family signature:   PROFILESCAN                           V181-D232                           PROTEIN TRANSMEMBRANE TRANSPORT   BLAST_PRODOM                           ATPBINDING TRANSPORTER MEMBRANE ABC                           GLYCOPROTEIN INNER PUTATIVE                           PD000633: T365-Y583                           do WHITE; FRUIT; FLY; SCARLET;   BLAST_DOMO                           DM05200|P45844|289-650: G277-L623                           ABC TRANSPORTERS FAMILY   BLAST_DOMO                           DM00008|P45844|73-287: I61-Q276                           ABC transporter motif:   MOTIFS                           L201-L215                           ATP/GTP binding site (P-loop):   MOTIFS                           G102-S109       4   7473053CD1   1190   S153 S259 S268   N579   Transmembrane domains:   HMMER                   S391 S413 S452       S77-V94, L276-W298, Y330-R350, L947-                   S493 S545 S573       I971, Q991-I1009                   S624 S631 S687       E1-E2 ATPase domains:   HMMER_PFAM                   S723 S739 S744       E381-V403, Q530-A562, Y633-G685, R788-                   S832 S1174 S1132       D818                   S1164 S1124       E1-E2 ATPases phosphorylation site   BLIMPS_BLOCKS                   S1143 S1168 T267       proteins                   T36 T370 T378       BL00154: G134-L151, V386-F404, D650-                   T514 T519 T580       M690, T809-S832                   T646 T705 T732       E1-E2 ATPases phosphorylation site:   PROFILESCAN                   T899 T980 T1098       A372-V417                   T1158 Y23 Y29       P-type cation-transporting ATPase   BLIMPS_PRINTS                   Y489 Y607       superfamily signature                           PR00119: F390-F404, A666-D676, I812-                           I831                           ATPASE HYDROLASE TRANSMEMBRANE   BLAST_PRODOM                           PHOSPHORYLATION ATPBINDING PROTEIN                           PROBABLE CALCIUMTRANSPORTING CALCIUM                           TRANSPORT                           PD004657: S846-P1093                           FIC1 PROTEIN   BLAST_PRODOM                           PD180313: H1039-W1165                           do ATPASE; CALCIUM; TRANSPORTING;   BLAST_DOMO                           DM02405|P32660|318-1225: W128-F418,                           E466-N910                           ATPase E1-E2 motif:   MOTIFS                           D392-T398       5   7473347CD1   467   S149 S175 S344   N126 N197   Transmembrane domain:   HMMER                   S37 S390 S411   N220   V332-V351                   S419 S427 S53                   S96 T100 T136                   T157 T355 T356                   T366 T41       5                   Neurotransmitter-gated ion-channel   HMMER_PFAM                           domain:                           P58-Q362, H441-W463                           Neurotransmitter-gated ion channels   BLIMPS_BLOCKS                           signature                           BL00236: V85-P122, I139-H148, D169-                           Y207, Y254-A295                           Neurotransmitter-gated ion-channels   PROFILESCAN                           signature:                           L164-H218                           Neurotransmitter-gated ion-channels   BLIMPS_PRINTS                           signature                           PR00252: T105-F121, K138-S149, C184-                           C198, S261-P273                           Gamma-aminobutyric acid A (GABAA)   BLIMPS_PRINTS                           receptor signature                           PR00253: F270-W290, V296-V317, V330-                           V351, Y446-Y466                           CHANNEL IONIC TRANSMEMBRANE   BLAST_PRODOM                           GLYCOPROTEIN POSTSYNAPTIC MEMBRANE                           RECEPTOR PRECURSOR SIGNAL PROTEIN                           PD000153: E62-S427                           NEUROTRANSMITTER-GATED ION-CHANNELS   BLAST_DOMO                           DM00560|P50573|34-464: S37-V467                           Neurotransmitter-gated ion channels   MOTIFS                           motif:                           C184-C198       6   7474240CD1   1196   S174 S187 S209   N102 N230   Transmembrane domain:   HMMER                   S211 S239 S269   N338 N369   V551-Y571                   S274 S275 S317   N600 N661   Transmembrane region cyclic nucleotide   HMMER_PFAM                   S349 S354 S514   N736 N881   gated ion channel:                   S55 S609 S639   N905 N1139   Y492-I731                   S821 S869 S879       Cyclic nucleotide-binding domain:   HMMER_PFAM                   S883 S896 S899       M759-E850                   S906 S922 S923       POTASSIUM CHANNEL IONIC CHANNEL   BLAST_PRODOM                   S939 S940 S963       PD104127: S852-Y1028                   S974 S985 S1020       POTASSIUM CHANNEL IONIC CHANNEL   BLAST_PRODOM                   S1091 S1170       PD104126: A1076-K1196                   S1096 T133 T169       CAMP RECEPTOR PROTEIN CYCLIC   BLAST_DOMO                   T344 T371 T392       NUCLEOTIDE-BINDING DOMAIN                   T528 T582 T637       DM01165|I38465|562-948: H564-A914                   T673 T74 T829       do POTASSIUM; CHANNEL; KST1; AKT1;   BLAST_DOMO                   T857 T916 T1022       DM02383|I38465|353-560: S353-A563                   T1027 T1134       do CHANNEL; POTASSIUM; EAG;   BLAST_DOMO                   T1099 Y248 Y446       DM05484|I38465|1-351: M1-P351                   Y98       7   7475338CD1   512   S222 S279 S412   N41 N57   Signal peptide:   SPSCAN                   S413 S438 T107       M1-A35                   T170 T235 T247       Transmembrane domains:   HMMER                   T473 T59 T66       C79-G96, M171-L188, Y322-V342, F448-                   Y380       I466                           Sugar (and other) transporter domain:   HMMER_PFAM                           A26-F481                           Sugar transport proteins signatures:   PROFILESCAN                           A119-I185, V323-S379                           Sugar transporter signature   BLIMPS_PRINTS                           PR00171: A35-V45, V135-M154, Q294-                           Y304, I383-V404, T406-F418                           Glucose transporter signature   BLIMPS_PRINTS                           PR00172: L284-Y305, Q321-V342, L352-                           Q372, I383-T406, A416-F434, Y446-I466       7                   SUGAR TRANSPORT PROTEINS   BLAST_DOMO                           DM00135|P22732|132-466: R138-T473                           Sugar transporter 1 motif:   MOTIFS                           S338-A353                           Sugar transporter 2 motif:   MOTIFS                           V140-R165       8   7476747CD1   568   S143 S365 S4   N141 N205   Transmembrane domains:   HMMER                   S456 S46 S51 S55   N214 N256   I242-F269, Y289-P308, I322-Y342                   T34 T430 Y45   N562 N62   Transmembrane amino acid transporter   HMMER_PFAM                       N76   protein domain:                           A102-G543                           ACID AMINO PROTEIN TRANSPORTER   BLAST_PRODOM                           PERMEASE TRANSMEMBRANE INTERGENIC                           REGION PUTATIVE PROLINE                           PD001875: W80-L380       9   7477898CD1   958   S105 S140 S145   N218 N449   Transmembrane domain:   HMMER                   S200 S26 S283   N510 N742   L300-N318                   S288 S458 S488       Transmembrane region cyclic nucleotide   HMMER_PFAM                   S55 S670 S706       gated ion channel:                   S724 S751 S774       Y341-I580                   S788 S864 S872       Cyclic nucleotide-binding domain:   HMMER_PFAM                   S879 S897 S929       V608-A699                   T13 T170 T202       POTASSIUM CHANNEL IONIC CHANNEL   BLAST_PRODOM                   T220 T301 T326       PD118772: E702-S955                   T363 T377 T486       CHANNEL PROTEIN IONIC POTASSIUM   BLAST_PRODOM                   T522 T678       NONPHOTOTROPIC HYPOCOTYL PUTATIVE                           SUBUNIT REPEAT EAG                           PD009483: M1-L86                           CAMP RECEPTOR PROTEIN CYCLIC   BLAST_DOMO                           NUCLEOTIDE-BINDING DOMAIN                           DM01165|I38465|562-948: H413-F738,                           do POTASSIUM; CHANNEL; KST1; AKT1;   BLAST_DOMO                           DM02383|I38465|353-560: T201-A412       10   7472728CD1   724   S229 S283 S303   N327 N330   Transmembrane domains:   HMMER                   S333 S512 S545   N331 N532   A370-L388, I419-F437, V486-M503                   S597 S666 S718   N664 N684   TASK K+ channel domain:   HMMER_PFAM                   T104 T19 T223   N716   M250-D646                   T444 T515 T540       TWIK1 RELATED POTASSIUM CHANNEL,   BLAST_PRODOM                   T557 T591 T636       SUBFAMILY K, MEMBER 2 TREK1 K+ CHANNEL                   T640 T650 T661       SUBUNIT IONIC CHANNEL                   T676       PD085853: P215-G326       11   7474322CD1   470   S134 S142 S245   N236 N256   Transmembrane domains:   HMMER                   S326 S355 S408   N321 N380   F62-Y87, F139-F163, F212-L230, I293-                   S411 S415 S432       I312                   S452 T15 T22       VANILLOID RECEPTOR SUBTYPE 1   BLAST_PRODOM                   T229 T265 T337       PD137334: C348-K470                   T341 T36       12   5455621CD1   618   S110 S265 S313   N219 N256   Transmembrane domains:   HMMER                   S373 S490 S550   N480 N574   D10-F28, F81-Y104, F278-M297, L439-                   S565 S576 S594       Y459, I502-R528                   T154 T237 T268       Sodium: solute symporter family domain:   HMMER_PFAM                   T360 T37 T526       F41-G445                   T567 T70       Sodium: solute symporter signature   BLIMPS_BLOCKS                           BL00456: T154-G208                           Sodium: solute symporter family   PROFILESCAN                           signature:                           N151-T198                           TRANSMEMBRANE TRANSPORT PERMEASE   BLAST_PRODOM                           PROTEIN SODIUM SYMPORT PROLINE                           COTRANSPORTER SYMPORTER GLYCOPROTEIN                           PD000991: F41-C304                           SYMPORTER SODIUM IODIDE THYROID   BLAST_PRODOM                           SODIUM/IODIDE NIS                           PD024705: I446-L489, S490-G575                           SODIUM: SOLUTE SYMPORTER FAMILY   BLAST_DOMO                           DM00745|P31636|24-561: D10-N219, G220-                           Y459       13   7477248CD1   631   S149 S212 S258   N352 N516   Transmembrane domains:   HMMER                   S522 S9 T518   N96   V22-F41, L159-M181, I391-A407                   T551 T73 T79 Y14       Sodium/hydrogen exchanger family domain:   HMMER_PFAM                           L25-V491                           Na+/H+ exchanger isoform 6 signature   BLIMPS_PRINTS                           PR01088: Y14-I38, W39-V57, Y58-V84,                           Q119-E132, A269-M288, T480-Q506, K515-                           D533, P539-Q567, P566-E593                           Na+/H+ exchanger signature   BLIMPS_PRINTS                           PR01084: I133-F144, G147-S161, I162-                           T170, G208-T218                           + TRANSPORT EXCHANGER NA PD01672:   BLIMPS_PRODOM                           I133-M181                           NA+/H+ PROTEIN TRANSMEMBRANE   BLAST_PRODOM                           TRANSPORT ANTIPORTER SYMPORT                           SODIUM EXCHANGER                           GLYCOPROTEIN SODIUM/HYDROGEN                           PD000631: G20-G63, E132-R490                           SODIUMHYDROGEN EXCHANGER 6   BLAST_PRODOM                           MYELOBLAST KIAA0267                           PD177855: G478-Y591                           do BETA; EXCHANGER; NA;   BLAST_DOMO                           DM02572|P48764|10-734: L124-L541       14   2944004CD1   1256   S103 S130 S144   N150 N23   Transmembrane domains:   HMMER                   S170 S227 S252   N300 N312   Y231-Y251, L415-L434, I933-I959, F966-                   S523 S802 S817   N318 N704   L985, I1002-F1020, N1104-M1122                   S899 S901 S98   N1045   E1-E2 ATPase domains:   HMMER_PFAM                   S1055 T269 T353   N1053   V274-V365, G490-D506, Q672-A785, L851-                   T358 T387 T502   N1059   S899                   T549 T576 T74   N1073   E1-E2 ATPases phosphorylation site   BLIMPS_BLOCKS                   T912 T1212 T1061   N1247   signature                   T1236 Y349 Y407       BL00154: V454-G490, L492-L510, K652-                           C662, N724-M764, V878-S901, A905-V938                           E1-E2 ATPases phosphorylation site:   PROFILESCAN                           I478-E526                           P-type cation-transporting ATPase   BLIMPS_PRINTS                           superfamily signature                           PR00119: N318-T332, C496-L510, A740-                           D750, C881-L900                           ATPASE PROBABLE CALCIUMTRANSPORTING   BLAST_PRODOM                           PROTEIN HYDROLASE CALCIUM TRANSPORT                           TRANSMEMBRANE PHOSPHORYLATION                           MAGNESIUM PD090368: Q995-Y1094,                           D1064-L1114                           E1-E2 ATPASES PHOSPHORYLATION SITE   BLAST_DOMO                           DM00115|P22189|49-801: S202-K331,                           P401-E505, S556-A575, V623-P767, H800-                           S984                           E1-E2 ATPase motif:   MOTIFS                           D498-T504       15   3046849CD1   499   S100 S118 S215   N292 N34   Signal peptide:   SPSCAN                   S285 T466 T487   N50   M1-G27                           Transmembrane domains:   HMMER                           M163-L181, T371-G389, M418-L440                           Sugar (and other) transporter signature:   HMMER_PFAM                           L18-L474                           Sugar transport proteins signature:   PROFILESCAN                           A112-V178                           Sugar transporter signature   BLIMPS_PRINTS                           PR00171: T28-I38, M128-M147, M376-                           L397, T399-C411                           Glucose transporter signature   BLIMPS_PRINTS                           PR00172: Q314-I335, M376-T399, A409-                           L427                           SUGAR TRANSPORT PROTEINS   BLAST_DOMO                           DM00135|P22732|132-466: R131-T466                           Sugar transporter 2 motif:   MOTIFS                           L133-R158       16   4538363CD1   596   S17 S290 S39 S5   N239 N386   Transmembrane domains:   HMMER                   T119 T211   N4 N545   S73-W95, I185-I212, L356-A376, L410-                       N96   V430, F473-F491, Y513-L533                           Sodium: solute symporter family domain:   HMMER_PFAM                           Y50-G479                           Sodium: solute symporter signature   BLIMPS_BLOCKS                           BL00456: Y27-G81, A103-R132, L165-                           G219, P452-G461                           Sodium: solute symporter family   PROFILESCAN                           signatures:                           H162-I209, V412-D502                           TRANSMEMBRANE TRANSPORT PERMEASE   BLAST_PRODOM                           PROTEIN SODIUM SYMPORT PROLINE                           COTRANSPORTER SYMPORTER GLYCOPROTEIN                           PD000991: Y50-G479                           NA+/GLUCOSE COTRANSPORTERRELATED   BLAST_PRODOM                           PROTEIN PD134393: L551-A596                           NA+/GLUCOSE COTRANSPORTERRELATED   BLAST_PRODOM                           PROTEIN PD166538: M1-G49                           SODIUM: SOLUTE SYMPORTER FAMILY   BLAST_DOMO                           DM00745|P13866|24-561: S17-W548                           Na solute symporter 2 motif:   MOTIFS                           G461-V481       17   6427460CD1   1192   S143 S169 S188   N397 N745   Transmembrane domains:   HMMER                   S283 S287 S335   N921 N989   V299-Y316, F1004-L1022, I1030-W1049,                   S451 S507 S508   N1001   A1075-L1092                   S52 S555 S561       E1-E2 ATPase domains:   HMMER_PFAM                   S722 S933 T203       E403-E425 I550-C698                   T255 T259 T269       E1-E2 ATPases phosphorylation site   BLIMPS_BLOCKS                   T333 T380 T413       signature                   T418 T659 T708       BL00154: G149-F166, V408-F426, D663-                   T714 T715 T910       L703                   T1103 T1017       E1-E2 ATPases phosphorylation site:   PROFILESCAN                   T1105 Y885 Y1026       L395-C442                           P-type cation-transporting ATPase   BLIMPS_PRINTS                           superfamily signature                           PR00119: F412-F426, A679-D689                           ATPASE HYDROLASE TRANSMEMBRANE   BLAST_PRODOM                           PHOSPHORYLATION ATPBINDING PROTEIN                           PROBABLE CALCIUMTRANSPORTING CALCIUM                           TRANSPORT                           PD004657: A857-V1108                           do ATPASE; CALCIUM; TRANSPORTING;   BLAST_DOMO                           DM02405|Q09891|206-1107; T105-Y436,                           F471-N921                           E1-E2 ATPase motif:   MOTIFS                           D414-T420       18   7474127CD1   638   S205 S224 S336   N259 N266   Transmembrane domains:   HMMER                   S378 S414 S541   N518 N536   I231-L248, F382-Y401, M451-V473                   S553 S564 S86   N84   Ion transport protein domain:   HMMER_PFAM                   T120 T146 T155       L240-I472                   T17 T21 T25 T283       Potassium channel signature   BLIMPS_PRINTS                   T374 T49 T520       PR00169: E101-T120, P222-T250, Y284-                   T546 T579       K307, F310-V330, F352-S378, E381-E404,                           F421-M443, G450-F476       18                   VOLTAGEGATED POTASSIUM CHANNEL   BLAST_PRODOM                           PROTEIN KV3.2 KSHIIIA IONIC                           TRANSMEMBRANE ION TRANSPORT                           GLYCOPROTEIN MULTIGENE FAMILY                           ALTERNATIVE SPLICING PHOSPHORYLATION                           PD085814: K495-S538                           do CHANNEL; POTASSIUM; CDRK; FORM;   BLAST_DOMO                           DM00436|P22462|189-350: R189-R351                           do CHANNEL; POTASSIUM; CDRK; SHAW;   BLAST_DOMO                           DM00490|P22462|34-151: L34-C152       19   7476949CD1   681   S307 S421 S56   N113 N251   Transmembrane domains:   HMMER                   S573 S582 S587   N256 N403   I38-I57, S90-W112, I150-I167, L188-                   S638 S651 T422   N603   M207, L373-A393, V432-I448, Y530-L550                   T485 T650 Y510       Sodium: solute symporter family domain:   HMMER_PFAM                           Y67-G496                           Sodium: solute symporter signature   BLIMPS_BLOCKS                           BL00456: Y44-G98, A120-R149, L182-                           G236, P469-A478                           Sodium: solute symporter family   PROFILESCAN                           signatures:                           Q179-V226, D458-D519                           TRANSMEMBRANE TRANSPORT PERMEASE   BLAST_PRODOM                           PROTEIN SODIUM SYMPORT PROLINE                           COTRANSPORTER SYMPORTER                           GLYCOPROTEIN PD000991: Y67-G496                           SODIUM: SOLUTE SYMPORTER FAMILY   BLAST_DOMO                           DM00745|P13866|24-561: H34-W565                           Na solute symporter 1 motif:   MOTIFS                           G183-A208       20   7477249CD1   1096   S115 S163 S276   N331 N383   Transmembrane domains:   HMMER                   S280 S332 S333   N395 N411   F289-L307, F935-L953, W967-V996,                   S404 S454 S46   N720 N932   F1008-D1028                   S461 S462 S508       E1-E2 ATPase domains:   HMMER_PFAM                   S514 S671 S863       T340-Q352, H502-V648                   S891 S1084 T262       E1-E2 ATPases phosphorylation site   BLIMPS_BLOCKS                   T340 T345 T347       signature                   T407 T570 T612       BL00154: G143-L160, V335-F353, K529-                   T687 T840 T948       C539, D616-H656                   T1034 T1036 Y322       P-type cation-transporting ATPase   BLIMPS_PRINTS                           superfamily signature                           PR00119: F339-F353, A632-D642                           H+-transporting ATPase signatur   BLIMPS_PRINTS                           PR00120: T547-A565                           ATPASE HYDROLASE TRANSMEMBRANE   BLAST_PRODOM                           PHOSPHORYLATION ATPBINDING PROTEIN                           PROBABLE CALCIUMTRANSPORTING CALCIUM                           TRANSPORT                           PD004657: A787-K1038                           do ATPASE; CALCIUM; TRANSPORTING;   BLAST_DOMO                           DM02405|P39524|236-1049: T83-I306,                           F422-N851                           E1-E2 ATPase motif:   MOTIFS                           D341-T347       21   7477720CD1   707   S204 S299 S360   N297 N31   Signal peptide:   SPSCAN                   S417 S488 S51   N342 N35   M1-A26                   S58 S585 S591       Transmembrane domains:   HMMER                   S620 S638 S679       I155-Y178, I271-T292,                   T334 T350 T483       Sodium/hydrogen exchanger family domain:   HMMER_PFAM                   T634 Y225 Y528       V73-K482                           Na+/H+ exchanger signature   BLIMPS_PRINTS                           PR01084: I158-A166, G200-A210, I129-                           L140, G143-S157                           Na+/H+ exchanger isoform 2 (NHE2)   BLIMPS_PRINTS                           signature                           PR01086: F115-S128, K616-I627                           + TRANSPORT EXCHANGER NA   BLIMPS_PRODOM                           PD01672: A83-I113, I129-L177, Y178-                           L212, A213-F249, D262-I287, S288-Y321,                           L322-M355, S359-F405, Y406-F452, I489-                           K531, I532-G562, R593-R640                           NA+/H+ PROTEIN TRANSMEMBRANE   BLAST_PRODOM                           TRANSPORT ANTIPORTER SYMPORT SODIUM                           EXCHANGER GLYCOPROTEIN SODIUM/                           HYDROGEN PD000631: I77-A438                           do BETA; EXCHANGER; NA;   BLAST_DOMO                           DM02572|P26434|14-716: L15-L687       22   7477852CD1   729   S142 S144 S155   N208 N358   Transmembrane domains:   HMMER                   S285 S291 S299   N717   F493-F512, M554-M570                   S318 S654 S664       Ankyrin repeats:   HMMER_PFAM                   S669 S697 S719       L78-E108, A116-T148, F162-S194                   T110 T138 T281       VANILLOID RECEPTOR SUBTYPE 1   BLAST_PRODOM                   T379 T447 T532       PD101189: F115-L220                   T539       ATP/GTP binding site (P-loop):   MOTIFS                           A412-T419       23   1471717CD1   492   S13 S18 S225   N229 N249   transmembrane domain:   HMMER                   S314 S373 T323       I48-V71, V86-F104, Y172-I199, I199-                   T33 T351 T426       V217, F384-F402, V452-C472                           Sugar (and other) transporter:   HMMER_PFAM                           I48-K492                           SUGAR TRANSPORT PROTEINS   BLAST_DOMO                           DM00032|P30638|80-152: R45-K115                           VESICLE; SYNAPTIC; SV2; FORM   BLAST_DOMO                           DM08835|S34961|180-344: I119-N249       24   3874406CD1   1494   S30 S50 S134   N109 N130   transmembrane domain:   HMMER                   S230 S368 S549   N313 N421   L204-F221, T272-L290, L735-Y753, F896-                   S638 S669 S686   N453 N71   S914, V941-I959, L975-R998, F1019-V1039                   S696 S792 S800   N788 N817   ABC transporter:   HMMER_PFAM                   S831 S912 S1004   N84 N867   G384-G566 G1190-G1366                   S1070 S1146   N91 N1182   ABC transporters family proteins   BLIMPS_BLOCKS                   S1172 S1206       BL00211: I389-L400, L492-D523                   S1365 T111 T435       ABC transporters family signature:   PROFILESCAN                   T449 T501 T520       V472-D523                   T632 T649 T657       ABC TRANSPORTERS FAMILY   BLAST_DOMO                   T729 T845 T1049       DM00008|P41233|839-1045: I355-N565,                   T1134 T1217       K1177-M1363                   T1247 T1295       DM00008|P34358|611-816: I355-N565,                   T1318 T1339       A1179-M1363                   T1422 T1482 Y824       DM00008|P41233|1851-2058: K1173-S1365,                           I355-N565                           DM00008|P23703|41-246: E1162-G1366,                           L377-G566                           ATP/GTP-binding site motif A (P-loop):   MOTIFS                           G391-S398, G1197-2004       25   4599654CD1   774   S355 S356 S40   N291 N416   transmembrane domain:   HMMER                   S505 S552 S559       Y95-F118, T203-L219, L327-L353                   S597 S61 S67       Transmembrane region cyclic Nucleotide   HMMER_PFAM                   S734 S736 T203       G:                   T418 T668 T764       Y168-I414                   Y490       Cyclic nucleotide-binding domain:   HMMER_PFAM                           K443-M531                           Cyclic nucleotide-binding domain   BLIMPS_BLOCKS                           proteins                           BL00888: G452-V475, G488-L497                           cAMP-dependent protein kinase signature   BLIMPS_PRINTS                           PR00103: F449-R463, S489-T498                           HYPERPOLARIZATIONACTIVATED CATION   BLAST_PRODOM                           CHANNEL, HAC3                           PD180735: T538-M774                           CHANNEL IONIC POTASSIUM K+ SUBUNIT   BLAST_PRODOM                           HYPERPOLARIZATIONACTIVATED PROTEIN                           PUTATIVE EAG LONG                           PD001039: E74-R167                           CAMP RECEPTOR PROTEIN CYCLIC   BLAST_DOMO                           NUCLEOTIDE-BINDING DOMAIN                           DM01165|A55251|333-706: H263-P561                           DM01165|P29973|311-684: H263-P561                           DM01165|Q03041|286-658: H263-G548                           DM01165|S52072|262-635: H263-Q595       26   5047435CD1   614   S116 S210 S290   N407 N599   transmembrane domain:   HMMER                   S538 S577 S606       V124-I142, A168-M190, A371-V390, W483-                   T267 T432 T443       I511, S526-I543, F552-V570                   T591       Sugar (and other) transporter:   HMMER_PFAM                           L83-F585                           Sugar transport proteins   BLIMPS_BLOCKS                           BL00216: L174-S223, G92-S103                           Sugar transporter signature   BLIMPS_PRINTS                           PR00171: G92-I102, V175-I194, L486-                           V507, S509-F521                           Glucose transporter signature   BLIMPS_PRINTS                           PR00172: V343-V364, L486-S509, R519-                           L537, W550-V570                           Sugar_Transport_1:   MOTIFS                           G138-G153 A360-A375                           Sugar transport proteins signatures   PROFILESCAN                           sugar_transport_1.prf: L344-S401                           sugar_transport_2.prf: A160-A225                           SUGAR TRANSPORT PROTEINS   BLAST_DOMO                           DM00135|S25015|122-478: A160-D417,                           L480-K574,                           DM00135|P09830|101-452: G161-V405,                           L481-K574                           DM00135|Q01440|101-433: R178-G388,                           R178-G388, L486-G575                           DM00135|P15729|242-463: A485-S577,                           R286-L414       27   7475603CD1   2180   S181 S216 S233   N112 N132   transmembrane domain:   HMMER                   S260 S409 S419   N346 N374   F630-L648, L664-L680, V1570-V1590,                   S842 S983 S1008   N1100   M1622-Q1641                   S1172 S1229   N1415   ABC transporter:   HMMER_PFAM                   S1237 S1269   N1420   G1854-G2035 G868-G1048                   S1349 S1353   N1491   ABC transporters family   BLIMPS_BLOCKS                   S1462 S1469   N1552   BL00211: F873-T884, L974-D1005                   S1504 S1566   N1695   ABC transporters family signature:   PROFILESCAN                   S1881 S1993   N1831   A1940-D1991, D955-D1005                   S2018 S2174       Abc_Transporter:   MOTIFS                   S2167 T120 T165       L974-F988                   T338 T348 T510       ATP/GTP-binding site motif A (P-loop):   MOTIFS                   T599 T614 T822       G875-T882, G1861-T1868                   T931 T1079 T1086       ATPBINDING TRANSPORTER CASSETTE ABC   BLAST_PRODOM                   T1094 T1171       TRANSPORT PROTEIN GLYCOPROTEIN                   T1181 T1209       TRANSMEMBRANE RIM ABCR                   T1219 T1417       PD005939: L1563-N1740                   T1439 T1822       ATPBINDING TRANSPORTER CASSETTE ABC   BLAST_PRODOM                   T1870 T1917       GLYCOPROTEIN TRANSMEMBRANE TRANSPORT                   T1988 T2057       ABCR RIM                   T2125 Y656 Y1448       PD010118: R238-R514, L95-R243                           ATPBINDING TRANSPORTER CASSETTE ABC   BLAST_PRODOM                           GLYCOPROTEIN TRANSMEMBRANE TRANSPORT                           ABCR RIM SIMILARITY                           PD008845: P1307-E1560                           ATPBINDING TRANSPORTER CASSETTE ABC   BLAST_PRODOM                           GLYCOPROTEIN TRANSMEMBRANE TRANSPORT                           RIM ABCR SIMILARITY                           PD006867: L540-S685, D515-Q541                           ABC TRANSPORTERS FAMILY   BLAST_DOMO                           DM00008|P41233|839-1045: V841-A1046,                           L1829-M2032                           DM00008|P41233|1851-2058: V1826-N2034,                           V841-V1045                           DM00008|P34358|1441-1640: L1827-M2032,                           V843-V1045       28   7477845CD1   1737   S23 S254 S687   N210 N216   transmembrane domain:   HMMER                   S692 S695 S7   N859 N1064   M1244-A1262, V1319-F1336, I1338-F1357,                   S713 S766 S773   N1371   A1423-I1446, W107-V126, V181-M199, S298-                   S8 S861 S1113   N1449   I321, L509-V531, V575-I598, Y879-M904,                   S1228 S1271       I1017-F1034, I1134-V1152                   S1455 S1463       Ion transport protein ion_trans:   HMMER_PFAM                   S1537 S1595       W32-I321 M380-I598 L884-V1155 I1206-                   S1647 S1652       I1446                   S1730 T272 T324       Calcium channel signature   BLIMPS_PRINTS                   T886 T1257 T1320       PR00167: D535-D561                   T1359 T1387       PROTEIN F17C8.6 C11D2.5 NEARLY IDENTICAL   BLAST_PRODOM                   T1406 T1456       C ELEGANS PREDICTED                   T1486 T1528       PD023984: V1447-S1637, E1714-T1720                   T1561 T1570       C11D2.6 PROTEIN   BLAST_PRODOM                   T1645 T1694 Y419       PD178227: L1241-R1368, I1206-F1292                   Y702 Y832       F585-E606                           C11D2.6 PROTEIN SIMILARITY ALONG ENTIRE   BLAST_PRODOM                           GENE CALCIUM CHANNEL ALPHA PROTEINS                           PD041964: L599-V885,                           CHANNEL CALCIUM IONIC SUBUNIT VOLTAGE   BLAST_PRODOM                           GATED SODIUM ALPHA TRANSMEMBRANE L                           TYPE PD000032: Y887-V1120, I33-V330,                           K1361-F1450, I1206-F1357, I577-I598,                           F1337-L1356, I1134-F1159, D1416-V1443                           III REPEAT   BLAST_DOMO                           DM00079|A55138|1052-1268: V1020-L1227                           DM00079|P35500|1424-1636: W1090-P1194,                           I1017-N1050                           IV REPEAT   BLAST_DOMO                           DM00277|P27732|1363-1572: F1337-L1536                           DM00277|P15381|1384-1595: F1337-L1536       29   168827CD1   547   S109 S167 S201   N102 N107   transmembrane domain:   HMMER                   S282 S336 S404   N56   F16-T35, Y180-C200, S201-V222, M410-                   S408 S526 T133       E429, T469-Y492, L496-L514                   T323 T35 T432       Sugar (and other) transporter:   HMMER_PFAM                   T453 T58       L13-Q528                           ORGANIC TRANSPORTERLIKE TRANSPORT   BLAST_PRODOM                           PROTEIN RENAL ANION TRANSPORTER                           CATIONIC KIDNEYSPECIFIC SOLUTE                           PD151320: N102-L144       30   7472734CD1   547   S143 S167 S201   N102 N39   transmembrane domain:   HMMER                   S282 S336 S404   N56 N62   I18-F32, M147-Y163, Y180-C200, S201-                   S408 S46 S526       V222, M410-E429, T469-Y492, L496-L514                   S60 S68 T133       Sugar (and other) transporter:   HMMER_PFAM                   T323 T432 T453       L18-Q528                   T58       SUGAR TRANSPORT PROTEINS   BLAST_DOMO                           DM00032|P46501|280-351: V121-K173                           ORGANIC TRANSPORTERLIKE TRANSPORT   BLAST_PRODOM                           PROTEIN RENAL ANION TRANSPORTER                           CATIONIC KIDNEYSPECIFIC SOLUTE                           PD151320: N102-K145       31   7473473CD1   988   S142 S237 S24   N170 N235   transmembrane domain:   HMMER                   S252 S322 S369   N403 N466   L342-A360                   S502 S680 S773   N663 N830   Transmembrane cyclic Nucleotide G:   HMMER_PFAM                   S847 S883 S925       Y288-I536                   S943 S952 S974       Cyclic nucleotide-binding domain:   HMMER_PFAM                   S981 T127 T14       V564-A655                   T215 T442 T478       PAC motif PA:   HMMER_PFAM                   T521 T634 T725       C92-T132                   T73 T832 T869       CHANNEL POTASSIUM IONIC EAG SUBUNIT   BLAST_PRODOM                   T909 T929       HEAG LONG ELECTOCARDIOGRAPHIC                           QT SYNDROME PD017645: K809-D984                           CHANNEL IONIC K+ SUBUNIT   BLAST_PRODOM                           HYPERPOLARIZATION ACTIVATED                           PUTATIVE EAG LONG PD001039: S179-I284                           CHANNEL K+ IONIC EAG SUBUNIT   BLAST_PRODOM                           TRANSMEMBRANE ION TRANSPORT                           VOLTAGEGATED PD011550: N658-E737                           CHANNEL PROTEIN IONIC POTASSIUM NON   BLAST_PRODOM                           PHOTOTROPIC HYPOCOTYL PUTATIVE SUBUNIT                           REPEAT EAG                           PD009483: M1-E89                           CAMP RECEPTOR PROTEIN CYCLIC   BLAST_DOMO                           NUCLEOTIDE-BINDING DOMAIN                           DM01165|I48912|391-786: H361-S756                           DM01165|Q02280|384-776: H361-E737                           DM01165|I38465|562-948: H361-R671,                           S974-E985                           POTASSIUM; CHANNEL; KST1; AKT1;   BLAST_DOMO                           DM02383|I48912|164-389: V162-E314,                           E314-A360, W362-V455       32   7477725CD1   533   S107 S109 S143   N102 N216   transmembrane domain:   HMMER                   S167 S282 S345   N56 N62   F150-D168, L380-N401, I407-V426, L486-                   S408 S469 S60       F504                   T133 T289 T323       Sugar (and other) transporter:   HMMER_PFAM                   T336 T432 T526       A111-K528                           ORGANIC TRANSPORTER LIKE TRANSPORT   BLAST_PRODOM                           PROTEIN RENAL ANION TRANSPORTER                           CATIONIC KIDNEY SPECIFIC SOLUTE                           PD151320: N102-K145                    
     [0372]                                       TABLE 4                       Polynucleotide   Incyte   Sequence   Selected                   SEQ ID NO:   Polynucleotide ID   Length   Fragment(s)   Sequence Fragments   5′ Position   3′ Position                                                            33   3474673CB1   1775   1-391, 578-786,   GNFL.g7798848_000003 —     1   1156                   1024-1301   004.edit                       6724643H1   861   1347                       (LUNLTMT01)                       3474673H1   249   568                       (LUNGNOT27)                       71495515V1   1205   1775       34   4588877CB1   1545   261-619, 1-193,   71495515V1)   975   1545                   794-1071   FL135171_00001   539   1534                       71497982V1   1   662       35   7472214CB1   1941   1483-1558, 1-413,   GBI: g8117242_000054 —     1171   1335                   495-616,   edit.8639-8803                   732-1149   GBI: g8117242_000054 —     544   684                       edit.4857-4997                       GBI: g8117242_000054.   1441   1599                       edit.10305-10463                       6891360H1   1433   1905                       (BRAITDR03)                       GBI: g8117242_000054 —     1   240                       edit.50-89                       GBI: g8117242_000054 —     925   1068                       edit.6950-7093                       GBI: g8117242_000054 —     358   492                       edit.4345-4478                       60124962D2   1735   1941                       GBI: g8117242_000054 —     1069   1170                       edit.8313-8414                       GBI: g8118985_000043 —     685   810                       edit.12301-12444.                       comp                       GBI: g8117242_000054 —     241   357                       edit.4112-4228                       GBI: g8117242_000054 —     1717   1941                       edit.10957-11181                       5500380H1   907   1119                       (BRABDIR01)                       GBI: g8117242_000054 —     1600   1716                       edit.10616-10732                       GBI: g8117242_000054 —     1336   1440                       edit.8907-9011                       GBI: g8117242_000054 —     811   924                       edit.6643-6756       36   7473053CB1   4971   3312-3482, 1-1466,   8035016H1   2315   2975                   4307-4971,   (SMCRUNE01)                   2184-2221   6822202J1   2145   2877                       (SINTNOR01)                       6781747H1   968   1449                       (OVARDIR01)                       8035016J1   2979   3643                       (SMCRUNE01)                       6824230H1   2867   3483                       (SINTNOR01)                       6894266H1   548   1157                       (BRAITDR03)                       6777836H1   1601   2238                       (OVARDIR01)                       6908503H1   1   667                       (PITUDIR01)                       6908503J1   1270   1830                       (PITUDIR01)                       6823447H1   3525   4260                       (SINTNOR01)                       6823447J1   4226   4829                       (SINTNOR01)                       6006310F8   4501   4969                       (FIBRUNT02)                       4171959T6   3637   4287                       (SINTNOT21)                       5088860F6   4461   4853                       (UTRSTMR01)       37   7473347CB1   1404   126-633, 1013-1404,   GBI.lee4.edit   1   1404                   768-838       38   7474240CB1   4048   3023-4048, 1753-2469,   71984804V1   964   1311                   1-920,   GBI: 7656646_edit   929   3418                   1593-1658, 2614-2908,   71986624V1   1369   1976                   1138-1367   55055014H1   1   130                       55037111J2   95   871                       71983668V1   1371   2043                       GBI: g5923734_edit   2612   4048                       55037119J2   224   875                       2502027F6   696   1235                       (ADRETUT05)       39   7475338CB1   1539   1412-1539, 1-328,   GBI: g7960701_000004 —     154   312                   495-837,   edit.549-713                   922-1218   GBI: g7960701_000004 —     1015   1113                       edit.13381-13480                       GBI: g7960701_000004 —     715   903                       edit.8755-8943                       GBI: g7960701_000004 —     313   438                       edit.4292-4417                       GBI: g7960701_000004 —     1114   1194                       edit.16237-16317                       GBI: g7960701_000004 —     1321   1539                       edit.20107-20325                       GBI: g7960701_000004 —     904   1014                       edit.9989-10099                       GBI: g7960701_000004 —     1195   1320                       edit.18748-18873                       GBI: g7960701_000003 —     52   153                       edit.9783-9884                       GBI: g7960701_000004 —     439   591                       edit.5251-5403                       GBI: g7960701_000004 —     592   714                       edit.8384-8506                       71906448V1   627   1082                       71753467V1   912   1539       40   7476747CB1   3114   1717-1870, 1-503,   3351512F6   2185   2724                   1468-1650   (PROSNOT28)                       7761783J1   1943   2570                       (THYMNOE02)                       6934981R8   78   860                       (SINTTMR02)                       6389368H1   1782   2075                       (PROSTMC01)                       70536163V1   2575   3114                       6934981F8   1   643                       (SINTTMR02)                       GNN.g7712065_000012 —     452   1922                       002                       7080657H1   838   1403                       (STOMTMR02)                       5633289H1   639   890                       (PLACFER01)                       g5746200   1215   1473       41   7477898CB1   2877   846-901, 1272-1378,   GBI.g2262095   1   2877                   2319-2877       42   7472728CB1   2820   1-1399, 2207-2229   55022826J1   1138   1834                       55030210H1   403   986                       4399366T6   2231   2777                       (TESTTUT03)                       55030274H1   1482   2153                       g565876   2597   2820                       55018149J1   1907   2585                       FL203597_00001   712   1807                       GNN.g7263861_026.edit   1   1052       43   7474322CB1   1440   1-604, 714-768   GBI.g8081632_edit   1   1440                       71228887V1   1090   1440                       70868623V1   988   1385       44   5455621CB1   2394   1483-1686, 1-329,   3696546T6   1833   2394                   838-1155,   (SININOT05)                   2201-2235   70674954V1   1520   2091                       1426382H1   1224   1492                       (SINTBST01)                       3696546F6   799   1381                       (SININOT05)                       6828352H1   530   1149                       (SINTNOR01)                       3699565H1   1   281                       (SININOT05)                       7700096H1   250   990                       (KIDPTDE01)                       70678552V1   1419   2055       45   7477248CB1   2890   1-58, 2739-2890,   2777287H1   2250   2498                   2310-2349, 329-1167   (OVARTUT03)                       7977733H1   841   1427                       (LSUBDMC01)                       7678168J1   1271   1827                       (NOSETUE01)                       7611941J1   2273   2890                       (KIDCTME01)                       6590507H1   179   672                       (TLYMUNT03)                       2701794F6   1208   1741                       (OVARTUT10)                       2544096F6   1732   2252                       (UTRSNOT11)                       60117044D2   1   431                       5020832H1   2195   2471                       (OVARNON03)                       7662529H1   526   926                       (UTRSTME01)       46   2944004CB1   3926   3338-3365, 1-687,   4762728F6   872   1387                   1222-2267   (PLACNOT05)                       g2264624   2268   2446                       6264977H1   1210   1797                       (MCLDTXN03)                       2944004F6   2790   3531                       (BRAITUT23)                       6610392H2   3306   3926                       (MUSTTMC01)                       GNN.g7328818_000024 —     2145   2648                       002.edit                       7035078H1   1   440                       (SINTFER03)                       7620248J1   2431   3039                       (HEARFEE03)                       496537H1   2329   2487                       (HNT2NOT01)                       6264427T8   453   1174                       (MCLDTXN03)                       6264427F8   170   842                       (MCLDTXN03)                       7673654H1   1733   2239                       (FIBPFEC01)       47   3046849CB1   2135   2072-2135, 596-711,   8262790U1   1383   2135                   1014-1263   71896642V1   1   592                       71247870V1   1050   1736                       FL3046849_g6815043 —     51   1520                       000004_g183298       48   4538363CB1   2637   1-183, 1575-1680,   FL4538363_g3126781 —     1   1917                   2094-2637   g520469                       71401405V1   1766   2637       49   6427460CB1   3783   985-1833, 2687-3204   70857895V1   416   1035                       7727961J1   3284   3783                       (UTRCDIE01)                       70857789V1   566   1109                       g5689372_edit   1092   3361                       g3801917   1   452       50   7474127CB1   2105   1078-2105   GBI.g8568959_edit_3   1119   2105                       g6140313   482   951                       5819744F7   168   479                       (PROSTUS23)                       g5920552   1   488                       55049678J1   862   1359       51   7476949CB1   2069   1233-1356, 1-117,   FL7476949_g6714723 —     1   2046                   2047-2069,   g338053                   347-503, 1536-1844   4669722H1   1801   2069                       (SINTNOT24)       52   7477249CB1   4245   2833-3018, 1869-2121,   71660072V1   2404   3156                   3707-4245,   71657569V1   3106   3854                   1-252, 982-1239,   7633968J1   2579   3175                   289-357   (SINTDIE01)                       6440145F8   938   1087                       (BRAENOT02)                       71664080V1   3228   3891                       GBI.g8567478.edit   1   2547                       71660176V1   3773   4245                       71662066V1   1802   2475                       2605539F6   433   939                       (LUNGTUT07)                       71659261V1   1690   2437                       3825558H1   1179   1270                       (BRAIHCT02)                       7765571H1   1   693                       (URETTUE01)                       5675861H1   1427   1716       53   7477720CB1   2124   1-936, 1200-1488,   FL7477720_g5836195 —     1   2124                   1982-2124,   g205709                   1562-1745       54   7477852CB1   2195   1-418, 1899-2195   GBI.g8748866.edit   1   2195       55   1471717CB1   2055   206-768, 881-931,   70464956V1   492   994                   1155-1323   72277206V1   1   297                       70469664V1   939   1582                       GNN.g7109510_000068 —     772   1500                       002.edit                       GBI.g8039708_50_63 —     238   897                       62_56.edit                       6540941H1   1571   2055                       (LNODNON02)                       70466394V1   1035   1616       56   3874406CB1   4727   1-1299, 1576-1632,   71793833V1   4117   4727                   2550-3619,   55052105J1   1673   2128                   2014-2192   71798347V1   3620   4358                       71798870V1   3575   4244                       55058313J1   1380   2125                       55051482J1   2475   3134                       FL3874406_g3810670 —     482   744                       g4240130_3_3-4                       55068154H1   2223   2741                       3133035F6   1   605                       (SMCCNOT01)                       55058329H1   723   1528                       55068182J1   2048   2685                       71795307V1   2902   3593       57   4599654CB1   3852   1-335, 2014-3231   8016331J1   1778   2424                       (BMARTXE01)                       71040001V1   3348   3852                       8041905H1   1666   2352                       (OVARTUE01)                       55062505H1   660   1233                       g7959336_CD   349   2540                       6772024J1   1   623                       (BRAUNOR01)                       55064208J1   1118   1718                       6617183H2   2981   3530                       (BRAXTDR14)                       6195941H1   2823   3458                       (PITUNON01)                       71909238V1   1225   1747                       2216896F6   2474   2923                       (SINTFET03)                       71042073V1   2276   2745       58   5047435CB1   1917   1-238, 1162-1474   7431853H1   1211   1917                       (UTRMTMR02)                       GNN: g4375937_004_edit   1   1845                       6426880H1   814   1336                       (LUNGNON07)                       6781142H1   224   941                       (OVARDIR01)                       2645767H1   128   394                       (OVARNOT09)       59   7475603CB1   6791   1-3283, 5952-6101,   71704421V1   6240   6791                   3793-4761   7726210H1   1885   2602                       (THYRDIE01)                       7721710J2   2696   3232                       (THYRDIE01)                       6340173F8   5516   6222                       (BRANDIN01)                       71704256V1   3025   3734                       7757131H1   2408   3093                       (SPLNTUE01)                       GNN.g7711543_000002 —     198   2751                       002.edit                       7464813H1   544   696                       (LIVRFEE04)                       71703676V1   3250   3947                       7760618H1   2183   2676                       (THYMNOE02)                       71970086V1   5817   6525                       7462584H1   1   578                       (LIVRFEE04)                       7760618J1   1251   1983                       (THYMNOE02)                       71762287V1   4313   4879                       7724639H1   951   1545                       (THYRDIE01)                       55052451J1   4792   5698                       7739867H1   5131   5794                       (THYMNOE01)                       6879936H1   697   1054                       (UTRSTMR02)                       55058371H1   3850   4747       60   7477845CB1   5214   2390-4599, 645-1796   GBI.g8346195_edit   1765   5214                       GBI.g8052096_edit   1132   1839                       8104845H1   2822   3367                       (MIXDDIE02)                       GBI.g8518014_edit   1   1266       61   168827CB1   1818   1-281, 796-912   g1081430   1036   1525                       168827H1   65   406                       (LIVRNOT01)                       55064792J1   1   209                       55072770H1   495   1110                       GNN.g6498074_012.edit   1321   1818                       087510H1   314   574                       (LIVRNOT01)                       g751568   1336   1773       62   7472734CB1   2245   1223-1339, 1-710   55055559H1   16   699                       55045003H2   1   697                       g5361744   908   1109                       GBI.g8118965_000015 —     602   2245                       000006_000001_000010 —                         000003.edit                       g751568   1763   2200       63   7473473CB1   3196   1-376, 460-1796   55049235H1   556   1287                       GBI.g8018151_000001.   1799   3196                       edit                       GBI.g6433826_000001.   1172   2052                       edit                       55063069J1   1   850                       g669271   1799   2106       64   7477725CB1   1602   1072-1602   7455614H1   416   835                       (LIVRTUE01)                       4288148H1   112   257                       (LIVRDIR01)                       GBI.g8131631_000007 —     1   1602                       000005.edit                       g2656651   829   1084                    
     [0373]                       TABLE 5                       Polynucleotide   Incyte           SEQ ID NO:   Project ID   Representative Library                                            33   3474673CB1   LUNLTMT01       34   4588877CB1   LUNLTMT01       35   7472214CB1   BRAENOT04       36   7473053CB1   SINTNOR01       38   7474240CB1   ADRETUT05       39   7475338CB1   SINTNOT18       40   7476747CB1   SINTTMR02       42   7472728CB1   TESTTUT03       43   7474322CB1   SINTBST01       44   5455621CB1   SININOT05       45   7477248CB1   UTRSNOT11       46   2944004CB1   MCLDTXN03       47   3046849CB1   HNT2AGT01       48   4538363CB1   PANCNOT07       49   6427460CB1   BRAUNOR01       50   7474127CB1   PROSTUS23       51   7476949CB1   COLNTMC01       52   7477249CB1   COLNPOT01       55   1471717CB1   OVARDIT01       56   3874406CB1   LIVRDIR01       57   4599654CB1   LUNGNOT23       58   5047435CB1   OVARDIR01       59   7475603CB1   THYRDIE01       60   7477845CB1   MIXDDIE02       61   168827CB1   LIVRNOT01       64   7477725CB1   LIVRTUE01                    
     [0374]                       TABLE 6                       Library   Vector   Library Description                  ADRETUT05   pINCY   Library was constructed using RNA isolated from adrenal tumor tissue removed from               a 52-year-old Caucasian female during a unilateral adrenalectomy. Pathology               indicated a pheochromocytoma.       BRAENOT04   pINCY   Library was constructed using RNA isolated from inferior parietal cortex tissue               removed from the brain of a 35-year-old Caucasian male who died from cardiac               failure. Pathology indicated moderate leptomeningeal fibrosis and multiple               microinfarctions of the cerebral neocortex. Patient history included dilated               cardiomyopathy, congestive heart failure, cardiomegaly and an enlarged spleen and               liver.       BRAUNOR01   pINCY   This random primed library was constructed using RNA isolated from striatum,               globus pallidus and posterior putamen tissue removed from an 81-year-old Caucasian               female who died from a hemorrhage and ruptured thoracic aorta due to               atherosclerosis. Pathology indicated moderate atherosclerosis involving the               internal carotids, bilaterally; microscopic infarcts of the frontal cortex and               hippocampus; and scattered diffuse amyloid plaques and neurofibrillary tangles,               consistent with age. Grossly, the leptomeninges showed only mild thickening and               hyalinization along the superior sagittal sinus. The remainder of the               leptomeninges was thin and contained some congested blood vessels. Mild atrophy               was found mostly in the frontal poles and lobes, and temporal lobes, bilaterally.               Microscopically, there were pairs of Alzheimer type II astrocytes within the deep               layers of the neocortex. There was increased satellitosis around neurons in the               deep gray matter in the middle frontal cortex. The amygdala contained rare diffuse               plaques and neurofibrillary tangles. The posterior hippocampus contained a               microscopic area of cystic cavitation with hemosiderin-laden macrophages               surrounded by reactive gliosis. Patient history included sepsis, cholangitis,               post-operative atelectasis, pneumonia CAD, cardiomegaly due to left ventricular               hypertrophy, splenomegaly, arteriolonephrosclerosis, nodular colloidal goiter,               emphysema, CHF, hypothyroidism, and peripheral vascular disease.       COLNPOT01   pINCY   Library was constructed using RNA isolated from colon polyp tissue removed from a               40-year-old Caucasian female during a total colectomy. Pathology indicated an               inflammatory pseudopolyp; this tissue was associated with a focally invasive grade               2 adenocarcinoma and multiple tubuvillous adenomas. Patient history included a               benign neoplasm of the bowel.       COLNTMC01   pINCY   This large size-fractionated library was constructed using pooled cDNA from three               different donors. cDNA was generated using mRNA isolated from colon epithelium               tissue removed from a 13-year-old Caucasian female (donor A) who died from a motor               vehicle accident; from ascending colon removed from a 29-year-old female (donor               B); and from colon tissue removed from the appendix of a 37-year-old Black female               (donor C) during myomectomy, dilation and curettage, right fimbrial region biopsy,               and incidental appendectomy. Pathology for donor B indicated the proximal and               distal resection margins of small bowel and colon away from the mass lesion were               uninvolved by lymphoma. Pathology for donor C indicated an unremarkable appendix.               Pathology for the matched tumor tissue (donor B) indicated malignant lymphoma,               small cell, non-cleaved (Burkitt&#39;s lymphoma, B-cell phenotype), forming a polypoid               mass in the region of the ileocecal valve, associated with intussusception and               obstruction clinically. The liver and multiple (3 of 12) ileocecal region lymph               nodes were also involved by lymphoma. Pathology for the associated tumor tissue               (donor C) indicated multiple uterine leiomyomata. Donor C presented with               deficiency anemia, an umbilical hernia, and premenopausal menorrhagia. Patient               history included sarcoidosis of the lung.       HNT2AGT01   PBLUESCRIPT   Library was constructed at Stratagene (STR937233), using RNA isolated from the               hNT2 cell line derived from a human teratocarcinoma that exhibited properties               characteristic of a committed neuronal precursor. Cells were treated with retinoic               acid for 5 weeks and with mitotic inhibitors for two weeks and allowed to mature               for an additional 4 weeks in conditioned medium.       LIVRDIR01   pINCY   The library was constructed using RNA isolated from diseased liver tissue removed               from a 63-year-old Caucasian female during a liver transplant. Patient history               included primary biliary cirrhosis diagnosed in 1989. Serology was positive for               anti-mitochondrial antibody.       LIVRNOT01   PBLUESCRIPT   Library was constructed at Stratagene, using RNA isolated from the liver tissue of               a 49-year-old male.       LIVRTUE01   PCDNA2.1   This 5′ biased random primed library was constructed using RNA isolated from liver               tumor tissue removed from a 72-year-old Caucasian male during partial hepatectomy.               Pathology indicated metastatic grade 2 (of 4) neuroendocrine carcinoma forming a               mass. The patient presented with metastatic liver cancer. Patient history included               benign hypertension, type I diabetes, prostatic hyperplasia, prostate cancer,               alcohol abuse in remission, and tobacco abuse in remission. Previous surgeries               included destruction of a pancreatic lesion, closed prostatic biopsy,               transurethral prostatectomy, removal of bilateral testes and total splenectomy.               Patient medications included Eulexin, Hytrin, Proscar, Ecotrin, and insulin.               Family history included atherosclerotic coronary artery disease and acute               myocardial infarction in the mother; atherosclerotic coronary artery disease and               type II diabetes in the father.       LUNGNOT23   pINCY   Library was constructed using RNA isolated from left lobe lung tissue removed from               a 58-year-old Caucasian male. Pathology for the associated tumor tissue indicated               metastatic grade 3 (of 4) osteosarcoma. Patient history included soft tissue               cancer, secondary cancer of the lung, prostate cancer, and an acute duodenal ulcer               with hemorrhage. Family history included prostate cancer, breast cancer, and acute               leukemia.       LUNLTMT01   pINCY   The library was constructed using RNA isolated from right middle lobe lung tissue               removed from a 63-year-old Caucasian female during a segmental lung resection.               Pathology for the associated tumor tissue indicated grade3 adenocarcinoma in the               right lower lobe and right middle lobe that infiltrated the parietal pleural               surface. Metastatic grade 3 adenocarcinoma was found in the diaphragm. The lymph               nodes contained metastatic grade 3 adenocarcinoma and involved the superior               mediastinal and inferior mediastinal lymph nodes. Patient history included               hyperlipidemia. Family history included benign hypertension, cerebrovascular               disease, breast cancer, and hyperlipidemia.       MCLDTXN03   pINCY   This normalized dendritic cell library was constructed from one million               independent clones from a pool of two derived dendritic cell libraries. Starting               libraries were constructed using RNA isolated from untreated and treated derived               dendritic cells from umbilical cord blood CD34+ precursor cells removed from a               male. The cells were derived with granulocyte/macrophage colony stimulating factor               (GM-CSF), tumor necrosis factor alpha (TNF alpha), and stem cell factor (SCF). The               GM-CSF was added at time 0 at 100 ng/ml, the TNF alpha was added at time 0 at 2.5               ng/ml, and the SCF was added at time 0 at 25 ng/ml. Incubation time was 13 days.               The treated cells were then exposed to phorbol myristate acetate (PMA), and               Ionomycin. The PMA and Ionomycin were added at 13 days for five hours. The library               was normalized in two rounds using conditions adapted from Soares et al., PNAS               (1994) 91: 9228-9232 and Bonaldo et al., Genome Research (1996) 6: 791, except that               a significantly longer (48 hours/round) reannealing hybridization was used.       MIXDDIE02   PBK-CMV   This 5′ biased random primed library was constructed using pooled cDNA from seven               donors. cDNA was generated using mRNA isolated from brain tissue removed from two               Caucasian male fetuses who died after 23 weeks gestation from hypoplastic left               heart (A) and prematurity (B); from posterior hippocampus from a 55-year-old male               who died from COPD (C); from cerebellum, corpus callosum, thalmus and temporal               lobe tissue from a 57-year-old Caucasian male who died from a CVA (D); from               dentate nucleus and vermis from an 82-year-old Caucasian male who died from a               myocardial infarction (E); from pituitary gland from a 74-year-old Caucasian               female who died from a myocardial infarction (F) and vermis tissue from a 77-year-               old Caucasian female who died from pneumonia (G). For donor C, pathology indicated               mild lateral ventricular enlargement. For donor F, pathology indicated moderate               Alzheimer&#39;s disease, recent multiple infarctions involving left thalamus, left               parietal and occipital lobes (microscopic) and right cerebellum (gross), mild               atherosclerosis involving middle cerebral arteries bilaterally and mild cerebral               amyloid angiopathy. For donor G, pathology indicated severe Alzheimer&#39;s disease,               mild atherosclerosis involving the middle cerebral and basilar arteries, and               cerebral atrophy consistent with Alzheimer&#39;s disease, For donor D, patient history               included Huntington&#39;s chorea. Donor E was taking nitroglycerin and dopamine; donor               F was taking Lopressor, heparin, ceftriaxone, captopril, Isordil, nitroglycerin,               Clinoril, Ecotrin and tacrine; and donor G was taking insulin.       OVARDIR01   PCDNA2.1   This random primed library was constructed using RNA isolated from right ovary               tissue removed from a 45-year-old Caucasian female during total abdominal               hysterectomy, bilateral salpingo-oophorectomy, vaginal suspension and fixation,               and incidental appendectomy. Pathology indicated stromal hyperthecosis of the               right and left ovaries. Pathology for the matched tumor tissue indicated a dermoid               cyst (benign cystic teratoma) in the left ovary. Multiple (3) intramural               leiomyomata were identified. The cervix showed squamous metaplasia. Patient               history included metrorrhagia, female stress incontinence, alopecia, depressive               disorder, pneumonia, normal delivery, and deficiency anemia. Family history               included benign hypertension, atherosclerotic coronary artery disease,               hyperlipidemia, and primary tuberculous complex.       OVARDIT01   pINCY   Library was constructed using RNA isolated from diseased ovary tissue removed from               a 39-year-old Caucasian female during total abdominal hysterectomy, bilateral               salpingo-oophorectomy, dilation and curettage, partial colectomy, incidental               appendectomy, and temporary colostomy. Pathology indicated the right and left               adnexa were extensively involved by endometriosis. Endometriosis also involved the               anterior and posterior serosal surfaces of the uterus and the cul-de-sac and the               mesentery and muscularis propria of the sigmoid colon. Pathology for the               associated tumor tissue indicated multiple (3 intramural, 1 subserosal)               leiomyomata. Family history included hyperlipidemia, benign hypertension,               atherosclerotic coronary artery disease, depressive disorder, brain cancer, and               type II diabetes.       PANCNOT07   pINCY   Library was constructed using RNA isolated from the pancreatic tissue of a               Caucasian male fetus, who died at 23 weeks&#39; gestation.       PROSTUS23   pINCY   This subtracted prostate tumor library was constructed using 10 million clones               from a pooled prostate tumor library that was subjected to 2 rounds of substractive               hybridization with 10 million clones from a pooled prostate tissue library. The               starting library for subtraction was constructed by pooling equal numbers of               clones from 4 prostate tumor libraries using mRNA isolated from prostate tumor               removed from Caucasian males at ages 58 (A), 61 (B), 66 (C), and 68 (D) during               prostatectomy with lymph node excision. Pathology indicated adenocarcinoma in all               donors. History included elevated PSA, induration and tobacco abuse in donor A;               elevated PSA, induration, prostate hyperplasia, renal failure, osteoarthritis,               renal artery stenosis, benign HTN, thrombocytopenia, hyperlipidemia,               tobacco/alcohol abuse and hepatitis C (carrier) in donor B; elevated PSA,               induration, and tobacco abuse in donor C; and elevated PSA, induration,               hypercholesterolemia, and kidney calculus in donor D. The hybridization probe for               subtraction was constructed by pooling equal numbers of cDNA clones from 3               prostate tissue libraries derived from prostate tissue, prostate epithelial cells,               and fibroblasts from prostate stroma from 3 different donors. Subtractive               hybridization conditions were based on the methodologies of Swaroop et al., NAR 19               (1991): 1954 and Bonaldo, et al. Genome Research 6 (1996): 791.       SININOT05   pINCY   Library was constructed using RNA isolated from ileum tissue obtained from a 30-               year-old Caucasian female during partial colectomy, open liver biopsy, incidental               appendectomy, and permanent colostomy. Patient history included endometriosis.               Family history included hyperlipidemia, anxiety, and upper lobe lung cancer,               stomach cancer, liver cancer, and cirrhosis.       SINTBST01   pINCY   Library was constructed using RNA isolated from the ileum tissue of an 18-year-old               Caucasian female. The ileum tissue, along with the cecum and appendix, were               removed               during bowel anastomosis. Pathology indicated Crohn&#39;s disease of the ileum,               involving 15 cm of the small bowel. The cecum and appendix were unremarkable, and               the margins were uninvolved. The patient presented with abdominal pain and               regional enteritis. Patient history included osteoporosis of the vertebra and               abnormal blood chemistry. Patient medications included Prilosec (omeprazole),               Pentasa (mesalamine), amoxicillin, and multivitamins. Family history included               cerebrovascular disease and atherosclerotic coronary artery disease.       SINTNOR01   PCDNA2.1   This random primed library was constructed using RNA isolated from small intestine               tissue removed from a 31-year-old Caucasian female during Roux-en-Y gastric               bypass. Patient history included clinical obesity.       SINTNOT18   pINCY   Library was constructed using RNA isolated from small intestine tissue obtained               from a 59-year-old male.       SINTTMR02   PCDNA2.1   This random primed library was constructed using RNA isolated from small intestine               tissue removed from a 59-year-old male. Pathology for the matched tumor tissue               indicated multiple (9) carcinoid tumors, grade 1, in the small bowel. The largest               tumor was associated with a large mesenteric mass. Multiple convoluted segments of               bowel were adhered to the tumor. A single (1 of 13) regional lymph node was               positive for malignancy. The peritoneal biopsy indicated focal fat necrosis.       TESTTUT03   pINCY   Library was constructed using RNA isolated from right testicular tumor tissue               removed from a 45-year-old Caucasian male during a unilateral orchiectomy.               Pathology indicated seminoma. Patient history included hyperlipidemia and stomach               ulcer. Family history included cerebrovascular disease, skin cancer,               hyperlipidemia, acute myocardial infarction, and atherosclerotic coronary artery               disease.       THYRDIE01   PCDNA2.1   This 5′ biased random primed library was constructed using RNA isolated from               diseased thyroid tissue removed from a 22-year-old Caucasian female during closed               thyroid biopsy, partial thyroidectomy, and regional lymph node excision. Pathology               indicated adenomatous hyperplasia. The patient presented with malignant neoplasm               of the thyroid. Patient history included normal delivery, alcohol abuse, and               tobacco abuse. Previous surgeries included myringotomy. Patient medications               included an unspecified type of birth control pills. Family history included               hyperlipidemia and depressive disorder in the mother; and benign hypertension,               congestive heart failure, and chronic leukemia in the grandparent(s).       UTRSNOT11   pINCY   Library was constructed using RNA isolated from uterine myometrial tissue removed               from a 43-year-old female during a vaginal hysterectomy and removal of the               fallopian tubes and ovaries. Pathology for the associated tumor tissue indicated               that the myometrium contained an intramural and a submucosal leiomyoma. Family               history included benign hypertension, hyperlipidemia, colon cancer, type II               diabetes, and atherosclerotic coronary artery disease.                    
     [0375]                           TABLE 7                                   Parameter       Program   Description   Reference   Threshold                  ABIFACTURA   A program that removes vector sequences and   Applied Biosystems, Foster City, CA.               masks ambiguous bases in nucleic acid sequences.       ABI/   A Fast Data Finder useful in comparing and   Applied Biosystems, Foster City, CA;   Mismatch &lt;       PARACEL   annotating amino acid or nucleic acid sequences.   Paracel Inc., Pasadena, CA.   50%       FDF       ABI   A program that assembles nucleic acid sequences.   Applied Biosystems, Foster City, CA.       AutoAssembler       BLAST   A Basic Local Alignment Search Tool useful in   Altschul, S. F. et al. (1990) J. Mol. Biol.   ESTs:           sequence similarity search for amino acid and   215: 403-410; Altschul, S. F. et al. (1997)   Probability           nucleic acid sequences. BLAST includes five   Nucleic Acids Res. 25: 3389-3402.   value = 1.0E−8           functions: blastp, blastn, blastx, tblastn, and tblastx.       or less Full                   Length                   sequences:                   Probability                   value =                   1.0E−10 or less       FASTA   A Pearson and Lipman algorithm that searches for   Pearson, W. R. and D. J. Lipman (1988) Proc.   ESTs: fasta E           similarity between a query sequence and a group of   Natl. Acad Sci. USA 85: 2444-2448; Pearson,   value =           sequences of the same type. FASTA comprises as   W. R. (1990) Methods Enzymol. 183: 63-98;   1.06E−6           least five functions: fasta, tfasta, fastx, tfastx, and   and Smith, T. F. and M. S. Waterman (1981)   Assembled           ssearch.   Adv. Appl. Math. 2: 482-489.   ESTs: fasta                   Identity = 95%                   or greater and                   Match length =                   200 bases or                   greater; fastx E                   value = 1.0E−8                   or less Full                   Length                   sequences:                   fastx score =                   100 or greater       BLIMPS   A BLocks IMProved Searcher that matches a   Henikoff, S. and J. G. Henikoff (1991) Nucleic   Probability           sequence against those in BLOCKS, PRINTS,   Acids Res. 19: 6565-6572; Henikoff, J. G. and   value = 1.0E−3           DOMO, PRODOM, and PFAM databases to search   S. Henikoff (1996) Methods Enzymol.   or less           for gene families, sequence homology, and structural   266: 88-105; and Attwood, T. K. et al. (1997) J.           fingerprint regions.   Chem. Inf. Comput. Sci. 37: 417-424.       HMMER   An algorithm for searching a query sequence against   Krogh, A. et al. (1994) J. Mol. Biol.   PFAM hits:           hidden Markov model (HMM)-based databases of   235: 1501-1531; Sonnhammer, E. L. L. et al.   Probability           protein family consensus sequences, such as PFAM.   (1988) Nucleic Acids Res. 26: 320-322;   value = 1.0E−3               Durbin, R. et al. (1998) Our World View, in a   or less               Nutshell, Cambridge Univ. Press, pp. 1-350.   Signal peptide                   hits: Score = 0                   or greater       ProfileScan   An algorithm that searches for structural and sequence   Gribskov, M. et al. (1988) CABIOS 4: 61-66;   Normalized           motifs in protein sequences that match sequence patterns   Gribskov, M. et al. (1989) Methods Enzymol.   quality score ≧           defined in Prosite.   183: 146-159; Bairoch, A. et al. (1997)   GCG-specified               Nucleic Acids Res. 25: 217-221.   “HIGH” value                   for that                   particular                   Prosite motif.                   Generally,                   score =                   1.4-2.1.       Phred   A base-calling algorithm that examines automated   Ewing, B. et al. (1998) Genome Res.           sequencer traces with high sensitivity and probability.   8: 175-185; Ewing, B. and P. Green               (1998) Genome Res. 8: 186-194.       Phrap   A Phils Revised Assembly Program including SWAT and   Smith, T. F. and M. S. Waterman (1981) Adv.   Score = 120 or           CrossMatch, programs based on efficient implementation   Appl. Math. 2: 482-489; Smith, T.F. and M.S.   greater;           of the Smith-Waterman algorithm, useful in searching   Waterman (1981) J. Mol. Biol. 147: 195-197;   Match length =           sequence homology and assembling DNA sequences.   and Green, P., University of Washington,   56 or greater               Seattle, WA.       Consed   A graphical tool for viewing and editing Phrap assemblies.   Gordon, D. et al. (1998) Genome Res. 8: 195-202.       SPScan   A weight matrix analysis program that scans protein   Nielson, H. et al. (1997) Protein Engineering   Score = 3.5 or           sequences for the presence of secretory signal peptides.   10: 1-6; Claverie, J.M. and S. Audic (1997)   greater               CABIOS 12: 431-439.       TMAP   A program that uses weight matrices to delineate   Persson, B. and P. Argos (1994) J. Mol. Biol.           transmembrane segments on protein sequences and   237: 182-192; Persson, B. and P. Argos (1996)           determine orientation.   Protein Sci. 5: 363-371.       TMHMMER   A program that uses a hidden Markov model (HMM) to   Sonnhammer, E. L. et al. (1998) Proc. Sixth Intl.           delineate transmembrane segments on protein sequences   Conf. on Intelligent Systems for Mol. Biol.,           and determine orientation.   Glasgow et al., eds., The Am. Assoc. for Artificial               Intelligence Press, Menlo Park, CA, pp. 175-182.       Motifs   A program that searches amino acid sequences for patterns   Bairoch, A. et al. (1997) Nucleic Acids           that matched those defined in Prosite.   Res. 25: 217-221;               Wisconsin Package Program Manual, version 9, page               M51-59, Genetics Computer Group, Madison, WI.                    
     [0376] 
    
     
       
         1 
         
           
             64  
           
           
             1  
             332  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3474673CD1  
             
           
            1 

Met Tyr Arg Pro Arg Ala Arg Ala Ala Pro Glu Gly Arg Val Arg 
1               5                   10                  15 

Gly Cys Ala Val Pro Ser Thr Val Leu Leu Leu Leu Ala Tyr Leu 
                20                  25                  30 

Ala Tyr Leu Ala Leu Gly Thr Gly Val Phe Trp Thr Leu Glu Gly 
                35                  40                  45 

Arg Ala Ala Gln Asp Ser Ser Arg Ser Phe Gln Arg Asp Lys Trp 
                50                  55                  60 

Glu Leu Leu Gln Asn Phe Thr Cys Leu Asp Arg Pro Ala Leu Asp 
                65                  70                  75 

Ser Leu Ile Arg Asp Val Val Gln Ala Tyr Lys Asn Gly Ala Ser 
                80                  85                  90 

Leu Leu Ser Asn Thr Thr Ser Met Gly Arg Trp Glu Leu Val Gly 
                95                  100                 105 

Ser Phe Phe Phe Ser Val Ser Thr Ile Thr Thr Ile Gly Tyr Gly 
                110                 115                 120 

Asn Leu Ser Pro Asn Thr Met Ala Ala Arg Leu Phe Cys Ile Phe 
                125                 130                 135 

Phe Ala Leu Val Gly Ile Pro Leu Asn Leu Val Val Leu Asn Arg 
                140                 145                 150 

Leu Gly His Leu Met Gln Gln Gly Val Asn His Trp Ala Ser Arg 
                155                 160                 165 

Leu Gly Gly Thr Trp Gln Asp Pro Asp Lys Ala Arg Trp Leu Ala 
                170                 175                 180 

Gly Ser Gly Ala Leu Leu Ser Gly Leu Leu Leu Phe Leu Leu Leu 
                185                 190                 195 

Pro Pro Leu Leu Phe Ser His Met Glu Gly Trp Ser Tyr Thr Glu 
                200                 205                 210 

Gly Phe Tyr Phe Ala Phe Ile Thr Leu Ser Thr Val Gly Phe Gly 
                215                 220                 225 

Asp Tyr Val Ile Gly Met Asn Pro Ser Gln Arg Tyr Pro Leu Trp 
                230                 235                 240 

Tyr Lys Asn Met Val Ser Leu Trp Ile Leu Phe Gly Met Ala Trp 
                245                 250                 255 

Leu Ala Leu Ile Ile Lys Leu Ile Leu Ser Gln Leu Glu Thr Pro 
                260                 265                 270 

Gly Arg Val Cys Ser Cys Cys His His Ser Ser Lys Glu Asp Phe 
                275                 280                 285 

Lys Ser Gln Ser Trp Arg Gln Gly Pro Asp Arg Glu Pro Glu Ser 
                290                 295                 300 

His Ser Pro Gln Gln Gly Cys Tyr Pro Glu Gly Pro Met Gly Ile 
                305                 310                 315 

Ile Gln His Leu Glu Pro Ser Ala His Ala Ala Gly Cys Gly Lys 
                320                 325                 330 

Asp Ser 

 
           
             2  
             226  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 4588877CD1  
             
           
            2 

Met Val Glu Met Gly Trp Asp Trp Ala Asp Arg Lys Asp Met Arg 
1               5                   10                  15 

His Arg Leu Gln Ala Gly Asn Leu Glu Asn Thr Asp Gln Val Lys 
                20                  25                  30 

Ser Pro Leu Leu Thr Gly Asp Ser Ser Gly Leu Pro Pro Ala Pro 
                35                  40                  45 

Ser Ala Pro Thr His Gly Val Lys Ala Ser Gly Gly Leu Gly Thr 
                50                  55                  60 

Ile Leu His Pro Gln Asp Pro Asp Lys Ala Arg Trp Leu Ala Gly 
                65                  70                  75 

Ser Gly Ala Leu Leu Ser Gly Leu Leu Leu Phe Leu Leu Leu Pro 
                80                  85                  90 

Pro Leu Leu Phe Ser His Met Glu Gly Trp Ser Tyr Thr Glu Gly 
                95                  100                 105 

Phe Tyr Phe Ala Phe Ile Thr Leu Ser Thr Val Gly Phe Gly Asp 
                110                 115                 120 

Tyr Val Ile Gly Met Asn Pro Ser Gln Arg Tyr Pro Leu Trp Tyr 
                125                 130                 135 

Lys Asn Met Val Ser Leu Trp Ile Leu Phe Gly Met Ala Trp Leu 
                140                 145                 150 

Ala Leu Ile Ile Lys Leu Ile Leu Ser Gln Leu Glu Thr Pro Gly 
                155                 160                 165 

Arg Val Cys Ser Cys Cys His His Ser Ser Lys Glu Asp Phe Lys 
                170                 175                 180 

Ser Gln Ser Trp Arg Gln Gly Pro Asp Arg Glu Pro Glu Ser His 
                185                 190                 195 

Ser Pro Gln Gln Gly Cys Tyr Pro Glu Gly Pro Met Gly Ile Ile 
                200                 205                 210 

Gln His Leu Glu Pro Ser Ala His Ala Ala Gly Cys Gly Lys Asp 
                215                 220                 225 
Ser 

 
           
             3  
             646  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7472214CD1  
             
           
            3 

Met Ala Glu Lys Ala Leu Glu Ala Val Gly Cys Gly Leu Gly Pro 
1               5                   10                  15 

Gly Ala Val Ala Met Ala Val Thr Leu Glu Asp Gly Ala Glu Pro 
                20                  25                  30 

Pro Val Leu Thr Thr His Leu Lys Lys Val Glu Asn His Ile Thr 
                35                  40                  45 

Glu Ala Gln Arg Phe Ser His Leu Pro Lys Arg Ser Ala Val Asp 
                50                  55                  60 

Ile Glu Phe Val Glu Leu Ser Tyr Ser Val Arg Glu Gly Pro Cys 
                65                  70                  75 

Trp Arg Lys Arg Gly Tyr Lys Thr Leu Leu Lys Cys Leu Ser Gly 
                80                  85                  90 

Lys Phe Cys Arg Arg Glu Leu Ile Gly Ile Met Gly Pro Ser Gly 
                95                  100                 105 

Ala Gly Lys Ser Thr Phe Met Asn Ile Leu Ala Gly Tyr Arg Glu 
                110                 115                 120 

Ser Gly Met Lys Gly Gln Ile Leu Val Asn Gly Arg Pro Arg Glu 
                125                 130                 135 

Leu Arg Thr Phe Arg Lys Met Ser Cys Tyr Ile Met Gln Asp Asp 
                140                 145                 150 

Met Leu Leu Pro His Leu Thr Val Leu Glu Ala Met Met Val Ser 
                155                 160                 165 

Ala Asn Leu Asn Leu Thr Glu Asn Pro Asp Val Lys Asn Asp Leu 
                170                 175                 180 

Val Thr Glu Ile Leu Thr Ala Leu Gly Leu Met Ser Cys Ser His 
                185                 190                 195 

Thr Arg Thr Ala Leu Leu Ser Gly Gly Gln Arg Lys Arg Leu Ala 
                200                 205                 210 

Ile Ala Leu Glu Leu Val Asn Asn Pro Pro Val Met Phe Phe Asp 
                215                 220                 225 

Glu Pro Thr Ser Gly Leu Asp Ser Ala Ser Cys Phe Gln Val Val 
                230                 235                 240 

Ser Leu Met Lys Ser Leu Ala Gln Gly Gly Arg Thr Ile Ile Cys 
                245                 250                 255 

Thr Ile His Gln Pro Ser Ala Lys Leu Phe Glu Met Phe Asp Lys 
                260                 265                 270 

Leu Tyr Ile Leu Ser Gln Gly Gln Cys Ile Phe Lys Gly Val Val 
                275                 280                 285 

Thr Asn Leu Ile Pro Tyr Leu Lys Gly Leu Gly Leu His Cys Pro 
                290                 295                 300 

Thr Tyr His Asn Pro Ala Asp Phe Val Ile Glu Val Ala Ser Gly 
                305                 310                 315 

Glu Tyr Gly Asp Leu Asn Pro Met Leu Phe Arg Ala Val Gln Asn 
                320                 325                 330 

Gly Leu Cys Ala Met Ala Glu Lys Lys Ser Ser Pro Glu Lys Asn 
                335                 340                 345 

Glu Val Pro Ala Pro Cys Pro Pro Cys Pro Pro Glu Val Asp Pro 
                350                 355                 360 

Ile Glu Ser His Thr Phe Ala Thr Ser Thr Leu Thr Gln Phe Cys 
                365                 370                 375 

Ile Leu Phe Lys Arg Thr Phe Leu Ser Ile Leu Arg Asp Thr Val 
                380                 385                 390 

Leu Thr His Leu Arg Phe Met Ser His Val Val Ile Gly Val Leu 
                395                 400                 405 

Ile Gly Leu Leu Tyr Leu His Ile Gly Asp Asp Ala Ser Lys Val 
                410                 415                 420 

Phe Asn Asn Thr Gly Cys Leu Phe Phe Ser Met Leu Phe Leu Met 
                425                 430                 435 

Phe Ala Ala Leu Met Pro Thr Val Leu Thr Val Pro Leu Glu Met 
                440                 445                 450 

Ala Val Phe Met Arg Glu His Leu Asn Tyr Trp Tyr Ser Leu Lys 
                455                 460                 465 

Ala Tyr Tyr Leu Ala Lys Thr Met Ala Asp Val Pro Phe Gln Val 
                470                 475                 480 

Val Cys Pro Val Val Tyr Cys Ser Ile Val Tyr Trp Met Thr Gly 
                485                 490                 495 

Gln Pro Ala Glu Thr Ser Arg Phe Leu Leu Phe Ser Ala Leu Ala 
                500                 505                 510 

Thr Ala Thr Ala Leu Val Ala Gln Ser Leu Gly Leu Leu Ile Gly 
                515                 520                 525 

Ala Ala Ser Asn Ser Leu Gln Val Ala Thr Phe Val Gly Pro Val 
                530                 535                 540 

Thr Ala Ile Pro Val Leu Leu Phe Ser Gly Phe Phe Val Ser Phe 
                545                 550                 555 

Lys Thr Ile Pro Thr Tyr Leu Gln Trp Ser Ser Tyr Leu Ser Tyr 
                560                 565                 570 

Val Arg Tyr Gly Phe Glu Gly Val Ile Leu Thr Ile Tyr Gly Met 
                575                 580                 585 

Glu Arg Gly Asp Leu Thr Cys Leu Glu Glu Arg Cys Pro Phe Arg 
                590                 595                 600 

Glu Pro Gln Ser Ile Leu Arg Ala Leu Asp Val Glu Asp Ala Lys 
                605                 610                 615 

Leu Tyr Met Asp Phe Leu Val Leu Gly Ile Phe Phe Leu Ala Leu 
                620                 625                 630 

Arg Leu Leu Ala Tyr Leu Val Leu Arg Tyr Arg Val Lys Ser Glu 
                635                 640                 645 

Arg 

 
           
             4  
             1190  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7473053CD1  
             
           
            4 

Met Ala Val Cys Ala Lys Lys Arg Pro Pro Glu Glu Glu Arg Arg 
1               5                   10                  15 

Ala Arg Ala Asn Asp Arg Glu Tyr Asn Glu Lys Phe Gln Tyr Ala 
                20                  25                  30 

Ser Asn Cys Ile Lys Thr Ser Lys Tyr Asn Ile Leu Thr Phe Leu 
                35                  40                  45 

Pro Val Asn Leu Phe Glu Gln Phe Gln Glu Val Ala Asn Thr Tyr 
                50                  55                  60 

Phe Leu Phe Leu Leu Ile Leu Gln Leu Ile Pro Gln Ile Ser Ser 
                65                  70                  75 

Leu Ser Trp Phe Thr Thr Ile Val Pro Leu Val Leu Val Leu Thr 
                80                  85                  90 

Ile Thr Ala Val Lys Asp Ala Thr Asp Asp Tyr Phe Arg His Lys 
                95                  100                 105 

Ser Asp Asn Gln Val Asn Asn Arg Gln Ser Gln Val Leu Ile Asn 
                110                 115                 120 

Gly Ile Leu Gln Gln Glu Gln Trp Met Asn Val Cys Val Gly Asp 
                125                 130                 135 

Ile Ile Lys Leu Glu Asn Asn Gln Phe Val Ala Ala Asp Leu Leu 
                140                 145                 150 

Leu Leu Ser Ser Ser Glu Pro His Gly Leu Cys Tyr Ile Glu Thr 
                155                 160                 165 

Ala Glu Leu Asp Gly Glu Thr Asn Met Lys Val Arg Gln Ala Ile 
                170                 175                 180 

Pro Val Thr Ser Glu Leu Gly Asp Ile Ser Lys Leu Ala Lys Phe 
                185                 190                 195 

Asp Gly Glu Val Ile Cys Glu Pro Pro Asn Asn Lys Leu Asp Lys 
                200                 205                 210 

Phe Ser Gly Thr Leu Tyr Trp Lys Glu Asn Lys Phe Pro Leu Ser 
                215                 220                 225 

Asn Gln Asn Met Leu Leu Arg Gly Cys Val Leu Arg Asn Thr Glu 
                230                 235                 240 

Trp Cys Phe Gly Leu Val Ile Phe Ala Gly Pro Asp Thr Lys Leu 
                245                 250                 255 

Met Gln Asn Ser Gly Arg Thr Lys Phe Lys Arg Thr Ser Ile Asp 
                260                 265                 270 

Arg Leu Met Asn Thr Leu Val Leu Trp Ile Phe Gly Phe Leu Val 
                275                 280                 285 

Cys Met Gly Val Ile Leu Ala Ile Gly Asn Ala Ile Trp Glu His 
                290                 295                 300 

Glu Val Gly Met Arg Phe Gln Val Tyr Leu Pro Trp Asp Glu Ala 
                305                 310                 315 

Val Asp Ser Ala Phe Phe Ser Gly Phe Leu Ser Phe Trp Ser Tyr 
                320                 325                 330 

Ile Ile Ile Leu Asn Thr Val Val Pro Ile Ser Leu Tyr Val Ser 
                335                 340                 345 

Val Glu Val Ile Arg Leu Gly His Ser Tyr Phe Ile Asn Trp Asp 
                350                 355                 360 

Lys Lys Met Phe Cys Met Lys Lys Arg Thr Pro Ala Glu Ala Arg 
                365                 370                 375 

Thr Thr Thr Leu Asn Glu Glu Leu Gly Gln Val Glu Tyr Ile Phe 
                380                 385                 390 

Ser Asp Lys Thr Gly Thr Leu Thr Gln Asn Ile Met Val Phe Asn 
                395                 400                 405 

Lys Cys Ser Ile Asn Gly His Ser Tyr Gly Asp Val Phe Asp Val 
                410                 415                 420 

Leu Gly His Lys Ala Glu Leu Gly Glu Arg Pro Glu Pro Val Asp 
                425                 430                 435 

Phe Ser Phe Asn Pro Leu Ala Asp Lys Lys Phe Leu Phe Trp Asp 
                440                 445                 450 

Pro Ser Leu Leu Glu Ala Val Lys Ile Gly Asp Pro His Thr His 
                455                 460                 465 

Glu Phe Phe Arg Leu Leu Ser Leu Cys His Thr Val Met Ser Glu 
                470                 475                 480 

Glu Lys Asn Glu Gly Glu Leu Tyr Tyr Lys Ala Gln Ser Pro Asp 
                485                 490                 495 

Glu Gly Ala Leu Val Thr Ala Ala Arg Asn Phe Gly Phe Val Phe 
                500                 505                 510 

Arg Ser Arg Thr Pro Lys Thr Ile Thr Val His Glu Met Gly Thr 
                515                 520                 525 

Ala Ile Thr Tyr Gln Leu Leu Ala Ile Leu Asp Phe Asn Asn Ile 
                530                 535                 540 

Arg Lys Arg Met Ser Val Ile Val Arg Asn Pro Glu Gly Lys Ile 
                545                 550                 555 

Arg Leu Tyr Cys Lys Gly Ala Asp Thr Ile Leu Leu Asp Arg Leu 
                560                 565                 570 

His His Ser Thr Gln Glu Leu Leu Asn Thr Thr Met Asp His Leu 
                575                 580                 585 

Asn Glu Tyr Ala Gly Glu Gly Leu Arg Thr Leu Val Leu Ala Tyr 
                590                 595                 600 

Lys Asp Leu Asp Glu Glu Tyr Tyr Glu Glu Trp Ala Glu Arg Arg 
                605                 610                 615 

Leu Gln Ala Ser Leu Ala Gln Asp Ser Arg Glu Asp Arg Leu Ala 
                620                 625                 630 

Ser Ile Tyr Glu Glu Val Glu Asn Asn Met Met Leu Leu Gly Ala 
                635                 640                 645 

Thr Ala Ile Glu Asp Lys Leu Gln Gln Gly Val Pro Glu Thr Ile 
                650                 655                 660 

Ala Leu Leu Thr Leu Ala Asn Ile Lys Ile Trp Val Leu Thr Gly 
                665                 670                 675 

Asp Lys Gln Glu Thr Ala Val Asn Ile Gly Tyr Ser Cys Lys Met 
                680                 685                 690 

Leu Thr Asp Asp Met Thr Glu Val Phe Ile Val Thr Gly His Thr 
                695                 700                 705 

Val Leu Glu Val Arg Glu Glu Leu Arg Lys Ala Arg Glu Lys Met 
                710                 715                 720 

Met Asp Ser Ser Arg Ser Val Gly Asn Gly Phe Thr Tyr Gln Asp 
                725                 730                 735 

Lys Leu Ser Ser Ser Lys Leu Thr Ser Val Leu Glu Ala Val Ala 
                740                 745                 750 

Gly Glu Tyr Ala Leu Val Ile Asn Gly His Ser Leu Ala His Ala 
                755                 760                 765 

Leu Glu Ala Asp Met Glu Leu Glu Phe Leu Glu Thr Ala Cys Ala 
                770                 775                 780 

Cys Lys Ala Val Ile Cys Cys Arg Val Thr Pro Leu Gln Lys Ala 
                785                 790                 795 

Gln Val Val Glu Leu Val Lys Lys Tyr Lys Lys Ala Val Thr Leu 
                800                 805                 810 

Ala Ile Gly Asp Gly Ala Asn Asp Val Ser Met Ile Lys Thr Ala 
                815                 820                 825 

His Ile Gly Val Gly Ile Ser Gly Gln Glu Gly Ile Gln Ala Val 
                830                 835                 840 

Leu Ala Ser Asp Tyr Ser Phe Ser Gln Phe Lys Phe Leu Gln Arg 
                845                 850                 855 

Leu Leu Leu Val His Gly Arg Trp Ser Tyr Leu Arg Met Cys Lys 
                860                 865                 870 

Phe Leu Cys Tyr Phe Phe Tyr Lys Asn Phe Ala Phe Thr Met Val 
                875                 880                 885 

His Phe Trp Phe Gly Phe Phe Cys Gly Phe Ser Ala Gln Thr Val 
                890                 895                 900 

Tyr Asp Gln Tyr Phe Ile Thr Leu Tyr Asn Ile Val Tyr Thr Ser 
                905                 910                 915 

Leu Pro Val Leu Ala Met Gly Val Phe Asp Gln Asp Val Pro Glu 
                920                 925                 930 

Gln Arg Ser Met Glu Tyr Pro Lys Leu Tyr Glu Pro Gly Gln Leu 
                935                 940                 945 

Asn Leu Leu Phe Asn Lys Arg Glu Phe Phe Ile Cys Ile Ala Gln 
                950                 955                 960 

Gly Ile Tyr Thr Ser Val Leu Met Phe Phe Ile Pro Tyr Gly Val 
                965                 970                 975 

Phe Ala Asp Ala Thr Arg Asp Asp Gly Thr Gln Leu Ala Asp Tyr 
                980                 985                 990 

Gln Ser Phe Ala Val Thr Val Ala Thr Ser Leu Val Ile Val Val 
                995                 1000                1005 

Ser Val Gln Ile Gly Leu Asp Thr Gly Tyr Trp Thr Ala Ile Asn 
                1010                1015                1020 

His Phe Phe Ile Trp Gly Ser Leu Ala Val Tyr Phe Ala Ile Leu 
                1025                1030                1035 

Phe Ala Met His Ser Asn Gly Leu Phe Asp Met Phe Pro Asn Gln 
                1040                1045                1050 

Phe Arg Phe Val Gly Asn Ala Gln Asn Thr Leu Ala Gln Pro Thr 
                1055                1060                1065 

Val Trp Leu Thr Ile Val Leu Thr Thr Val Val Cys Ile Met Pro 
                1070                1075                1080 

Val Val Ala Phe Arg Phe Leu Arg Leu Asn Leu Lys Pro Asp Leu 
                1085                1090                1095 

Ser Asp Thr Val Arg Tyr Thr Gln Leu Val Arg Lys Lys Gln Lys 
                1100                1105                1110 

Ala Gln His Arg Cys Met Arg Arg Val Gly Arg Thr Gly Ser Arg 
                1115                1120                1125 

Arg Ser Gly Tyr Ala Phe Ser His Gln Glu Gly Phe Gly Glu Leu 
                1130                1135                1140 

Ile Met Ser Gly Lys Asn Met Arg Leu Ser Ser Leu Ala Leu Ser 
                1145                1150                1155 

Ser Phe Thr Thr Arg Ser Ser Ser Ser Trp Ile Glu Ser Leu Arg 
                1160                1165                1170 

Arg Lys Lys Ser Asp Ser Ala Ser Ser Pro Ser Gly Gly Ala Asp 
                1175                1180                1185 

Lys Pro Leu Lys Gly 
                1190 

 
           
             5  
             467  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7473347CD1  
             
           
            5 

Met Val Leu Ala Phe Gln Leu Val Ser Phe Thr Tyr Ile Trp Ile 
1               5                   10                  15 

Ile Leu Lys Pro Asn Val Cys Ala Ala Ser Asn Ile Lys Met Thr 
                20                  25                  30 

His Gln Arg Cys Ser Ser Ser Met Lys Gln Thr Cys Lys Gln Glu 
                35                  40                  45 

Thr Arg Met Lys Lys Asp Asp Ser Thr Lys Ala Arg Pro Gln Lys 
                50                  55                  60 

Tyr Glu Gln Leu Leu His Ile Glu Asp Asn Asp Phe Ala Met Arg 
                65                  70                  75 

Pro Gly Phe Gly Gly Ser Pro Val Pro Val Gly Ile Asp Val His 
                80                  85                  90 

Val Glu Ser Ile Asp Ser Ile Ser Glu Thr Asn Met Asp Phe Thr 
                95                  100                 105 

Met Thr Phe Tyr Leu Arg His Tyr Trp Lys Asp Glu Arg Leu Ser 
                110                 115                 120 

Phe Pro Ser Thr Ala Asn Lys Ser Met Thr Phe Asp His Arg Leu 
                125                 130                 135 

Thr Arg Lys Ile Trp Val Pro Asp Ile Phe Phe Val His Ser Lys 
                140                 145                 150 

Arg Ser Phe Ile His Asp Thr Thr Met Glu Asn Ile Met Leu Arg 
                155                 160                 165 

Val His Pro Asp Gly Asn Val Leu Leu Ser Leu Arg Ile Thr Val 
                170                 175                 180 

Ser Ala Met Cys Phe Met Asp Phe Ser Arg Phe Pro Leu Asp Thr 
                185                 190                 195 

Gln Asn Cys Ser Leu Glu Leu Glu Ser Tyr Ala Tyr Asn Glu Asp 
                200                 205                 210 

Asp Leu Met Leu Tyr Trp Lys His Gly Asn Lys Ser Leu Asn Thr 
                215                 220                 225 

Glu Glu His Met Ser Leu Ser Gln Phe Phe Ile Glu Asp Phe Ser 
                230                 235                 240 

Ala Ser Ser Gly Leu Ala Phe Tyr Ser Ser Thr Gly Trp Tyr Asn 
                245                 250                 255 

Arg Leu Phe Ile Ile Ser Val Leu Arg Arg His Val Phe Phe Phe 
                260                 265                 270 

Val Leu Pro Thr Tyr Tyr Pro Ala Ile Leu Met Val Met Leu Ser 
                275                 280                 285 

Trp Val Ser Phe Trp Ile Asp Arg Arg Ala Val Pro Ala Arg Val 
                290                 295                 300 

Ser Leu Gly Ile Thr Thr Val Leu Thr Met Ser Thr Ile Ile Thr 
                305                 310                 315 

Ala Val Ser Ala Ser Met Pro Gln Val Ser Tyr Leu Lys Ala Val 
                320                 325                 330 

Asp Val Tyr Leu Trp Val Ser Ser Leu Phe Val Phe Leu Ser Val 
                335                 340                 345 

Ile Glu Tyr Ala Ala Val Asn Tyr Leu Thr Thr Val Glu Glu Arg 
                350                 355                 360 

Lys Gln Phe Lys Lys Thr Gly Lys Ile Ser Arg Met Tyr Asn Ile 
                365                 370                 375 

Asp Ala Val Gln Ala Met Ala Phe Asp Gly Cys Tyr His Asp Ser 
                380                 385                 390 

Glu Ile Asp Met Asp Gln Thr Ser Leu Ser Leu Asn Ser Glu Asp 
                395                 400                 405 

Phe Met Arg Arg Lys Ser Ile Cys Ser Pro Ser Thr Asp Ser Ser 
                410                 415                 420 

Arg Ile Lys Arg Arg Lys Ser Leu Gly Gly His Val Gly Arg Ile 
                425                 430                 435 

Ile Leu Glu Asn Asn His Val Ile Asp Thr Tyr Ser Arg Ile Leu 
                440                 445                 450 

Phe Pro Ile Val Tyr Ile Leu Phe Asn Leu Phe Tyr Trp Gly Val 
                455                 460                 465 

Tyr Val 

 
           
             6  
             1196  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7474240CD1  
             
           
            6 

Met Pro Val Arg Arg Gly His Val Ala Pro Gln Asn Thr Phe Leu 
1               5                   10                  15 

Gly Thr Ile Ile Arg Lys Phe Glu Gly Gln Asn Lys Lys Phe Ile 
                20                  25                  30 

Ile Ala Asn Ala Arg Val Gln Asn Cys Ala Ile Ile Tyr Cys Asn 
                35                  40                  45 

Asp Gly Phe Cys Glu Met Thr Gly Phe Ser Arg Pro Asp Val Met 
                50                  55                  60 

Gln Lys Pro Cys Thr Cys Asp Phe Leu His Gly Pro Glu Thr Lys 
                65                  70                  75 

Arg His Asp Ile Ala Gln Ile Ala Gln Ala Leu Leu Gly Ser Glu 
                80                  85                  90 

Glu Arg Lys Val Glu Val Thr Tyr Tyr His Lys Asn Gly Ser Thr 
                95                  100                 105 

Phe Ile Cys Asn Thr His Ile Ile Pro Val Lys Asn Gln Glu Gly 
                110                 115                 120 

Val Ala Met Met Phe Ile Ile Asn Phe Glu Tyr Val Thr Asp Asn 
                125                 130                 135 

Glu Asn Ala Ala Thr Pro Glu Arg Val Asn Pro Ile Leu Pro Ile 
                140                 145                 150 

Lys Thr Val Asn Arg Lys Phe Phe Gly Phe Lys Phe Pro Gly Leu 
                155                 160                 165 

Arg Val Leu Thr Tyr Arg Lys Gln Ser Leu Pro Gln Glu Asp Pro 
                170                 175                 180 

Asp Val Val Val Ile Asp Ser Ser Lys His Ser Asp Asp Ser Val 
                185                 190                 195 

Ala Met Lys His Phe Lys Ser Pro Thr Lys Glu Ser Cys Ser Pro 
                200                 205                 210 

Ser Glu Ala Asp Asp Thr Lys Ala Leu Ile Gln Pro Ser Lys Cys 
                215                 220                 225 

Ser Pro Leu Val Asn Ile Ser Gly Pro Leu Asp His Ser Ser Pro 
                230                 235                 240 

Lys Arg Gln Trp Asp Arg Leu Tyr Pro Asp Met Leu Gln Ser Ser 
                245                 250                 255 

Ser Gln Leu Ser His Ser Arg Ser Arg Glu Ser Leu Cys Ser Ile 
                260                 265                 270 

Arg Arg Ala Ser Ser Val His Asp Ile Glu Gly Phe Gly Val His 
                275                 280                 285 

Pro Lys Asn Ile Phe Arg Asp Arg His Ala Ser Glu Asp Asn Gly 
                290                 295                 300 

Arg Asn Val Lys Gly Pro Phe Asn His Ile Lys Ser Ser Leu Leu 
                305                 310                 315 

Gly Ser Thr Ser Asp Ser Asn Leu Asn Lys Tyr Ser Thr Ile Asn 
                320                 325                 330 

Lys Ile Pro Gln Leu Thr Leu Asn Phe Ser Glu Val Lys Thr Glu 
                335                 340                 345 

Lys Lys Asn Ser Ser Pro Pro Ser Ser Asp Lys Thr Ile Ile Ala 
                350                 355                 360 

Pro Lys Val Lys Asp Arg Thr His Asn Val Thr Glu Lys Val Thr 
                365                 370                 375 

Gln Val Leu Ser Leu Gly Ala Asp Val Leu Pro Glu Tyr Lys Leu 
                380                 385                 390 

Gln Thr Pro Arg Ile Asn Lys Phe Thr Ile Leu His Tyr Ser Pro 
                395                 400                 405 

Phe Lys Ala Val Trp Asp Trp Leu Ile Leu Leu Leu Val Ile Tyr 
                410                 415                 420 

Thr Ala Ile Phe Thr Pro Tyr Ser Ala Ala Phe Leu Leu Asn Asp 
                425                 430                 435 

Arg Glu Glu Gln Lys Arg Arg Glu Cys Gly Tyr Ser Cys Ser Pro 
                440                 445                 450 

Leu Asn Val Val Asp Leu Ile Val Asp Ile Met Phe Ile Ile Asp 
                455                 460                 465 

Ile Leu Ile Asn Phe Arg Thr Thr Tyr Val Asn Gln Asn Glu Glu 
                470                 475                 480 

Val Val Ser Asp Pro Ala Lys Ile Ala Ile His Tyr Phe Lys Gly 
                485                 490                 495 

Trp Phe Leu Ile Asp Met Val Ala Ala Ile Pro Phe Asp Leu Leu 
                500                 505                 510 

Ile Phe Gly Ser Gly Ser Asp Glu Thr Thr Thr Leu Ile Gly Leu 
                515                 520                 525 

Leu Lys Thr Ala Arg Leu Leu Arg Leu Val Arg Val Ala Arg Lys 
                530                 535                 540 

Leu Asp Arg Tyr Ser Glu Tyr Gly Ala Ala Val Leu Met Leu Leu 
                545                 550                 555 

Met Cys Ile Phe Ala Leu Ile Ala His Trp Leu Ala Cys Ile Trp 
                560                 565                 570 

Tyr Ala Ile Gly Asn Val Glu Arg Pro Tyr Leu Thr Asp Lys Ile 
                575                 580                 585 

Gly Trp Leu Asp Ser Leu Gly Gln Gln Ile Gly Lys Arg Tyr Asn 
                590                 595                 600 

Asp Ser Asp Ser Ser Ser Gly Pro Ser Ile Lys Asp Lys Tyr Val 
                605                 610                 615 

Thr Ala Leu Tyr Phe Thr Phe Ser Ser Leu Thr Ser Val Gly Phe 
                620                 625                 630 

Gly Asn Val Ser Pro Asn Thr Asn Ser Glu Lys Ile Phe Ser Ile 
                635                 640                 645 

Cys Val Met Leu Ile Gly Ser Leu Met Tyr Ala Ser Ile Phe Gly 
                650                 655                 660 

Asn Val Ser Ala Ile Ile Gln Arg Leu Tyr Ser Gly Thr Ala Arg 
                665                 670                 675 

Tyr His Met Gln Met Leu Arg Val Lys Glu Phe Ile Arg Phe His 
                680                 685                 690 

Gln Ile Pro Asn Pro Leu Arg Gln Arg Leu Glu Glu Tyr Phe Gln 
                695                 700                 705 

His Ala Trp Thr Tyr Thr Asn Gly Ile Asp Met Asn Met Val Leu 
                710                 715                 720 

Lys Gly Phe Pro Glu Cys Leu Gln Ala Asp Ile Cys Leu His Leu 
                725                 730                 735 

Asn Gln Thr Leu Leu Gln Asn Cys Lys Ala Phe Arg Gly Ala Ser 
                740                 745                 750 

Lys Gly Cys Leu Arg Ala Leu Ala Met Lys Phe Lys Thr Thr His 
                755                 760                 765 

Ala Pro Pro Gly Asp Thr Leu Val His Cys Gly Asp Val Leu Thr 
                770                 775                 780 

Ala Leu Tyr Phe Leu Ser Arg Gly Ser Ile Glu Ile Leu Lys Asp 
                785                 790                 795 

Asp Ile Val Val Ala Ile Leu Gly Lys Asn Asp Ile Phe Gly Glu 
                800                 805                 810 

Met Val His Leu Tyr Ala Lys Pro Gly Lys Ser Asn Ala Asp Val 
                815                 820                 825 

Arg Ala Leu Thr Tyr Cys Asp Leu His Lys Ile Gln Arg Glu Asp 
                830                 835                 840 

Leu Leu Glu Val Leu Asp Met Tyr Pro Glu Phe Ser Asp His Phe 
                845                 850                 855 

Leu Thr Asn Leu Glu Leu Thr Phe Asn Leu Arg His Glu Ser Ala 
                860                 865                 870 

Lys Ala Asp Leu Leu Arg Ser Gln Ser Met Asn Asp Ser Glu Gly 
                875                 880                 885 

Asp Asn Cys Lys Leu Arg Arg Arg Lys Leu Ser Phe Glu Ser Glu 
                890                 895                 900 

Gly Glu Lys Glu Asn Ser Thr Asn Asp Pro Glu Asp Ser Ala Asp 
                905                 910                 915 

Thr Ile Arg His Tyr Gln Ser Ser Lys Arg His Phe Glu Glu Lys 
                920                 925                 930 

Lys Ser Arg Ser Ser Ser Phe Ile Ser Ser Ile Asp Asp Glu Gln 
                935                 940                 945 

Lys Pro Leu Phe Ser Gly Ile Val Asp Ser Ser Pro Gly Ile Gly 
                950                 955                 960 

Lys Ala Ser Gly Leu Asp Phe Glu Glu Thr Val Pro Thr Ser Gly 
                965                 970                 975 

Arg Met His Ile Asp Lys Arg Ser His Ser Cys Lys Asp Ile Thr 
                980                 985                 990 

Asp Met Arg Ser Trp Glu Arg Glu Asn Ala His Pro Gln Pro Glu 
                995                 1000                1005 

Asp Ser Ser Pro Ser Ala Leu Gln Arg Ala Ala Trp Gly Ile Ser 
                1010                1015                1020 

Glu Thr Glu Ser Asp Leu Thr Tyr Gly Glu Val Glu Gln Arg Leu 
                1025                1030                1035 

Asp Leu Leu Gln Glu Gln Leu Asn Arg Leu Glu Ser Gln Met Thr 
                1040                1045                1050 

Thr Asp Ile Gln Thr Ile Leu Gln Leu Leu Gln Lys Gln Thr Thr 
                1055                1060                1065 

Val Val Pro Pro Ala Tyr Ser Met Val Thr Ala Gly Ser Glu Tyr 
                1070                1075                1080 

Gln Arg Pro Ile Ile Gln Leu Met Arg Thr Ser Gln Pro Glu Ala 
                1085                1090                1095 

Ser Ile Lys Thr Asp Arg Ser Phe Ser Pro Ser Ser Gln Cys Pro 
                1100                1105                1110 

Glu Phe Leu Asp Leu Glu Lys Ser Lys Leu Lys Ser Lys Glu Ser 
                1115                1120                1125 

Leu Ser Ser Gly Val His Leu Asn Thr Ala Ser Glu Asp Asn Leu 
                1130                1135                1140 

Thr Ser Leu Leu Lys Gln Asp Ser Asp Leu Ser Leu Glu Leu His 
                1145                1150                1155 

Leu Arg Gln Arg Lys Thr Tyr Val His Pro Ile Arg His Pro Ser 
                1160                1165                1170 

Leu Pro Asp Ser Ser Leu Ser Thr Val Gly Ile Val Gly Leu His 
                1175                1180                1185 

Arg His Val Ser Asp Pro Gly Leu Pro Gly Lys 
                1190                1195 

 
           
             7  
             512  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7475338CD1  
             
           
            7 

Met Glu Asn Lys Glu Ala Gly Thr Pro Pro Pro Ile Pro Ser Arg 
1               5                   10                  15 

Glu Gly Arg Leu Gln Pro Thr Leu Leu Leu Ala Thr Leu Ser Ala 
                20                  25                  30 

Ala Phe Gly Ser Ala Phe Gln Tyr Gly Tyr Asn Leu Ser Val Val 
                35                  40                  45 

Asn Thr Pro His Lys Val Phe Lys Ser Phe Tyr Asn Glu Thr Tyr 
                50                  55                  60 

Phe Glu Arg His Ala Thr Phe Met Asp Gly Lys Leu Met Leu Leu 
                65                  70                  75 

Leu Trp Ser Cys Thr Val Ser Met Phe Pro Leu Gly Gly Leu Leu 
                80                  85                  90 

Gly Ser Leu Leu Val Gly Leu Leu Val Asp Ser Cys Gly Arg Lys 
                95                  100                 105 

Gly Thr Leu Leu Ile Asn Asn Ile Phe Ala Ile Ile Pro Ala Ile 
                110                 115                 120 

Leu Met Gly Val Ser Lys Val Ala Lys Ala Phe Glu Leu Ile Val 
                125                 130                 135 

Phe Ser Arg Val Val Leu Gly Val Cys Ala Gly Ile Ser Tyr Ser 
                140                 145                 150 

Ala Leu Pro Met Tyr Leu Gly Glu Leu Ala Pro Lys Asn Leu Arg 
                155                 160                 165 

Gly Met Val Gly Thr Met Thr Glu Val Phe Val Ile Val Gly Val 
                170                 175                 180 

Phe Leu Ala Gln Ile Phe Ser Leu Gln Ala Ile Leu Gly Asn Pro 
                185                 190                 195 

Ala Gly Trp Pro Val Leu Leu Ala Leu Thr Gly Val Pro Ala Leu 
                200                 205                 210 

Leu Gln Leu Leu Thr Leu Pro Phe Phe Pro Glu Ser Pro Arg Tyr 
                215                 220                 225 

Ser Leu Ile Gln Lys Gly Asp Glu Ala Thr Ala Arg Gln Ala Leu 
                230                 235                 240 

Arg Arg Leu Arg Gly His Thr Asp Met Glu Ala Glu Leu Glu Asp 
                245                 250                 255 

Met Arg Ala Glu Ala Arg Ala Glu Arg Ala Glu Gly His Leu Ser 
                260                 265                 270 

Val Leu His Leu Cys Ala Leu Arg Ser Leu Arg Trp Gln Leu Leu 
                275                 280                 285 

Ser Ile Ile Val Leu Met Ala Gly Gln Gln Leu Ser Gly Ile Asn 
                290                 295                 300 

Ala Ile Asn Tyr Tyr Ala Asp Thr Ile Tyr Thr Ser Ala Gly Val 
                305                 310                 315 

Glu Ala Ala His Ser Gln Tyr Val Thr Val Gly Ser Gly Val Val 
                320                 325                 330 

Asn Ile Val Met Thr Ile Thr Ser Ala Val Leu Val Glu Arg Leu 
                335                 340                 345 

Gly Arg Arg His Leu Leu Leu Ala Gly Tyr Gly Ile Cys Gly Ser 
                350                 355                 360 

Ala Cys Leu Val Leu Thr Val Val Leu Leu Phe Gln Asn Arg Val 
                365                 370                 375 

Pro Glu Leu Ser Tyr Leu Gly Ile Ile Cys Val Phe Ala Tyr Ile 
                380                 385                 390 

Ala Gly His Ser Ile Gly Pro Ser Pro Val Pro Ser Val Val Arg 
                395                 400                 405 

Thr Glu Ile Phe Leu Gln Ser Ser Arg Arg Ala Ala Phe Met Val 
                410                 415                 420 

Asp Gly Ala Val His Trp Leu Thr Asn Phe Ile Ile Gly Phe Leu 
                425                 430                 435 

Phe Pro Ser Ile Gln Glu Ala Ile Gly Ala Tyr Ser Phe Ile Ile 
                440                 445                 450 

Phe Ala Gly Ile Cys Leu Leu Thr Ala Ile Tyr Ile Tyr Val Val 
                455                 460                 465 

Ile Pro Glu Thr Lys Gly Lys Thr Phe Val Glu Ile Asn Arg Ile 
                470                 475                 480 

Phe Ala Lys Arg Asn Arg Val Lys Leu Pro Glu Glu Lys Glu Glu 
                485                 490                 495 

Thr Ile Asp Ala Gly Pro Pro Thr Ala Ser Pro Ala Lys Glu Thr 
                500                 505                 510 

Ser Phe 

 
           
             8  
             568  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7476747CD1  
             
           
            8 

Met Thr Ala Ser Thr Pro Glu Ala Thr Pro Asn Met Glu Leu Lys 
1               5                   10                  15 

Ala Pro Ala Ala Gly Gly Leu Asn Ala Gly Pro Val Pro Pro Ala 
                20                  25                  30 

Ala Met Ser Thr Gln Arg Leu Arg Asn Glu Asp Tyr His Asp Tyr 
                35                  40                  45 

Ser Ser Thr Asp Val Ser Pro Glu Glu Ser Pro Ser Glu Gly Leu 
                50                  55                  60 

Asn Asn Leu Ser Ser Pro Gly Ser Tyr Gln Arg Phe Gly Gln Ser 
                65                  70                  75 

Asn Ser Thr Thr Trp Phe Gln Thr Leu Ile His Leu Leu Lys Gly 
                80                  85                  90 

Asn Ile Gly Thr Gly Leu Leu Gly Leu Pro Leu Ala Val Lys Asn 
                95                  100                 105 

Ala Gly Ile Val Met Gly Pro Ile Ser Leu Leu Ile Ile Gly Ile 
                110                 115                 120 

Val Ala Val His Cys Met Gly Ile Leu Val Lys Cys Ala His His 
                125                 130                 135 

Phe Cys Arg Arg Leu Asn Lys Ser Phe Val Asp Tyr Gly Asp Thr 
                140                 145                 150 

Val Met Tyr Gly Leu Glu Ser Ser Pro Cys Ser Trp Leu Arg Asn 
                155                 160                 165 

His Ala His Trp Gly Arg Arg Val Val Asp Phe Phe Leu Ile Val 
                170                 175                 180 

Thr Gln Leu Gly Phe Cys Cys Val Tyr Phe Val Phe Leu Ala Asp 
                185                 190                 195 

Asn Phe Lys Gln Val Ile Glu Ala Ala Asn Gly Thr Thr Asn Asn 
                200                 205                 210 

Cys His Asn Asn Glu Thr Val Ile Leu Thr Pro Thr Met Asp Ser 
                215                 220                 225 

Arg Leu Tyr Met Leu Ser Phe Leu Pro Phe Leu Val Leu Leu Val 
                230                 235                 240 

Phe Ile Arg Asn Leu Arg Ala Leu Ser Ile Phe Ser Leu Leu Ala 
                245                 250                 255 

Asn Ile Thr Met Leu Val Ser Leu Val Met Ile Tyr Gln Phe Ile 
                260                 265                 270 

Val Gln Arg Ile Pro Asp Pro Ser His Leu Pro Leu Val Ala Pro 
                275                 280                 285 

Trp Lys Thr Tyr Pro Leu Phe Phe Gly Thr Ala Ile Phe Ser Phe 
                290                 295                 300 

Glu Gly Ile Gly Met Val Leu Pro Leu Glu Asn Lys Met Lys Asp 
                305                 310                 315 

Pro Arg Lys Phe Pro Leu Ile Leu Tyr Leu Gly Met Val Ile Val 
                320                 325                 330 

Thr Ile Leu Tyr Ile Ser Leu Gly Cys Leu Gly Tyr Leu Gln Phe 
                335                 340                 345 

Gly Ala Asn Ile Gln Gly Ser Ile Thr Leu Asn Leu Pro Asn Cys 
                350                 355                 360 

Trp Leu Tyr Gln Ser Val Lys Leu Leu Tyr Ser Ile Gly Ile Phe 
                365                 370                 375 

Phe Thr Tyr Ala Leu Gln Phe Tyr Val Pro Ala Glu Ile Ile Ile 
                380                 385                 390 

Pro Phe Phe Val Ser Arg Ala Pro Glu Pro Cys Glu Leu Val Val 
                395                 400                 405 

Asp Leu Phe Val Arg Pro Val Leu Val Cys Leu Thr Ser Leu Ser 
                410                 415                 420 

Gly Ser Val Asp Asn Gly Trp Tyr Gly Thr Glu Ala Asp Gly Thr 
                425                 430                 435 

Ser Cys Gly Ser Ala Pro Leu Val Phe Val Ser Ser Ser Phe Leu 
                440                 445                 450 

Ala His Pro Trp Leu Ser Phe Arg Cys Glu Ser Gln Trp Val Ser 
                455                 460                 465 

Cys His Arg Asp Thr Val Val Val Trp Gly Phe Ala Arg Gly Ile 
                470                 475                 480 

Leu Ala Ile Leu Ile Pro Arg Leu Asp Leu Val Ile Ser Leu Val 
                485                 490                 495 

Gly Ser Val Ser Ser Ser Ala Leu Ala Leu Ile Ile Pro Pro Leu 
                500                 505                 510 

Leu Glu Val Thr Thr Phe Tyr Ser Glu Gly Met Ser Pro Leu Thr 
                515                 520                 525 

Ile Phe Lys Asp Ala Leu Ile Ser Ile Leu Gly Phe Val Gly Phe 
                530                 535                 540 

Val Val Gly Thr Tyr Glu Ala Leu Tyr Glu Leu Ile Gln Pro Ser 
                545                 550                 555 

Asn Ala Pro Ile Phe Ile Asn Ser Thr Cys Ala Phe Ile 
                560                 565 

 
           
             9  
             958  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477898CD1  
             
           
            9 

Met Pro Val Arg Arg Gly His Val Ala Pro Gln Asn Thr Tyr Leu 
1               5                   10                  15 

Asp Thr Ile Ile Arg Lys Phe Glu Gly Gln Ser Arg Lys Phe Leu 
                20                  25                  30 

Ile Ala Asn Ala Gln Met Glu Asn Cys Ala Ile Ile Tyr Cys Asn 
                35                  40                  45 

Asp Gly Phe Cys Glu Leu Phe Gly Tyr Ser Arg Val Glu Val Met 
                50                  55                  60 

Gln Gln Pro Cys Thr Cys Asp Phe Leu Thr Gly Pro Asn Thr Pro 
                65                  70                  75 

Ser Ser Ala Val Ser Arg Leu Ala Gln Ala Leu Leu Gly Ala Glu 
                80                  85                  90 

Glu Cys Lys Val Asp Ile Leu Tyr Tyr Arg Lys Asp Ala Ser Ser 
                95                  100                 105 

Phe Arg Cys Leu Val Asp Val Val Pro Val Lys Asn Glu Asp Gly 
                110                 115                 120 

Ala Val Ile Met Phe Ile Leu Asn Phe Glu Asp Leu Ala Gln Leu 
                125                 130                 135 

Leu Ala Lys Cys Ser Ser Arg Ser Leu Ser Gln Arg Leu Leu Ser 
                140                 145                 150 

Gln Ser Phe Leu Gly Ser Glu Gly Ser His Gly Arg Pro Gly Gly 
                155                 160                 165 

Pro Gly Pro Gly Thr Gly Arg Gly Lys Tyr Arg Thr Ile Ser Gln 
                170                 175                 180 

Ile Pro Gln Phe Thr Leu Asn Phe Val Glu Phe Asn Leu Glu Lys 
                185                 190                 195 

His Arg Ser Ser Ser Thr Thr Glu Ile Glu Ile Ile Ala Pro His 
                200                 205                 210 

Lys Val Val Glu Arg Thr Gln Asn Val Thr Glu Lys Val Thr Gln 
                215                 220                 225 

Val Leu Ser Leu Gly Ala Asp Val Leu Pro Glu Tyr Lys Leu Gln 
                230                 235                 240 

Ala Pro Arg Ile His Arg Trp Thr Ile Leu His Tyr Ser Pro Phe 
                245                 250                 255 

Lys Ala Val Trp Asp Trp Leu Ile Leu Leu Leu Val Ile Tyr Thr 
                260                 265                 270 

Ala Val Phe Thr Pro Tyr Ser Ala Ala Phe Leu Leu Ser Asp Gln 
                275                 280                 285 

Asp Glu Ser Arg Arg Gly Ala Cys Ser Tyr Thr Cys Ser Pro Leu 
                290                 295                 300 

Thr Val Val Asp Leu Ile Val Asp Ile Met Phe Val Val Asp Ile 
                305                 310                 315 

Val Ile Asn Phe Arg Thr Thr Tyr Val Asn Thr Asn Asp Glu Val 
                320                 325                 330 

Val Ser His Pro Arg Arg Ile Ala Val His Tyr Phe Lys Gly Trp 
                335                 340                 345 

Phe Leu Ile Asp Met Val Ala Ala Ile Pro Phe Asp Leu Leu Ile 
                350                 355                 360 

Phe Arg Thr Gly Ser Asp Glu Thr Thr Thr Leu Ile Gly Leu Leu 
                365                 370                 375 

Lys Thr Ala Arg Leu Leu Arg Leu Val Arg Val Ala Arg Lys Leu 
                380                 385                 390 

Asp Arg Tyr Ser Glu Tyr Gly Ala Ala Val Leu Phe Leu Leu Met 
                395                 400                 405 

Cys Thr Phe Pro Leu Ile Ala His Trp Leu Ala Cys Ile Trp Tyr 
                410                 415                 420 

Ala Ile Gly Asn Val Glu Arg Pro Tyr Leu Glu His Lys Ile Gly 
                425                 430                 435 

Trp Leu Asp Ser Leu Gly Val Gln Leu Gly Lys Arg Tyr Asn Gly 
                440                 445                 450 

Ser Asp Pro Ala Ser Gly Pro Ser Val Gln Asp Lys Tyr Val Thr 
                455                 460                 465 

Ala Leu Tyr Phe Thr Phe Ser Ser Leu Thr Ser Val Gly Phe Gly 
                470                 475                 480 

Asn Val Ser Pro Asn Thr Asn Ser Glu Lys Val Phe Ser Ile Cys 
                485                 490                 495 

Val Met Leu Ile Gly Ser Leu Met Tyr Ala Ser Ile Phe Gly Asn 
                500                 505                 510 

Val Ser Ala Ile Ile Gln Arg Leu Tyr Ser Gly Thr Ala Arg Tyr 
                515                 520                 525 

His Thr Gln Met Leu Arg Val Lys Glu Phe Ile Arg Phe His Gln 
                530                 535                 540 

Ile Pro Asn Pro Leu Arg Gln Arg Leu Glu Glu Tyr Phe Gln His 
                545                 550                 555 

Ala Trp Ser Tyr Thr Asn Gly Ile Asp Met Asn Ala Val Leu Lys 
                560                 565                 570 

Gly Phe Pro Glu Cys Leu Gln Ala Asp Ile Cys Leu His Leu His 
                575                 580                 585 

Arg Ala Leu Leu Gln His Cys Pro Ala Phe Ser Gly Ala Gly Lys 
                590                 595                 600 

Gly Cys Leu Arg Ala Leu Ala Val Lys Phe Lys Thr Thr His Ala 
                605                 610                 615 

Pro Pro Gly Asp Thr Leu Val His Leu Gly Asp Val Leu Ser Thr 
                620                 625                 630 

Leu Tyr Phe Ile Ser Arg Gly Ser Ile Glu Ile Leu Arg Asp Asp 
                635                 640                 645 

Val Val Val Ala Ile Leu Gly Lys Asn Asp Ile Phe Gly Glu Pro 
                650                 655                 660 

Val Ser Leu His Ala Gln Pro Gly Lys Ser Ser Ala Asp Val Arg 
                665                 670                 675 

Ala Leu Thr Tyr Cys Asp Leu His Lys Ile Gln Arg Ala Asp Leu 
                680                 685                 690 

Leu Glu Val Leu Asp Met Tyr Pro Ala Phe Ala Glu Ser Phe Trp 
                695                 700                 705 

Ser Lys Leu Glu Val Thr Phe Asn Leu Arg Asp Val Thr Gly Gly 
                710                 715                 720 

Leu His Ser Ser Pro Arg Gln Ala Pro Gly Ser Gln Asp His Gln 
                725                 730                 735 

Gly Phe Phe Leu Ser Asp Asn Gln Ser Asp Ala Ala Pro Pro Leu 
                740                 745                 750 

Ser Ile Ser Asp Ala Phe Trp Leu Trp Pro Glu Leu Leu Gln Glu 
                755                 760                 765 

Met Pro Pro Lys His Ser Pro Gln Ser Pro Gln Glu Asp Pro Asp 
                770                 775                 780 

Cys Trp Pro Leu Lys Leu Gly Ser Arg Leu Glu Gln Leu Gln Ala 
                785                 790                 795 

Gln Met Asn Arg Leu Glu Ser Arg Val Ser Ser Asp Leu Ser Arg 
                800                 805                 810 

Ile Leu Gln Leu Leu Gln Lys Pro Met Pro Gln Gly His Ala Ser 
                815                 820                 825 

Tyr Ile Leu Glu Ala Pro Ala Ser Asn Asp Leu Ala Leu Val Pro 
                830                 835                 840 

Ile Ala Ser Glu Thr Thr Ser Pro Gly Pro Arg Leu Pro Gln Gly 
                845                 850                 855 

Phe Leu Pro Pro Ala Gln Thr Pro Ser Tyr Gly Asp Leu Asp Asp 
                860                 865                 870 

Cys Ser Pro Lys His Arg Asn Ser Ser Pro Arg Met Pro His Leu 
                875                 880                 885 

Ala Val Ala Met Asp Lys Thr Leu Ala Pro Ser Ser Glu Gln Glu 
                890                 895                 900 

Gln Pro Glu Gly Leu Trp Pro Pro Leu Ala Ser Pro Leu His Pro 
                905                 910                 915 

Leu Glu Val Gln Gly Leu Ile Cys Gly Pro Cys Phe Ser Ser Leu 
                920                 925                 930 

Pro Glu His Leu Gly Ser Val Pro Lys Gln Leu Asp Phe Gln Arg 
                935                 940                 945 

His Gly Ser Asp Pro Gly Phe Ala Gly Ser Trp Gly His 
                950                 955 

 
           
             10  
             724  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7472728CD1  
             
           
            10 

Met Gly His Gln Gly Pro Phe Glu Glu Gly Asn Gly Gly Leu Arg 
1               5                   10                  15 

Val Ile Ala Thr Trp Arg Arg Lys Glu Ala Trp Arg Arg Asp Cys 
                20                  25                  30 

Leu Leu Gly Ala Leu Pro Ser Val Ser Cys Gly Gly Trp Gly His 
                35                  40                  45 

Arg Gly Arg Gln Thr Tyr Gly Arg Ala Cys Gly Val Lys Glu Lys 
                50                  55                  60 

Pro Phe Ser Leu Leu Gly Pro Gln Ile Thr Val Tyr Ala Val Trp 
                65                  70                  75 

Pro Gln Ser Glu Gly Pro Gln Glu Gly Arg Leu Arg Val Asn Ser 
                80                  85                  90 

Ala Cys Leu Pro Pro Glu Arg Gly Leu Thr Asn Ala Cys Thr Asn 
                95                  100                 105 

His Glu Glu Leu Ser Leu Asp Cys Leu Leu Phe Glu Asn Val Asn 
                110                 115                 120 

Thr Leu Thr Leu Asp Phe Cys Leu Trp Glu Lys Thr Thr Ile Val 
                125                 130                 135 

Pro Gly Val Leu Pro Tyr Ala Gly Leu Thr Leu Gln Ser Lys Phe 
                140                 145                 150 

Leu Leu Gly Arg Ala Leu Leu Ala Gly Val His Val Ile Thr Leu 
                155                 160                 165 

Thr Pro Glu Arg Val Thr His His Val His Gly Trp Tyr Met Glu 
                170                 175                 180 

Asp Gly Phe Lys Gly Asp Arg Thr Glu Gly Cys Arg Ser Asp Ser 
                185                 190                 195 

Val Ala Val Pro Ala Ala Ala Pro Val Cys Gln Pro Lys Ser Ala 
                200                 205                 210 

Thr Asn Gly Gln Pro Pro Ala Pro Ala Pro Thr Pro Thr Pro Arg 
                215                 220                 225 

Leu Ser Ile Ser Ser Arg Ala Thr Val Val Ala Arg Met Glu Gly 
                230                 235                 240 

Thr Ser Gln Gly Gly Leu Gln Thr Val Met Lys Trp Lys Thr Val 
                245                 250                 255 

Val Ala Ile Phe Val Val Val Val Val Tyr Leu Val Thr Gly Gly 
                260                 265                 270 

Leu Val Phe Arg Ala Leu Glu Gln Pro Phe Glu Ser Ser Gln Lys 
                275                 280                 285 

Asn Thr Ile Ala Leu Glu Lys Ala Glu Phe Leu Arg Asp His Val 
                290                 295                 300 

Cys Val Ser Pro Gln Glu Leu Glu Thr Leu Ile Gln His Ala Leu 
                305                 310                 315 

Asp Ala Asp Asn Ala Gly Val Ser Pro Ile Gly Asn Ser Ser Asn 
                320                 325                 330 

Asn Ser Ser His Trp Asp Leu Gly Ser Ala Phe Phe Phe Ala Gly 
                335                 340                 345 

Thr Val Ile Thr Thr Met Tyr Gly Asn Ile Ala Pro Ser Thr Glu 
                350                 355                 360 

Gly Gly Lys Ile Phe Cys Ile Leu Tyr Ala Ile Phe Gly Ile Pro 
                365                 370                 375 

Leu Phe Gly Phe Leu Leu Ala Gly Ile Gly Asp Gln Leu Gly Thr 
                380                 385                 390 

Ile Phe Gly Lys Ser Ile Ala Arg Val Glu Lys Val Phe Arg Lys 
                395                 400                 405 

Lys Gln Val Ser Gln Thr Lys Ile Arg Val Ile Ser Thr Ile Leu 
                410                 415                 420 

Phe Ile Leu Ala Gly Cys Ile Val Phe Val Thr Ile Pro Ala Val 
                425                 430                 435 

Ile Phe Lys Tyr Ile Glu Gly Trp Thr Ala Leu Glu Ser Ile Tyr 
                440                 445                 450 

Phe Val Val Val Thr Leu Thr Thr Val Gly Phe Gly Asp Phe Val 
                455                 460                 465 

Ala Val Val Val Phe Arg Gly Asn Ala Gly Ile Asn Tyr Arg Glu 
                470                 475                 480 

Trp Tyr Lys Pro Leu Val Trp Phe Trp Ile Leu Val Gly Leu Ala 
                485                 490                 495 

Tyr Phe Ala Ala Val Leu Ser Met Ile Gly Asp Trp Leu Arg Val 
                500                 505                 510 

Leu Ser Lys Lys Thr Lys Glu Glu Val Gly Glu Ile Lys Ala His 
                515                 520                 525 

Ala Ala Glu Trp Lys Ala Asn Val Thr Ala Glu Phe Arg Glu Thr 
                530                 535                 540 

Arg Arg Arg Leu Ser Val Glu Ile His Asp Lys Leu Gln Arg Ala 
                545                 550                 555 

Ala Thr Ile Arg Ser Met Glu Arg Arg Arg Leu Gly Leu Asp Gln 
                560                 565                 570 

Arg Ala His Ser Leu Asp Met Leu Ser Pro Glu Lys Arg Ser Val 
                575                 580                 585 

Phe Ala Ala Leu Asp Thr Gly Arg Phe Lys Ala Ser Ser Gln Glu 
                590                 595                 600 

Ser Ile Asn Asn Arg Pro Asn Asn Leu Arg Leu Lys Gly Pro Glu 
                605                 610                 615 

Gln Leu Asn Lys His Gly Gln Gly Ala Ser Glu Asp Asn Ile Ile 
                620                 625                 630 

Asn Lys Phe Gly Ser Thr Ser Arg Leu Thr Lys Arg Lys Asn Lys 
                635                 640                 645 

Asp Leu Lys Lys Thr Leu Pro Glu Asp Val Gln Lys Ile Tyr Lys 
                650                 655                 660 

Thr Phe Arg Asn Tyr Ser Leu Asp Glu Glu Lys Lys Glu Glu Glu 
                665                 670                 675 

Thr Glu Lys Met Cys Asn Ser Asp Asn Ser Ser Thr Ala Met Leu 
                680                 685                 690 

Thr Asp Cys Ile Gln Gln His Ala Glu Leu Glu Asn Gly Met Ile 
                695                 700                 705 

Pro Thr Asp Thr Lys Asp Arg Glu Pro Glu Asn Asn Ser Leu Leu 
                710                 715                 720 

Glu Asp Arg Asn 

 
           
             11  
             470  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7474322CD1  
             
           
            11 

Met Tyr Asn Glu Ile Leu Met Leu Gly Ala Lys Leu His Pro Thr 
1               5                   10                  15 

Leu Lys Leu Glu Glu Leu Thr Asn Lys Lys Gly Met Thr Pro Leu 
                20                  25                  30 

Ala Leu Ala Ala Gly Thr Gly Lys Ile Gly Asn Arg His Asp Met 
                35                  40                  45 

Leu Leu Val Glu Pro Leu Asn Arg Leu Leu Gln Asp Lys Trp Asp 
                50                  55                  60 

Arg Phe Val Lys Arg Ile Phe Tyr Phe Asn Phe Leu Val Tyr Cys 
                65                  70                  75 

Leu Tyr Met Ile Ile Phe Thr Met Ala Ala Tyr Tyr Arg Pro Val 
                80                  85                  90 

Asp Gly Leu Pro Pro Phe Lys Met Glu Lys Thr Gly Asp Tyr Phe 
                95                  100                 105 

Arg Val Thr Gly Glu Ile Leu Ser Val Leu Gly Gly Val Tyr Phe 
                110                 115                 120 

Phe Phe Arg Gly Ile Gln Tyr Phe Leu Gln Arg Arg Pro Ser Met 
                125                 130                 135 

Lys Thr Leu Phe Val Asp Ser Tyr Ser Glu Met Leu Leu Phe Leu 
                140                 145                 150 

Gln Ser Leu Phe Met Leu Ala Thr Val Val Leu Tyr Phe Ser His 
                155                 160                 165 

Leu Lys Glu Tyr Val Ala Ser Met Val Phe Ser Leu Ala Leu Gly 
                170                 175                 180 

Trp Thr Asn Met Leu Tyr Tyr Thr Arg Gly Phe Gln Gln Met Gly 
                185                 190                 195 

Ile Tyr Ala Val Met Ile Glu Lys Met Ile Leu Arg Asp Leu Cys 
                200                 205                 210 

Arg Phe Met Phe Val Tyr Ile Val Phe Leu Phe Gly Phe Ser Thr 
                215                 220                 225 

Ala Val Val Thr Leu Ile Glu Asp Gly Lys Asn Asp Ser Leu Pro 
                230                 235                 240 

Ser Glu Ser Thr Ser His Arg Trp Arg Gly Pro Ala Xaa Arg Pro 
                245                 250                 255 

Asn Ser Ser Tyr Asn Ser Leu Tyr Ser Thr Cys Leu Glu Leu Phe 
                260                 265                 270 

Lys Phe Thr Ile Gly Met Gly Asp Leu Glu Phe Thr Glu Asn Tyr 
                275                 280                 285 

Asp Phe Lys Ala Val Phe Ile Ile Leu Leu Leu Ala Tyr Val Ile 
                290                 295                 300 

Leu Thr Tyr Ile Val Leu Leu Leu Asn Met Leu Ile Ala Leu Met 
                305                 310                 315 

Gly Glu Thr Val Glu Asn Val Ser Lys Glu Ser Glu Arg Ile Trp 
                320                 325                 330 

Arg Leu Gln Arg Ala Ile Thr Ile Leu Asp Thr Glu Lys Ser Phe 
                335                 340                 345 

Leu Lys Cys Met Arg Lys Ala Phe Arg Ser Gly Lys Leu Leu Gln 
                350                 355                 360 

Val Gly Tyr Thr Pro Asp Gly Lys Asp Asp Tyr Arg Trp Cys Phe 
                365                 370                 375 

Val Asp Glu Val Asn Trp Thr Thr Trp Asn Thr Asn Val Gly Ile 
                380                 385                 390 

Ile Asn Glu Asp Pro Gly Asn Cys Glu Gly Val Lys Arg Thr Leu 
                395                 400                 405 

Ser Phe Ser Leu Arg Ser Ser Arg Val Ser Gly Arg His Trp Lys 
                410                 415                 420 

Asn Phe Ala Leu Val Pro Leu Leu Arg Glu Ala Ser Ala Arg Asp 
                425                 430                 435 

Arg Gln Ser Ala Gln Pro Glu Glu Val Tyr Leu Arg Gln Phe Ser 
                440                 445                 450 

Gly Ser Leu Lys Pro Glu Asp Ala Glu Val Phe Lys Ser Pro Ala 
                455                 460                 465 

Ala Ser Gly Glu Lys 
                470 

 
           
             12  
             618  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 5455621CD1  
             
           
            12 

Met Glu Val Lys Asn Phe Ala Val Trp Asp Tyr Val Val Phe Ala 
1               5                   10                  15 

Ala Leu Phe Phe Ile Ser Ser Gly Ile Gly Val Phe Phe Ala Ile 
                20                  25                  30 

Lys Glu Arg Lys Lys Ala Thr Ser Arg Glu Phe Leu Val Gly Gly 
                35                  40                  45 

Arg Gln Met Ser Phe Gly Pro Val Gly Leu Ser Leu Thr Ala Ser 
                50                  55                  60 

Phe Met Ser Ala Val Thr Val Leu Gly Thr Pro Ser Glu Val Tyr 
                65                  70                  75 

Arg Phe Gly Ala Ser Phe Leu Val Phe Phe Ile Ala Tyr Leu Phe 
                80                  85                  90 

Val Ile Leu Leu Thr Ser Glu Leu Phe Leu Pro Val Phe Tyr Arg 
                95                  100                 105 

Ser Gly Ile Thr Ser Thr Tyr Glu Tyr Leu Gln Leu Arg Phe Asn 
                110                 115                 120 

Lys Pro Val Arg Tyr Ala Ala Thr Val Ile Tyr Ile Val Gln Thr 
                125                 130                 135 

Ile Leu Tyr Thr Gly Val Val Val Tyr Ala Pro Ala Leu Ala Leu 
                140                 145                 150 

Asn Gln Val Thr Gly Phe Asp Leu Trp Gly Ser Val Phe Ala Thr 
                155                 160                 165 

Gly Ile Val Cys Thr Phe Tyr Cys Thr Leu Gly Gly Leu Lys Ala 
                170                 175                 180 

Val Val Trp Thr Asp Ala Phe Gln Met Val Val Met Ile Val Gly 
                185                 190                 195 

Phe Leu Thr Val Leu Ile Gln Gly Ser Thr His Ala Gly Gly Phe 
                200                 205                 210 

His Asn Val Leu Glu Gln Ser Thr Asn Gly Ser Arg Leu His Ile 
                215                 220                 225 

Phe Asp Phe Asp Val Asp Pro Leu Arg Arg His Thr Phe Trp Thr 
                230                 235                 240 

Ile Thr Val Gly Gly Thr Phe Thr Trp Leu Gly Ile Tyr Gly Val 
                245                 250                 255 

Asn Gln Ser Thr Ile Gln Arg Cys Ile Ser Cys Lys Thr Glu Lys 
                260                 265                 270 

His Ala Lys Leu Ala Leu Tyr Phe Asn Leu Leu Gly Leu Trp Ile 
                275                 280                 285 

Ile Leu Val Cys Ala Val Phe Ser Gly Leu Ile Met Tyr Ser His 
                290                 295                 300 

Phe Lys Asp Cys Asp Pro Trp Thr Ser Gly Ile Ile Ser Ala Pro 
                305                 310                 315 

Asp Gln Leu Met Pro Tyr Phe Val Met Glu Ile Phe Ala Thr Met 
                320                 325                 330 

Pro Gly Leu Pro Gly Leu Phe Val Ala Cys Ala Phe Ser Gly Thr 
                335                 340                 345 

Leu Ser Thr Val Ala Ser Ser Ile Asn Ala Leu Ala Thr Val Thr 
                350                 355                 360 

Phe Glu Asp Phe Val Lys Ser Cys Phe Pro His Leu Ser Asp Lys 
                365                 370                 375 

Leu Ser Thr Trp Ile Ser Lys Gly Leu Cys Leu Leu Phe Gly Val 
                380                 385                 390 

Met Cys Thr Ser Met Ala Val Ala Ala Ser Val Met Gly Gly Val 
                395                 400                 405 

Val Gln Ala Ser Leu Ser Ile His Gly Met Cys Gly Gly Pro Met 
                410                 415                 420 

Leu Gly Leu Phe Ser Leu Gly Ile Val Phe Pro Phe Val Asn Trp 
                425                 430                 435 

Lys Gly Ala Leu Gly Gly Leu Leu Thr Gly Ile Thr Leu Ser Phe 
                440                 445                 450 

Trp Val Ala Ile Gly Ala Phe Ile Tyr Pro Ala Pro Ala Ser Lys 
                455                 460                 465 

Thr Trp Pro Leu Pro Leu Ser Thr Asp Gln Cys Ile Lys Ser Asn 
                470                 475                 480 

Val Thr Ala Thr Gly Pro Pro Val Leu Ser Ser Arg Pro Gly Ile 
                485                 490                 495 

Ala Asp Thr Trp Tyr Ser Ile Ser Tyr Leu Tyr Tyr Ser Ala Leu 
                500                 505                 510 

Gly Cys Leu Gly Cys Ile Val Ala Gly Val Ile Ile Ser Leu Ile 
                515                 520                 525 

Thr Gly Arg Gln Arg Gly Glu Asp Ile Gln Pro Leu Leu Ile Arg 
                530                 535                 540 

Pro Val Cys Asn Leu Phe Cys Phe Trp Ser Lys Lys Tyr Lys Thr 
                545                 550                 555 

Leu Cys Trp Cys Gly Val Gln His Asp Ser Gly Thr Glu Gln Glu 
                560                 565                 570 

Asn Leu Glu Asn Gly Ser Ala Arg Lys Gln Gly Ala Glu Ser Val 
                575                 580                 585 

Leu Gln Asn Gly Leu Arg Arg Glu Ser Leu Val His Val Pro Gly 
                590                 595                 600 

Tyr Asp Pro Lys Asp Lys Ser Tyr Asn Asn Met Ala Phe Glu Thr 
                605                 610                 615 

Thr His Phe 

 
           
             13  
             631  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477248CD1  
             
           
            13 

Met Glu Arg Gln Ser Arg Val Met Ser Glu Lys Asp Glu Tyr Gln 
1               5                   10                  15 

Phe Gln His Gln Gly Ala Val Glu Leu Leu Val Phe Asn Phe Leu 
                20                  25                  30 

Leu Ile Leu Thr Ile Leu Thr Ile Trp Leu Phe Lys Asn His Arg 
                35                  40                  45 

Phe Arg Phe Leu His Glu Thr Gly Gly Ala Met Val Tyr Gly Leu 
                50                  55                  60 

Ile Met Gly Leu Ile Leu Arg Tyr Ala Thr Ala Pro Thr Asp Ile 
                65                  70                  75 

Glu Ser Gly Thr Val Tyr Asp Cys Val Lys Leu Thr Phe Ser Pro 
                80                  85                  90 

Ser Thr Leu Leu Val Asn Ile Thr Asp Gln Val Tyr Glu Tyr Lys 
                95                  100                 105 

Tyr Lys Arg Glu Ile Ser Gln His Asn Ile Asn Pro His Gln Gly 
                110                 115                 120 

Asn Ala Ile Leu Glu Lys Met Thr Phe Asp Pro Glu Ile Phe Phe 
                125                 130                 135 

Asn Val Leu Leu Pro Pro Ile Ile Phe His Ala Gly Tyr Ser Leu 
                140                 145                 150 

Lys Lys Arg His Phe Phe Gln Asn Leu Gly Ser Ile Leu Thr Tyr 
                155                 160                 165 

Ala Phe Leu Gly Thr Ala Ile Ser Cys Ile Val Ile Gly Leu Ile 
                170                 175                 180 

Met Tyr Gly Phe Val Lys Ala Met Ile His Ala Gly Gln Leu Lys 
                185                 190                 195 

Asn Gly Asp Phe His Phe Thr Asp Cys Leu Phe Phe Gly Ser Leu 
                200                 205                 210 

Met Ser Ala Thr Asp Pro Val Thr Val Leu Ala Ile Phe His Glu 
                215                 220                 225 

Leu His Val Asp Pro Asp Leu Tyr Thr Leu Leu Phe Gly Glu Ser 
                230                 235                 240 

Val Leu Asn Asp Ala Val Ala Ile Val Leu Thr Tyr Ser Ile Ser 
                245                 250                 255 

Ile Tyr Ser Pro Lys Glu Asn Pro Asn Ala Phe Asp Ala Ala Ala 
                260                 265                 270 

Phe Phe Gln Ser Val Gly Asn Phe Leu Gly Ile Phe Ala Gly Ser 
                275                 280                 285 

Phe Ala Met Gly Ser Ala Tyr Ala Ile Ile Thr Ala Leu Leu Thr 
                290                 295                 300 

Lys Phe Thr Lys Leu Cys Glu Phe Pro Met Leu Glu Thr Gly Leu 
                305                 310                 315 

Phe Phe Leu Leu Ser Trp Ser Ala Phe Leu Ser Ala Glu Ala Ala 
                320                 325                 330 

Gly Leu Thr Gly Ile Val Ala Val Leu Phe Cys Gly Val Thr Gln 
                335                 340                 345 

Ala His Tyr Thr Tyr Asn Asn Leu Ser Ser Asp Ser Lys Ile Arg 
                350                 355                 360 

Thr Lys Gln Leu Phe Glu Phe Met Asn Phe Leu Ala Glu Asn Val 
                365                 370                 375 

Ile Phe Cys Tyr Met Gly Leu Ala Leu Phe Thr Phe Gln Asn His 
                380                 385                 390 

Ile Phe Asn Ala Leu Phe Ile Leu Gly Ala Phe Leu Ala Ile Phe 
                395                 400                 405 

Val Ala Arg Ala Cys Asn Ile Tyr Pro Leu Ser Phe Leu Leu Asn 
                410                 415                 420 

Leu Gly Arg Lys Gln Lys Ile Pro Trp Asn Phe Gln His Met Met 
                425                 430                 435 

Met Phe Ser Gly Leu Arg Gly Ala Ile Ala Phe Ala Leu Ala Ile 
                440                 445                 450 

Arg Asn Thr Glu Ser Gln Pro Lys Gln Met Met Phe Thr Thr Thr 
                455                 460                 465 

Leu Leu Leu Val Phe Phe Thr Val Trp Val Phe Gly Gly Gly Thr 
                470                 475                 480 

Thr Pro Met Leu Thr Trp Leu Gln Ile Arg Val Gly Val Asp Leu 
                485                 490                 495 

Asp Glu Asn Leu Lys Glu Asp Pro Ser Ser Gln His Gln Glu Ala 
                500                 505                 510 

Asn Asn Leu Asp Lys Asn Met Thr Lys Ala Glu Ser Ala Arg Leu 
                515                 520                 525 

Phe Arg Met Trp Tyr Ser Phe Asp His Lys Tyr Leu Lys Pro Ile 
                530                 535                 540 

Leu Thr His Ser Gly Pro Pro Leu Thr Thr Thr Leu Pro Glu Trp 
                545                 550                 555 

Cys Gly Pro Ile Ser Arg Leu Leu Thr Ser Pro Gln Ala Tyr Gly 
                560                 565                 570 

Glu Gln Leu Lys Glu Asp Asp Val Glu Cys Ile Val Asn Gln Asp 
                575                 580                 585 

Glu Leu Ala Ile Asn Tyr Gln Glu Gln Ala Ser Ser Pro Cys Ser 
                590                 595                 600 

Pro Pro Ala Arg Leu Gly Leu Asp Gln Lys Ala Ser Pro Gln Thr 
                605                 610                 615 

Pro Gly Lys Glu Asn Ile Tyr Glu Gly Asp Leu Gly Pro Gly Arg 
                620                 625                 630 

Leu 

 
           
             14  
             1256  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 2944004CD1  
             
           
            14 

Met Asp Arg Glu Glu Arg Lys Thr Ile Asn Gln Gly Gln Glu Asp 
1               5                   10                  15 

Glu Met Glu Ile Tyr Gly Tyr Asn Leu Ser Arg Trp Lys Leu Ala 
                20                  25                  30 

Ile Val Ser Leu Gly Val Ile Cys Ser Gly Gly Val Ser Pro Pro 
                35                  40                  45 

Pro Leu Tyr Trp Met Pro Glu Trp Arg Val Lys Ala Thr Cys Val 
                50                  55                  60 

Arg Ala Ala Ile Lys Asp Cys Glu Val Val Leu Leu Arg Thr Thr 
                65                  70                  75 

Asp Glu Phe Lys Met Trp Phe Cys Ala Lys Ile Arg Val Leu Ser 
                80                  85                  90 

Leu Glu Thr Tyr Pro Val Ser Ser Pro Lys Ser Met Ser Asn Lys 
                95                  100                 105 

Leu Ser Asn Gly His Ala Val Cys Leu Ile Glu Asn Pro Thr Glu 
                110                 115                 120 

Glu Asn Arg His Arg Ile Ser Lys Tyr Ser Gln Thr Glu Ser Gln 
                125                 130                 135 

Gln Ile Arg Tyr Phe Thr His His Ser Val Lys Tyr Phe Trp Asn 
                140                 145                 150 

Asp Thr Ile His Asn Phe Asp Phe Leu Lys Gly Leu Asp Glu Gly 
                155                 160                 165 

Val Ser Cys Thr Ser Ile Tyr Glu Lys His Ser Ala Gly Leu Thr 
                170                 175                 180 

Lys Gly Met His Ala Tyr Arg Lys Leu Leu Tyr Gly Val Asn Glu 
                185                 190                 195 

Ile Ala Val Lys Val Pro Ser Val Phe Lys Leu Leu Ile Lys Glu 
                200                 205                 210 

Val Leu Asn Pro Phe Tyr Ile Phe Gln Leu Phe Ser Val Ile Leu 
                215                 220                 225 

Trp Ser Thr Asp Glu Tyr Tyr Tyr Tyr Ala Leu Ala Ile Val Val 
                230                 235                 240 

Met Ser Ile Val Ser Ile Val Ser Ser Leu Tyr Ser Ile Arg Lys 
                245                 250                 255 

Gln Tyr Val Met Leu His Asp Met Val Ala Thr His Ser Thr Val 
                260                 265                 270 

Arg Val Ser Val Cys Arg Val Asn Glu Glu Ile Glu Glu Ile Phe 
                275                 280                 285 

Ser Thr Asp Leu Val Pro Gly Asp Val Met Val Ile Pro Leu Asn 
                290                 295                 300 

Gly Thr Ile Met Pro Cys Asp Ala Val Leu Ile Asn Gly Thr Cys 
                305                 310                 315 

Ile Val Asn Glu Ser Met Leu Thr Gly Glu Ser Val Pro Val Thr 
                320                 325                 330 

Lys Thr Asn Leu Pro Asn Pro Ser Val Asp Val Lys Gly Ile Gly 
                335                 340                 345 

Asp Glu Leu Tyr Asn Pro Glu Thr His Lys Arg His Thr Leu Phe 
                350                 355                 360 

Cys Gly Thr Thr Val Ile Gln Thr Arg Phe Tyr Thr Gly Glu Leu 
                365                 370                 375 

Val Lys Ala Ile Val Val Arg Thr Gly Phe Ser Thr Ser Lys Gly 
                380                 385                 390 

Gln Leu Val Arg Ser Ile Leu Tyr Pro Lys Pro Thr Asp Phe Lys 
                395                 400                 405 

Leu Tyr Arg Asp Ala Tyr Leu Phe Leu Leu Cys Leu Val Ala Val 
                410                 415                 420 

Ala Gly Ile Gly Phe Ile Tyr Thr Ile Ile Asn Ser Ile Leu Asn 
                425                 430                 435 

Glu Val Gln Val Gly Val Ile Ile Ile Glu Ser Leu Asp Ile Ile 
                440                 445                 450 

Thr Ile Thr Val Pro Pro Ala Leu Pro Ala Ala Met Thr Ala Gly 
                455                 460                 465 

Ile Val Tyr Ala Gln Arg Arg Leu Lys Lys Ile Gly Ile Phe Cys 
                470                 475                 480 

Ile Ser Pro Gln Arg Ile Asn Ile Cys Gly Gln Leu Asn Leu Val 
                485                 490                 495 

Cys Phe Asp Lys Thr Gly Thr Leu Thr Glu Asp Gly Leu Asp Leu 
                500                 505                 510 

Trp Gly Ile Gln Arg Val Glu Asn Ala Arg Phe Leu Ser Pro Glu 
                515                 520                 525 

Glu Asn Val Cys Asn Glu Met Leu Val Lys Ser Gln Phe Val Ala 
                530                 535                 540 

Cys Met Ala Thr Cys His Ser Leu Thr Lys Ile Glu Gly Val Leu 
                545                 550                 555 

Ser Gly Asp Pro Leu Asp Leu Lys Met Phe Glu Ala Ile Gly Trp 
                560                 565                 570 

Ile Leu Glu Glu Ala Thr Glu Glu Glu Thr Ala Leu His Asn Arg 
                575                 580                 585 

Ile Met Pro Thr Val Val Arg Pro Pro Lys Gln Leu Leu Pro Glu 
                590                 595                 600 

Ser Thr Pro Ala Gly Asn Gln Glu Met Glu Leu Phe Glu Leu Pro 
                605                 610                 615 

Ala Thr Tyr Glu Ile Gly Ile Val Arg Gln Phe Pro Phe Ser Ser 
                620                 625                 630 

Ala Leu Gln Arg Met Ser Val Val Ala Arg Val Leu Gly Asp Arg 
                635                 640                 645 

Lys Met Asp Ala Tyr Met Lys Gly Ala Pro Glu Ala Ile Ala Gly 
                650                 655                 660 

Leu Cys Lys Pro Glu Thr Val Pro Val Asp Phe Gln Asn Val Leu 
                665                 670                 675 

Glu Asp Phe Thr Lys Gln Gly Phe Arg Val Ile Ala Leu Ala His 
                680                 685                 690 

Arg Lys Leu Glu Ser Lys Leu Thr Trp His Lys Val Gln Asn Ile 
                695                 700                 705 

Ser Arg Asp Ala Ile Glu Asn Asn Met Asp Phe Met Gly Leu Ile 
                710                 715                 720 

Ile Met Gln Asn Lys Leu Lys Gln Lys Thr Pro Ala Val Leu Glu 
                725                 730                 735 

Asp Leu His Lys Ala Asn Ile Arg Thr Val Met Val Thr Gly Asp 
                740                 745                 750 

Ser Met Leu Thr Ala Val Ser Val Ala Arg Asp Cys Gly Met Ile 
                755                 760                 765 

Leu Pro Gln Asp Lys Val Ile Ile Ala Glu Ala Leu Pro Pro Lys 
                770                 775                 780 

Asp Gly Lys Val Ala Lys Ile Asn Trp His Tyr Ala Asp Ser Leu 
                785                 790                 795 

Thr Gln Cys Ser His Pro Ser Ala Ile Asp Pro Glu Ala Ile Pro 
                800                 805                 810 

Val Lys Leu Val His Asp Ser Leu Glu Asp Leu Gln Met Thr Arg 
                815                 820                 825 

Tyr His Phe Ala Met Asn Gly Lys Ser Phe Ser Val Ile Leu Glu 
                830                 835                 840 

His Phe Gln Asp Leu Val Pro Lys Leu Met Leu His Gly Thr Val 
                845                 850                 855 

Phe Ala Arg Met Ala Pro Asp Gln Lys Thr Gln Leu Ile Glu Ala 
                860                 865                 870 

Leu Gln Asn Val Asp Tyr Phe Val Gly Met Cys Gly Asp Gly Ala 
                875                 880                 885 

Asn Asp Cys Gly Ala Leu Lys Arg Ala His Gly Gly Ile Ser Leu 
                890                 895                 900 

Ser Glu Leu Glu Ala Ser Val Ala Ser Pro Phe Thr Ser Lys Thr 
                905                 910                 915 

Pro Ser Ile Ser Cys Val Pro Asn Leu Ile Arg Glu Gly Arg Ala 
                920                 925                 930 

Ala Leu Ile Thr Ser Phe Cys Val Phe Lys Phe Met Ala Leu Tyr 
                935                 940                 945 

Ser Ile Ile Gln Tyr Phe Ser Val Thr Leu Leu Tyr Ser Ile Leu 
                950                 955                 960 

Ser Asn Leu Gly Asp Phe Gln Phe Leu Phe Ile Asp Leu Ala Ile 
                965                 970                 975 

Ile Leu Val Val Val Phe Thr Met Ser Leu Asn Pro Ala Trp Lys 
                980                 985                 990 

Glu Leu Val Ala Gln Arg Pro Pro Ser Gly Leu Ile Ser Gly Ala 
                995                 1000                1005 

Leu Leu Phe Ser Val Leu Ser Gln Ile Ile Ile Cys Ile Gly Phe 
                1010                1015                1020 

Gln Ser Leu Gly Phe Phe Trp Val Lys Gln Gln Pro Trp Tyr Glu 
                1025                1030                1035 

Val Trp His Pro Lys Ser Asp Ala Cys Asn Thr Thr Gly Ser Gly 
                1040                1045                1050 

Phe Trp Asn Ser Ser His Val Asp Asn Glu Thr Glu Leu Asp Glu 
                1055                1060                1065 

His Asn Ile Gln Asn Tyr Glu Asn Thr Thr Val Phe Phe Ile Ser 
                1070                1075                1080 

Ser Phe Gln Tyr Leu Ile Val Ala Ile Ala Phe Ser Lys Gly Lys 
                1085                1090                1095 

Pro Phe Arg Gln Pro Cys Tyr Lys Asn Tyr Phe Phe Val Phe Ser 
                1100                1105                1110 

Val Ile Phe Leu Tyr Ile Phe Ile Leu Phe Ile Met Leu Tyr Pro 
                1115                1120                1125 

Val Ala Ser Val Asp Gln Val Leu Gln Ile Val Cys Val Pro Tyr 
                1130                1135                1140 

Gln Trp Arg Val Thr Met Leu Ile Ile Val Leu Val Asn Ala Phe 
                1145                1150                1155 

Val Ser Ile Thr Val Glu Asn Phe Phe Leu Asp Met Val Leu Trp 
                1160                1165                1170 

Lys Val Val Phe Asn Arg Asp Lys Gln Gly Glu Tyr Arg Phe Ser 
                1175                1180                1185 

Thr Thr Gln Pro Pro Gln Glu Ser Val Asp Arg Trp Gly Lys Cys 
                1190                1195                1200 

Cys Leu Pro Trp Ala Leu Gly Cys Arg Lys Lys Thr Pro Lys Ala 
                1205                1210                1215 

Lys Tyr Met Tyr Leu Ala Gln Glu Leu Leu Val Asp Pro Glu Trp 
                1220                1225                1230 

Pro Pro Lys Pro Gln Thr Thr Thr Glu Ala Lys Ala Leu Val Lys 
                1235                1240                1245 

Glu Asn Gly Ser Cys Gln Ile Ile Thr Ile Thr 
                1250                1255 

 
           
             15  
             499  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3046849CD1  
             
           
            15 

Met Leu His Ala Leu Leu Arg Ser Arg Thr Ile Gln Gly Arg Ile 
1               5                   10                  15 

Leu Leu Leu Thr Ile Cys Ala Ala Gly Ile Gly Gly Thr Phe Gln 
                20                  25                  30 

Phe Gly Tyr Asn Leu Ser Ile Ile Asn Ala Pro Thr Leu His Ile 
                35                  40                  45 

Gln Glu Phe Thr Asn Glu Thr Trp Gln Ala Arg Thr Gly Glu Pro 
                50                  55                  60 

Leu Pro Asp His Leu Val Leu Leu Met Trp Ser Leu Ile Val Ser 
                65                  70                  75 

Leu Tyr Pro Leu Gly Gly Leu Phe Gly Ala Leu Leu Ala Gly Pro 
                80                  85                  90 

Leu Ala Ile Thr Leu Gly Arg Lys Lys Ser Leu Leu Val Asn Asn 
                95                  100                 105 

Ile Phe Val Val Ser Ala Ala Ile Leu Phe Gly Phe Ser Arg Lys 
                110                 115                 120 

Ala Gly Ser Phe Glu Met Ile Met Leu Gly Arg Leu Leu Val Gly 
                125                 130                 135 

Val Asn Ala Gly Val Ser Met Asn Ile Gln Pro Met Tyr Leu Gly 
                140                 145                 150 

Glu Ser Ala Pro Lys Glu Leu Arg Gly Ala Val Ala Met Ser Ser 
                155                 160                 165 

Ala Ile Phe Thr Ala Leu Gly Ile Val Met Gly Gln Val Val Gly 
                170                 175                 180 

Leu Arg Glu Leu Leu Gly Gly Pro Gln Ala Trp Pro Leu Leu Leu 
                185                 190                 195 

Ala Ser Cys Leu Val Pro Gly Ala Leu Gln Leu Ala Ser Leu Pro 
                200                 205                 210 

Leu Leu Pro Glu Ser Pro Arg Tyr Leu Leu Ile Asp Cys Gly Asp 
                215                 220                 225 

Thr Glu Ala Cys Leu Ala Ala Leu Arg Gln Leu Arg Gly Ser Gly 
                230                 235                 240 

Asp Leu Ala Gly Glu Leu Glu Glu Leu Glu Glu Glu Arg Ala Ala 
                245                 250                 255 

Cys Gln Gly Cys Arg Ala Arg Arg Pro Trp Glu Leu Phe Gln His 
                260                 265                 270 

Arg Ala Leu Arg Arg Gln Val Thr Ser Leu Val Val Leu Gly Ser 
                275                 280                 285 

Ala Met Glu Leu Cys Gly Asn Asp Ser Val Tyr Ala Tyr Ala Ser 
                290                 295                 300 

Ser Val Phe Arg Lys Ala Gly Val Pro Glu Ala Lys Ile Gln Tyr 
                305                 310                 315 

Ala Ile Ile Gly Thr Gly Ser Cys Glu Leu Leu Thr Ala Val Val 
                320                 325                 330 

Ser Cys Val Val Ile Glu Arg Val Gly Arg Arg Val Leu Leu Ile 
                335                 340                 345 

Gly Gly Tyr Ser Leu Met Thr Cys Trp Gly Ser Ile Phe Thr Val 
                350                 355                 360 

Ala Leu Cys Leu Gln Ser Ser Phe Pro Trp Thr Leu Tyr Leu Ala 
                365                 370                 375 

Met Ala Cys Ile Phe Ala Phe Ile Leu Ser Phe Gly Ile Gly Pro 
                380                 385                 390 

Ala Gly Val Thr Gly Ile Leu Ala Thr Glu Leu Phe Asp Gln Met 
                395                 400                 405 

Ala Arg Pro Ala Ala Cys Met Val Cys Gly Ala Leu Met Trp Ile 
                410                 415                 420 

Met Leu Ile Leu Val Gly Leu Gly Phe Pro Phe Ile Met Glu Ala 
                425                 430                 435 

Leu Ser His Phe Leu Tyr Val Pro Phe Leu Gly Val Cys Val Cys 
                440                 445                 450 

Gly Ala Ile Tyr Thr Gly Leu Phe Leu Pro Glu Thr Lys Gly Lys 
                455                 460                 465 

Thr Phe Gln Glu Ile Ser Lys Glu Leu His Arg Leu Asn Phe Pro 
                470                 475                 480 

Arg Arg Ala Gln Gly Pro Thr Trp Arg Ser Leu Glu Val Ile Gln 
                485                 490                 495 

Ser Thr Glu Leu 

 
           
             16  
             596  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 4538363CD1  
             
           
            16 

Met Ala Ala Asn Ser Thr Ser Asp Leu His Thr Pro Gly Thr Gln 
1               5                   10                  15 

Leu Ser Val Ala Asp Ile Ile Val Ile Thr Val Tyr Phe Ala Leu 
                20                  25                  30 

Asn Val Ala Val Gly Ile Trp Ser Ser Cys Arg Ala Ser Arg Asn 
                35                  40                  45 

Thr Val Asn Gly Tyr Phe Leu Ala Gly Arg Asp Met Thr Trp Trp 
                50                  55                  60 

Pro Ile Gly Ala Ser Leu Phe Ala Ser Ser Glu Gly Ser Gly Leu 
                65                  70                  75 

Phe Ile Gly Leu Ala Gly Ser Gly Ala Ala Gly Gly Leu Ala Val 
                80                  85                  90 

Ala Gly Phe Glu Trp Asn Ala Thr Tyr Val Leu Leu Ala Leu Ala 
                95                  100                 105 

Trp Val Phe Val Pro Ile Tyr Ile Ser Ser Glu Ile Val Thr Leu 
                110                 115                 120 

Pro Glu Tyr Ile Gln Lys Arg Tyr Gly Gly Gln Arg Ile Arg Met 
                125                 130                 135 

Tyr Leu Ser Val Leu Ser Leu Leu Leu Ser Val Phe Thr Lys Ile 
                140                 145                 150 

Ser Leu Asp Leu Tyr Ala Gly Ala Leu Phe Val His Ile Cys Leu 
                155                 160                 165 

Gly Trp Asn Phe Tyr Leu Ser Thr Ile Leu Thr Leu Gly Ile Thr 
                170                 175                 180 

Ala Leu Tyr Thr Ile Ala Gly Gly Leu Ala Ala Val Ile Tyr Thr 
                185                 190                 195 

Asp Ala Leu Gln Thr Leu Ile Met Val Val Gly Ala Val Ile Leu 
                200                 205                 210 

Thr Ile Lys Ala Phe Asp Gln Ile Gly Gly Tyr Gly Gln Leu Glu 
                215                 220                 225 

Ala Ala Tyr Ala Gln Ala Ile Pro Ser Arg Thr Ile Ala Asn Thr 
                230                 235                 240 

Thr Cys His Leu Pro Arg Thr Asp Ala Met His Met Phe Arg Asp 
                245                 250                 255 

Pro His Thr Gly Asp Leu Pro Trp Thr Gly Met Thr Phe Gly Leu 
                260                 265                 270 

Thr Ile Met Ala Thr Trp Tyr Trp Cys Thr Asp Gln Val Ile Val 
                275                 280                 285 

Gln Arg Ser Leu Ser Ala Arg Asp Leu Asn His Ala Lys Ala Gly 
                290                 295                 300 

Ser Ile Leu Ala Ser Tyr Leu Lys Met Leu Pro Met Gly Leu Ile 
                305                 310                 315 

Ile Met Pro Gly Met Ile Ser Arg Ala Leu Phe Pro Asp Asp Val 
                320                 325                 330 

Gly Cys Val Val Pro Ser Glu Cys Leu Arg Ala Cys Gly Ala Glu 
                335                 340                 345 

Val Gly Cys Ser Asn Ile Ala Tyr Pro Lys Leu Val Met Glu Leu 
                350                 355                 360 

Met Pro Ile Gly Leu Arg Gly Leu Met Ile Ala Val Met Leu Ala 
                365                 370                 375 

Ala Leu Met Ser Ser Leu Thr Ser Ile Phe Asn Ser Ser Ser Thr 
                380                 385                 390 

Leu Phe Thr Met Asp Ile Trp Arg Arg Leu Arg Pro Arg Ser Gly 
                395                 400                 405 

Glu Arg Glu Leu Leu Leu Val Gly Arg Leu Val Ile Val Ala Leu 
                410                 415                 420 

Ile Gly Val Ser Val Ala Trp Ile Pro Val Leu Gln Asp Ser Asn 
                425                 430                 435 

Ser Gly Gln Leu Phe Ile Tyr Met Gln Ser Val Thr Ser Ser Leu 
                440                 445                 450 

Ala Pro Pro Val Thr Ala Val Phe Val Leu Gly Val Phe Trp Arg 
                455                 460                 465 

Arg Ala Asn Glu Gln Gly Ala Phe Trp Gly Leu Ile Ala Gly Leu 
                470                 475                 480 

Val Val Gly Ala Thr Arg Leu Val Leu Glu Phe Leu Asn Pro Ala 
                485                 490                 495 

Pro Pro Cys Gly Glu Pro Asp Thr Arg Pro Ala Val Leu Gly Ser 
                500                 505                 510 

Ile His Tyr Leu His Phe Ala Val Ala Leu Phe Ala Leu Ser Gly 
                515                 520                 525 

Ala Val Val Val Ala Gly Ser Leu Leu Thr Pro Pro Pro Gln Ser 
                530                 535                 540 

Val Gln Ile Glu Asn Leu Thr Trp Trp Thr Leu Ala Gln Asp Val 
                545                 550                 555 

Pro Leu Gly Thr Lys Ala Gly Asp Gly Gln Thr Pro Gln Lys His 
                560                 565                 570 

Ala Phe Trp Ala Arg Val Cys Gly Phe Asn Ala Ile Leu Leu Met 
                575                 580                 585 

Cys Val Asn Ile Phe Phe Tyr Ala Tyr Phe Ala 
                590                 595 

 
           
             17  
             1192  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 6427460CD1  
             
           
            17 

Met Asp Cys Ser Leu Val Arg Thr Leu Val His Arg Tyr Cys Ala 
1               5                   10                  15 

Gly Glu Glu Asn Trp Val Asp Ser Arg Thr Ile Tyr Val Gly His 
                20                  25                  30 

Arg Glu Pro Pro Pro Gly Ala Glu Ala Tyr Ile Pro Gln Arg Tyr 
                35                  40                  45 

Pro Asp Asn Arg Ile Val Ser Ser Lys Tyr Thr Phe Trp Asn Phe 
                50                  55                  60 

Ile Pro Lys Asn Leu Phe Glu Gln Phe Arg Arg Val Ala Asn Phe 
                65                  70                  75 

Tyr Phe Leu Ile Ile Phe Leu Val Gln Leu Ile Ile Asp Thr Pro 
                80                  85                  90 

Thr Ser Pro Val Thr Ser Gly Leu Pro Leu Phe Phe Val Ile Thr 
                95                  100                 105 

Val Thr Ala Ile Lys Gln Gly Tyr Glu Asp Trp Leu Arg His Lys 
                110                 115                 120 

Ala Asp Asn Ala Met Asn Gln Cys Pro Val His Phe Ile Gln His 
                125                 130                 135 

Gly Lys Leu Val Arg Lys Gln Ser Arg Lys Leu Arg Val Gly Asp 
                140                 145                 150 

Ile Val Met Val Lys Glu Asp Glu Thr Phe Pro Cys Asp Leu Ile 
                155                 160                 165 

Phe Leu Ser Ser Asn Arg Gly Asp Gly Thr Cys His Val Thr Thr 
                170                 175                 180 

Ala Ser Leu Asp Gly Glu Ser Ser His Lys Thr His Tyr Ala Val 
                185                 190                 195 

Gln Asp Thr Lys Gly Phe His Thr Glu Glu Asp Ile Gly Gly Leu 
                200                 205                 210 

His Ala Thr Ile Glu Cys Glu Gln Pro Gln Pro Asp Leu Tyr Lys 
                215                 220                 225 

Phe Val Gly Arg Ile Asn Val Tyr Ser Asp Leu Asn Asp Pro Val 
                230                 235                 240 

Val Arg Pro Leu Gly Ser Glu Asn Leu Leu Leu Arg Gly Ala Thr 
                245                 250                 255 

Leu Lys Asn Thr Glu Lys Ile Phe Gly Val Ala Ile Tyr Thr Gly 
                260                 265                 270 

Met Glu Thr Lys Met Ala Leu Asn Tyr Gln Ser Lys Ser Gln Lys 
                275                 280                 285 

Arg Ser Ala Val Glu Lys Ser Met Asn Ala Phe Leu Ile Val Tyr 
                290                 295                 300 

Leu Cys Ile Leu Ile Ser Lys Ala Leu Ile Asn Thr Val Leu Lys 
                305                 310                 315 

Tyr Val Trp Gln Ser Glu Pro Phe Arg Asp Glu Pro Trp Tyr Asn 
                320                 325                 330 

Gln Lys Thr Glu Ser Glu Arg Gln Arg Asn Leu Phe Leu Lys Ala 
                335                 340                 345 

Phe Thr Asp Phe Leu Ala Phe Met Val Leu Phe Asn Tyr Ile Ile 
                350                 355                 360 

Pro Val Ser Met Tyr Val Thr Val Glu Met Gln Lys Phe Leu Gly 
                365                 370                 375 

Ser Tyr Phe Ile Thr Trp Asp Glu Asp Met Phe Asp Glu Glu Thr 
                380                 385                 390 

Gly Glu Gly Pro Leu Val Asn Thr Ser Asp Leu Asn Glu Glu Leu 
                395                 400                 405 

Gly Gln Val Glu Tyr Ile Phe Thr Asp Lys Thr Gly Thr Leu Thr 
                410                 415                 420 

Glu Asn Asn Met Glu Phe Lys Glu Cys Cys Ile Glu Gly His Val 
                425                 430                 435 

Tyr Val Pro His Val Ile Cys Asn Gly Gln Val Leu Pro Glu Ser 
                440                 445                 450 

Ser Gly Ile Asp Met Ile Asp Ser Ser Pro Ser Val Asn Gly Arg 
                455                 460                 465 

Glu Arg Glu Glu Leu Phe Phe Arg Ala Leu Cys Leu Cys His Thr 
                470                 475                 480 

Val Gln Val Lys Asp Asp Asp Ser Val Asp Gly Pro Arg Lys Ser 
                485                 490                 495 

Pro Asp Gly Gly Lys Ser Cys Val Tyr Ile Ser Ser Ser Pro Asp 
                500                 505                 510 

Glu Val Ala Leu Val Glu Gly Val Gln Arg Leu Gly Phe Thr Tyr 
                515                 520                 525 

Leu Arg Leu Lys Asp Asn Tyr Met Glu Ile Leu Asn Arg Glu Asn 
                530                 535                 540 

His Ile Glu Arg Phe Glu Leu Leu Glu Ile Leu Ser Phe Asp Ser 
                545                 550                 555 

Val Arg Arg Arg Met Ser Val Ile Val Lys Ser Ala Thr Gly Glu 
                560                 565                 570 

Ile Tyr Leu Phe Cys Lys Gly Ala Asp Ser Ser Ile Phe Pro Arg 
                575                 580                 585 

Val Ile Glu Gly Lys Val Asp Gln Ile Arg Ala Arg Val Glu Arg 
                590                 595                 600 

Asn Ala Val Glu Gly Leu Arg Thr Leu Cys Val Ala Tyr Lys Arg 
                605                 610                 615 

Leu Ile Gln Glu Glu Tyr Glu Gly Ile Cys Lys Leu Leu Gln Ala 
                620                 625                 630 

Ala Lys Val Ala Leu Gln Asp Arg Glu Lys Lys Leu Ala Glu Ala 
                635                 640                 645 

Tyr Glu Gln Ile Glu Lys Asp Leu Thr Leu Leu Gly Ala Thr Ala 
                650                 655                 660 

Val Glu Asp Arg Leu Gln Glu Lys Ala Ala Asp Thr Ile Glu Ala 
                665                 670                 675 

Leu Gln Lys Ala Gly Ile Lys Val Trp Val Leu Thr Gly Asp Lys 
                680                 685                 690 

Met Glu Thr Ala Ala Ala Thr Cys Tyr Ala Cys Lys Leu Phe Arg 
                695                 700                 705 

Arg Asn Thr Gln Leu Leu Glu Leu Thr Thr Lys Arg Ile Glu Glu 
                710                 715                 720 

Gln Ser Leu His Asp Val Leu Phe Glu Leu Ser Lys Thr Val Leu 
                725                 730                 735 

Arg His Ser Gly Ser Leu Thr Arg Asp Asn Leu Ser Gly Leu Ser 
                740                 745                 750 

Ala Asp Met Gln Asp Tyr Gly Leu Ile Ile Asp Gly Ala Ala Leu 
                755                 760                 765 

Ser Leu Ile Met Lys Pro Arg Glu Asp Gly Ser Ser Gly Asn Tyr 
                770                 775                 780 

Arg Glu Leu Phe Leu Glu Ile Cys Arg Ser Cys Ser Ala Val Leu 
                785                 790                 795 

Cys Cys Arg Met Ala Pro Leu Gln Lys Ala Gln Ile Val Lys Leu 
                800                 805                 810 

Ile Lys Phe Ser Lys Glu His Pro Ile Thr Leu Ala Ile Gly Asp 
                815                 820                 825 

Gly Ala Asn Asp Val Ser Met Ile Leu Glu Ala His Val Gly Ile 
                830                 835                 840 

Gly Val Ile Gly Lys Glu Gly Arg Gln Ala Ala Arg Asn Ser Asp 
                845                 850                 855 

Tyr Ala Ile Pro Lys Phe Lys His Leu Lys Lys Met Leu Leu Val 
                860                 865                 870 

His Gly His Phe Tyr Tyr Ile Arg Ile Ser Glu Leu Val Gln Tyr 
                875                 880                 885 

Phe Phe Tyr Lys Asn Val Cys Phe Ile Phe Pro Gln Phe Leu Tyr 
                890                 895                 900 

Gln Phe Phe Cys Gly Phe Ser Gln Gln Thr Leu Tyr Asp Thr Ala 
                905                 910                 915 

Tyr Leu Thr Leu Tyr Asn Ile Ser Phe Thr Ser Leu Pro Ile Leu 
                920                 925                 930 

Leu Tyr Ser Leu Met Glu Gln His Val Gly Ile Asp Val Leu Lys 
                935                 940                 945 

Arg Asp Pro Thr Leu Tyr Arg Asp Val Ala Lys Asn Ala Leu Leu 
                950                 955                 960 

Arg Trp Arg Val Phe Ile Tyr Trp Thr Leu Leu Gly Leu Phe Asp 
                965                 970                 975 

Ala Leu Val Phe Phe Phe Gly Ala Tyr Phe Val Phe Glu Asn Thr 
                980                 985                 990 

Thr Val Thr Ser Asn Gly Gln Ile Phe Gly Asn Trp Thr Phe Gly 
                995                 1000                1005 

Thr Leu Val Phe Thr Val Met Val Phe Thr Val Thr Leu Lys Leu 
                1010                1015                1020 

Ala Leu Asp Thr His Tyr Trp Thr Trp Ile Asn His Phe Val Ile 
                1025                1030                1035 

Trp Gly Ser Leu Leu Phe Tyr Val Val Phe Ser Leu Leu Trp Gly 
                1040                1045                1050 

Gly Val Ile Trp Pro Phe Leu Asn Tyr Gln Arg Met Tyr Tyr Val 
                1055                1060                1065 

Phe Ile Gln Met Leu Ser Ser Gly Pro Ala Trp Leu Ala Ile Val 
                1070                1075                1080 

Leu Leu Val Thr Ile Ser Leu Leu Pro Asp Val Leu Lys Lys Val 
                1085                1090                1095 

Leu Cys Arg Gln Leu Trp Pro Thr Ala Thr Glu Arg Val Gln Gln 
                1100                1105                1110 

Asn Gly Cys Ala Gln Pro Arg Asp Arg Asp Ser Glu Phe Thr Pro 
                1115                1120                1125 

Leu Ala Ser Leu Gln Ser Pro Gly Tyr Gln Ser Thr Cys Pro Ser 
                1130                1135                1140 

Ala Ala Trp Tyr Ser Ser His Ser Gln Gln Val Thr Leu Ala Ala 
                1145                1150                1155 

Trp Lys Glu Lys Val Ser Thr Glu Pro Pro Pro Ile Leu Gly Gly 
                1160                1165                1170 

Ser His His His Cys Ser Ser Ile Pro Ser His Ser Cys Pro Arg 
                1175                1180                1185 

Ser Arg Val Gly Met Leu Val 
                1190 

 
           
             18  
             638  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7474127CD1  
             
           
            18 

Met Gly Lys Ile Glu Asn Asn Glu Arg Val Ile Leu Asn Val Gly 
1               5                   10                  15 

Gly Thr Arg His Glu Thr Tyr Arg Ser Thr Leu Lys Thr Leu Pro 
                20                  25                  30 

Gly Thr Arg Leu Ala Leu Leu Ala Ser Ser Glu Pro Pro Gly Asp 
                35                  40                  45 

Cys Leu Thr Thr Ala Gly Asp Lys Leu Gln Pro Ser Pro Pro Pro 
                50                  55                  60 

Leu Ser Pro Pro Pro Arg Ala Pro Pro Leu Ser Pro Gly Pro Gly 
                65                  70                  75 

Gly Cys Phe Glu Gly Gly Ala Gly Asn Cys Ser Ser Arg Gly Gly 
                80                  85                  90 

Arg Ala Ser Asp His Pro Gly Gly Gly Arg Glu Phe Phe Phe Asp 
                95                  100                 105 

Arg His Pro Gly Val Phe Ala Tyr Val Leu Asn Tyr Tyr Arg Thr 
                110                 115                 120 

Gly Lys Leu His Cys Pro Ala Asp Val Cys Gly Pro Leu Phe Glu 
                125                 130                 135 

Glu Glu Leu Ala Phe Trp Gly Ile Asp Glu Thr Asp Val Glu Pro 
                140                 145                 150 

Cys Cys Trp Met Thr Tyr Arg Gln His Arg Asp Ala Glu Glu Ala 
                155                 160                 165 

Leu Asp Ile Phe Glu Thr Pro Asp Leu Ile Gly Gly Asp Pro Gly 
                170                 175                 180 

Asp Asp Glu Asp Leu Ala Ala Lys Arg Leu Gly Ile Glu Asp Ala 
                185                 190                 195 

Ala Gly Leu Gly Gly Pro Asp Gly Lys Ser Gly Arg Trp Arg Arg 
                200                 205                 210 

Leu Gln Pro Arg Met Trp Ala Leu Phe Glu Asp Pro Tyr Ser Ser 
                215                 220                 225 

Arg Ala Ala Arg Phe Ile Ala Phe Ala Ser Leu Phe Phe Ile Leu 
                230                 235                 240 

Val Ser Ile Thr Thr Phe Cys Leu Glu Thr His Glu Ala Phe Asn 
                245                 250                 255 

Ile Val Lys Asn Lys Thr Glu Pro Val Ile Asn Gly Thr Ser Val 
                260                 265                 270 

Val Leu Gln Tyr Glu Ile Glu Thr Asp Pro Ala Leu Thr Tyr Val 
                275                 280                 285 

Glu Gly Val Cys Val Val Trp Phe Thr Phe Glu Phe Leu Val Arg 
                290                 295                 300 

Ile Val Phe Ser Pro Asn Lys Leu Glu Phe Ile Lys Asn Leu Leu 
                305                 310                 315 

Asn Ile Ile Asp Phe Val Ala Ile Leu Pro Phe Tyr Leu Glu Val 
                320                 325                 330 

Gly Leu Ser Gly Leu Ser Ser Lys Ala Ala Lys Asp Val Leu Gly 
                335                 340                 345 

Phe Leu Arg Val Val Arg Phe Val Arg Ile Leu Arg Ile Phe Lys 
                350                 355                 360 

Leu Thr Arg His Phe Val Gly Leu Arg Val Leu Gly His Thr Leu 
                365                 370                 375 

Arg Ala Ser Thr Asn Glu Phe Leu Leu Leu Ile Ile Phe Leu Ala 
                380                 385                 390 

Leu Gly Val Leu Ile Phe Ala Thr Met Ile Tyr Tyr Ala Glu Arg 
                395                 400                 405 

Val Gly Ala Gln Pro Asn Asp Pro Ser Ala Ser Glu His Thr Gln 
                410                 415                 420 

Phe Lys Asn Ile Pro Ile Gly Phe Trp Trp Ala Val Val Thr Met 
                425                 430                 435 

Thr Thr Leu Gly Tyr Gly Asp Met Tyr Pro Gln Thr Trp Ser Gly 
                440                 445                 450 

Met Leu Val Gly Ala Leu Cys Ala Leu Ala Gly Val Leu Thr Ile 
                455                 460                 465 

Ala Met Pro Val Pro Val Ile Val Asn Asn Phe Gly Met Tyr Tyr 
                470                 475                 480 

Ser Leu Ala Met Ala Lys Gln Lys Leu Pro Arg Lys Arg Lys Lys 
                485                 490                 495 

His Ile Pro Pro Ala Pro Gln Ala Ser Ser Pro Thr Phe Cys Lys 
                500                 505                 510 

Thr Glu Leu Asn Met Ala Cys Asn Ser Thr Gln Ser Asp Thr Cys 
                515                 520                 525 

Leu Gly Lys Asp Asn Arg Leu Leu Glu His Asn Arg Ser Val Leu 
                530                 535                 540 

Ser Gly Asp Asp Ser Thr Gly Ser Glu Pro Pro Leu Ser Pro Pro 
                545                 550                 555 

Glu Arg Leu Pro Ile Arg Arg Ser Ser Thr Arg Asp Lys Asn Arg 
                560                 565                 570 

Arg Gly Glu Thr Cys Phe Leu Leu Thr Thr Gly Asp Tyr Thr Cys 
                575                 580                 585 

Ala Ser Asp Gly Gly Ile Arg Lys Gly Tyr Glu Lys Ser Arg Ser 
                590                 595                 600 

Leu Asn Asn Ile Ala Gly Leu Ala Gly Asn Ala Leu Arg Leu Ser 
                605                 610                 615 

Pro Val Thr Ser Pro Tyr Asn Ser Pro Cys Pro Leu Arg Arg Ser 
                620                 625                 630 

Arg Ser Pro Ile Pro Ser Ile Leu 
                635 

 
           
             19  
             681  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7476949CD1  
             
           
            19 

Met Ser Lys Asp Leu Ala Ala Met Gly Pro Gly Ala Ser Gly Asp 
1               5                   10                  15 

Gly Val Arg Thr Glu Thr Ala Pro His Ile Ala Leu Asp Ser Arg 
                20                  25                  30 

Val Gly Leu His Ala Tyr Asp Ile Ser Val Val Val Ile Tyr Phe 
                35                  40                  45 

Val Phe Val Ile Ala Val Gly Ile Trp Ser Ser Ile Arg Ala Ser 
                50                  55                  60 

Arg Gly Thr Ile Gly Gly Tyr Phe Leu Ala Gly Arg Ser Met Ser 
                65                  70                  75 

Trp Trp Pro Ile Gly Ala Ser Leu Met Ser Ser Asn Val Gly Ser 
                80                  85                  90 

Gly Leu Phe Ile Gly Leu Ala Gly Thr Gly Ala Ala Gly Gly Leu 
                95                  100                 105 

Ala Val Gly Gly Phe Glu Trp Asn Ala Thr Trp Leu Leu Leu Ala 
                110                 115                 120 

Leu Gly Trp Val Phe Val Pro Val Tyr Ile Ala Ala Gly Val Val 
                125                 130                 135 

Thr Met Pro Gln Tyr Leu Lys Lys Arg Phe Gly Gly Gln Arg Ile 
                140                 145                 150 

Gln Val Tyr Met Ser Val Leu Ser Leu Ile Leu Tyr Ile Phe Thr 
                155                 160                 165 

Lys Ile Ser Thr Asp Ile Phe Ser Gly Ala Leu Phe Ile Gln Met 
                170                 175                 180 

Ala Leu Gly Trp Asn Leu Tyr Leu Ser Thr Gly Ile Leu Leu Val 
                185                 190                 195 

Val Thr Ala Val Tyr Thr Ile Ala Gly Gly Leu Met Ala Val Ile 
                200                 205                 210 

Tyr Thr Asp Ala Leu Gln Thr Val Ile Met Val Gly Gly Ala Leu 
                215                 220                 225 

Val Leu Met Phe Leu Gly Phe Gln Asp Val Gly Trp Tyr Pro Gly 
                230                 235                 240 

Leu Glu Gln Arg Tyr Arg Gln Ala Ile Pro Asn Val Thr Val Pro 
                245                 250                 255 

Asn Thr Thr Cys His Leu Pro Arg Pro Asp Ala Phe His Ile Leu 
                260                 265                 270 

Arg Asp Pro Val Ser Gly Asp Ile Pro Trp Pro Gly Leu Ile Phe 
                275                 280                 285 

Gly Leu Thr Val Leu Ala Thr Trp Cys Trp Cys Thr Asp Gln Val 
                290                 295                 300 

Ile Val Gln Arg Ser Leu Ser Ala Lys Ser Leu Ser His Ala Lys 
                305                 310                 315 

Gly Gly Ser Val Leu Gly Gly Tyr Leu Lys Ile Leu Pro Met Phe 
                320                 325                 330 

Phe Ile Val Met Pro Gly Met Ile Ser Arg Ala Leu Phe Pro Asp 
                335                 340                 345 

Glu Val Gly Cys Val Asp Pro Asp Val Cys Gln Arg Ile Cys Gly 
                350                 355                 360 

Ala Arg Val Gly Cys Ser Asn Ile Ala Tyr Pro Lys Leu Val Met 
                365                 370                 375 

Ala Leu Met Pro Val Gly Leu Arg Gly Leu Met Ile Ala Val Ile 
                380                 385                 390 

Met Ala Ala Leu Met Ser Ser Leu Thr Ser Ile Phe Asn Ser Ser 
                395                 400                 405 

Ser Thr Leu Phe Thr Ile Asp Val Trp Gln Arg Phe Arg Arg Lys 
                410                 415                 420 

Ser Thr Glu Gln Glu Leu Met Val Val Gly Arg Val Phe Val Val 
                425                 430                 435 

Phe Leu Val Val Ile Ser Ile Leu Trp Ile Pro Ile Ile Gln Ser 
                440                 445                 450 

Ser Asn Ser Gly Gln Leu Phe Asp Tyr Ile Gln Ala Val Thr Ser 
                455                 460                 465 

Tyr Leu Ala Pro Pro Ile Thr Ala Leu Phe Leu Leu Ala Ile Phe 
                470                 475                 480 

Cys Lys Arg Val Thr Glu Pro Gly Ala Phe Trp Gly Leu Val Phe 
                485                 490                 495 

Gly Leu Gly Val Gly Leu Leu Arg Met Ile Leu Glu Phe Ser Tyr 
                500                 505                 510 

Pro Ala Pro Ala Cys Gly Glu Val Asp Arg Arg Pro Ala Val Leu 
                515                 520                 525 

Lys Asp Phe His Tyr Leu Tyr Phe Ala Ile Leu Leu Cys Gly Leu 
                530                 535                 540 

Thr Ala Ile Val Ile Val Ile Val Ser Leu Cys Thr Thr Pro Ile 
                545                 550                 555 

Pro Glu Glu Gln Leu Thr Arg Leu Thr Trp Trp Thr Arg Asn Cys 
                560                 565                 570 

Pro Leu Ser Glu Leu Glu Lys Glu Ala His Glu Ser Thr Pro Glu 
                575                 580                 585 

Ile Ser Glu Arg Pro Ala Gly Glu Cys Pro Ala Gly Gly Gly Ala 
                590                 595                 600 

Ala Glu Asn Ser Ser Leu Gly Gln Glu Gln Pro Glu Ala Pro Ser 
                605                 610                 615 

Arg Ser Trp Gly Lys Leu Leu Trp Ser Trp Phe Cys Gly Leu Ser 
                620                 625                 630 

Gly Thr Pro Glu Gln Ala Leu Ser Pro Ala Glu Lys Ala Ala Leu 
                635                 640                 645 

Glu Gln Lys Leu Thr Ser Ile Glu Glu Glu Pro Leu Trp Arg His 
                650                 655                 660 

Val Cys Asn Ile Asn Ala Val Leu Leu Leu Ala Ile Asn Ile Phe 
                665                 670                 675 

Leu Trp Gly Tyr Phe Ala 
                680 

 
           
             20  
             1096  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477249CD1  
             
           
            20 

Met Trp Arg Trp Ile Arg Gln Gln Leu Gly Phe Asp Pro Pro His 
1               5                   10                  15 

Gln Ser Asp Thr Arg Thr Ile Tyr Val Ala Asn Arg Phe Pro Gln 
                20                  25                  30 

Asn Gly Leu Tyr Thr Pro Gln Lys Phe Ile Asp Asn Arg Ile Ile 
                35                  40                  45 

Ser Ser Lys Tyr Thr Val Trp Asn Phe Val Pro Lys Asn Leu Phe 
                50                  55                  60 

Glu Gln Phe Arg Arg Val Ala Asn Phe Tyr Phe Leu Ile Ile Phe 
                65                  70                  75 

Leu Val Gln Leu Met Ile Asp Thr Pro Thr Ser Pro Val Thr Ser 
                80                  85                  90 

Gly Leu Pro Leu Phe Phe Val Ile Thr Val Thr Ala Ile Lys Gln 
                95                  100                 105 

Gly Tyr Glu Asp Trp Leu Arg His Asn Ser Asp Asn Glu Val Asn 
                110                 115                 120 

Gly Ala Pro Val Tyr Val Val Arg Ser Gly Gly Leu Val Lys Thr 
                125                 130                 135 

Arg Ser Lys Asn Ile Arg Val Gly Asp Ile Val Arg Ile Ala Lys 
                140                 145                 150 

Asp Glu Ile Phe Pro Ala Asp Leu Val Leu Leu Ser Ser Asp Arg 
                155                 160                 165 

Leu Asp Gly Ser Cys His Val Thr Thr Ala Ser Leu Asp Gly Glu 
                170                 175                 180 

Thr Asn Leu Lys Thr His Val Ala Val Pro Glu Thr Ala Leu Leu 
                185                 190                 195 

Gln Thr Val Ala Asn Leu Asp Thr Leu Val Ala Val Ile Glu Cys 
                200                 205                 210 

Gln Gln Pro Glu Ala Asp Leu Tyr Arg Phe Met Gly Arg Met Ile 
                215                 220                 225 

Ile Thr Gln Gln Met Glu Glu Ile Val Arg Pro Leu Gly Pro Glu 
                230                 235                 240 

Ser Leu Leu Leu Arg Gly Ala Arg Leu Lys Asn Thr Lys Glu Ile 
                245                 250                 255 

Phe Gly Val Ala Val Tyr Thr Gly Met Glu Thr Lys Met Ala Leu 
                260                 265                 270 

Asn Tyr Lys Ser Lys Ser Gln Lys Arg Ser Ala Val Glu Lys Ser 
                275                 280                 285 

Met Asn Thr Phe Leu Ile Ile Tyr Leu Val Ile Leu Ile Ser Glu 
                290                 295                 300 

Ala Val Ile Ser Thr Ile Leu Lys Tyr Thr Trp Gln Ala Glu Glu 
                305                 310                 315 

Lys Trp Asp Glu Pro Trp Tyr Asn Gln Lys Thr Glu His Gln Arg 
                320                 325                 330 

Asn Ser Ser Lys Val Glu Tyr Val Phe Thr Asp Lys Thr Gly Thr 
                335                 340                 345 

Leu Thr Glu Asn Glu Met Gln Phe Arg Glu Cys Ser Ile Asn Gly 
                350                 355                 360 

Met Lys Tyr Gln Glu Ile Asn Gly Arg Leu Val Pro Glu Gly Pro 
                365                 370                 375 

Thr Pro Asp Ser Ser Glu Gly Asn Leu Ser Tyr Leu Ser Ser Leu 
                380                 385                 390 

Ser His Leu Asn Asn Leu Ser His Leu Thr Thr Ser Ser Ser Phe 
                395                 400                 405 

Arg Thr Ser Pro Glu Asn Glu Thr Glu Leu Ile Lys Glu His Asp 
                410                 415                 420 

Leu Phe Phe Lys Ala Val Ser Leu Cys His Thr Val Gln Ile Ser 
                425                 430                 435 

Asn Val Gln Thr Asp Cys Thr Gly Asp Gly Pro Trp Gln Ser Asn 
                440                 445                 450 

Leu Ala Pro Ser Gln Leu Glu Tyr Tyr Ala Ser Ser Pro Asp Glu 
                455                 460                 465 

Lys Ala Leu Val Glu Ala Ala Ala Arg Ile Gly Ile Val Phe Ile 
                470                 475                 480 

Gly Asn Ser Glu Glu Thr Met Glu Val Lys Thr Leu Gly Lys Leu 
                485                 490                 495 

Glu Arg Tyr Lys Leu Leu His Ile Leu Glu Phe Asp Ser Asp Arg 
                500                 505                 510 

Arg Arg Met Ser Val Ile Val Gln Ala Pro Ser Gly Glu Lys Leu 
                515                 520                 525 

Leu Phe Ala Lys Gly Ala Glu Ser Ser Ile Leu Pro Lys Cys Ile 
                530                 535                 540 

Gly Gly Glu Ile Glu Lys Thr Arg Ile His Val Asp Glu Phe Ala 
                545                 550                 555 

Leu Lys Gly Leu Arg Thr Leu Cys Ile Ala Tyr Arg Lys Phe Thr 
                560                 565                 570 

Ser Lys Glu Tyr Glu Glu Ile Asp Lys Arg Ile Phe Glu Ala Arg 
                575                 580                 585 

Thr Ala Leu Gln Gln Arg Glu Glu Lys Leu Ala Ala Val Phe Gln 
                590                 595                 600 

Phe Ile Glu Lys Asp Leu Ile Leu Leu Gly Ala Thr Ala Val Glu 
                605                 610                 615 

Asp Arg Leu Gln Asp Lys Val Arg Glu Thr Ile Glu Ala Leu Arg 
                620                 625                 630 

Met Ala Gly Ile Lys Val Trp Val Leu Thr Gly Asp Lys His Glu 
                635                 640                 645 

Thr Ala Val Ser Val Ser Leu Ser Cys Gly His Phe His Arg Thr 
                650                 655                 660 

Met Asn Ile Leu Glu Leu Ile Asn Gln Lys Ser Asp Ser Glu Cys 
                665                 670                 675 

Ala Glu Gln Leu Arg Gln Leu Ala Arg Arg Ile Thr Glu Asp His 
                680                 685                 690 

Val Ile Gln His Gly Leu Val Val Asp Gly Thr Ser Leu Ser Leu 
                695                 700                 705 

Ala Leu Arg Glu His Glu Lys Leu Phe Met Glu Val Cys Arg Asn 
                710                 715                 720 

Cys Ser Ala Val Leu Cys Cys Arg Met Ala Pro Leu Gln Lys Ala 
                725                 730                 735 

Lys Val Ile Arg Leu Ile Lys Ile Ser Pro Glu Lys Pro Ile Thr 
                740                 745                 750 

Leu Ala Val Gly Asp Gly Ala Asn Asp Val Ser Met Ile Gln Glu 
                755                 760                 765 

Ala His Val Gly Ile Gly Ile Met Gly Lys Glu Gly Arg Gln Ala 
                770                 775                 780 

Ala Arg Asn Ser Asp Tyr Ala Ile Ala Arg Phe Lys Phe Leu Ser 
                785                 790                 795 

Lys Leu Leu Phe Val His Gly His Phe Tyr Tyr Ile Arg Ile Ala 
                800                 805                 810 

Thr Leu Val Gln Tyr Phe Phe Tyr Lys Asn Val Cys Phe Ile Thr 
                815                 820                 825 

Pro Gln Phe Leu Tyr Gln Phe Tyr Cys Leu Phe Ser Gln Gln Thr 
                830                 835                 840 

Leu Tyr Asp Ser Val Tyr Leu Thr Leu Tyr Asn Ile Cys Phe Thr 
                845                 850                 855 

Ser Leu Pro Ile Leu Ile Tyr Ser Leu Leu Glu Gln His Val Asp 
                860                 865                 870 

Pro His Val Leu Gln Asn Lys Pro Thr Leu Tyr Arg Asp Ile Ser 
                875                 880                 885 

Lys Asn Arg Leu Leu Ser Ile Lys Thr Phe Leu Tyr Trp Thr Ile 
                890                 895                 900 

Leu Gly Phe Ser His Ala Phe Ile Phe Phe Phe Gly Ser Tyr Leu 
                905                 910                 915 

Leu Ile Gly Lys Asp Thr Ser Leu Leu Gly Asn Gly Gln Met Phe 
                920                 925                 930 

Gly Asn Trp Thr Phe Gly Thr Leu Val Phe Thr Val Met Val Ile 
                935                 940                 945 

Thr Val Thr Val Lys Met Ala Leu Glu Thr His Phe Trp Thr Trp 
                950                 955                 960 

Ile Asn His Leu Val Thr Trp Gly Ser Ile Ile Phe Tyr Phe Val 
                965                 970                 975 

Phe Ser Leu Phe Tyr Gly Gly Ile Leu Trp Pro Phe Leu Gly Ser 
                980                 985                 990 

Gln Asn Met Tyr Phe Val Phe Ile Gln Leu Leu Ser Ser Gly Ser 
                995                 1000                1005 

Ala Trp Phe Ala Ile Ile Leu Met Val Val Thr Cys Leu Phe Leu 
                1010                1015                1020 

Asp Ile Ile Lys Lys Val Phe Asp Arg His Leu His Pro Thr Ser 
                1025                1030                1035 

Thr Glu Lys Ala Gln Leu Thr Glu Thr Asn Ala Gly Ile Lys Cys 
                1040                1045                1050 

Leu Asp Ser Met Cys Cys Phe Pro Glu Gly Glu Ala Ala Cys Ala 
                1055                1060                1065 

Ser Val Gly Arg Met Leu Glu Arg Val Ile Gly Arg Cys Ser Pro 
                1070                1075                1080 

Thr His Ile Ser Arg Cys Glu Ile Ser Leu Ser Ser Leu Cys Cys 
                1085                1090                1095 

Arg 

 
           
             21  
             707  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477720CD1  
             
           
            21 

Met Ala Leu Gln Met Phe Val Thr Tyr Ser Pro Trp Asn Cys Leu 
1               5                   10                  15 

Leu Leu Leu Val Ala Leu Glu Cys Ser Glu Ala Ser Ser Asp Leu 
                20                  25                  30 

Asn Glu Ser Ala Asn Ser Thr Ala Gln Tyr Ala Ser Asn Ala Trp 
                35                  40                  45 

Phe Ala Ala Ala Ser Ser Glu Pro Glu Glu Gly Ile Ser Val Phe 
                50                  55                  60 

Glu Leu Asp Tyr Asp Tyr Val Gln Ile Pro Tyr Glu Val Thr Leu 
                65                  70                  75 

Trp Ile Leu Leu Ala Ser Leu Ala Lys Ile Gly Phe His Leu Tyr 
                80                  85                  90 

His Arg Leu Pro Gly Leu Met Pro Glu Ser Cys Leu Leu Ile Leu 
                95                  100                 105 

Val Gly Ala Leu Val Gly Gly Ile Ile Phe Gly Thr Asp His Lys 
                110                 115                 120 

Ser Pro Pro Val Met Asp Ser Ser Ile Tyr Phe Leu Tyr Leu Leu 
                125                 130                 135 

Pro Pro Ile Val Leu Glu Gly Gly Tyr Phe Met Pro Thr Arg Pro 
                140                 145                 150 

Phe Phe Glu Asn Ile Gly Ser Ile Leu Trp Trp Ala Val Leu Gly 
                155                 160                 165 

Ala Leu Ile Asn Ala Leu Gly Ile Gly Leu Ser Leu Tyr Leu Ile 
                170                 175                 180 

Cys Gln Val Lys Ala Phe Gly Leu Gly Asp Val Asn Leu Leu Gln 
                185                 190                 195 

Asn Leu Leu Phe Gly Ser Leu Ile Ser Ala Val Asp Pro Val Ala 
                200                 205                 210 

Val Leu Ala Val Phe Glu Glu Ala Arg Val Asn Glu Gln Leu Tyr 
                215                 220                 225 

Met Met Ile Phe Gly Glu Ala Leu Leu Asn Asp Gly Ile Thr Val 
                230                 235                 240 

Val Leu Tyr Asn Met Leu Ile Ala Phe Thr Lys Met His Lys Phe 
                245                 250                 255 

Glu Asp Ile Glu Thr Val Asp Ile Leu Ala Gly Cys Ala Arg Phe 
                260                 265                 270 

Ile Val Val Gly Leu Gly Gly Val Leu Phe Gly Ile Val Phe Gly 
                275                 280                 285 

Phe Ile Ser Ala Phe Ile Thr Arg Phe Thr Gln Asn Ile Ser Ala 
                290                 295                 300 

Ile Glu Pro Leu Ile Val Phe Met Phe Ser Tyr Leu Ser Tyr Leu 
                305                 310                 315 

Ala Ala Glu Thr Leu Tyr Leu Ser Gly Ile Leu Ala Ile Thr Ala 
                320                 325                 330 

Cys Ala Val Thr Met Lys Lys Tyr Val Glu Glu Asn Val Ser Gln 
                335                 340                 345 

Thr Ser Tyr Thr Thr Ile Lys Tyr Phe Met Lys Met Leu Ser Ser 
                350                 355                 360 

Val Ser Glu Thr Leu Ile Phe Ile Phe Met Gly Val Ser Thr Val 
                365                 370                 375 

Gly Lys Asn His Glu Trp Asn Trp Ala Phe Ile Cys Phe Thr Leu 
                380                 385                 390 

Ala Phe Cys Gln Ile Trp Arg Ala Ile Ser Val Phe Ala Leu Phe 
                395                 400                 405 

Tyr Ile Ser Asn Gln Phe Arg Thr Phe Pro Phe Ser Ile Lys Asp 
                410                 415                 420 

Gln Cys Ile Ile Phe Tyr Ser Gly Val Arg Gly Ala Gly Ser Phe 
                425                 430                 435 

Ser Leu Ala Phe Leu Leu Pro Leu Ser Leu Phe Pro Arg Lys Lys 
                440                 445                 450 

Met Phe Val Thr Ala Thr Leu Val Val Ile Tyr Phe Thr Val Phe 
                455                 460                 465 

Ile Gln Gly Ile Thr Val Gly Pro Leu Val Arg Tyr Leu Asp Val 
                470                 475                 480 

Lys Lys Thr Asn Lys Lys Glu Ser Ile Asn Glu Glu Leu His Ile 
                485                 490                 495 

Arg Leu Met Asp His Leu Lys Ala Gly Ile Glu Asp Val Cys Gly 
                500                 505                 510 

His Trp Ser His Tyr Gln Val Arg Asp Lys Phe Lys Lys Phe Asp 
                515                 520                 525 

His Arg Tyr Leu Arg Lys Ile Leu Ile Arg Lys Asn Leu Pro Lys 
                530                 535                 540 

Ser Ser Ile Val Ser Leu Tyr Lys Lys Leu Glu Met Lys Gln Ala 
                545                 550                 555 

Ile Glu Met Val Glu Thr Gly Ile Leu Ser Ser Thr Ala Phe Ser 
                560                 565                 570 

Ile Pro His Gln Ala Gln Arg Ile Gln Gly Ile Lys Arg Leu Ser 
                575                 580                 585 

Pro Glu Asp Val Glu Ser Ile Arg Asp Ile Leu Thr Ser Asn Met 
                590                 595                 600 

Tyr Gln Val Arg Gln Arg Thr Leu Ser Tyr Asn Lys Tyr Asn Leu 
                605                 610                 615 

Lys Pro Gln Thr Ser Glu Lys Gln Ala Lys Glu Ile Leu Ile Arg 
                620                 625                 630 

Arg Gln Asn Thr Leu Arg Glu Ser Met Arg Lys Gly His Ser Leu 
                635                 640                 645 

Pro Trp Gly Lys Pro Ala Gly Thr Lys Asn Ile Arg Tyr Leu Ser 
                650                 655                 660 

Tyr Pro Tyr Gly Asn Pro Gln Ser Ala Gly Arg Asp Thr Arg Ala 
                665                 670                 675 

Ala Gly Phe Ser Gly Lys Leu Pro Thr Trp Leu Leu Cys Cys Phe 
                680                 685                 690 

Ser Val Glu Ser Gly Gly Lys Tyr Leu Gly Val Trp Ala Lys Arg 
                695                 700                 705 

Gln His 

 
           
             22  
             729  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477852CD1  
             
           
            22 

Met Gly Gly Phe Leu Pro Lys Ala Glu Gly Pro Gly Ser Gln Leu 
1               5                   10                  15 

Gln Lys Leu Leu Pro Ser Phe Leu Val Arg Glu Gln Asp Trp Asp 
                20                  25                  30 

Gln His Leu Asp Lys Leu His Met Leu Gln Gln Lys Arg Ile Leu 
                35                  40                  45 

Glu Ser Pro Leu Leu Arg Ala Ser Lys Glu Asn Asp Leu Ser Val 
                50                  55                  60 

Leu Arg Gln Leu Leu Leu Asp Cys Thr Cys Asp Val Arg Gln Arg 
                65                  70                  75 

Gly Ala Leu Gly Glu Thr Ala Leu His Ile Ala Ala Leu Tyr Asp 
                80                  85                  90 

Asn Leu Glu Ala Ala Leu Val Leu Met Glu Ala Ala Pro Glu Leu 
                95                  100                 105 

Val Phe Glu Pro Thr Thr Cys Glu Ala Phe Ala Gly Gln Thr Ala 
                110                 115                 120 

Leu His Ile Ala Val Val Asn Gln Asn Val Asn Leu Val Arg Ala 
                125                 130                 135 

Leu Leu Thr Arg Arg Ala Ser Val Ser Ala Arg Ala Thr Gly Thr 
                140                 145                 150 

Ala Phe Arg Arg Ser Pro Arg Asn Leu Ile Tyr Phe Gly Glu His 
                155                 160                 165 

Pro Leu Ser Phe Ala Ala Cys Val Asn Ser Glu Glu Ile Val Arg 
                170                 175                 180 

Leu Leu Ile Glu His Gly Ala Asp Ile Arg Ala Gln Asp Ser Leu 
                185                 190                 195 

Gly Asn Thr Val Leu His Ile Leu Ile Leu Gln Pro Asn Lys Thr 
                200                 205                 210 

Phe Ala Cys Gln Met Tyr Asn Leu Leu Leu Ser Tyr Asp Gly His 
                215                 220                 225 

Gly Asp His Leu Gln Pro Leu Asp Leu Val Pro Asn His Gln Gly 
                230                 235                 240 

Leu Thr Pro Phe Lys Leu Ala Gly Val Glu Gly Asn Thr Val Met 
                245                 250                 255 

Phe Gln His Leu Met Gln Lys Arg Arg His Ile Gln Trp Thr Tyr 
                260                 265                 270 

Gly Pro Leu Thr Ser Ile Leu Tyr Asp Leu Thr Glu Ile Asp Ser 
                275                 280                 285 

Trp Gly Glu Glu Leu Ser Phe Leu Glu Leu Val Val Ser Ser Asp 
                290                 295                 300 

Lys Arg Glu Ala Arg Gln Ile Leu Glu Gln Thr Pro Val Lys Glu 
                305                 310                 315 

Leu Val Ser Phe Lys Trp Asn Lys Tyr Gly Arg Pro Tyr Phe Cys 
                320                 325                 330 

Ile Leu Ala Ala Leu Tyr Leu Leu Tyr Met Ile Cys Phe Thr Thr 
                335                 340                 345 

Cys Cys Val Tyr Arg Pro Leu Lys Phe Arg Gly Gly Asn Arg Thr 
                350                 355                 360 

His Ser Arg Asp Ile Thr Ile Leu Gln Gln Lys Leu Leu Gln Glu 
                365                 370                 375 

Ala Tyr Glu Thr Arg Glu Asp Ile Ile Arg Leu Val Gly Glu Leu 
                380                 385                 390 

Val Ser Ile Val Gly Ala Val Ile Ile Leu Leu Leu Glu Ile Pro 
                395                 400                 405 

Asp Ile Phe Arg Val Gly Ala Ser Arg Tyr Phe Gly Lys Thr Ile 
                410                 415                 420 

Leu Gly Gly Pro Phe His Val Ile Met Ile Thr Tyr Ala Ser Leu 
                425                 430                 435 

Val Leu Val Thr Met Val Met Arg Leu Thr Asn Thr Asn Gly Glu 
                440                 445                 450 

Val Val Pro Met Ser Phe Ala Leu Val Leu Gly Trp Cys Ser Val 
                455                 460                 465 

Met Tyr Phe Thr Arg Gly Phe Gln Met Leu Gly Pro Phe Thr Ile 
                470                 475                 480 

Met Ile Gln Lys Met Ile Phe Gly Asp Leu Met Arg Phe Cys Trp 
                485                 490                 495 

Leu Met Ala Val Val Ile Leu Gly Phe Ala Ser Ala Phe Tyr Ile 
                500                 505                 510 

Ile Phe Gln Thr Glu Asp Pro Thr Ser Leu Gly Gln Phe Tyr Asp 
                515                 520                 525 

Tyr Pro Met Ala Leu Phe Thr Thr Phe Glu Leu Phe Leu Thr Val 
                530                 535                 540 

Ile Asp Ala Pro Ala Asn Tyr Asp Val Asp Leu Pro Phe Met Phe 
                545                 550                 555 

Ser Ile Val Asn Phe Ala Phe Ala Ile Ile Ala Thr Leu Leu Met 
                560                 565                 570 

Leu Asn Leu Phe Ile Ala Met Met Gly Asp Thr His Trp Arg Val 
                575                 580                 585 

Ala Gln Glu Arg Asp Glu Leu Trp Arg Ala Gln Val Val Ala Thr 
                590                 595                 600 

Thr Val Met Leu Glu Arg Lys Leu Pro Arg Cys Leu Trp Pro Arg 
                605                 610                 615 

Ser Gly Ile Cys Gly Cys Glu Phe Gly Leu Gly Asp Arg Trp Phe 
                620                 625                 630 

Leu Arg Val Glu Asn His Asn Asp Gln Asn Pro Leu Arg Val Leu 
                635                 640                 645 

Arg Tyr Val Glu Val Phe Lys Asn Ser Asp Lys Glu Asp Asp Gln 
                650                 655                 660 

Glu His Pro Ser Glu Lys Gln Pro Ser Gly Ala Glu Ser Gly Thr 
                665                 670                 675 

Leu Ala Arg Ala Ser Leu Ala Leu Pro Thr Ser Ser Leu Ser Arg 
                680                 685                 690 

Thr Ala Ser Gln Ser Ser Ser His Arg Gly Trp Glu Ile Leu Arg 
                695                 700                 705 

Gln Asn Thr Leu Gly His Leu Asn Leu Gly Leu Asn Leu Ser Glu 
                710                 715                 720 

Gly Asp Gly Glu Glu Val Tyr His Phe 
                725 

 
           
             23  
             492  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1471717CD1  
             
           
            23 

Met Ala Thr Lys Pro Thr Glu Pro Val Thr Ile Leu Ser Leu Arg 
1               5                   10                  15 

Lys Leu Ser Leu Gly Thr Ala Glu Pro Gln Val Lys Glu Pro Lys 
                20                  25                  30 

Thr Phe Thr Val Glu Asp Ala Val Glu Thr Ile Gly Phe Gly Arg 
                35                  40                  45 

Phe His Ile Ala Leu Phe Leu Ile Met Gly Ser Thr Gly Val Val 
                50                  55                  60 

Glu Ala Met Glu Ile Met Leu Ile Ala Val Val Ser Pro Val Ile 
                65                  70                  75 

Arg Cys Glu Trp Gln Leu Glu Asn Trp Gln Val Ala Leu Val Thr 
                80                  85                  90 

Thr Met Val Phe Phe Gly Tyr Met Val Phe Ser Ile Leu Phe Gly 
                95                  100                 105 

Leu Leu Ala Asp Arg Tyr Gly Arg Trp Lys Ile Leu Leu Ile Ser 
                110                 115                 120 

Phe Leu Trp Gly Ala Tyr Phe Ser Leu Leu Thr Ser Phe Ala Pro 
                125                 130                 135 

Ser Tyr Ile Trp Phe Val Phe Leu Arg Thr Met Val Gly Cys Gly 
                140                 145                 150 

Val Ser Gly His Ser Gln Gly Leu Ile Ile Lys Thr Glu Phe Leu 
                155                 160                 165 

Pro Thr Lys Tyr Arg Gly Tyr Met Leu Pro Leu Ser Gln Val Phe 
                170                 175                 180 

Trp Leu Ala Gly Ser Leu Leu Ile Ile Gly Leu Ala Ser Val Ile 
                185                 190                 195 

Ile Pro Thr Ile Gly Trp Arg Trp Leu Ile Arg Val Ala Ser Ile 
                200                 205                 210 

Pro Gly Ile Ile Leu Ile Val Ala Phe Lys Phe Ile Pro Glu Ser 
                215                 220                 225 

Ala Arg Phe Asn Val Ser Thr Gly Asn Thr Arg Ala Ala Leu Ala 
                230                 235                 240 

Thr Leu Glu Arg Val Ala Lys Met Asn Arg Ser Val Met Pro Glu 
                245                 250                 255 

Gly Lys Leu Val Glu Pro Val Leu Glu Lys Arg Gly Arg Phe Ala 
                260                 265                 270 

Asp Leu Leu Asp Ala Lys Tyr Leu Arg Thr Thr Leu Gln Ile Trp 
                275                 280                 285 

Val Ile Trp Leu Gly Ile Ser Phe Ala Tyr Tyr Gly Val Ile Leu 
                290                 295                 300 

Ala Ser Ala Glu Leu Leu Glu Arg Asp Leu Val Cys Gly Ser Lys 
                305                 310                 315 

Ser Asp Ser Ala Val Val Val Thr Gly Gly Asp Ser Gly Glu Ser 
                320                 325                 330 

Gln Ser Pro Cys Tyr Cys His Met Phe Ala Pro Ser Asp Tyr Arg 
                335                 340                 345 

Thr Met Ile Ile Ser Thr Ile Gly Glu Ile Ala Leu Asn Pro Leu 
                350                 355                 360 

Asn Ile Leu Gly Ile Asn Phe Leu Gly Arg Arg Leu Ser Leu Ser 
                365                 370                 375 

Ile Thr Met Gly Cys Thr Ala Leu Phe Cys Leu Leu Leu Asn Ile 
                380                 385                 390 

Cys Thr Ser Ser Ala Gly Leu Ile Gly Phe Leu Phe Met Leu Arg 
                395                 400                 405 

Ala Leu Val Ala Ala Asn Phe Asn Thr Val Tyr Ile Tyr Thr Ala 
                410                 415                 420 

Glu Val Tyr Pro Thr Thr Met Arg Ala Leu Gly Met Gly Thr Ser 
                425                 430                 435 

Gly Ser Leu Cys Arg Ile Gly Ala Met Val Ala Pro Phe Ile Ser 
                440                 445                 450 

Gln Val Leu Met Ser Ala Ser Ile Leu Gly Ala Leu Cys Leu Phe 
                455                 460                 465 

Ser Ser Val Cys Val Val Cys Ala Ile Ser Ala Phe Thr Leu Pro 
                470                 475                 480 

Ile Glu Thr Lys Gly Arg Ala Leu Gln Gln Ile Lys 
                485                 490 

 
           
             24  
             1494  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3874406CD1  
             
           
            24 

Met Asn Met Lys Gln Lys Ser Val Tyr Gln Gln Thr Lys Ala Leu 
1               5                   10                  15 

Leu Cys Lys Asn Phe Leu Lys Lys Trp Arg Met Lys Arg Glu Ser 
                20                  25                  30 

Leu Leu Glu Trp Gly Leu Ser Ile Leu Leu Gly Leu Cys Ile Ala 
                35                  40                  45 

Leu Phe Ser Ser Ser Met Arg Asn Val Gln Phe Pro Gly Met Ala 
                50                  55                  60 

Pro Gln Asn Leu Gly Arg Val Asp Lys Phe Asn Ser Ser Ser Leu 
                65                  70                  75 

Met Val Val Tyr Thr Pro Ile Ser Asn Leu Thr Gln Gln Ile Met 
                80                  85                  90 

Asn Lys Thr Ala Leu Ala Pro Leu Leu Lys Gly Thr Ser Val Ile 
                95                  100                 105 

Gly Ala Pro Asn Lys Thr His Met Asp Glu Ile Leu Leu Glu Asn 
                110                 115                 120 

Leu Pro Tyr Ala Met Gly Ile Ile Phe Asn Glu Thr Phe Ser Tyr 
                125                 130                 135 

Lys Leu Ile Phe Phe Gln Gly Tyr Asn Ser Pro Leu Trp Lys Glu 
                140                 145                 150 

Asp Phe Ser Ala His Cys Trp Asp Gly Tyr Gly Glu Phe Ser Cys 
                155                 160                 165 

Thr Leu Thr Lys Tyr Trp Asn Arg Gly Phe Val Ala Leu Gln Thr 
                170                 175                 180 

Ala Ile Asn Thr Ala Ile Ile Glu Val Ala Leu Val Phe Leu Met 
                185                 190                 195 

Ser Val Leu Leu Lys Lys Ala Val Leu Thr Asn Leu Val Val Phe 
                200                 205                 210 

Leu Leu Thr Leu Phe Trp Gly Cys Leu Gly Phe Thr Val Phe Tyr 
                215                 220                 225 

Glu Gln Leu Pro Ser Ser Leu Glu Trp Ile Leu Asn Ile Cys Ser 
                230                 235                 240 

Pro Phe Ala Phe Thr Thr Gly Met Ile Gln Ile Ile Lys Leu Asp 
                245                 250                 255 

Tyr Asn Leu Asn Gly Val Ile Phe Pro Asp Pro Ser Gly Asp Ser 
                260                 265                 270 

Tyr Thr Met Ile Ala Thr Phe Ser Met Leu Leu Leu Asp Gly Leu 
                275                 280                 285 

Ile Tyr Leu Leu Leu Ala Leu Tyr Phe Asp Lys Ile Leu Pro Tyr 
                290                 295                 300 

Gly Asp Glu Arg His Tyr Ser Pro Leu Phe Phe Leu Asn Ser Ser 
                305                 310                 315 

Ser Cys Phe Gln His Gln Arg Thr Asn Ala Lys Val Ile Glu Lys 
                320                 325                 330 

Glu Ile Asp Ala Glu His Pro Ser Asp Asp Tyr Phe Glu Pro Val 
                335                 340                 345 

Ala Pro Glu Phe Gln Gly Lys Glu Ala Ile Arg Ile Arg Asn Val 
                350                 355                 360 

Lys Lys Glu Tyr Lys Gly Lys Ser Gly Lys Val Glu Ala Leu Lys 
                365                 370                 375 

Gly Leu Leu Phe Asp Ile Tyr Glu Gly Gln Ile Thr Ala Ile Leu 
                380                 385                 390 

Gly His Ser Gly Ala Gly Lys Ser Ser Leu Leu Asn Ile Leu Asn 
                395                 400                 405 

Gly Leu Ser Val Pro Thr Glu Gly Ser Val Thr Ile Tyr Asn Lys 
                410                 415                 420 

Asn Leu Ser Glu Met Gln Asp Leu Glu Glu Ile Arg Lys Ile Thr 
                425                 430                 435 

Gly Val Cys Pro Gln Phe Asn Val Gln Phe Asp Ile Leu Thr Val 
                440                 445                 450 

Lys Glu Asn Leu Ser Leu Phe Ala Lys Ile Lys Gly Ile His Leu 
                455                 460                 465 

Lys Glu Val Glu Gln Glu Val Gln Arg Ile Leu Leu Glu Leu Asp 
                470                 475                 480 

Met Gln Asn Ile Gln Asp Asn Leu Ala Lys His Leu Ser Glu Gly 
                485                 490                 495 

Gln Lys Arg Lys Leu Thr Phe Gly Ile Thr Ile Leu Gly Asp Pro 
                500                 505                 510 

Gln Ile Leu Leu Leu Asp Glu Pro Thr Thr Gly Leu Asp Pro Phe 
                515                 520                 525 

Ser Arg Asp Gln Val Trp Ser Leu Leu Arg Glu Arg Arg Ala Asp 
                530                 535                 540 

His Val Ile Leu Phe Ser Thr Gln Ser Met Asp Glu Ala Asp Ile 
                545                 550                 555 

Leu Ala Asp Arg Lys Val Ile Met Ser Asn Gly Arg Leu Lys Cys 
                560                 565                 570 

Ala Gly Ser Ser Ile Phe Leu Lys Arg Arg Trp Gly Leu Gly Tyr 
                575                 580                 585 

His Leu Ser Leu His Arg Asn Glu Ile Cys Asn Pro Glu Gln Ile 
                590                 595                 600 

Thr Ser Phe Ile Thr His His Ile Pro Asp Ala Lys Leu Lys Thr 
                605                 610                 615 

Glu Asn Lys Glu Lys Leu Val Tyr Thr Leu Pro Leu Glu Arg Thr 
                620                 625                 630 

Asn Thr Phe Pro Asp Leu Phe Ser Asp Leu Asp Lys Cys Ser Asp 
                635                 640                 645 

Gln Gly Val Thr Gly Tyr Asp Ile Ser Met Ser Thr Leu Asn Glu 
                650                 655                 660 

Val Phe Met Lys Leu Glu Gly Gln Ser Thr Ile Glu Gln Asp Phe 
                665                 670                 675 

Glu Gln Val Glu Met Ile Arg Asp Ser Glu Ser Leu Asn Glu Met 
                680                 685                 690 

Glu Leu Ala His Ser Ser Phe Ser Glu Met Gln Thr Ala Val Ser 
                695                 700                 705 

Asp Met Gly Leu Trp Arg Met Gln Val Phe Ala Met Ala Arg Leu 
                710                 715                 720 

Arg Phe Leu Lys Leu Lys Arg Gln Thr Lys Val Leu Leu Thr Leu 
                725                 730                 735 

Leu Leu Val Phe Gly Ile Ala Ile Phe Pro Leu Ile Val Glu Asn 
                740                 745                 750 

Ile Ile Tyr Ala Met Leu Asn Glu Lys Ile Asp Trp Glu Phe Lys 
                755                 760                 765 

Asn Glu Leu Tyr Phe Leu Ser Pro Gly Gln Leu Pro Gln Glu Pro 
                770                 775                 780 

Arg Thr Ser Leu Leu Ile Ile Asn Asn Thr Glu Ser Asn Ile Glu 
                785                 790                 795 

Asp Phe Ile Lys Ser Leu Lys His Gln Asn Ile Leu Leu Glu Val 
                800                 805                 810 

Asp Asp Phe Glu Asn Arg Asn Gly Thr Asp Gly Leu Ser Tyr Asn 
                815                 820                 825 

Gly Ala Ile Ile Val Ser Gly Lys Gln Lys Asp Tyr Arg Phe Ser 
                830                 835                 840 

Val Val Cys Asn Thr Lys Arg Leu His Cys Phe Pro Ile Leu Met 
                845                 850                 855 

Asn Ile Ile Ser Asn Gly Leu Leu Gln Met Phe Asn His Thr Gln 
                860                 865                 870 

His Ile Arg Ile Glu Ser Ser Pro Phe Pro Leu Ser His Ile Gly 
                875                 880                 885 

Leu Trp Thr Gly Leu Pro Asp Gly Ser Phe Phe Leu Phe Leu Val 
                890                 895                 900 

Leu Cys Ser Ile Ser Pro Tyr Ile Thr Met Gly Ser Ile Ser Asp 
                905                 910                 915 

Tyr Lys Lys Asn Ala Lys Ser Gln Leu Trp Ile Ser Gly Leu Tyr 
                920                 925                 930 

Thr Ser Ala Tyr Trp Cys Gly Gln Ala Leu Val Asp Val Ser Phe 
                935                 940                 945 

Phe Ile Leu Ile Leu Leu Leu Met Tyr Leu Ile Phe Tyr Ile Glu 
                950                 955                 960 

Asn Met Gln Tyr Leu Leu Ile Thr Ser Gln Ile Val Phe Ala Leu 
                965                 970                 975 

Val Ile Val Thr Pro Gly Tyr Ala Ala Ser Leu Val Phe Phe Ile 
                980                 985                 990 

Tyr Met Ile Ser Phe Ile Phe Arg Lys Arg Arg Lys Asn Ser Gly 
                995                 1000                1005 

Leu Trp Ser Phe Tyr Phe Phe Phe Ala Ser Thr Ile Met Phe Ser 
                1010                1015                1020 

Ile Thr Leu Ile Asn His Phe Asp Leu Ser Ile Leu Ile Thr Thr 
                1025                1030                1035 

Met Val Leu Val Pro Ser Tyr Thr Leu Leu Gly Phe Lys Thr Phe 
                1040                1045                1050 

Leu Glu Val Arg Asp Gln Glu His Tyr Arg Glu Phe Pro Glu Ala 
                1055                1060                1065 

Asn Phe Glu Leu Ser Ala Thr Asp Phe Leu Val Cys Phe Ile Pro 
                1070                1075                1080 

Tyr Phe Gln Thr Leu Leu Phe Val Phe Val Leu Arg Cys Met Glu 
                1085                1090                1095 

Leu Lys Cys Gly Lys Lys Arg Met Arg Lys Asp Pro Val Phe Arg 
                1100                1105                1110 

Ile Ser Pro Gln Ser Arg Asp Ala Lys Pro Asn Pro Glu Glu Pro 
                1115                1120                1125 

Ile Asp Glu Asp Glu Asp Ile Gln Thr Glu Arg Ile Arg Thr Val 
                1130                1135                1140 

Thr Ala Leu Thr Thr Ser Ile Leu Asp Glu Lys Pro Val Ile Ile 
                1145                1150                1155 

Ala Ser Cys Leu His Lys Glu Tyr Ala Gly Gln Lys Lys Ser Cys 
                1160                1165                1170 

Phe Ser Lys Arg Lys Lys Lys Ile Ala Ala Arg Asn Ile Ser Phe 
                1175                1180                1185 

Cys Val Gln Glu Gly Glu Ile Leu Gly Leu Leu Gly Pro Ser Gly 
                1190                1195                1200 

Ala Gly Lys Ser Ser Ser Ile Arg Met Ile Ser Gly Ile Thr Lys 
                1205                1210                1215 

Pro Thr Ala Gly Glu Val Glu Leu Lys Gly Cys Ser Ser Val Leu 
                1220                1225                1230 

Gly His Leu Gly Tyr Cys Pro Gln Glu Asn Val Leu Trp Pro Met 
                1235                1240                1245 

Leu Thr Leu Arg Glu His Leu Glu Val Tyr Ala Ala Val Lys Gly 
                1250                1255                1260 

Leu Arg Glu Ala Asp Ala Arg Leu Ala Ile Ala Arg Leu Val Ser 
                1265                1270                1275 

Ala Phe Lys Leu His Glu Gln Leu Asn Val Pro Val Gln Lys Leu 
                1280                1285                1290 

Thr Ala Gly Ile Thr Arg Lys Leu Cys Phe Val Leu Ser Leu Leu 
                1295                1300                1305 

Gly Asn Ser Pro Val Leu Leu Leu Asp Glu Pro Ser Thr Gly Ile 
                1310                1315                1320 

Asp Pro Thr Gly Gln Gln Gln Met Trp Gln Ala Ile Gln Ala Val 
                1325                1330                1335 

Val Lys Asn Thr Glu Arg Gly Val Leu Leu Thr Thr His Asn Leu 
                1340                1345                1350 

Ala Glu Ala Glu Ala Leu Cys Asp Arg Val Ala Ile Met Val Ser 
                1355                1360                1365 

Gly Arg Leu Arg Cys Ile Gly Ser Ile Gln His Leu Lys Asn Lys 
                1370                1375                1380 

Leu Gly Lys Asp Tyr Ile Leu Glu Leu Lys Val Lys Glu Thr Ser 
                1385                1390                1395 

Gln Val Thr Leu Val His Thr Glu Ile Leu Lys Leu Phe Pro Gln 
                1400                1405                1410 

Ala Ala Gly Gln Gln Arg Tyr Ser Ser Leu Leu Thr Tyr Lys Leu 
                1415                1420                1425 

Pro Val Ala Asp Val Tyr Pro Leu Ser Gln Thr Phe His Lys Leu 
                1430                1435                1440 

Glu Ala Val Lys His Asn Phe Asn Leu Glu Glu Tyr Ser Leu Ser 
                1445                1450                1455 

Gln Cys Thr Leu Glu Lys Val Phe Leu Glu Leu Ser Lys Glu Gln 
                1460                1465                1470 

Glu Val Gly Asn Phe Asp Glu Glu Ile Asp Thr Thr Met Arg Trp 
                1475                1480                1485 

Lys Leu Leu Pro His Ser Asp Glu Pro 
                1490 

 
           
             25  
             774  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 4599654CD1  
             
           
            25 

Met Glu Ala Glu Gln Arg Pro Ala Ala Gly Ala Ser Glu Gly Ala 
1               5                   10                  15 

Thr Pro Gly Leu Glu Ala Val Pro Pro Val Ala Pro Pro Pro Ala 
                20                  25                  30 

Thr Ala Ala Ser Gly Pro Ile Pro Lys Ser Gly Pro Glu Pro Lys 
                35                  40                  45 

Arg Arg His Leu Gly Thr Leu Leu Gln Pro Thr Val Asn Lys Phe 
                50                  55                  60 

Ser Leu Arg Val Phe Gly Ser His Lys Ala Val Glu Ile Glu Gln 
                65                  70                  75 

Glu Arg Val Lys Ser Ala Gly Ala Trp Ile Ile His Pro Tyr Ser 
                80                  85                  90 

Asp Phe Arg Phe Tyr Trp Asp Leu Ile Met Leu Leu Leu Met Val 
                95                  100                 105 

Gly Asn Leu Ile Val Leu Pro Val Gly Ile Thr Phe Phe Lys Glu 
                110                 115                 120 

Glu Asn Ser Pro Pro Trp Ile Val Phe Asn Val Leu Ser Asp Thr 
                125                 130                 135 

Phe Phe Leu Leu Asp Leu Val Leu Asn Phe Arg Thr Gly Ile Val 
                140                 145                 150 

Val Glu Glu Gly Ala Glu Ile Leu Leu Ala Pro Arg Ala Ile Arg 
                155                 160                 165 

Thr Arg Tyr Leu Arg Thr Trp Phe Leu Val Asp Leu Ile Ser Ser 
                170                 175                 180 

Ile Pro Val Asp Tyr Ile Phe Leu Val Val Glu Leu Glu Pro Arg 
                185                 190                 195 

Leu Asp Ala Glu Val Tyr Lys Thr Ala Arg Ala Leu Arg Ile Val 
                200                 205                 210 

Arg Phe Thr Lys Ile Leu Ser Leu Leu Arg Leu Leu Arg Leu Ser 
                215                 220                 225 

Arg Leu Ile Arg Tyr Ile His Gln Trp Glu Glu Ile Phe His Met 
                230                 235                 240 

Thr Tyr Asp Leu Ala Ser Ala Val Val Arg Ile Phe Asn Leu Ile 
                245                 250                 255 

Gly Met Met Leu Leu Leu Cys His Trp Asp Gly Cys Leu Gln Phe 
                260                 265                 270 

Leu Val Pro Met Leu Gln Asp Phe Pro Pro Asp Cys Trp Val Ser 
                275                 280                 285 

Ile Asn His Met Val Asn His Ser Trp Gly Arg Gln Tyr Ser His 
                290                 295                 300 

Ala Leu Phe Lys Ala Met Ser His Met Leu Cys Ile Gly Tyr Gly 
                305                 310                 315 

Gln Gln Ala Pro Val Gly Met Pro Asp Val Trp Leu Thr Met Leu 
                320                 325                 330 

Ser Met Ile Val Gly Ala Thr Cys Tyr Ala Met Phe Ile Gly His 
                335                 340                 345 

Ala Thr Ala Leu Ile Gln Ser Leu Asp Ser Ser Arg Arg Gln Tyr 
                350                 355                 360 

Gln Glu Lys Tyr Lys Gln Val Glu Gln Tyr Met Ser Phe His Lys 
                365                 370                 375 

Leu Pro Ala Asp Thr Arg Gln Arg Ile His Glu Tyr Tyr Glu His 
                380                 385                 390 

Arg Tyr Gln Gly Lys Met Phe Asp Glu Glu Ser Ile Leu Gly Glu 
                395                 400                 405 

Leu Ser Glu Pro Leu Arg Glu Glu Ile Ile Asn Phe Thr Cys Arg 
                410                 415                 420 

Gly Leu Val Ala His Met Pro Leu Phe Ala His Ala Asp Pro Ser 
                425                 430                 435 

Phe Val Thr Ala Val Leu Thr Lys Leu Arg Phe Glu Val Phe Gln 
                440                 445                 450 

Pro Gly Asp Leu Val Val Arg Glu Gly Ser Val Gly Arg Lys Met 
                455                 460                 465 

Tyr Phe Ile Gln His Gly Leu Leu Ser Val Leu Ala Arg Gly Ala 
                470                 475                 480 

Arg Asp Thr Arg Leu Thr Asp Gly Ser Tyr Phe Gly Glu Ile Cys 
                485                 490                 495 

Leu Leu Thr Arg Gly Arg Arg Thr Ala Ser Val Arg Ala Asp Thr 
                500                 505                 510 

Tyr Cys Arg Leu Tyr Ser Leu Ser Val Asp His Phe Asn Ala Val 
                515                 520                 525 

Leu Glu Glu Phe Pro Met Met Arg Arg Ala Phe Glu Thr Val Ala 
                530                 535                 540 

Met Asp Arg Leu Leu Arg Ile Gly Lys Lys Asn Ser Ile Leu Gln 
                545                 550                 555 

Arg Lys Arg Ser Glu Pro Ser Pro Gly Ser Ser Gly Gly Ile Met 
                560                 565                 570 

Glu Gln His Leu Val Gln His Asp Arg Asp Met Ala Arg Gly Val 
                575                 580                 585 

Arg Gly Arg Ala Pro Ser Thr Gly Ala Gln Leu Ser Gly Lys Pro 
                590                 595                 600 

Val Leu Trp Glu Pro Leu Val His Ala Pro Leu Gln Ala Ala Ala 
                605                 610                 615 

Val Thr Ser Asn Val Ala Ile Ala Leu Thr His Gln Arg Gly Pro 
                620                 625                 630 

Leu Pro Leu Ser Pro Asp Ser Pro Ala Thr Leu Leu Ala Arg Ser 
                635                 640                 645 

Ala Trp Arg Ser Ala Gly Ser Pro Ala Ser Pro Leu Val Pro Val 
                650                 655                 660 

Arg Ala Gly Pro Trp Ala Ser Thr Ser Arg Leu Pro Ala Pro Pro 
                665                 670                 675 

Ala Arg Thr Leu His Ala Ser Leu Ser Arg Ala Gly Arg Ser Gln 
                680                 685                 690 

Val Ser Leu Leu Gly Pro Pro Pro Gly Gly Gly Gly Arg Arg Leu 
                695                 700                 705 

Gly Pro Arg Gly Arg Pro Leu Ser Ala Ser Gln Pro Ser Leu Pro 
                710                 715                 720 

Gln Arg Ala Thr Gly Asp Gly Ser Pro Gly Arg Lys Gly Ser Gly 
                725                 730                 735 

Ser Glu Arg Leu Pro Pro Ser Gly Leu Leu Ala Lys Pro Pro Arg 
                740                 745                 750 

Thr Ala Gln Pro Pro Arg Pro Pro Val Pro Glu Pro Ala Thr Pro 
                755                 760                 765 

Arg Gly Leu Gln Leu Ser Ala Asn Met 
                770 

 
           
             26  
             614  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 5047435CD1  
             
           
            26 

Met Ala Glu Gly Glu Arg Gly Ala Asp Val Pro His Gly Leu Gly 
1               5                   10                  15 

Ala Trp Leu Ala Asp Val Ala Leu Ala Ala Leu Arg Ala Gly Gly 
                20                  25                  30 

Gln Gly Arg Arg Asp Arg Gly Gly Gly Gly Pro Glu Ser Leu Ser 
                35                  40                  45 

Gly Gly Ser Gly Val Gly Asp Ser Gly Gly Gly Cys Ala Pro Gly 
                50                  55                  60 

Pro Ser Ala Pro Pro Ala Arg Arg Arg Val Pro Leu Ala Met Gly 
                65                  70                  75 

His Ser Pro Pro Val Leu Pro Leu Cys Ala Ser Val Ser Leu Leu 
                80                  85                  90 

Gly Gly Leu Thr Phe Gly Tyr Glu Leu Ala Val Ile Ser Gly Ala 
                95                  100                 105 

Leu Leu Pro Leu Gln Leu Asp Phe Gly Leu Ser Cys Leu Glu Gln 
                110                 115                 120 

Glu Phe Leu Val Gly Ser Leu Leu Leu Gly Ala Leu Leu Ala Ser 
                125                 130                 135 

Leu Val Gly Gly Phe Leu Ile Asp Cys Tyr Gly Arg Lys Gln Ala 
                140                 145                 150 

Ile Leu Gly Ser Asn Leu Val Leu Leu Ala Gly Ser Leu Thr Leu 
                155                 160                 165 

Gly Leu Ala Gly Ser Leu Ala Trp Leu Val Leu Gly Arg Ala Val 
                170                 175                 180 

Val Gly Phe Ala Ile Ser Leu Ser Ser Met Ala Cys Cys Ile Tyr 
                185                 190                 195 

Val Ser Glu Leu Val Gly Pro Arg Gln Arg Gly Val Leu Val Ser 
                200                 205                 210 

Leu Tyr Glu Ala Gly Ile Thr Val Gly Ile Leu Leu Ser Tyr Ala 
                215                 220                 225 

Leu Asn Tyr Ala Leu Ala Gly Thr Pro Trp Gly Trp Arg His Met 
                230                 235                 240 

Phe Gly Trp Ala Thr Ala Pro Ala Val Leu Gln Ser Leu Ser Leu 
                245                 250                 255 

Leu Phe Leu Pro Ala Gly Thr Asp Glu Thr Ala Thr His Lys Asp 
                260                 265                 270 

Leu Ile Pro Leu Gln Gly Gly Glu Ala Pro Lys Leu Gly Pro Gly 
                275                 280                 285 

Arg Pro Arg Tyr Ser Phe Leu Asp Leu Phe Arg Ala Arg Asp Asn 
                290                 295                 300 

Met Arg Gly Arg Thr Thr Val Gly Leu Gly Leu Val Leu Phe Gln 
                305                 310                 315 

Gln Leu Thr Gly Gln Pro Asn Val Leu Cys Tyr Ala Ser Thr Ile 
                320                 325                 330 

Phe Ser Ser Val Gly Phe His Gly Gly Ser Ser Ala Val Leu Ala 
                335                 340                 345 

Ser Val Gly Leu Gly Ala Val Lys Val Ala Ala Thr Leu Thr Ala 
                350                 355                 360 

Met Gly Leu Val Asp Arg Ala Gly Arg Arg Ala Leu Leu Leu Ala 
                365                 370                 375 

Gly Cys Ala Leu Met Ala Leu Ser Val Ser Gly Ile Gly Leu Val 
                380                 385                 390 

Ser Phe Ala Val Pro Met Asp Ser Gly Pro Ser Cys Leu Ala Val 
                395                 400                 405 

Pro Asn Ala Thr Gly Gln Thr Gly Leu Pro Gly Asp Ser Gly Leu 
                410                 415                 420 

Leu Gln Asp Ser Ser Leu Pro Pro Ile Pro Arg Thr Asn Glu Asp 
                425                 430                 435 

Gln Arg Glu Pro Ile Leu Ser Thr Ala Lys Lys Thr Lys Pro His 
                440                 445                 450 

Pro Arg Ser Gly Asp Pro Ser Ala Pro Pro Arg Leu Ala Leu Ser 
                455                 460                 465 

Ser Ala Leu Pro Gly Pro Pro Leu Pro Ala Arg Gly His Ala Leu 
                470                 475                 480 

Leu Arg Trp Thr Ala Leu Leu Cys Leu Met Val Phe Val Ser Ala 
                485                 490                 495 

Phe Ser Phe Gly Phe Gly Pro Val Thr Trp Leu Val Leu Ser Glu 
                500                 505                 510 

Ile Tyr Pro Val Glu Ile Arg Gly Arg Ala Phe Ala Phe Cys Asn 
                515                 520                 525 

Ser Phe Asn Trp Ala Ala Asn Leu Phe Ile Ser Leu Ser Phe Leu 
                530                 535                 540 

Asp Leu Ile Gly Thr Ile Gly Leu Ser Trp Thr Phe Leu Leu Tyr 
                545                 550                 555 

Gly Leu Thr Ala Val Leu Gly Leu Gly Phe Ile Tyr Leu Phe Val 
                560                 565                 570 

Pro Glu Thr Lys Gly Gln Ser Leu Ala Glu Ile Asp Gln Gln Phe 
                575                 580                 585 

Gln Lys Arg Arg Phe Thr Leu Ser Phe Gly His Arg Gln Asn Ser 
                590                 595                 600 

Thr Gly Ile Pro Tyr Ser Arg Ile Glu Ile Ser Ala Ala Ser 
                605                 610 

 
           
             27  
             2180  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7475603CD1  
             
           
            27 

Met Arg Phe Arg Lys Gly Gln Glu Leu Pro Ala Ala Ala Pro His 
1               5                   10                  15 

Val Phe Ser Pro Thr Val Val Leu Thr Ser Leu Ser Arg Pro Leu 
                20                  25                  30 

Pro Ser Leu Thr Met Ala Phe Trp Thr Gln Leu Met Leu Leu Leu 
                35                  40                  45 

Trp Lys Asn Phe Met Tyr Arg Arg Arg Gln Pro Val Gln Leu Leu 
                50                  55                  60 

Val Glu Leu Leu Trp Pro Leu Phe Leu Phe Phe Ile Leu Val Ala 
                65                  70                  75 

Val Arg His Ser His Pro Pro Leu Glu His His Glu Cys His Phe 
                80                  85                  90 

Pro Asn Lys Pro Leu Pro Ser Ala Gly Thr Val Pro Trp Leu Gln 
                95                  100                 105 

Gly Leu Ile Cys Asn Val Asn Asn Thr Cys Phe Pro Gln Leu Thr 
                110                 115                 120 

Pro Gly Glu Glu Pro Gly Arg Leu Ser Asn Phe Asn Asp Ser Leu 
                125                 130                 135 

Val Ser Arg Leu Leu Ala Asp Ala Arg Thr Val Leu Gly Gly Ala 
                140                 145                 150 

Ser Ala His Arg Thr Leu Ala Gly Leu Gly Lys Leu Ile Ala Thr 
                155                 160                 165 

Leu Arg Ala Ala Arg Ser Thr Ala Gln Pro Gln Pro Thr Lys Gln 
                170                 175                 180 

Ser Pro Leu Glu Pro Pro Met Leu Asp Val Ala Glu Leu Leu Thr 
                185                 190                 195 

Ser Leu Leu Arg Thr Glu Ser Leu Gly Leu Ala Leu Gly Gln Ala 
                200                 205                 210 

Gln Glu Pro Leu His Ser Leu Leu Glu Ala Ala Glu Asp Leu Ala 
                215                 220                 225 

Gln Glu Leu Leu Ala Leu Arg Ser Leu Val Glu Leu Arg Ala Leu 
                230                 235                 240 

Leu Gln Arg Pro Arg Gly Thr Ser Gly Pro Leu Glu Leu Leu Ser 
                245                 250                 255 

Glu Ala Leu Cys Ser Val Arg Gly Pro Ser Ser Thr Val Gly Pro 
                260                 265                 270 

Ser Leu Asn Trp Tyr Glu Ala Ser Asp Leu Met Glu Leu Val Gly 
                275                 280                 285 

Gln Glu Pro Glu Ser Ala Leu Pro Asp Ser Ser Leu Ser Pro Ala 
                290                 295                 300 

Cys Ser Glu Leu Ile Gly Ala Leu Asp Ser His Pro Leu Ser Arg 
                305                 310                 315 

Leu Leu Trp Arg Arg Leu Lys Pro Leu Ile Leu Gly Lys Leu Leu 
                320                 325                 330 

Phe Ala Pro Asp Thr Pro Phe Thr Arg Lys Leu Met Ala Gln Val 
                335                 340                 345 

Asn Arg Thr Phe Glu Glu Leu Thr Leu Leu Arg Asp Val Arg Glu 
                350                 355                 360 

Val Trp Glu Met Leu Gly Pro Arg Ile Phe Thr Phe Met Asn Asp 
                365                 370                 375 

Ser Ser Asn Val Ala Met Leu Gln Arg Leu Leu Gln Met Gln Asp 
                380                 385                 390 

Glu Gly Arg Arg Gln Pro Arg Pro Gly Gly Arg Asp His Met Glu 
                395                 400                 405 

Ala Leu Arg Ser Phe Leu Asp Pro Gly Ser Gly Gly Tyr Ser Trp 
                410                 415                 420 

Gln Asp Ala His Ala Asp Val Gly His Leu Val Gly Thr Leu Gly 
                425                 430                 435 

Arg Val Thr Glu Cys Leu Ser Leu Asp Lys Leu Glu Ala Ala Pro 
                440                 445                 450 

Ser Glu Ala Ala Leu Val Ser Arg Ala Leu Gln Leu Leu Ala Glu 
                455                 460                 465 

His Arg Phe Trp Ala Gly Val Val Phe Leu Gly Pro Glu Asp Ser 
                470                 475                 480 

Ser Asp Pro Thr Glu His Pro Thr Pro Asp Leu Gly Pro Gly His 
                485                 490                 495 

Val Arg Ile Lys Ile Arg Met Asp Ile Asp Val Val Thr Arg Thr 
                500                 505                 510 

Asn Lys Ile Arg Asp Arg Phe Trp Asp Pro Gly Pro Ala Ala Asp 
                515                 520                 525 

Pro Leu Thr Asp Leu Arg Tyr Val Trp Gly Gly Phe Val Tyr Leu 
                530                 535                 540 

Gln Asp Leu Val Glu Arg Ala Ala Val Arg Val Leu Ser Gly Ala 
                545                 550                 555 

Asn Pro Arg Ala Gly Leu Tyr Leu Gln Gln Met Pro Tyr Pro Cys 
                560                 565                 570 

Tyr Val Asp Asp Val Phe Leu Arg Val Leu Ser Arg Ser Leu Pro 
                575                 580                 585 

Leu Phe Leu Thr Leu Ala Trp Ile Tyr Ser Val Thr Leu Thr Val 
                590                 595                 600 

Lys Ala Val Val Arg Glu Lys Glu Thr Arg Leu Arg Asp Thr Met 
                605                 610                 615 

Arg Ala Met Gly Leu Ser Arg Ala Val Leu Trp Leu Gly Trp Phe 
                620                 625                 630 

Leu Ser Cys Leu Gly Pro Phe Leu Leu Ser Ala Ala Leu Leu Val 
                635                 640                 645 

Leu Val Leu Lys Leu Gly Asp Ile Leu Pro Tyr Ser His Pro Gly 
                650                 655                 660 

Val Val Phe Leu Phe Leu Ala Ala Phe Ala Val Ala Thr Val Thr 
                665                 670                 675 

Gln Ser Phe Leu Leu Ser Ala Phe Phe Ser Arg Ala Asn Leu Ala 
                680                 685                 690 

Ala Ala Cys Gly Gly Leu Ala Tyr Phe Ser Leu Tyr Leu Pro Tyr 
                695                 700                 705 

Val Leu Cys Val Ala Trp Arg Asp Arg Leu Pro Ala Gly Gly Arg 
                710                 715                 720 

Val Ala Ala Ser Leu Leu Ser Pro Val Ala Phe Gly Phe Gly Cys 
                725                 730                 735 

Glu Ser Leu Ala Leu Leu Glu Glu Gln Gly Glu Gly Ala Gln Trp 
                740                 745                 750 

His Asn Val Gly Thr Arg Pro Thr Ala Asp Val Phe Ser Leu Ala 
                755                 760                 765 

Gln Val Ser Gly Leu Leu Leu Leu Asp Ala Ala Leu Tyr Gly Leu 
                770                 775                 780 

Ala Thr Trp Tyr Leu Glu Ala Val Cys Pro Gly Gln Tyr Gly Ile 
                785                 790                 795 

Pro Glu Pro Trp Asn Phe Pro Phe Arg Arg Ser Tyr Trp Cys Gly 
                800                 805                 810 

Pro Arg Pro Pro Lys Ser Pro Ala Pro Cys Pro Thr Pro Leu Asp 
                815                 820                 825 

Pro Lys Val Leu Val Glu Glu Ala Pro Pro Gly Leu Ser Pro Gly 
                830                 835                 840 

Val Ser Val Arg Ser Leu Glu Lys Arg Phe Pro Gly Ser Pro Gln 
                845                 850                 855 

Pro Ala Leu Arg Gly Leu Ser Leu Asp Phe Tyr Gln Gly His Ile 
                860                 865                 870 

Thr Ala Phe Leu Gly His Asn Gly Ala Gly Lys Thr Thr Thr Leu 
                875                 880                 885 

Ser Ile Leu Ser Gly Leu Phe Pro Pro Ser Gly Gly Ser Ala Phe 
                890                 895                 900 

Ile Leu Gly His Asp Val Arg Ser Ser Met Ala Ala Ile Arg Pro 
                905                 910                 915 

His Leu Gly Val Cys Pro Gln Tyr Asn Val Leu Phe Asp Met Leu 
                920                 925                 930 

Thr Val Asp Glu His Val Trp Phe Tyr Gly Arg Leu Lys Gly Leu 
                935                 940                 945 

Ser Ala Ala Val Val Gly Pro Glu Gln Asp Arg Leu Leu Gln Asp 
                950                 955                 960 

Val Gly Leu Val Ser Lys Gln Ser Val Gln Thr Arg His Leu Ser 
                965                 970                 975 

Gly Gly Met Gln Arg Lys Leu Ser Val Ala Ile Ala Phe Val Gly 
                980                 985                 990 

Gly Ser Gln Val Val Ile Leu Asp Glu Pro Thr Ala Gly Val Asp 
                995                 1000                1005 

Pro Ala Ser Arg Arg Gly Ile Trp Glu Leu Leu Leu Lys Tyr Arg 
                1010                1015                1020 

Glu Gly Arg Thr Leu Ile Leu Ser Thr His His Leu Asp Glu Ala 
                1025                1030                1035 

Glu Leu Leu Gly Asp Arg Val Ala Val Val Ala Gly Gly Arg Leu 
                1040                1045                1050 

Cys Cys Cys Gly Ser Pro Leu Phe Leu Arg Arg His Leu Gly Ser 
                1055                1060                1065 

Gly Tyr Tyr Leu Thr Leu Val Lys Ala Arg Leu Pro Leu Thr Thr 
                1070                1075                1080 

Asn Glu Lys Ala Asp Thr Asp Met Glu Gly Ser Val Asp Thr Arg 
                1085                1090                1095 

Gln Glu Lys Lys Asn Gly Ser Gln Gly Ser Arg Val Gly Thr Pro 
                1100                1105                1110 

Gln Leu Leu Ala Leu Val Gln His Trp Val Pro Gly Ala Arg Leu 
                1115                1120                1125 

Val Glu Glu Leu Pro His Glu Leu Val Leu Val Leu Pro Tyr Thr 
                1130                1135                1140 

Gly Ala His Asp Gly Ser Phe Ala Thr Leu Phe Arg Glu Leu Asp 
                1145                1150                1155 

Thr Arg Leu Ala Glu Leu Arg Leu Thr Gly Tyr Gly Ile Ser Asp 
                1160                1165                1170 

Thr Ser Leu Glu Glu Ile Phe Leu Lys Val Val Glu Glu Cys Ala 
                1175                1180                1185 

Ala Asp Thr Asp Met Glu Asp Gly Ser Cys Gly Gln His Leu Cys 
                1190                1195                1200 

Thr Gly Ile Ala Gly Leu Asp Val Thr Leu Arg Leu Lys Met Pro 
                1205                1210                1215 

Pro Gln Glu Thr Ala Leu Glu Asn Gly Glu Pro Ala Gly Ser Ala 
                1220                1225                1230 

Pro Glu Thr Asp Gln Gly Ser Gly Pro Asp Ala Val Gly Arg Val 
                1235                1240                1245 

Gln Gly Trp Ala Leu Thr Arg Gln Gln Leu Gln Ala Leu Leu Leu 
                1250                1255                1260 

Lys Arg Phe Leu Leu Ala Arg Arg Ser Arg Arg Gly Leu Phe Ala 
                1265                1270                1275 

Gln Ile Val Leu Pro Ala Leu Phe Val Gly Leu Ala Leu Val Phe 
                1280                1285                1290 

Ser Leu Ile Val Pro Pro Phe Gly His Tyr Pro Ala Leu Arg Leu 
                1295                1300                1305 

Ser Pro Thr Met Tyr Gly Ala Gln Val Ser Phe Phe Ser Glu Asp 
                1310                1315                1320 

Ala Pro Gly Asp Pro Gly Arg Ala Arg Leu Leu Glu Ala Leu Leu 
                1325                1330                1335 

Gln Glu Ala Gly Leu Glu Glu Pro Pro Val Gln His Ser Ser His 
                1340                1345                1350 

Arg Phe Ser Ala Pro Glu Val Pro Ala Glu Val Ala Lys Val Leu 
                1355                1360                1365 

Ala Ser Gly Asn Trp Thr Pro Glu Ser Pro Ser Pro Ala Cys Gln 
                1370                1375                1380 

Cys Ser Arg Pro Gly Ala Arg Arg Leu Leu Pro Asp Cys Pro Ala 
                1385                1390                1395 

Ala Ala Gly Gly Pro Pro Pro Pro Gln Ala Val Thr Gly Ser Gly 
                1400                1405                1410 

Glu Val Val Gln Asn Gln Thr Gly Arg Asn Leu Ser Asp Phe Leu 
                1415                1420                1425 

Val Lys Thr Tyr Pro Arg Leu Val Arg Gln Gly Leu Lys Thr Lys 
                1430                1435                1440 

Lys Trp Val Asn Glu Val Arg Tyr Gly Gly Phe Ser Leu Gly Gly 
                1445                1450                1455 

Arg Asp Pro Gly Leu Pro Ser Gly Gln Glu Leu Gly Arg Ser Val 
                1460                1465                1470 

Glu Glu Leu Trp Ala Leu Leu Ser Pro Leu Pro Gly Gly Ala Leu 
                1475                1480                1485 

Asp Arg Val Leu Lys Asn Leu Thr Ala Trp Ala His Ser Leu Asp 
                1490                1495                1500 

Ala Gln Asp Ser Leu Lys Ile Trp Phe Asn Asn Lys Gly Trp His 
                1505                1510                1515 

Ser Met Val Ala Phe Val Asn Arg Ala Ser Asn Ala Ile Leu Arg 
                1520                1525                1530 

Ala His Leu Pro Pro Gly Pro Ala Arg His Ala His Ser Ile Thr 
                1535                1540                1545 

Thr Leu Asn His Pro Leu Asn Leu Thr Lys Glu Gln Leu Ser Glu 
                1550                1555                1560 

Ala Ala Leu Met Ala Ser Ser Val Asp Val Leu Val Ser Ile Cys 
                1565                1570                1575 

Val Val Phe Ala Met Ser Phe Val Pro Ala Ser Phe Thr Leu Val 
                1580                1585                1590 

Leu Ile Glu Glu Arg Val Thr Arg Ala Lys His Leu Gln Leu Met 
                1595                1600                1605 

Gly Gly Leu Ser Pro Thr Leu Tyr Trp Leu Gly Asn Phe Leu Trp 
                1610                1615                1620 

Asp Met Cys Asn Tyr Leu Val Pro Ala Cys Ile Val Val Leu Ile 
                1625                1630                1635 

Phe Leu Ala Phe Gln Gln Arg Ala Tyr Val Ala Pro Ala Asn Leu 
                1640                1645                1650 

Pro Ala Leu Leu Leu Leu Leu Leu Leu Tyr Gly Trp Ser Ile Thr 
                1655                1660                1665 

Pro Leu Met Tyr Pro Ala Ser Phe Phe Phe Ser Val Pro Ser Thr 
                1670                1675                1680 

Ala Tyr Val Val Leu Thr Cys Ile Asn Leu Phe Ile Gly Ile Asn 
                1685                1690                1695 

Gly Ser Met Ala Thr Phe Val Leu Glu Leu Phe Ser Asp Gln Lys 
                1700                1705                1710 

Leu Gln Glu Val Ser Arg Ile Leu Lys Gln Val Phe Leu Ile Phe 
                1715                1720                1725 

Pro His Phe Cys Leu Gly Arg Gly Leu Ile Asp Met Val Arg Asn 
                1730                1735                1740 

Gln Ala Met Ala Asp Ala Phe Glu Arg Leu Gly Asp Arg Gln Phe 
                1745                1750                1755 

Gln Ser Pro Leu Arg Trp Glu Val Val Gly Lys Asn Leu Leu Ala 
                1760                1765                1770 

Met Val Ile Gln Gly Pro Leu Phe Leu Leu Phe Thr Leu Leu Leu 
                1775                1780                1785 

Gln His Arg Ser Gln Leu Leu Pro Gln Pro Arg Val Arg Ser Leu 
                1790                1795                1800 

Pro Leu Leu Gly Glu Glu Asp Glu Asp Val Ala Arg Glu Arg Glu 
                1805                1810                1815 

Arg Val Val Gln Gly Ala Thr Gln Gly Asp Val Leu Val Leu Arg 
                1820                1825                1830 

Asn Leu Thr Lys Val Tyr Arg Gly Gln Arg Met Pro Ala Val Asp 
                1835                1840                1845 

Arg Leu Cys Leu Gly Ile Pro Pro Gly Glu Cys Phe Gly Leu Leu 
                1850                1855                1860 

Gly Val Asn Gly Ala Gly Lys Thr Ser Thr Phe Arg Met Val Thr 
                1865                1870                1875 

Gly Asp Thr Leu Ala Ser Arg Gly Glu Ala Val Leu Ala Gly His 
                1880                1885                1890 

Ser Val Ala Arg Glu Pro Ser Ala Ala His Leu Ser Met Gly Tyr 
                1895                1900                1905 

Cys Pro Gln Ser Asp Ala Ile Phe Glu Leu Leu Thr Gly Arg Glu 
                1910                1915                1920 

His Leu Glu Leu Leu Ala Arg Leu Arg Gly Val Pro Glu Ala Gln 
                1925                1930                1935 

Val Ala Gln Thr Ala Gly Ser Gly Leu Ala Arg Leu Gly Leu Ser 
                1940                1945                1950 

Trp Tyr Ala Asp Arg Pro Ala Gly Thr Tyr Ser Gly Gly Asn Lys 
                1955                1960                1965 

Arg Lys Leu Ala Thr Ala Leu Ala Leu Val Gly Asp Pro Ala Val 
                1970                1975                1980 

Val Phe Leu Asp Glu Pro Thr Thr Gly Met Asp Pro Ser Ala Arg 
                1985                1990                1995 

Arg Phe Leu Trp Asn Ser Leu Leu Ala Val Val Arg Glu Gly Arg 
                2000                2005                2010 

Ser Val Met Leu Thr Ser His Ser Met Glu Glu Cys Glu Ala Leu 
                2015                2020                2025 

Cys Ser Arg Leu Ala Ile Met Val Asn Gly Arg Phe Arg Cys Leu 
                2030                2035                2040 

Gly Ser Pro Gln His Leu Lys Gly Arg Phe Ala Ala Gly His Thr 
                2045                2050                2055 

Leu Thr Leu Arg Val Pro Ala Ala Arg Ser Gln Pro Ala Ala Ala 
                2060                2065                2070 

Phe Val Ala Ala Glu Phe Pro Gly Ala Glu Leu Arg Glu Ala His 
                2075                2080                2085 

Gly Gly Arg Leu Arg Phe Gln Leu Pro Pro Gly Gly Arg Cys Ala 
                2090                2095                2100 

Leu Ala Arg Val Phe Gly Glu Leu Ala Val His Gly Ala Glu His 
                2105                2110                2115 

Gly Val Glu Asp Phe Ser Val Ser Gln Thr Met Leu Glu Glu Val 
                2120                2125                2130 

Phe Leu Tyr Phe Ser Lys Asp Gln Gly Lys Asp Glu Asp Thr Glu 
                2135                2140                2145 

Glu Gln Lys Glu Ala Gly Val Gly Val Asp Pro Ala Pro Gly Leu 
                2150                2155                2160 

Gln His Pro Lys Arg Val Ser Gln Phe Leu Asp Asp Pro Ser Thr 
                2165                2170                2175 

Ala Glu Thr Val Leu 
                2180 

 
           
             28  
             1737  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477845CD1  
             
           
            28 

Met Leu Lys Arg Lys Gln Ser Ser Arg Val Glu Ala Gln Pro Val 
1               5                   10                  15 

Thr Asp Phe Gly Pro Asp Glu Ser Leu Ser Asp Asn Ala Asp Ile 
                20                  25                  30 

Leu Trp Ile Asn Lys Pro Trp Val His Ser Leu Leu Arg Ile Cys 
                35                  40                  45 

Ala Ile Ile Ser Val Ile Ser Val Cys Met Asn Thr Pro Met Thr 
                50                  55                  60 

Phe Glu His Tyr Pro Pro Leu Gln Tyr Val Thr Phe Thr Leu Asp 
                65                  70                  75 

Thr Leu Leu Met Phe Leu Tyr Thr Ala Glu Met Ile Ala Lys Met 
                80                  85                  90 

His Ile Arg Gly Ile Val Lys Gly Asp Ser Ser Tyr Val Lys Asp 
                95                  100                 105 

Arg Trp Cys Val Phe Asp Gly Phe Met Val Phe Cys Leu Trp Val 
                110                 115                 120 

Ser Leu Val Leu Gln Val Phe Glu Ile Ala Asp Ile Val Asp Gln 
                125                 130                 135 

Met Ser Pro Trp Gly Met Leu Arg Ile Pro Arg Pro Leu Ile Met 
                140                 145                 150 

Ile Arg Ala Phe Arg Ile Tyr Phe Arg Phe Glu Leu Pro Arg Thr 
                155                 160                 165 

Arg Ile Thr Asn Ile Leu Lys Arg Ser Gly Glu Gln Ile Trp Ser 
                170                 175                 180 

Val Ser Ile Phe Leu Leu Phe Phe Leu Leu Leu Tyr Gly Ile Leu 
                185                 190                 195 

Gly Val Gln Met Phe Gly Thr Phe Thr Tyr His Cys Val Val Asn 
                200                 205                 210 

Asp Thr Lys Pro Gly Asn Val Thr Trp Asn Ser Leu Ala Ile Pro 
                215                 220                 225 

Asp Thr His Cys Ser Pro Glu Leu Glu Glu Gly Tyr Gln Cys Pro 
                230                 235                 240 

Pro Gly Phe Lys Cys Met Asp Leu Glu Asp Leu Gly Leu Ser Arg 
                245                 250                 255 

Gln Glu Leu Gly Tyr Ser Gly Phe Asn Glu Ile Gly Thr Ser Ile 
                260                 265                 270 

Phe Thr Val Tyr Glu Ala Ala Ser Gln Glu Gly Trp Val Phe Leu 
                275                 280                 285 

Met Tyr Arg Ala Ile Asp Ser Phe Pro Arg Trp Arg Ser Tyr Phe 
                290                 295                 300 

Tyr Phe Ile Thr Leu Ile Phe Phe Leu Ala Trp Leu Val Lys Asn 
                305                 310                 315 

Val Phe Ile Ala Val Ile Ile Glu Thr Phe Ala Glu Ile Arg Val 
                320                 325                 330 

Gln Phe Gln Gln Met Trp Gly Ser Arg Ser Ser Thr Thr Ser Thr 
                335                 340                 345 

Ala Thr Thr Gln Met Phe His Glu Asp Ala Ala Gly Gly Trp Gln 
                350                 355                 360 

Leu Val Ala Val Asp Val Asn Lys Pro Gln Gly Arg Ala Pro Ala 
                365                 370                 375 

Cys Leu Gln Lys Met Met Arg Ser Ser Val Phe His Met Phe Ile 
                380                 385                 390 

Leu Ser Met Val Thr Val Asp Val Ile Val Ala Ala Ser Asn Tyr 
                395                 400                 405 

Tyr Lys Gly Glu Asn Phe Arg Arg Gln Tyr Asp Glu Phe Tyr Leu 
                410                 415                 420 

Ala Glu Val Ala Phe Thr Val Leu Phe Asp Leu Glu Ala Leu Leu 
                425                 430                 435 

Lys Ile Trp Cys Leu Gly Phe Thr Gly Tyr Ile Ser Ser Ser Leu 
                440                 445                 450 

His Lys Phe Glu Leu Leu Leu Val Ile Gly Thr Thr Leu His Val 
                455                 460                 465 

Tyr Pro Asp Leu Tyr His Ser Gln Phe Thr Tyr Phe Gln Val Leu 
                470                 475                 480 

Arg Val Val Arg Leu Ile Lys Ile Ser Pro Ala Leu Glu Asp Phe 
                485                 490                 495 

Val Tyr Lys Ile Phe Gly Pro Gly Lys Lys Leu Gly Ser Leu Val 
                500                 505                 510 

Val Phe Thr Ala Ser Leu Leu Ile Val Met Ser Ala Ile Ser Leu 
                515                 520                 525 

Gln Met Phe Cys Phe Val Glu Glu Leu Asp Arg Phe Thr Thr Phe 
                530                 535                 540 

Pro Arg Ala Phe Met Ser Met Phe Gln Ile Leu Thr Gln Glu Gly 
                545                 550                 555 

Trp Val Asp Val Met Asp Gln Thr Leu Asn Ala Val Gly His Met 
                560                 565                 570 

Trp Ala Pro Val Val Ala Ile Tyr Phe Ile Leu Tyr His Leu Phe 
                575                 580                 585 

Ala Thr Leu Ile Leu Leu Ser Leu Phe Val Ala Val Ile Leu Asp 
                590                 595                 600 

Asn Leu Glu Leu Asp Glu Asp Leu Lys Lys Leu Lys Gln Leu Lys 
                605                 610                 615 

Gln Ser Glu Ala Asn Ala Asp Thr Lys Glu Lys Leu Pro Leu Arg 
                620                 625                 630 

Leu Arg Ile Phe Glu Lys Phe Pro Asn Arg Pro Gln Met Val Lys 
                635                 640                 645 

Ile Ser Lys Leu Pro Ser Asp Phe Thr Val Pro Lys Ile Arg Glu 
                650                 655                 660 

Ser Phe Met Lys Gln Phe Ile Asp Arg Gln Gln Gln Asp Thr Cys 
                665                 670                 675 

Cys Leu Leu Arg Ser Leu Pro Thr Thr Ser Ser Ser Ser Cys Asp 
                680                 685                 690 

His Ser Lys Arg Ser Ala Ile Glu Asp Asn Lys Tyr Ile Asp Gln 
                695                 700                 705 

Lys Leu Arg Lys Ser Val Phe Ser Ile Arg Ala Arg Asn Leu Leu 
                710                 715                 720 

Glu Lys Glu Thr Ala Val Thr Lys Ile Leu Arg Ala Cys Thr Arg 
                725                 730                 735 

Gln Arg Met Leu Ser Gly Ser Phe Glu Gly Gln Pro Ala Lys Glu 
                740                 745                 750 

Arg Ser Ile Leu Ser Val Gln His His Ile Arg Gln Glu Arg Arg 
                755                 760                 765 

Ser Leu Arg His Gly Ser Asn Ser Gln Arg Ile Ser Arg Gly Lys 
                770                 775                 780 

Ser Leu Glu Thr Leu Thr Gln Asp His Cys Asn Thr Val Ile Tyr 
                785                 790                 795 

Arg Asn Ala Gln Arg Glu Val Ser Glu Ile Lys Met Ile Gln Glu 
                800                 805                 810 

Lys Lys Glu Leu Ala Glu Met Leu Gln Gly Lys Cys Lys Lys Glu 
                815                 820                 825 

Leu Arg Glu Ser His Pro Tyr Phe Asp Lys Pro Leu Phe Ile Val 
                830                 835                 840 

Gly Arg Glu His Arg Phe Arg Asn Phe Cys Arg Val Val Val Arg 
                845                 850                 855 

Ala Arg Phe Asn Ala Ser Lys Thr Asp Pro Val Thr Gly Ala Val 
                860                 865                 870 

Lys Asn Thr Lys Tyr His Leu Leu Tyr Asp Leu Leu Gly Leu Val 
                875                 880                 885 

Thr Tyr Leu Asp Trp Val Met Ile Ile Val Thr Ser Asp Ser Cys 
                890                 895                 900 

Ile Ser Met Met Phe Glu Ser Pro Phe Arg Arg Val Met His Ala 
                905                 910                 915 

Pro Thr Leu Gln Ile Ala Glu Tyr Val Phe Val Ile Phe Met Ser 
                920                 925                 930 

Ile Glu Leu Asn Leu Lys Ile Met Ala Asp Gly Leu Phe Phe Thr 
                935                 940                 945 

Pro Thr Ala Val Ile Arg Asp Phe Gly Gly Val Met Asp Ile Phe 
                950                 955                 960 

Ile Tyr Leu Val Ser Leu Ile Phe Leu Cys Trp Met Pro Gln Asn 
                965                 970                 975 

Val Pro Ala Glu Ser Gly Ala Gln Leu Leu Met Val Leu Arg Cys 
                980                 985                 990 

Leu Arg Pro Leu Arg Ile Phe Lys Leu Val Pro Gln Met Arg Lys 
                995                 1000                1005 

Val Val Arg Glu Leu Phe Ser Gly Phe Lys Glu Ile Phe Leu Val 
                1010                1015                1020 

Ser Ile Leu Leu Leu Thr Leu Met Leu Val Phe Ala Ser Phe Gly 
                1025                1030                1035 

Val Gln Leu Phe Ala Gly Lys Leu Ala Lys Cys Asn Asp Pro Asn 
                1040                1045                1050 

Ile Ile Arg Arg Glu Asp Cys Asn Gly Ile Phe Arg Ile Asn Val 
                1055                1060                1065 

Ser Val Ser Lys Asn Leu Asn Leu Lys Leu Arg Pro Gly Glu Lys 
                1070                1075                1080 

Lys Pro Gly Phe Trp Val Pro Arg Val Trp Ala Asn Pro Arg Asn 
                1085                1090                1095 

Phe Asn Phe Asp Asn Val Gly Asn Ala Met Leu Ala Leu Phe Glu 
                1100                1105                1110 

Val Leu Ser Leu Lys Gly Trp Val Glu Val Arg Asp Val Ile Ile 
                1115                1120                1125 

His Arg Val Gly Pro Ile His Gly Ile Tyr Ile His Val Phe Val 
                1130                1135                1140 

Phe Leu Gly Cys Met Ile Gly Leu Thr Leu Phe Val Gly Val Val 
                1145                1150                1155 

Ile Ala Asn Phe Asn Glu Asn Lys Gly Thr Ala Leu Leu Thr Val 
                1160                1165                1170 

Asp Gln Arg Arg Trp Glu Asp Leu Lys Ser Arg Leu Lys Ile Ala 
                1175                1180                1185 

Gln Pro Leu His Leu Pro Pro Arg Pro Asp Asn Asp Gly Phe Arg 
                1190                1195                1200 

Ala Lys Met Tyr Asp Ile Thr Gln His Pro Phe Phe Lys Arg Thr 
                1205                1210                1215 

Ile Ala Leu Leu Val Leu Ala Gln Ser Val Leu Leu Ser Val Lys 
                1220                1225                1230 

Trp Asp Val Glu Asp Pro Val Thr Val Pro Leu Ala Thr Met Ser 
                1235                1240                1245 

Val Val Phe Thr Phe Ile Phe Val Leu Glu Val Thr Met Lys Ile 
                1250                1255                1260 

Ile Ala Met Ser Pro Ala Gly Phe Trp Gln Ser Arg Arg Asn Arg 
                1265                1270                1275 

Tyr Asp Leu Leu Val Thr Ser Leu Gly Val Val Trp Val Val Leu 
                1280                1285                1290 

His Phe Ala Leu Leu Asn Ala Tyr Thr Tyr Met Met Gly Ala Cys 
                1295                1300                1305 

Val Ile Val Phe Arg Phe Phe Ser Ile Cys Gly Lys His Val Thr 
                1310                1315                1320 

Leu Lys Met Leu Leu Leu Thr Val Val Val Ser Met Tyr Lys Ser 
                1325                1330                1335 

Phe Phe Ile Ile Val Gly Met Phe Leu Leu Leu Leu Cys Tyr Ala 
                1340                1345                1350 

Phe Ala Gly Val Val Leu Phe Gly Thr Val Lys Tyr Gly Glu Asn 
                1355                1360                1365 

Ile Asn Arg His Ala Asn Phe Ser Ser Ala Gly Lys Ala Ile Thr 
                1370                1375                1380 

Val Leu Phe Arg Ile Val Thr Gly Glu Asp Trp Asn Lys Ile Met 
                1385                1390                1395 

His Asp Cys Met Val Gln Pro Pro Phe Cys Thr Pro Asp Glu Phe 
                1400                1405                1410 

Thr Tyr Trp Ala Thr Asp Cys Gly Asn Tyr Ala Gly Ala Leu Met 
                1415                1420                1425 

Tyr Phe Cys Ser Phe Tyr Val Ile Ile Ala Tyr Ile Met Leu Asn 
                1430                1435                1440 

Leu Leu Val Ala Ile Ile Val Glu Asn Phe Ser Leu Ile Tyr Ser 
                1445                1450                1455 

Thr Glu Glu Asp Gln Leu Leu Ser Tyr Asn Asp Leu Arg His Phe 
                1460                1465                1470 

Gln Ile Ile Trp Asn Met Val Asp Asp Lys Arg Glu Val Phe Pro 
                1475                1480                1485 

Thr Phe Arg Val Lys Phe Leu Leu Arg Leu Leu Arg Gly Arg Leu 
                1490                1495                1500 

Glu Val Asp Leu Asp Lys Asp Lys Leu Leu Phe Lys His Met Cys 
                1505                1510                1515 

Tyr Glu Met Glu Arg Leu His Asn Gly Gly Asp Val Thr Phe His 
                1520                1525                1530 

Asp Val Leu Ser Met Leu Ser Tyr Arg Ser Val Asp Ile Arg Lys 
                1535                1540                1545 

Ser Leu Gln Leu Glu Glu Leu Leu Ala Arg Glu Gln Leu Glu Tyr 
                1550                1555                1560 

Thr Ile Glu Glu Glu Val Ala Lys Gln Thr Ile Arg Met Trp Leu 
                1565                1570                1575 

Lys Lys Cys Leu Lys Arg Ile Arg Ala Lys Gln Gln Gln Ser Cys 
                1580                1585                1590 

Ser Ile Ile His Ser Leu Arg Glu Ser Gln Gln Gln Glu Leu Ser 
                1595                1600                1605 

Arg Phe Leu Asn Pro Pro Ser Ile Glu Thr Thr Gln Pro Ser Glu 
                1610                1615                1620 

Asp Thr Asn Ala Asn Ser Gln Asp Asn Ser Met Gln Pro Glu Thr 
                1625                1630                1635 

Ser Ser Gln Gln Gln Leu Leu Ser Pro Thr Leu Ser Asp Arg Gly 
                1640                1645                1650 

Gly Ser Arg Gln Asp Ala Ala Asp Ala Gly Lys Pro Gln Arg Lys 
                1655                1660                1665 

Phe Gly Gln Trp Arg Leu Pro Ser Ala Pro Lys Pro Ile Ser His 
                1670                1675                1680 

Ser Val Ser Ser Val Asn Leu Arg Phe Gly Gly Arg Thr Thr Met 
                1685                1690                1695 

Lys Ser Val Val Cys Lys Met Asn Pro Met Thr Asp Ala Ala Ser 
                1700                1705                1710 

Cys Gly Ser Glu Val Lys Lys Trp Trp Thr Arg Gln Leu Thr Val 
                1715                1720                1725 

Glu Ser Asp Glu Ser Gly Asp Asp Leu Leu Asp Ile 
                1730                1735 

 
           
             29  
             547  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 168827CD1  
             
           
            29 

Met Ala Phe Gln Asp Leu Leu Asp Gln Val Gly Gly Leu Gly Arg 
1               5                   10                  15 

Phe Gln Ile Leu Gln Met Val Phe Leu Ile Met Phe Asn Val Ile 
                20                  25                  30 

Val Tyr His Gln Thr Gln Leu Glu Asn Phe Ala Ala Phe Ile Leu 
                35                  40                  45 

Asp His Arg Cys Trp Val His Ile Leu Asp Asn Asp Thr Ile Pro 
                50                  55                  60 

Asp Asn Asp Pro Gly Thr Leu Ser Gln Asp Ala Leu Leu Arg Ile 
                65                  70                  75 

Ser Ile Pro Phe Asp Ser Asn Leu Arg Pro Glu Lys Cys Arg Arg 
                80                  85                  90 

Phe Val His Pro Gln Trp Lys Leu Ile His Leu Asn Gly Thr Phe 
                95                  100                 105 

Pro Asn Thr Ser Glu Pro Asp Thr Glu Pro Cys Val Asp Gly Trp 
                110                 115                 120 

Val Tyr Asp Gln Ser Ser Phe Pro Ser Thr Ile Val Thr Lys Trp 
                125                 130                 135 

Asp Leu Val Cys Glu Ser Gln Pro Leu Asn Ser Val Ala Lys Phe 
                140                 145                 150 

Leu Phe Met Ala Gly Met Met Val Gly Gly Asn Leu Tyr Gly His 
                155                 160                 165 

Leu Ser Asp Arg Phe Gly Arg Lys Phe Val Leu Arg Trp Ser Tyr 
                170                 175                 180 

Leu Gln Leu Ala Ile Val Gly Thr Cys Ala Ala Phe Ala Pro Thr 
                185                 190                 195 

Ile Leu Val Tyr Cys Ser Leu Arg Phe Leu Ala Gly Ala Ala Thr 
                200                 205                 210 

Phe Ser Ile Ile Val Asn Thr Val Leu Leu Ile Val Glu Trp Ile 
                215                 220                 225 

Thr His Gln Phe Cys Ala Met Ala Leu Thr Leu Thr Leu Cys Ala 
                230                 235                 240 

Ala Ser Ile Gly His Ile Thr Leu Gly Ser Leu Ala Phe Val Ile 
                245                 250                 255 

Arg Asp Gln Cys Ile Leu Gln Leu Val Met Ser Ala Pro Cys Phe 
                260                 265                 270 

Val Phe Phe Leu Phe Ser Arg Trp Leu Ala Glu Ser Ala Arg Trp 
                275                 280                 285 

Leu Ile Ile Asn Asn Lys Pro Glu Glu Gly Leu Lys Glu Leu Thr 
                290                 295                 300 

Lys Ala Ala His Arg Asn Gly Met Lys Asn Ala Glu Asp Ile Leu 
                305                 310                 315 

Thr Met Glu Val Leu Lys Ser Thr Met Lys Gln Glu Leu Glu Ala 
                320                 325                 330 

Ala Gln Lys Lys His Ser Leu Cys Glu Leu Leu Arg Ile Pro Asn 
                335                 340                 345 

Ile Cys Lys Arg Ile Cys Phe Leu Ser Phe Val Arg Phe Ala Ser 
                350                 355                 360 

Thr Ile Pro Phe Trp Gly Leu Thr Leu His Leu Gln His Leu Gly 
                365                 370                 375 

Asn Asn Val Phe Leu Leu Gln Thr Leu Phe Gly Ala Val Thr Leu 
                380                 385                 390 

Leu Ala Asn Cys Val Ala Pro Trp Ala Leu Asn His Met Ser Arg 
                395                 400                 405 

Arg Leu Ser Gln Met Leu Leu Met Phe Leu Leu Ala Thr Cys Leu 
                410                 415                 420 

Leu Ala Ile Ile Phe Val Pro Gln Glu Met Gln Thr Leu Arg Val 
                425                 430                 435 

Val Leu Ala Thr Leu Gly Val Gly Ala Ala Ser Leu Gly Ile Thr 
                440                 445                 450 

Cys Ser Thr Ala Gln Glu Asn Glu Leu Ile Pro Ser Ile Ile Arg 
                455                 460                 465 

Gly Arg Ala Thr Gly Ile Thr Gly Asn Phe Ala Asn Ile Gly Gly 
                470                 475                 480 

Ala Leu Ala Ser Leu Met Met Ile Leu Ser Ile Tyr Ser Arg Pro 
                485                 490                 495 

Leu Pro Trp Ile Ile Tyr Gly Val Phe Ala Ile Leu Ser Gly Leu 
                500                 505                 510 

Val Val Leu Leu Leu Pro Glu Thr Arg Asn Gln Pro Leu Leu Asp 
                515                 520                 525 

Ser Ile Gln Asp Val Glu Asn Glu Gly Val Asn Ser Leu Ala Ala 
                530                 535                 540 

Pro Gln Arg Ser Ser Val Leu 
                545 

 
           
             30  
             547  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7472734CD1  
             
           
            30 

Met Gly Phe Asp Val Leu Leu Asp Gln Val Gly Gly Met Gly Arg 
1               5                   10                  15 

Phe Gln Ile Cys Leu Ile Ala Phe Phe Cys Ile Thr Asn Ile Leu 
                20                  25                  30 

Leu Phe Pro Asn Ile Val Leu Glu Asn Phe Thr Ala Phe Thr Pro 
                35                  40                  45 

Ser His Arg Cys Trp Val Pro Leu Leu Asp Asn Asp Thr Val Ser 
                50                  55                  60 

Asp Asn Asp Thr Gly Thr Leu Ser Lys Asp Asp Leu Leu Arg Ile 
                65                  70                  75 

Ser Ile Pro Leu Asp Ser Asn Leu Arg Pro Gln Lys Cys Gln Arg 
                80                  85                  90 

Phe Ile His Pro Gln Trp Gln Leu Leu His Leu Asn Gly Thr Phe 
                95                  100                 105 

Pro Asn Thr Asn Glu Pro Asp Thr Glu Pro Cys Val Asp Gly Trp 
                110                 115                 120 

Val Tyr Asp Arg Ser Ser Phe Leu Ser Thr Ile Val Thr Glu Trp 
                125                 130                 135 

Asp Leu Val Cys Glu Ser Gln Ser Leu Lys Ser Met Val Gln Ser 
                140                 145                 150 

Leu Phe Met Ala Gly Ser Leu Leu Gly Gly Leu Ile Tyr Gly His 
                155                 160                 165 

Leu Ser Asp Arg Phe Gly Arg Lys Phe Val Leu Arg Trp Ser Tyr 
                170                 175                 180 

Leu Gln Leu Ala Ile Val Gly Thr Cys Ala Ala Phe Ala Pro Thr 
                185                 190                 195 

Ile Leu Val Tyr Cys Ser Leu Arg Phe Leu Ala Gly Ala Ala Thr 
                200                 205                 210 

Phe Ser Ile Ile Val Asn Thr Val Leu Leu Ile Val Glu Trp Ile 
                215                 220                 225 

Thr His Gln Phe Cys Ala Met Ala Leu Thr Leu Thr Leu Cys Ala 
                230                 235                 240 

Ala Ser Ile Gly His Ile Thr Leu Gly Ser Leu Ala Phe Val Ile 
                245                 250                 255 

Arg Asp Gln Cys Ile Leu Gln Leu Val Met Ser Ala Pro Cys Phe 
                260                 265                 270 

Val Phe Phe Leu Phe Ser Arg Trp Leu Ala Glu Ser Ala Arg Trp 
                275                 280                 285 

Leu Ile Ile Asn Asn Lys Pro Glu Glu Gly Leu Lys Glu Leu Arg 
                290                 295                 300 

Lys Ala Ala His Arg Asn Gly Met Lys Asn Ala Glu Asp Ile Leu 
                305                 310                 315 

Thr Met Glu Val Leu Lys Ser Thr Met Lys Gln Glu Leu Glu Ala 
                320                 325                 330 

Ala Gln Lys Lys His Ser Leu Cys Glu Leu Leu Arg Ile Pro Asn 
                335                 340                 345 

Ile Cys Lys Arg Ile Cys Phe Leu Ser Phe Val Arg Phe Ala Ser 
                350                 355                 360 

Thr Ile Pro Phe Trp Gly Leu Thr Leu His Leu Gln His Leu Gly 
                365                 370                 375 

Asn Asn Val Phe Leu Leu Gln Thr Leu Phe Gly Ala Val Thr Leu 
                380                 385                 390 

Leu Ala Asn Cys Val Ala Pro Trp Ala Leu Asn His Met Ser Arg 
                395                 400                 405 

Arg Leu Ser Gln Met Leu Leu Met Phe Leu Leu Ala Thr Cys Leu 
                410                 415                 420 

Leu Ala Ile Ile Phe Val Pro Gln Glu Met Gln Thr Leu Arg Val 
                425                 430                 435 

Val Leu Ala Thr Leu Gly Val Gly Ala Ala Ser Leu Gly Ile Thr 
                440                 445                 450 

Cys Ser Thr Ala Gln Glu Asn Glu Leu Ile Pro Ser Ile Ile Arg 
                455                 460                 465 

Gly Arg Ala Thr Gly Ile Thr Gly Asn Phe Ala Asn Ile Gly Gly 
                470                 475                 480 

Ala Leu Ala Ser Leu Met Met Ile Leu Ser Ile Tyr Ser Arg Pro 
                485                 490                 495 

Leu Pro Trp Ile Ile Tyr Gly Val Phe Ala Ile Leu Ser Gly Leu 
                500                 505                 510 

Val Val Leu Leu Leu Pro Glu Thr Arg Asn Gln Pro Leu Leu Asp 
                515                 520                 525 

Ser Ile Gln Asp Val Glu Asn Glu Gly Val Asn Ser Leu Ala Ala 
                530                 535                 540 

Pro Gln Arg Ser Ser Val Leu 
                545 

 
           
             31  
             988  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7473473CD1  
             
           
            31 

Met Pro Gly Gly Lys Arg Gly Leu Val Ala Pro Gln Asn Thr Phe 
1               5                   10                  15 

Leu Glu Asn Ile Val Arg Arg Ser Ser Glu Ser Ser Phe Leu Leu 
                20                  25                  30 

Gly Asn Ala Gln Ile Val Asp Trp Pro Val Val Tyr Ser Asn Asp 
                35                  40                  45 

Gly Phe Cys Lys Leu Ser Gly Tyr His Arg Ala Asp Val Met Gln 
                50                  55                  60 

Lys Ser Ser Thr Cys Ser Phe Met Tyr Gly Glu Leu Thr Asp Lys 
                65                  70                  75 

Lys Thr Ile Glu Lys Val Arg Gln Thr Phe Asp Asn Tyr Glu Ser 
                80                  85                  90 

Asn Cys Phe Glu Val Leu Leu Tyr Lys Lys Asn Arg Thr Pro Val 
                95                  100                 105 

Trp Phe Tyr Met Gln Ile Ala Pro Ile Arg Asn Glu His Glu Lys 
                110                 115                 120 

Val Val Leu Phe Leu Cys Thr Phe Lys Asp Ile Thr Leu Phe Lys 
                125                 130                 135 

Gln Pro Ile Glu Asp Asp Ser Thr Lys Gly Trp Thr Lys Phe Ala 
                140                 145                 150 

Arg Leu Thr Arg Ala Leu Thr Asn Ser Arg Ser Val Leu Gln Gln 
                155                 160                 165 

Leu Thr Pro Met Asn Lys Thr Glu Val Val His Lys His Ser Arg 
                170                 175                 180 

Leu Ala Glu Val Leu Gln Leu Gly Ser Asp Ile Leu Pro Gln Tyr 
                185                 190                 195 

Lys Gln Glu Ala Pro Lys Thr Pro Pro His Ile Ile Leu His Tyr 
                200                 205                 210 

Cys Ala Phe Lys Thr Thr Trp Asp Trp Val Ile Leu Ile Leu Thr 
                215                 220                 225 

Phe Tyr Thr Ala Ile Met Val Pro Tyr Asn Val Ser Phe Lys Thr 
                230                 235                 240 

Lys Gln Asn Asn Ile Ala Trp Leu Val Leu Asp Ser Val Val Asp 
                245                 250                 255 

Val Ile Phe Leu Val Asp Ile Val Leu Asn Phe His Thr Thr Phe 
                260                 265                 270 

Val Gly Pro Gly Gly Glu Val Ile Ser Asp Pro Lys Leu Ile Arg 
                275                 280                 285 

Met Asn Tyr Leu Lys Thr Trp Phe Val Ile Asp Leu Leu Ser Cys 
                290                 295                 300 

Leu Pro Tyr Asp Ile Ile Asn Ala Phe Glu Asn Val Asp Glu Gly 
                305                 310                 315 

Ile Ser Ser Leu Phe Ser Ser Leu Lys Val Val Arg Leu Leu Arg 
                320                 325                 330 

Leu Gly Arg Val Ala Arg Lys Leu Asp His Tyr Leu Glu Tyr Gly 
                335                 340                 345 

Ala Ala Val Leu Val Leu Leu Val Cys Val Phe Gly Leu Val Ala 
                350                 355                 360 

His Trp Leu Ala Cys Ile Trp Tyr Ser Ile Gly Asp Tyr Glu Val 
                365                 370                 375 

Ile Asp Glu Val Thr Asn Thr Ile Gln Ile Asp Ser Trp Leu Tyr 
                380                 385                 390 

Gln Leu Ala Leu Ser Ile Gly Thr Pro Tyr Arg Tyr Asn Thr Ser 
                395                 400                 405 

Ala Gly Ile Trp Glu Gly Gly Pro Ser Lys Asp Ser Leu Tyr Val 
                410                 415                 420 

Ser Ser Leu Tyr Phe Thr Met Thr Ser Leu Thr Thr Ile Gly Phe 
                425                 430                 435 

Gly Asn Ile Ala Pro Thr Thr Asp Val Glu Lys Met Phe Ser Val 
                440                 445                 450 

Ala Met Met Met Val Gly Ala Leu Leu Tyr Ala Thr Ile Phe Gly 
                455                 460                 465 

Asn Val Thr Thr Ile Phe Gln Gln Met Tyr Ala Asn Thr Asn Arg 
                470                 475                 480 

Tyr His Glu Met Leu Asn Asn Val Arg Asp Phe Leu Lys Leu Tyr 
                485                 490                 495 

Gln Val Pro Lys Gly Leu Ser Glu Arg Val Met Asp Tyr Ile Val 
                500                 505                 510 

Ser Thr Trp Ser Met Ser Lys Gly Ile Asp Thr Glu Lys Val Leu 
                515                 520                 525 

Ser Ile Cys Pro Lys Asp Met Arg Ala Asp Ile Cys Val His Leu 
                530                 535                 540 

Asn Arg Lys Val Phe Asn Glu His Pro Ala Phe Arg Leu Ala Ser 
                545                 550                 555 

Asp Gly Cys Leu Arg Ala Leu Ala Val Glu Phe Gln Thr Ile His 
                560                 565                 570 

Cys Ala Pro Gly Asp Leu Ile Tyr His Ala Gly Glu Ser Val Asp 
                575                 580                 585 

Ala Leu Cys Phe Val Val Ser Gly Ser Leu Glu Val Ile Gln Asp 
                590                 595                 600 

Asp Glu Val Val Ala Ile Leu Gly Lys Gly Asp Val Phe Gly Asp 
                605                 610                 615 

Ile Phe Trp Lys Glu Thr Thr Leu Ala His Ala Cys Ala Asn Val 
                620                 625                 630 

Arg Ala Leu Thr Tyr Cys Asp Leu His Ile Ile Lys Arg Glu Ala 
                635                 640                 645 

Leu Leu Lys Val Leu Asp Phe Tyr Thr Ala Phe Ala Asn Ser Phe 
                650                 655                 660 

Ser Arg Asn Leu Thr Leu Thr Cys Asn Leu Arg Lys Arg Ile Ile 
                665                 670                 675 

Phe Arg Lys Ile Ser Asp Val Lys Lys Glu Glu Glu Glu Arg Leu 
                680                 685                 690 

Arg Gln Lys Asn Glu Val Thr Leu Ser Ile Pro Val Asp His Pro 
                695                 700                 705 

Val Arg Lys Leu Phe Gln Lys Phe Lys Gln Gln Lys Glu Leu Arg 
                710                 715                 720 

Asn Gln Gly Ser Thr Gln Gly Asp Pro Glu Arg Asn Gln Leu Gln 
                725                 730                 735 

Val Glu Ser Arg Ser Leu Gln Asn Gly Ala Ser Ile Thr Gly Thr 
                740                 745                 750 

Ser Val Val Thr Val Ser Gln Ile Thr Pro Ile Gln Thr Ser Leu 
                755                 760                 765 

Ala Tyr Val Lys Thr Ser Glu Ser Leu Lys Gln Asn Asn Arg Asp 
                770                 775                 780 

Ala Met Glu Leu Lys Pro Asn Gly Gly Ala Asp Gln Lys Cys Leu 
                785                 790                 795 

Lys Val Asn Ser Pro Ile Arg Met Lys Asn Gly Asn Gly Lys Gly 
                800                 805                 810 

Trp Leu Arg Leu Lys Asn Asn Met Gly Ala His Glu Glu Lys Lys 
                815                 820                 825 

Glu Asp Trp Asn Asn Val Thr Lys Ala Glu Ser Met Gly Leu Leu 
                830                 835                 840 

Ser Glu Asp Pro Lys Ser Ser Asp Ser Glu Asn Ser Val Thr Lys 
                845                 850                 855 

Asn Pro Leu Arg Lys Thr Asp Ser Cys Asp Ser Gly Ile Thr Lys 
                860                 865                 870 

Ser Asp Leu Arg Leu Asp Lys Ala Gly Glu Ala Arg Ser Pro Leu 
                875                 880                 885 

Glu His Ser Pro Ile Gln Ala Asp Ala Lys His Pro Phe Tyr Pro 
                890                 895                 900 

Ile Pro Glu Gln Ala Leu Gln Thr Thr Leu Gln Glu Val Lys His 
                905                 910                 915 

Glu Leu Lys Glu Asp Ile Gln Leu Leu Ser Cys Arg Met Thr Ala 
                920                 925                 930 

Leu Glu Lys Gln Val Ala Glu Ile Leu Lys Ile Leu Ser Glu Lys 
                935                 940                 945 

Ser Val Pro Gln Ala Ser Ser Pro Lys Ser Gln Met Pro Leu Gln 
                950                 955                 960 

Val Pro Pro Gln Ile Pro Cys Gln Asp Ile Phe Ser Val Ser Arg 
                965                 970                 975 

Pro Glu Ser Pro Glu Ser Asp Lys Asp Glu Ile His Phe 
                980                 985 

 
           
             32  
             533  
             PRT  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477725CD1  
             
           
            32 

Met Ala Phe Glu Glu Leu Leu Ser Gln Val Gly Gly Leu Gly Arg 
1               5                   10                  15 

Phe Gln Met Leu His Leu Val Phe Ile Leu Pro Ser Leu Met Leu 
                20                  25                  30 

Leu Ile Pro His Ile Leu Leu Glu Asn Phe Ala Ala Ala Ile Pro 
                35                  40                  45 

Gly His Arg Cys Trp Val His Met Leu Asp Asn Asn Thr Gly Ser 
                50                  55                  60 

Gly Asn Glu Thr Gly Ile Leu Ser Glu Asp Ala Leu Leu Arg Ile 
                65                  70                  75 

Ser Ile Pro Leu Asp Ser Asn Leu Arg Pro Glu Lys Cys Arg Arg 
                80                  85                  90 

Phe Val His Pro Gln Trp Gln Leu Leu His Leu Asn Gly Thr Ile 
                95                  100                 105 

His Ser Thr Ser Glu Ala Asp Thr Glu Pro Cys Val Asp Gly Trp 
                110                 115                 120 

Val Tyr Asp Gln Ser Tyr Phe Pro Ser Thr Ile Val Thr Lys Trp 
                125                 130                 135 

Asp Leu Val Cys Asp Tyr Gln Ser Leu Lys Ser Val Val Gln Phe 
                140                 145                 150 

Leu Leu Leu Thr Gly Met Leu Val Gly Gly Ile Ile Gly Gly His 
                155                 160                 165 

Val Ser Asp Arg Phe Gly Arg Arg Phe Ile Leu Arg Trp Cys Leu 
                170                 175                 180 

Leu Gln Leu Ala Ile Thr Asp Thr Cys Ala Ala Phe Ala Pro Thr 
                185                 190                 195 

Phe Pro Val Tyr Cys Val Leu Arg Phe Leu Ala Gly Phe Ser Ser 
                200                 205                 210 

Met Ile Ile Ile Ser Asn Asn Ser Leu Pro Ile Thr Glu Trp Ile 
                215                 220                 225 

Arg Pro Asn Ser Lys Ala Leu Val Val Ile Leu Ser Ser Gly Ala 
                230                 235                 240 

Leu Ser Ile Gly Gln Ile Ile Leu Gly Gly Leu Ala Tyr Val Phe 
                245                 250                 255 

Arg Asp Trp Gln Thr Leu His Val Val Ala Ser Val Pro Phe Phe 
                260                 265                 270 

Val Phe Phe Leu Leu Ser Arg Trp Leu Val Glu Ser Ala Arg Trp 
                275                 280                 285 

Leu Ile Ile Thr Asn Lys Leu Asp Glu Gly Leu Lys Ala Leu Arg 
                290                 295                 300 

Lys Val Ala Arg Thr Asn Gly Ile Lys Asn Ala Glu Glu Thr Leu 
                305                 310                 315 

Asn Ile Glu Val Val Arg Ser Thr Met Gln Glu Glu Leu Asp Ala 
                320                 325                 330 

Ala Gln Thr Lys Thr Thr Val Cys Asp Leu Phe Arg Asn Pro Ser 
                335                 340                 345 

Met Arg Lys Arg Ile Cys Ile Leu Val Phe Leu Arg Phe Ala Asn 
                350                 355                 360 

Thr Ile Pro Phe Tyr Gly Thr Met Val Asn Leu Gln His Val Gly 
                365                 370                 375 

Ser Asn Ile Phe Leu Leu Gln Val Leu Tyr Gly Ala Val Ala Leu 
                380                 385                 390 

Ile Val Arg Cys Leu Ala Leu Leu Thr Leu Asn His Met Gly Arg 
                395                 400                 405 

Arg Ile Ser Gln Ile Leu Phe Met Phe Leu Val Gly Leu Ser Ile 
                410                 415                 420 

Leu Ala Asn Thr Phe Val Pro Lys Glu Met Gln Thr Leu Arg Val 
                425                 430                 435 

Ala Leu Ala Cys Leu Gly Ile Gly Cys Ser Ala Ala Thr Phe Ser 
                440                 445                 450 

Ser Val Ala Val His Phe Ile Glu Leu Ile Pro Thr Val Leu Arg 
                455                 460                 465 

Ala Arg Ala Ser Gly Ile Asp Leu Thr Ala Ser Arg Ile Gly Ala 
                470                 475                 480 

Ala Leu Ala Pro Leu Leu Met Thr Leu Thr Val Phe Phe Thr Thr 
                485                 490                 495 

Leu Pro Trp Ile Ile Tyr Gly Ile Phe Pro Ile Ile Gly Gly Leu 
                500                 505                 510 

Ile Val Phe Leu Leu Pro Glu Thr Lys Asn Leu Pro Leu Pro Asp 
                515                 520                 525 

Thr Ile Lys Asp Val Glu Asn Gln 
                530 

 
           
             33  
             1775  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3474673CB1  
             
           
            33 

atttcaggaa atgtgagggg gctctgggcc ccttccctca gcgcctgcgg tcacccagca     60 

gcttcctcct tctccctggc ctaggcctag caggtgggca ccccgcacac atttgaggcg    120 

gggccagatg cccacagttc agagcctctt tttgtcccgg ggattggatc ccagggctgg    180 

gtggggccag gctgtcccat tccccaacac tcctcctccc cggcgaaacc gggcaccagc    240 

aggcgtttgc gagaggagat acgagctgga cgcctggccc ttccctccca ccgggtccta    300 

gtccaccgct cccggcgccg gctccccgcc tctcccgcta tgtaccgacc gcgagcccgg    360 

gcggctcccg agggcagggt ccggggctgc gcggtgccca gcaccgtgct cctgctgctc    420 

gcctacctgg cttacctggc gctgggcacc ggcgtgttct ggacgctgga gggccgcgcg    480 

gcgcaggact ccagccgcag cttccagcgc gacaagtggg agctgttgca gaacttcacg    540 

tgtctggacc gcccggcgct ggactcgctg atccgggatg tcgtccaagc atacaaaaac    600 

ggagccagcc tcctcagcaa caccaccagc atggggcgct gggagctcgt gggctccttc    660 

ttcttttctg tgtccaccat caccaccatt ggctatggca acctgagccc caacacgatg    720 

gctgcccgcc tcttctgcat cttctttgcc cttgtgggga tcccactcaa cctcgtggtg    780 

ctcaaccgac tggggcatct catgcagcag ggagtaaacc actgggccag caggctgggg    840 

ggcacctggc aggatcctga caaggcgcgg tggctggcgg gctctggcgc cctcctctcg    900 

ggcctcctgc tcttcctgct gctgccaccg ctgctcttct cccacatgga gggctggagc    960 

tacacagagg gcttctactt cgccttcatc accctcagca ccgtgggctt cggcgactac   1020 

gtgattggaa tgaacccctc ccagaggtac ccactgtggt acaagaacat ggtgtccctg   1080 

tggatcctct ttgggatggc atggctggcc ttgatcatca aactcatcct ctcccagctg   1140 

gagacgccag ggagggtatg ttcctgctgc caccacagct ctaaggaaga cttcaagtcc   1200 

caaagctgga gacagggacc tgaccgggag ccagagtccc actccccaca gcaaggatgc   1260 

tatccagagg gacccatggg aatcatacag catctggaac cttctgctca cgctgcaggc   1320 

tgtggcaagg acagctagtt atactccatt ctttggtcgt cgtcctcggt agcaagaccc   1380 

ctgattttaa gctttgcaca tgtccaccca aactaaagac tacattttcc atccacccta   1440 

gaggctgggt gcagctatat gattaattct gcccaatagg gtatacagag acatgtcctg   1500 

ggtgacatgg gatgtgactt tcgggtgtcg gggcagcatg cccttctccc ccacttcctt   1560 

actttagcgg gctgcaatgc cgccgatatg atggctggga gctctggcag ccatacggca   1620 

ccatgaagta gcggcaatgt ttgagcggca caataagata ggaagagtct ggatctctga   1680 

tgatcacaga gccatcctaa caaacggaat atcacccgac ctcctttatg tgagagagaa   1740 

ataaacatct tatgtaaaat accaaaaaaa aaaaa                              1775 

 
           
             34  
             1545  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 4588877CB1  
             
           
            34 

aatgagggcc ctgggggttg ggcccaggag tggggctgtg gtggtgagtg gacagggctg     60 

ggctggaaat gtcccctgag tgccccctct cacctcaggc tatggcaacc tgagccccaa    120 

cacgatggct gcccgcctct tctgcatctt ctttgccctt gtggggatcc cactcaacct    180 

cgtggtgctc aaccgactgg ggcatctcat gcagcaggga gtaaaccact gggccagcag    240 

gctggggggc acctggcagg tgagggggct gctggacggg gtggggatgg gtcacttcta    300 

gaatgagggg ctgtggtggg aattggggtt actaatgaca agaggtggga gcaagtgtta    360 

ctggtgaggt tgtgttggga ttgggggtca ctgctcagaa tagggtcctt agtgaaaaag    420 

ggcattaatg gtggagatgg ggtgggactg ggcagacagg aaggacatga ggcacaggct    480 

ccaggcaggg aacctggaga acacagacca ggtgaagagc ccccttctta ctggggacag    540 

ctctggcctg cctccagctc cctcggctcc cacgcatggg gtgaaggcct caggaggcct    600 

ggggacaata ttgcacccac aggatcctga caaggcgcgg tggctggcgg gctctggcgc    660 

cctcctctcg ggcctcctgc tcttcctgct gctgccaccg ctgctcttct cccacatgga    720 

gggctggagc tacacagagg gcttctactt cgccttcatc accctcagca ccgtgggctt    780 

cggcgactac gtgattggaa tgaacccctc ccagaggtac ccactgtggt acaagaacat    840 

ggtgtccctg tggatcctct ttgggatggc atggctggcc ttgatcatca aactcatcct    900 

ctcccagctg gagacgccag ggagggtatg ttcctgctgc caccacagct ctaaggaaga    960 

cttcaagtcc caaagctgga gacagggacc tgaccgggag ccagagtccc actccccaca   1020 

gcaaggatgc tatccagagg gacccatggg aatcatacag catctggaac cttctgctca   1080 

cgctgcaggc tgtggcaagg acagctagtt atactccatt ctttggtcgt cgtcctcggt   1140 

agcaagaccc ctgattttaa gctttgcaca tgtccaccca aactaaagac tacattttcc   1200 

atccacccta gaggctgggt gcagctatat gattaattct gcccaatagg gtatacagag   1260 

acatgtcctg ggtgacatgg gatgtgactt tcgggtgtcg gggcagcatg cccttctccc   1320 

ccacttcctt actttagcgg gctgcaatgc cgccgatatg atggctggga gctctggcag   1380 

ccatacggca ccatgaagta gcggcaatgt ttgagcggca caataagata ggaagagtct   1440 

ggatctctga tgatcacaga gccatcctaa caaacggaat atcacccgac ctcctttatg   1500 

tgagagagaa ataaacatct tatgtaaaat accaaaaaaa aaaaa                   1545 

 
           
             35  
             1941  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7472214CB1  
             
           
            35 

atggcggaga aggcgctgga ggccgtgggc tgtggactag ggccgggggc tgtggccatg     60 

gccgtgacgc tggaggacgg ggcggaaccc cctgtgctga ccacgcacct gaagaaggtg    120 

gagaaccaca tcactgaagc ccagcgcttc tcccacctac ccaagcgctc agccgtggac    180 

atcgagttcg tggagctgtc ctattccgtg cgggaggggc cctgctggcg caaaaggggt    240 

tataagaccc ttctcaagtg cctctcaggt aaattctgcc gccgggagct gattggcatc    300 

atgggcccct caggggctgg caagtctaca ttcatgaaca tcttggcagg atacagggag    360 

tctggaatga aggggcagat cctggttaat ggaaggccac gggagctgag gaccttccgc    420 

aagatgtcct gctacatcat gcaagatgac atgctgctgc cgcacctcac ggtgttggaa    480 

gccatgatgg tgtctgctaa cctgaatctt actgagaatc ccgatgtgaa aaacgatctc    540 

gtgacagaga tcctgacggc actgggcctg atgtcgtgct cccacacgag gacagccctg    600 

ctctctggcg ggcagaggaa gcgtctggcc atcgccctgg agctggtcaa caacccgcct    660 

gtcatgttct ttgatgagcc caccagtggt ctggatagcg cctcttgttt ccaagtggtg    720 

tccctcatga agtccctggc acaggggggc cgtaccatca tctgcaccat ccaccagccc    780 

agtgccaagc tctttgagat gtttgacaag ctctacatcc tgagccaggg tcagtgcatc    840 

ttcaaaggcg tggtcaccaa cctgatcccc tatctaaagg gactcggctt gcattgcccc    900 

acctaccaca acccggctga cttcgtcatc gaggtggcct ctggcgagta tggagacctg    960 

aaccccatgt tgttcagggc tgtgcagaat gggctgtgcg ctatggctga gaagaagagc   1020 

agccctgaga agaacgaggt ccctgcccca tgccctcctt gtcctccgga agtggatccc   1080 

attgaaagcc acacctttgc caccagcacc ctcacacagt tctgcatcct cttcaagagg   1140 

accttcctgt ccatcctcag ggacacggtg ctgacccacc tacggttcat gtcccacgtg   1200 

gttattggcg tgctcatcgg cctcctctac ctgcatattg gcgacgatgc cagcaaggtc   1260 

ttcaacaaca ccggctgcct cttcttctcc atgctgttcc tcatgttcgc cgccctcatg   1320 

ccaactgtgc tcaccgtccc cttagagatg gcggtcttca tgagggagca cctcaactac   1380 

tggtacagcc tcaaagcgta ttacctggcc aagaccatgg ctgacgtgcc ctttcaggtg   1440 

gtgtgtccgg tggtctactg cagcattgtg tactggatga cgggccagcc cgctgagacc   1500 

agccgcttcc tgctcttctc agccctggcc accgccaccg ccttggtggc ccaatctttg   1560 

gggctgctga tcggagctgc ttccaactcc ctacaggtgg ccacttttgt gggcccagtt   1620 

accgccatcc ctgtcctctt gttctccggc ttctttgtca gcttcaagac catccccact   1680 

tacctgcaat ggagctccta tctctcctat gtcaggtatg gctttgaggg tgtgatcctg   1740 

acgatctatg gcatggagcg aggagacctg acatgtttag aggaacgctg cccgttccgg   1800 

gagccacaga gcatcctccg agcgctggat gtggaggatg ccaagctcta catggacttc   1860 

ctggtcttgg gcatcttctt cctagccctg cggctgctgg cctaccttgt gctgcgttac   1920 

cgggtcaagt cagagagata g                                             1941 

 
           
             36  
             4971  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7473053CB1  
             
           
            36 

caaagtagcg ggccgaggcc cgggggagcg gggccgcagc tgggggggcg ggagcccgtg     60 

gggagccgag ccgagcgccc cccgccccag cccccggcat gggcagtacg gggccgccgg    120 

ggcgggcgcc gagcgctgag cgctgagggt ctcccatggg attgctggga tcttgctggg    180 

tgagatggca gtgtgtgcaa aaaagcgccc cccagaagaa gaaaggaggg cgcgggctaa    240 

tgaccgagaa tacaatgaga aattccagta tgcgagtaac tgcatcaaga cctccaagta    300 

caatattctc accttcctgc ctgtcaacct ctttgagcag ttccaggaag ttgccaacac    360 

ttacttcctg ttcctcctca ttctgcagtt gatcccccag atctcttccc tgtcctggtt    420 

caccaccatt gtgcctttgg ttcttgtcct caccatcaca gctgttaaag atgccactga    480 

tgactatttc cgccacaaga gcgataacca ggtgaataac cgccagtctc aggtgctgat    540 

caacggaatc ctccagcagg agcagtggat gaatgtctgt gttggtgata ttatcaagct    600 

agaaaataac cagtttgtgg cggcggatct cctcctcctt tccagcagtg agccccatgg    660 

gctgtgttac atagagacag cagaacttga tggcgagacc aacatgaaag tacgtcaggc    720 

gattccagtc acctcagaat tgggagacat cagtaagctt gccaagtttg acggtgaagt    780 

gatctgtgaa cctcccaaca acaaactgga caaattcagc ggaaccctct actggaagga    840 

aaataagttc cctctgagca accagaacat gctgctgcgg ggctgtgtgc tgcgaaacac    900 

cgagtggtgc ttcgggctgg tcatctttgc aggtcccgac actaagctga tgcaaaacag    960 

cggcagaaca aagttcaaaa gaacgagtat cgatcgccta atgaataccc tggtgctctg   1020 

gatttttgga ttcctggttt gcatgggggt gatcctggcc attggcaatg ccatctggga   1080 

gcacgaggtg gggatgcgtt tccaggtcta cctgccgtgg gatgaggcag tggacagtgc   1140 

cttcttctct ggcttcctct ccttctggtc ctacatcatc atcctcaaca ccgttgtgcc   1200 

catttcactc tatgtcagtg tggaggtcat ccgtctgggc cacagctact tcatcaactg   1260 

ggataagaag atgttctgca tgaagaagcg gacgcctgca gaagcccgca ccaccaccct   1320 

aaacgaggag ctgggccagg tggagtacat cttctccgac aagacgggca ccctcaccca   1380 

gaacatcatg gttttcaaca agtgctccat caatggccac agctatggtg atgtgtttga   1440 

cgtcctggga cacaaagctg aattgggaga gaggcctgaa cctgttgact tctccttcaa   1500 

tcctctggct gacaagaagt tcttattttg ggaccccagc ctgctggagg ctgtcaagat   1560 

cggggacccc cacacgcatg agttcttccg cctcctttcc ctgtgtcata ctgtcatgtc   1620 

agaagaaaag aacgaaggag agctgtacta caaagctcag tccccagatg agggggccct   1680 

ggtcaccgca gccaggaact ttggttttgt tttccgctct cgcaccccca aaacaatcac   1740 

cgtccatgag atgggcacag ccatcaccta ccagctgctg gccatcctgg acttcaacaa   1800 

catccgcaag cggatgtcgg tcatagtgcg gaatccagag gggaagatcc gactctactg   1860 

caaaggggct gacactatcc tactggacag actgcaccac tccactcaag agctgctcaa   1920 

caccaccatg gaccacctta atgagtacgc aggggaaggg ctgaggaccc tggtgctggc   1980 

ctacaaggat ctggatgaag agtactatga ggagtgggct gagcgacgcc tccaggccag   2040 

cctggcccag gacagccggg aggacaggct ggctagcatc tatgaggagg ttgagaacaa   2100 

catgatgctg ctgggtgcaa cggccattga ggacaaactt cagcaagggg ttccagagac   2160 

cattgccctc ctgacactgg ccaacatcaa gatttgggtg ctaaccggag acaagcaaga   2220 

gacggctgtg aacatcggct attcctgcaa gatgctgacg gatgacatga ctgaggtttt   2280 

catagtcact ggccatactg tcctggaggt gcgggaggag ctcaggaaag cccgggagaa   2340 

gatgatggac tcatcccgct ctgtaggcaa cggcttcacc tatcaggaca agctttcttc   2400 

ttccaagcta acttctgtcc tggaggccgt tgctggggag tacgccctgg tcataaatgg   2460 

tcacagcctg gcccacgcac tggaggcaga catggagctg gagtttctgg agacagcgtg   2520 

tgcctgcaaa gctgtcatct gctgccgggt gacccccttg cagaaggcac aggtggtaga   2580 

actggtcaag aagtacaaga aggctgtgac gcttgccatt ggagacggag ccaatgatgt   2640 

cagcatgatc aaaacggctc acattggtgt ggggatcagt gggcaggaag ggatccaggc   2700 

tgtcttggcc tccgattact ccttctccca gttcaagttc ctgcagcgcc tcctgctggt   2760 

gcatgggcgc tggtcctacc tgcgaatgtg caagtttctt tgctatttct tctacaaaaa   2820 

ctttgctttc accatggtcc acttctggtt tggcttcttc tgtggcttct cagcccagac   2880 

cgtctatgac cagtatttca tcaccctgta taacatcgtg tacacctccc tgccagtcct   2940 

ggctatgggg gtctttgatc aggatgtccc cgagcagcgg agcatggagt accctaagct   3000 

gtatgagccg ggccagctga accttctctt caacaagcgg gagttcttca tctgcatcgc   3060 

ccagggcatc tacacctccg tgctcatgtt cttcattccc tatggggtgt ttgctgatgc   3120 

cacccgggat gatggcactc agctggctga ctaccagtcc tttgcagtca ctgtggccac   3180 

atccttggtc attgtggtta gcgtgcagat tgggctcgac acaggctact ggacggccat   3240 

caaccacttc ttcatctggg gaagccttgc tgtttacttt gccatcctct ttgccatgca   3300 

cagcaatggg ctcttcgaca tgtttcccaa ccagttccgg tttgtgggga atgcccagaa   3360 

caccttggcc cagcccacgg tgtggctgac cattgtgctc accacagtcg tctgcatcat   3420 

gcccgtggtt gccttccgat tcctcaggct caacctgaag ccggatctct ccgacacggt   3480 

ccgctacaca cagctcgtga ggaagaagca gaaggcccag caccgctgca tgcggcgggt   3540 

tggccgcact ggctcccggc gctccggcta tgccttctcc catcaggagg gcttcgggga   3600 

gctcatcatg tctggcaaga acatgcggct gagctctctc gcgctctcca gcttcaccac   3660 

ccgctccagc tccagctgga ttgagagcct gcgcaggaag aagagtgaca gtgccagtag   3720 

ccccagtggc ggtgccgaca agcccctcaa gggctgaagg ccgaggatgg atgccctgtg   3780 

ccagtgacca gagcacccag ggctggccag tcactgaggg aacagcgtct cggaactgct   3840 

ggtcctcatt ccttgcttcc cgtccccccg gtagactctg tcctgctggt cccaccacac   3900 

atggctggga catctgttcc cagctgtagg cccttccacc agctggggag ctagagggag   3960 

caggcccaag ggcagagcag aggctgaggc acggggagcc agccccactc ggggaccaga   4020 

agtggaacca aaaacaagaa aaaactgtga gagattgtgt ctgcccctgc cctgcctggg   4080 

acccacaggg agactataat ctccttattt ttttactcct actccccaga ggggccctag   4140 

tgcctctgtt cctgaattac ataagaatgt accatgccgg gaagccagag acctgcaggg   4200 

gcctcggccc ctcacatcgt gtatgtctct ccttgatttg tgttgtgtcc agtttggttt   4260 

tgtctttttt tatttggcaa gtggaggagg cttttatgtg acttttatgt tgtggttggt   4320 

gtcttaactc tcctgggaaa aggaggctgg cacacactgg gatgccgcag cctggccggc   4380 

tgtggggtgg tttgggagga tccatgtcgg ctctgcctgc agtgaccagt gctctgtggg   4440 

gcagaggagc tgaccaggga gggaggtacc catgagcaga gggtagtggg agagtgtaaa   4500 

ggagggtttg gtcctgtctg cttcctcacc ttgagagtaa agtgctgccc tctgccccca   4560 

acacacacac atatcaattc ctggattcct tagtcctgct ggccttgggc tggagcctag   4620 

gaaagtggcc cccaaatcct tagtgagcta aagctgggtc tgaaatttgg tcagtgggga   4680 

ggggtagttt tcttttcttt tttctttttc tttttttctt tttttttttg agatggagtc   4740 

tcactcttgt cacctaggca agagtgcaat ggcacaatct cagctcactg caacctccac   4800 

ctcctgggtt caagcgattc tcctgcctcc ccggacccaa ccactggact taatctcact   4860 

ttcttaaatt cttctattct cagacacggg tctagtacca ttccttcctc ttagccccag   4920 

ggagcaaatt aaagaggtta cgagttaaaa tcctaaaaaa aaaaaaaaaa a            4971 

 
           
             37  
             1404  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7473347CB1  
             
           
            37 

atggtcctgg ctttccagtt agtctccttc acctacatct ggatcatatt gaaaccaaat     60 

gtttgtgctg cttctaacat caagatgaca caccagcggt gctcctcttc aatgaaacaa    120 

acctgcaaac aagaaactag aatgaagaaa gatgacagta ccaaagcgcg gcctcagaaa    180 

tatgagcaac ttctccatat agaggacaac gatttcgcaa tgagacctgg atttggaggg    240 

tctccagtgc cagtaggtat agatgtccat gttgaaagca ttgacagcat ttcagagact    300 

aacatggact ttacaatgac tttttatctc aggcattact ggaaagacga gaggctctcc    360 

tttcctagca cagcaaacaa aagcatgaca tttgatcata gattgaccag aaagatctgg    420 

gtgcctgata tcttttttgt ccactctaaa agatccttca tccatgatac aactatggag    480 

aatatcatgc tgcgcgtaca ccctgatgga aacgtcctcc taagtctcag gataacggtt    540 

tcggccatgt gctttatgga tttcagcagg tttcctcttg acactcaaaa ttgttctctt    600 

gaactggaaa gctatgccta caatgaggat gacctaatgc tatactggaa acacggaaac    660 

aagtccttaa atactgaaga acatatgtcc ctttctcagt tcttcattga agacttcagt    720 

gcatctagtg gattagcttt ctatagcagc acaggctggt acaataggct tttcatcatc    780 

tctgtgctaa ggaggcatgt tttcttcttt gtgctgccaa cctattaccc agccatattg    840 

atggtgatgc tttcatgggt ttcattttgg attgaccgaa gagctgttcc tgcaagagtt    900 

tccctgggaa tcaccacagt gctgaccatg tccacaatca tcactgctgt gagcgcctcc    960 

atgccccagg tgtcctacct caaggctgtg gatgtgtacc tgtgggtcag ctccctcttt   1020 

gtgttcctgt cagtcattga gtatgcagct gtgaactacc tcaccacagt ggaagagcgg   1080 

aaacaattca agaagacagg aaagatttct aggatgtaca atattgatgc agttcaagct   1140 

atggcctttg atggttgtta ccatgacagc gagattgaca tggaccagac ttccctctct   1200 

ctaaactcag aagacttcat gagaagaaaa tcgatatgca gccccagcac cgattcatct   1260 

cggataaaga gaagaaaatc cctaggagga catgttggta gaatcattct ggaaaacaac   1320 

catgtcattg acacctattc taggatttta ttccccattg tgtatatttt atttaatttg   1380 

ttttactggg gtgtatatgt atga                                          1404 

 
           
             38  
             4048  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7474240CB1  
             
           
            38 

cttccatccc ccctcagcca ttccttactg ctctgggcaa ccgccaggtt aagcccattt     60 

gcactgggaa attggcgctg tttgggagaa gagaaacaga tcgattgccc ttgtgactcc    120 

ccgccccctt cccatcccca cccccaccgc tctctccctc tttccctccc ccgccacctc    180 

ccctcacccc gcctccttcc cgttccccac ccccaaaccc tctcacccgc ggcagtccgg    240 

tgcgaggccc cctccggaag gtgaggggaa tggattggac tccggtggag aaagcgggtg    300 

tctagaagtg gtgctaatgg gaagagaatt ctggtttcaa aagaggatgc tctgccacaa    360 

agagcggctc gcgcgctggc ctgggctcta gccgaggaga gatcccggga ggactccaga    420 

gctccggggg agcgctcctc ggaagaccgg ggccaacatg cctgtgcgca gggggcatgt    480 

ggcaccacaa aatacatttc tggggaccat cattcggaaa tttgaagggc aaaataaaaa    540 

atttatcatt gcaaatgcca gagtgcagaa ctgtgccatc atttattgca acgatgggtt    600 

ctgtgagatg actggtttct ccaggccaga tgtcatgcaa aagccatgca cctgcgactt    660 

tctccatgga cccgagacca agaggcatga tattgcccaa attgcccagg cattgctggg    720 

gtcagaagag aggaaagtgg aggtcaccta ctatcacaaa aatgggtcca cttttatttg    780 

taacactcac ataattccag tgaaaaacca agagggcgtg gctatgatgt tcatcattaa    840 

ttttgaatat gtgacggata atgaaaacgc tgccacccca gagagggtaa acccaatatt    900 

accaatcaaa actgtaaacc ggaaattttt tgggttcaaa ttccctggtc tgagagttct    960 

cacttacaga aagcagtcct taccacaaga agaccccgat gtggtggtca tcgattcatc   1020 

taaacacagt gatgattcag tagccatgaa gcattttaag tctcctacaa aagaaagctg   1080 

cagcccctct gaagcagatg acacaaaagc tttgatacag cccagcaaat gttctccctt   1140 

ggtgaatata tccggacctc ttgaccattc ctctcccaaa aggcaatggg accgactcta   1200 

ccctgacatg ctgcagtcaa gttcccagct gtcccattcc agatcaaggg aaagcttatg   1260 

tagtatacgg agagcatctt cggtccatga tatagaagga ttcggcgtcc accccaagaa   1320 

catatttaga gaccgacatg ccagcgaaga caatggtcgc aatgtcaaag ggccttttaa   1380 

tcatatcaag tcaagcctcc tgggatccac atcagattca aacctcaaca aatacagcac   1440 

cattaacaag attccacagc tcactctgaa tttttcagag gtcaaaactg agaaaaagaa   1500 

ttcatcacct ccttcttcag ataaaaccat tattgcaccc aaggttaaag atcgaacaca   1560 

caatgtgact gagaaagtga cccaggttct ctctttagga gcagatgtcc tacctgaata   1620 

caaactgcag acaccacgca tcaacaagtt tacgatattg cactacagcc ctttcaaggc   1680 

agtctgggac tggcttatcc tgctgttggt catatacact gctatattta ctccctactc   1740 

tgcagccttc ctcctcaatg acagagaaga acagaaaaga cgagaatgtg gctattcttg   1800 

tagccctttg aatgtggtag acttgattgt ggatattatg tttatcatag atattttaat   1860 

aaacttcaga acaacatatg taaatcagaa tgaagaagtg gtaagtgatc ccgccaaaat   1920 

agcaatacac tacttcaaag gctggttcct gattgacatg gttgcagcaa ttccttttga   1980 

cttgctgatt tttggatcag gttctgatga gacaacaaca ttaattggtc ttttgaagac   2040 

tgcccgactc ctccgtcttg tgcgcgtggc caggaaactg gatcgatatt cagaatatgg   2100 

cgctgctgtt ctaatgctct taatgtgcat ctttgccctg attgctcact ggctggcttg   2160 

catttggtat gcgattggga atgtagaaag gccttacctg actgacaaaa tcggatggtt   2220 

ggattcctta ggacagcaaa ttgggaaacg ttacaatgac agtgactcaa gttctggacc   2280 

atccattaaa gacaaatacg tcacagcact ttattttacc ttcagcagtt taaccagtgt   2340 

aggattcggg aatgtgtctc ctaacacgaa ttcggagaaa atcttttcaa tttgtgtcat   2400 

gttgattggc tcactaatgt atgcaagcat ttttgggaat gtatctgcaa ttatccaaag   2460 

actatactcg ggaactgcca ggtaccacat gcagatgctg cgagtaaaag agttcattcg   2520 

ctttcaccaa atccccaacc ctctgaggca acgtcttgaa gaatatttcc agcacgcatg   2580 

gacttacacc aatggcattg acatgaacat ggtcctaaag ggtttcccag aatgcttaca   2640 

agcagacatt tgtctacatc tcaaccagac attgctgcaa aactgcaaag cctttcgggg   2700 

ggcaagtaaa ggttgcctta gagctttggc aatgaagttc aaaaccaccc atgcacctcc   2760 

aggagacacc ctcgttcact gtggggatgt cctcactgca ctttatttct tatccagagg   2820 

ctccattgaa attctcaaag atgacattgt ggtggctatt ctgggaaaaa atgatatatt   2880 

tggagaaatg gttcatcttt atgccaaacc tggaaagtct aatgcagatg taagagccct   2940 

cacatactgt gacttgcata agattcagcg agaagacttg ttagaggttt tggatatgta   3000 

tcctgagttt tctgatcact ttctaacaaa cctagagttg actttcaacc taaggcatga   3060 

gagcgcaaag gctgatctcc tacgatcaca atccatgaat gattcagaag gagacaactg   3120 

taaactaaga agaaggaaat tgtcatttga aagtgaagga gagaaagaaa acagtacaaa   3180 

tgatcctgaa gactctgcag ataccataag acattatcag agttccaaga gacactttga   3240 

agagaaaaaa agcagatcct catctttcat ctcctccatt gatgatgaac aaaagccgct   3300 

cttctcagga atagtagact cttctccagg aatagggaaa gcatctgggc tcgattttga   3360 

agaaacagtg cccacctcag gaagaatgca catagataaa agaagtcact cttgcaaaga   3420 

tatcactgac atgcgaagct gggaacgaga aaatgcacat ccccagcctg aagactccag   3480 

tccatctgca cttcagcgag ctgcctgggg tatctctgaa accgaaagcg acctcaccta   3540 

cggggaagtg gaacaaagat tagatctgct ccaggagcaa cttaacaggc ttgaatccca   3600 

aatgaccact gacatccaga ccatcttaca gttgctgcag aaacaaacca ctgtggtccc   3660 

cccagcctac agtatggtaa cagcaggatc agaatatcag agacccatca tccagctgat   3720 

gagaaccagt caaccggaag catccatcaa aactgaccga agtttcagcc cttcctcaca   3780 

atgtcctgaa tttctagacc ttgaaaaatc taaacttaaa tccaaagaat ccctttcaag   3840 

tggggtgcat ctgaacacag cttcagaaga caacttgact tcacttttaa aacaagacag   3900 

tgatctctct ttagagcttc acctgcggca aagaaaaact tacgttcatc caattaggca   3960 

tccttctttg ccagattcat ccctaagcac tgtaggaatc gtgggtcttc ataggcatgt   4020 

ttctgatcct ggtcttccag ggaaataa                                      4048 

 
           
             39  
             1539  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7475338CB1  
             
           
            39 

atggagaaca aagaggcggg aacccctcca cccattccat ccagggaggg gcggctccag     60 

ccgacgctgt tgctggcgac actgagcgcg gcctttggct cagccttcca gtacggctac    120 

aacctctctg tggtcaacac gccgcacaag gtgttcaagt cattttacaa cgaaacctac    180 

tttgagcgac acgcaacatt catggacggg aagctcatgc tgcttctatg gtcttgcacc    240 

gtctccatgt ttcctctggg cggcctgttg gggtcattgc tcgtgggcct gctggttgat    300 

agctgcggca ggaaggggac cctgctgatc aacaacatct ttgccatcat ccccgccatc    360 

ctgatgggag tcagcaaagt ggccaaggct tttgagctga tcgtcttttc ccgagtggtg    420 

ctgggagtct gtgcaggtat ctcctacagc gcccttccca tgtacctggg agaactggcc    480 

cccaagaacc tgagaggcat ggtgggaaca atgaccgagg ttttcgtcat cgttggagtc    540 

ttcctagcac agatcttcag cctccaggcc atcttgggca acccggcagg ttggccggtg    600 

cttctggcgc tcacaggggt gcccgccctg ctgcagctgc tgaccctgcc cttcttcccc    660 

gaaagccccc gctactccct gattcagaaa ggagatgaag ccacagcgcg acaagctctg    720 

aggaggctga gaggccacac ggacatggag gccgagctgg aggacatgcg tgcggaggcc    780 

cgggccgagc gcgccgaggg ccacctgtct gtgctgcacc tctgtgccct gcggtccctg    840 

cgctggcagc tcctctccat catcgtgctc atggccggcc agcagctgtc gggcatcaat    900 

gcgatcaact actatgcgga caccatctac acatctgcgg gcgtggaggc cgctcactcc    960 

caatatgtaa cggtgggctc tggcgtcgtc aacatagtga tgaccatcac ctcggctgtc   1020 

cttgtggagc ggctgggacg gcggcacctc ctgctggccg gctacggcat ctgcggctct   1080 

gcctgcctgg tgctgacggt ggtgctccta ttccagaaca gggtccccga gctgtcctac   1140 

ctcggcatca tctgtgtctt tgcctacatc gcgggacatt ccattgggcc cagtcctgtc   1200 

ccctcggtgg tgaggaccga gatcttcctg cagtcctccc ggcgggcagc tttcatggtg   1260 

gacggggcag tgcactggct caccaacttc atcataggct tcctgttccc atccatccag   1320 

gaggccatcg gtgcctacag tttcatcatc tttgccggaa tctgcctcct cactgcgatt   1380 

tacatctacg tggttattcc ggagaccaag ggcaaaacat ttgtggagat aaaccgcatt   1440 

tttgccaaga gaaacagggt gaagcttcca gaggagaaag aagaaaccat tgatgctggg   1500 

cctcccacag cctctcctgc caaggaaact tccttttag                          1539 

 
           
             40  
             3114  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7476747CB1  
             
           
            40 

ccaagcagtg cctcacttct gccttgtcta gctgtactct ggaaaattaa gaaatttatg     60 

agtgtagcac caagtatacc aatgggaagg atgggagtca gaagtcaagt gaactcagcc    120 

cgcctctgtg tactttgcac ttttccattt cccttggtac caggcacttt catacttaat    180 

ccatagtgga gctgtcacag tgagcaactc tgacaatgac agcttctacc ccagaggcga    240 

ccccaaacat ggagctaaag gctccagctg caggaggtct taatgctggc cctgtccccc    300 

cagctgccat gtccacgcag agacttcgga atgaagacta ccacgactac agctccacgg    360 

acgtgagccc tgaggagagc ccgtcggaag gcctcaacaa cctctcctcc ccgggctcct    420 

accagcgctt tggtcaaagc aatagcacaa catggttcca gaccttgatc cacctgttaa    480 

aaggcaacat tggcacagga ctcctgggac tccctctggc ggtgaaaaat gcaggcatcg    540 

tgatgggtcc catcagcctg ctgatcatag gcatcgtggc cgtgcactgc atgggtatcc    600 

tggtgaaatg tgctcaccac ttctgccgca ggctgaataa atcctttgtg gattatggtg    660 

atactgtgat gtatggacta gaatccagcc cctgctcctg gctccggaac cacgcacact    720 

ggggaagacg tgttgtggac ttcttcctga ttgtcaccca gctgggattc tgctgtgtct    780 

attttgtgtt tctggctgac aactttaaac aggtgataga agcggccaat gggaccacca    840 

ataactgcca caacaatgag acggtgattc tgacgcctac catggactcg cgactctaca    900 

tgctctcctt cctgcccttc ctggtgctgc tggttttcat caggaacctc cgagccctgt    960 

ccatcttctc cctgttggcc aacatcacca tgctggtcag cttggtcatg atctaccagt   1020 

tcattgttca gaggatccca gaccccagcc acctcccctt ggtggcccct tggaagacct   1080 

accctctctt ctttggcaca gcgatttttt catttgaagg cattggaatg gttctgcccc   1140 

tggaaaacaa aatgaaggat cctcggaagt tcccactcat cctgtacctg ggcatggtca   1200 

tcgtcaccat cctctacatc agcctggggt gtctggggta cctgcaattt ggagctaata   1260 

tccaaggcag cataaccctc aacctgccca actgctggtt gtaccagtca gttaagctgc   1320 

tgtactccat cgggatcttt ttcacctacg cactccagtt ctacgtcccg gctgagatca   1380 

tcatcccctt ctttgtgtcc cgagcgcccg agccctgtga gttagtggtg gacctgtttg   1440 

tgcgcccagt gctggtctgc ctgacatcac tgtctggcag tgttgacaat ggctggtatg   1500 

gcacggaagc cgatggcacc tcctgcggca gtgcaccatt ggtcttcgtc agttcctcct   1560 

tcctggctca cccgtggctg agtttcagat gtgagagcca gtgggtgtcc tgtcacagag   1620 

atacggtcgt cgtgtggggc ttcgccaggg gcatcttggc catcctcatc ccccgcctgg   1680 

acctggtcat ctccctggtg ggctccgtga gcagcagcgc cctggccctc atcatcccac   1740 

cgctcctgga ggtcaccacc ttctactcag agggcatgag ccccctcacc atctttaagg   1800 

acgccctgat cagcatcctg ggcttcgtgg gctttgtggt ggggacctat gaggctctct   1860 

atgagctgat ccagccaagc aatgctccca tcttcatcaa ttccacctgt gccttcatat   1920 

agggatctgg gttcgtctct gcagctgcct acccctgccc catgtgtccc ccgttacctg   1980 

tcctcagagc ctcaggtatg gtccaggctc tgaggaaagt cagggttgct gtgtgggaac   2040 

ccctctgcct ggcacctgga taccctgggc caggtaacct gagggcagtg gagaggtggg   2100 

gtggcagaca cgcagaagtg ctactagtga cagggctgcc atcgctcacc tgtacctatt   2160 

tacacccaga actttccagc tccccctcat catgcctcct ccttcctacc tgcctcccct   2220 

ctgctggtgc acctcgccca actcattctt actgcacagt tcactttatt taacaatttt   2280 

catgtccccc acctcatgtt ttcacctttt ctgggccagg catagattaa gtaactggga   2340 

acgccccctc tttataaagc tgggcttctt tctcatctct ctcccaaatg ttgtatctca   2400 

gtattcttcc tattcgagtc tccagggggt ggctggacct acctggtcat ttgaaacagg   2460 

cccccaagct ggagttttta atctggactc tctggcttgc tgtgacccct aaggcaatgc   2520 

ttctcttccc tggattcctt agtgtgggtc acagtactgt gttcttagtt gctttagctc   2580 

ttaaaacata cgaagtgttg cctaaactga aaatatttat cttttattta aaatcagatt   2640 

tttgttttta gactgtctta gatctggggc tattacgaat cacttcttct tcagtaaact   2700 

ttgactcaac ttctcctgct gaaaagaagc tcgctccaga tgtctgcatg ggtcctcggc   2760 

actcttggct gaggactcaa aggttttaat caggatcgtc taaaaatgta cctcggtgag   2820 

gaggcacaga ttttgcctcc tgttgaccag cctggtttca taccgaaaag acattgaagg   2880 

actgcagaaa tgtatgggtg caccgggccg agggaagggt ggctgagtga gaggcgtata   2940 

aaatggggct gtgtgcatgc aggcccatgt ttcagcctca gcccacgcca ggtgaaagga   3000 

tcagcaatgc tctgttgcca tcgtgctggg acgacaccag ctctattgcc accgatgagt   3060 

agctgaggtc agtgtgcaca gagtttgaaa ttaagttaat agactttaca gcag         3114 

 
           
             41  
             2877  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477898CB1  
             
           
            41 

atgccggtcc gcaggggcca cgtcgctccc caaaacactt acctggacac catcatccgc     60 

aagttcgagg gccaaagtcg gaagttcctg attgccaatg ctcagatgga gaactgcgcc    120 

atcatttact gcaacgacgg cttctgcgaa ctcttcggct actcccgagt ggaggtgatg    180 

cagcaaccct gcacctgcga cttcctcaca ggccccaaca caccaagcag cgccgtgtcc    240 

cgcctagcgc aggccctgct gggggctgag gagtgcaagg tggacatcct ctactaccgc    300 

aaggatgcct ccagcttccg ctgcctggta gatgtggtgc ccgtgaagaa cgaggacggg    360 

gctgtcatca tgttcattct caacttcgag gacctggccc agctcctggc caagtgcagc    420 

agccgcagct tgtcccagcg cctgttgtcc cagagcttcc tgggctccga gggctctcat    480 

ggcaggccag gcggaccagg gccaggcaca ggcaggggca agtacaggac catcagccag    540 

atcccacagt tcacgctcaa cttcgtggag ttcaacttgg agaagcaccg ctccagctcc    600 

accacggaga ttgagatcat cgcgccccat aaggtggtgg agcggacaca gaacgtcact    660 

gagaaggtca cccaggtcct gtccctgggc gcggatgtgc tgccggagta caagctgcag    720 

gcgccgcgca tccaccgctg gaccatcctg cactacagcc ccttcaaggc cgtgtgggac    780 

tggctcatcc tgctgctggt catctacacg gctgtcttca cgccctactc agccgccttc    840 

ctgctcagcg atcaggacga atcacggcgt ggggcctgca gctatacctg cagtcccctc    900 

actgtggtgg atctcatcgt ggacatcatg ttcgtcgtgg acatcgtcat caacttccgc    960 

accacctatg tcaacaccaa tgatgaggtg gtcagccacc cccgccgcat cgccgtccac   1020 

tacttcaagg gctggttcct cattgacatg gtggccgcca tccctttcga cctcctgatc   1080 

ttccgcactg gctccgatga gaccacaacc ctgattgggc tattgaagac agcgcggctg   1140 

ctgcggctgg tgcgcgtagc acggaagctg gaccgctact ctgagtatgg ggcggctgtg   1200 

ctcttcttgc tcatgtgcac ctttccgctc atagcgcact ggctggcctg catctggtac   1260 

gccatcggca atgtggagcg gccctaccta gaacacaaga tcggctggct ggacagcctg   1320 

ggtgtgcagc ttggcaagcg ctacaacggc agcgacccag cctcgggccc ctcggtgcag   1380 

gacaagtatg tcacagccct ctacttcacc ttcagcagcc tcaccagcgt gggcttcggc   1440 

aatgtctcgc ccaacaccaa ctccgagaag gtcttctcca tctgcgtcat gctcatcggc   1500 

tccctgatgt acgccagcat cttcgggaac gtgtccgcga tcatccagcg cctgtactcg   1560 

ggcaccgcgc gctaccacac gcagatgctg cgtgtcaagg agttcatccg cttccaccag   1620 

atccccaacc cactgcgcca gcgcctggag gagtatttcc agcacgcctg gtcctacacc   1680 

aatggcattg acatgaacgc ggtgctgaag ggcttccccg agtgcctgca ggctgacatc   1740 

tgcctgcacc tgcaccgcgc actgctgcag cactgcccag ctttcagcgg cgccggcaag   1800 

ggctgcctgc gcgcgctagc cgtcaagttc aagaccaccc acgcgccgcc tggggacacg   1860 

ctggtgcacc tcggcgacgt gctctccacc ctctacttca tctcccgagg ctccatcgag   1920 

atcctgcgcg acgacgtggt cgtggccatc ctaggaaaga atgacatctt tggggaaccc   1980 

gtcagcctcc atgcccagcc aggcaagtcc agtgcagacg tgcgggctct gacctactgc   2040 

gacctgcaca agatccagcg ggcagatctg ctggaggtgc tggacatgta cccggccttt   2100 

gcggagagct tctggagtaa gctggaggtc accttcaacc tgcgggacgt aaccgggggt   2160 

ctccactcat ccccccgaca ggctcctggc agccaagacc accaaggttt ctttctcagt   2220 

gacaaccagt cagatgcagc ccctcccctg agcatctcag atgcattctg gctctggcct   2280 

gagctactgc aggaaatgcc cccaaagcac agcccccaaa gccctcagga agacccagat   2340 

tgctggcctc tgaagctggg ctccaggcta gagcagctcc aggcccagat gaacaggctg   2400 

gagtcccgcg tgtcctcaga cctcagccgc atcttgcagc tcctccagaa gcccatgccc   2460 

cagggccacg ccagctacat tctggaagcc cctgcctcca atgacctggc cttggttcct   2520 

atagcctcgg agacgacgag tccagggccc aggctgcccc agggctttct gcctcctgca   2580 

cagaccccaa gctatggaga cttggatgac tgtagtccaa agcacaggaa ctcctccccc   2640 

aggatgcctc acctggctgt ggcaatggac aaaactctgg caccatcctc agaacaggaa   2700 

cagcctgagg ggctctggcc acccctagcc tcacctctac atcccctgga agtacaagga   2760 

ctcatctgtg gtccctgctt ctcctccctc cctgaacacc ttggctctgt tcccaagcag   2820 

ctggacttcc agagacatgg ctcagatcct ggatttgcag ggagttgggg ccactga      2877 

 
           
             42  
             2820  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7472728CB1  
             
           
            42 

atggggcatc aagggccatt tgaagaagga aatggtggac tgagagtgat agcgacctgg     60 

aggaggaagg aggcttggag aagggactgt cttttaggag ccctgcccag tgtttcctgt    120 

ggagggtggg gccatcgtgg aagacagacc tatggtaggg cttgtggggt gaaagaaaag    180 

ccctttagtc ttttgggtcc tcaaatcaca gtttatgcag tttggcccca gtcagaggga    240 

ccccaggaag gcagactcag ggtaaattct gcctgtcttc caccagagag gggactcacc    300 

aacgcttgta caaaccatga agaactctct ttggactgtt tgctttttga gaatgttaac    360 

accttgactc tggatttctg cctatgggaa aaaaccacaa tagtgccagg ggtgcttcca    420 

tatgcaggat taactctgca gtcaaagttt ctgttgggca gagcattgtt agcaggggtc    480 

catgtgatca cactgacacc tgagagagtg acacaccatg tacatggctg gtatatggag    540 

gatggattta agggggacag gactgaaggc tgtcgcagtg attcagtggc cgttcccgca    600 

gcagcaccgg tgtgccagcc caagagcgcc actaacgggc aacccccggc tccggctccg    660 

actccaactc cgcgcctgtc catttcctcc cgagccacag tggtagccag gatggaaggc    720 

acctcccaag ggggcttgca gaccgtcatg aagtggaaga cggtggttgc catctttgtg    780 

gttgtggtgg tctaccttgt cactggcggt cttgtcttcc gggcattgga gcagcccttt    840 

gagagcagcc agaagaatac catcgccttg gagaaggcgg aattcctgcg ggatcatgtc    900 

tgtgtgagcc cccaggagct ggagacgttg atccagcatg ctcttgatgc tgacaatgcg    960 

ggagtcagtc caataggaaa ctcttccaac aacagcagcc actgggacct cggcagtgcc   1020 

tttttctttg ctggaactgt cattacgacc atgtatggga atattgctcc gagcactgaa   1080 

ggaggcaaaa tcttttgtat tttatatgcc atctttggaa ttccactctt tggtttctta   1140 

ttggctggaa ttggagacca acttggaacc atctttggga aaagcattgc aagagtggag   1200 

aaggtctttc gaaaaaagca agtgagtcag accaagatcc gggtcatctc aaccatcctg   1260 

ttcatcttgg ccggctgcat tgtgtttgtg acgatccctg ctgtcatctt taagtacatc   1320 

gagggctgga cggccttgga gtccatttac tttgtggtgg tcactctgac cacggtgggc   1380 

tttggtgatt ttgtggcagt ggttgttttc aggggaaacg ctggcatcaa ttatcgggag   1440 

tggtataagc ccctagtgtg gttttggatc cttgttggcc ttgcctactt tgcagctgtc   1500 

ctcagtatga tcggagattg gctacgggtt ctgtccaaaa agacaaaaga agaggtgggt   1560 

gaaatcaagg cccatgcggc agagtggaag gccaatgtca cggctgagtt ccgggagaca   1620 

cggcgaaggc tcagcgtgga gatccacgat aagctgcagc gggcagccac catccgcagc   1680 

atggagcgcc ggcggctggg cctggaccag cgggcccact cactggacat gctgtccccc   1740 

gagaagcgct ctgtctttgc tgccctggac accggccgct tcaaggcctc atcccaggag   1800 

agcatcaaca accggcccaa caacctgcgc ctgaaggggc cggagcagct gaacaagcat   1860 

gggcagggtg cgtccgagga caacatcatc aacaagttcg ggtccacctc cagactcacc   1920 

aagaggaaaa acaaggacct caaaaagacc ttgcccgagg acgttcagaa aatctacaag   1980 

accttccgga attactccct ggacgaggag aagaaagagg aggagacgga aaagatgtgt   2040 

aactcagaca actccagcac agccatgctg acggactgta tccagcagca cgctgagttg   2100 

gagaacggaa tgatacccac ggacaccaaa gaccgggagc cggagaacaa ctcattactt   2160 

gaagacagaa actaaatgtg aaggacattg gtcttggact gagcgttgtg tgtgtgtgtg   2220 

tgtgtgtgtt tttaatattc acactgagac atgtgcctta aacagacttt ttagtccaaa   2280 

attacatagc attgaagaat atatttcact gtgccataaa caactgaaag cttgctctgc   2340 

caaaaggaat cagagaacaa gaacttcatt tcagatagca aacgcaggac acaccaagag   2400 

tgtccgtgca cgtagccggt tctggccgta catgttaagg gcatttcagt ggcagtgctg   2460 

tacccctggg cagtgctacc tgggcacaca cgtagacaag ggcagctatt ccttagacca   2520 

gcctcctgaa agaaacaggt gtgtcttttt agtggagtcg tagtaatatg tgcacacaca   2580 

gaaggggacc tgattgggtg ggagctggtt atgtgtaact agcgttggag ttgacatttt   2640 

ggcatgtgct ctgagcttga attttgatac caaccattca gtgcatcata cctagtcttt   2700 

ctatgctcca aatgaatgtc tgtggggacc tgagagcacc tggaatttgt tggaagcaga   2760 

tcagagcaca cgtacgaaaa ggtgcaattc cttttctcat gacaaaaggg aaaaaaataa   2820 

 
           
             43  
             1440  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7474322CB1  
             
           
            43 

atgtacaatg agattctgat gctgggggcc aaactgcacc cgacgctgaa gctggaggag     60 

ctcaccaaca agaagggaat gacgccgctg gctctggcag ctgggaccgg gaagatcggg    120 

aatcgccacg acatgctctt ggtggagccg ctgaaccgac tcctgcagga caagtgggac    180 

agattcgtca agcgcatctt ctacttcaac ttcctggtct actgcctgta catgatcatc    240 

ttcaccatgg ctgcctacta caggcccgtg gatggcttgc ctccctttaa gatggaaaaa    300 

actggagact atttccgagt tactggagag atcctgtctg tgttaggagg agtctacttc    360 

tttttccgag ggattcagta tttcctgcag aggcggccgt cgatgaagac cctgtttgtg    420 

gacagctaca gtgagatgct tttgtttctg cagtcactgt tcatgctggc caccgtggtg    480 

ctgtacttca gccacctcaa ggagtatgtg gcttccatgg tattctccct ggccttgggc    540 

tggaccaaca tgctctacta cacccgcggt ttccagcaga tgggcatcta tgccgtcatg    600 

atagagaaga tgatcctgag agacctgtgc cgtttcatgt ttgtctacat cgtcttcttg    660 

ttcgggtttt ccacagcggt ggtgacgctg attgaagacg ggaagaatga ctccctgccg    720 

tctgagtcca cgtcgcacag gtggcggggg cctgctngca ggcccaatag ctcctacaac    780 

agcctgtact ccacctgcct ggagctgttc aagttcacca tcggcatggg cgacctggag    840 

ttcactgaga actatgactt caaggctgtc ttcatcatcc tgctgctggc ctatgtaatt    900 

ctcacctaca tagttctcct cctcaacatg ctcattgctc tgatgggcga gactgtggag    960 

aacgtctcca aggagagcga acgcatctgg cgcctgcaga gagccatcac catcctggac   1020 

acggagaaga gcttccttaa gtgcatgagg aaggccttcc gctcaggcaa gctgctgcag   1080 

gtggggtaca cacctgatgg caaggacgac taccggtggt gcttcgtgga cgaggtgaac   1140 

tggaccacct ggaacaccaa cgtgggcatc atcaacgaag acccgggcaa ctgtgagggc   1200 

gtcaagcgca ccctgagctt ctccctgcgg tcaagcagag tttcaggcag acactggaag   1260 

aactttgccc tggtccccct tttaagagag gcaagtgctc gagataggca gtctgctcag   1320 

cccgaggaag tttatctgcg acagttttca gggtctctga agccagagga cgctgaggtt   1380 

ttcaagagtc ctgccgcttc cggggagaag tgaggacgtc acgcagacag cactgtcaac   1440 

 
           
             44  
             2394  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 5455621CB1  
             
           
            44 

atttcagaac acatctgaat tccttctctg tggcatatgc tttaggagag gagcagacag     60 

ctcttagcta gggtcagatt tcaaattctc atctcttggt gccaatacca ccaccagatt    120 

cttctttgaa gtcaactttt gagatcttca ctaagtacac gttggtgtct gaagattcac    180 

acgagtgcct ctggtaatca ttttcttcag ggaatcacag tctctcctct cagcaaagca    240 

tccactgtac tgaactttgc ttttggaaac atcttcttcc tgagacctcg ttgaaagaaa    300 

ctctctggtg tcatactttc caatatggag gtgaagaact ttgcagtttg ggattatgtt    360 

gtatttgcag ccctcttttt catttcctct ggaattgggg tgttctttgc cattaaggag    420 

agaaaaaagg caacttcccg agagttcctg gttgggggaa ggcaaatgag ctttggccct    480 

gtcggcttgt ctctgacagc cagcttcatg tcagctgtca cggtcctggg gaccccttct    540 

gaagtctacc gctttggggc atccttccta gtcttcttca ttgcttacct atttgtcatc    600 

ctcttaacat cagagctctt tctccctgtg ttctacagat ctggtatcac cagcacttat    660 

gagtacttac aactacgatt caacaaacca gttcgctatg ctgccacagt catctacatt    720 

gtacagacga ttctctacac aggagtggtg gtgtatgctc ctgccctggc actcaatcaa    780 

gtgactgggt ttgatctctg gggctctgtg tttgcaacag gaattgtttg cacattctac    840 

tgtaccctgg gaggattaaa agcagtggtg tggacagatg catttcagat ggttgtcatg    900 

attgtgggct tcttaacggt tctcattcaa ggatcaactc atgctggggg attccacaat    960 

gtattagagc aatcaacaaa tggatctcga ctacatatat ttgactttga tgtagatcct   1020 

ctcaggcgac acactttttg gactatcaca gtgggaggaa cttttacttg gctcggaatc   1080 

tatggggtca atcaatcaac tattcagcga tgcatctctt gcaaaacaga aaagcatgct   1140 

aagcttgcct tgtattttaa cttgctgggt ctctggatca ttctggtgtg tgctgtcttc   1200 

tctggcttaa tcatgtactc tcactttaaa gactgtgacc cttggacttc tggcatcatc   1260 

tcagcaccag accagctgat gccgtacttt gtcatggaga tatttgccac aatgccagga   1320 

ctgccaggac tttttgtggc ttgtgccttc agtggaactc tgagcaccgt ggcttccagc   1380 

atcaatgcct tggcaacagt gacctttgag gattttgtca agagctgttt tcctcatctc   1440 

tccgacaagc tgagcacctg gatcagtaaa ggcttatgtc tcttatttgg cgtgatgtgt   1500 

acctctatgg ctgtggctgc atctgtcatg ggaggtgttg tgcaggcttc cctcagcatt   1560 

cacggcatgt gtggaggacc aatgctgggc ttattctccc tgggaatcgt gttccctttt   1620 

gtgaactgga agggtgcact aggaggtctt cttactggaa tcaccttgtc attttgggtg   1680 

gccattgggg ccttcattta ccctgcacca gcctctaaga catggccttt gcctctatca   1740 

acagaccaat gtatcaaatc aaatgtgaca gcaacagggc ctccagtact atccagcaga   1800 

cctggaatag ctgatacctg gtactcgatc tcctaccttt actacagtgc actgggctgc   1860 

ttaggatgca ttgttgctgg agtaatcatc agcctcataa caggtcgcca aagaggtgag   1920 

gatattcaac cactgttaat tagaccagtt tgtaatttat tttgcttttg gtctaagaag   1980 

tacaaaacac tatgctggtg tggagttcag catgacagtg ggacagagca ggaaaacctt   2040 

gagaatggca gtgcccggaa acagggggct gaatctgtct tacagaacgg actcagaaga   2100 

gaaagcctgg tacatgttcc aggctatgat cctaaggaca aaagctacaa caatatggca   2160 

tttgagacta cccatttcta aggcaatacc tgtatgaatg cacacacaca cgtgcaatac   2220 

acacacacac acacaaactc cacatacttc ttgcctactt gttagtagat atgtatagtt   2280 

gccattgcta gaagacaggg atgtctggtg cctatttcta cttatttata actacatgca   2340 

aaatgactgt ctctcgggat attctttgaa agactccaac tttcacagag aaaa         2394 

 
           
             45  
             2890  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477248CB1  
             
           
            45 

gaatactaag ccagggcaga atgcttgtga agtagcaact aaagtggcag tgtttcttct     60 

gaaattctca ggcagtcaga ctgtcttagg caaatcttga taaaatagcc cttatccagg    120 

tttttatcta aggaatccca agaagactgg ggaatggaga gacagtcaag ggttatgtca    180 

gaaaaggatg agtatcagtt tcaacatcag ggagcggtgg agctgcttgt cttcaatttt    240 

ttgctcatcc ttaccatttt gacaatctgg ttatttaaaa atcatcgatt ccgcttcttg    300 

catgaaactg gaggagcaat ggtgtatggc cttataatgg gactaatttt acgatatgct    360 

acagcaccaa ctgatattga aagtggaact gtctatgact gtgtaaaact aactttcagt    420 

ccatcaactc tgctggttaa tatcactgac caagtttatg aatataaata caaaagagaa    480 

ataagtcagc acaacatcaa tcctcatcaa ggaaatgcta tacttgaaaa gatgacattt    540 

gatccagaaa tcttcttcaa tgttttactg ccaccaatta tatttcatgc aggatatagt    600 

ctaaagaaga gacacttttt tcaaaactta ggatctattt taacgtatgc cttcttggga    660 

actgccatct cctgcatcgt catagggtta attatgtatg gttttgtgaa ggctatgata    720 

catgctggcc agctgaaaaa tggagacttt catttcactg actgtttatt ttttggttca    780 

ctgatgtctg ctacagatcc agtgacagtg ctggccattt tccatgaact gcacgtcgac    840 

cctgacctgt acacactctt gtttggagag agtgtgttga atgatgcagt ggccatagtc    900 

cttacatatt ctatatccat ttacagtccc aaggagaatc caaatgcatt tgatgccgca    960 

gcattcttcc agtctgtggg gaatttcctg ggaatcttcg ctggctcatt tgcaatgggg   1020 

tctgcgtatg ccatcatcac agcactgttg accaaattta ccaagctgtg tgagttcccg   1080 

atgctggaaa ccggcctgtt tttcctgctt tcttggagtg ccttcctgtc tgccgaggct   1140 

gccggcctaa cagggatagt tgctgttctc ttctgtggag tcacacaagc acattatacc   1200 

tacaacaatc tgtcttcgga ttccaaaata agaactaaac agttgtttga atttatgaac   1260 

tttttggcgg agaacgtcat cttctgttac atgggcctgg cactgttcac gttccagaat   1320 

catatcttta atgctctttt tatacttgga gcctttctag caatttttgt tgccagagcc   1380 

tgcaacatat atcccctctc cttcctcctg aatctaggcc gaaaacagaa gatcccctgg   1440 

aactttcagc acatgatgat gttttcaggt ttgcgaggag cgatcgcatt tgccttagct   1500 

attcggaaca cagaatctca gcccaaacaa atgatgttta ccactacgct gctcctcgtg   1560 

ttcttcactg tctgggtatt tggaggagga acaaccccca tgttgacttg gcttcagatc   1620 

agagttggcg tggacctgga tgaaaatctg aaggaggacc cctcctcaca acaccaggaa   1680 

gcaaataact tggataaaaa catgacgaaa gcagagagtg ctcggctctt cagaatgtgg   1740 

tatagctttg accacaagta tctgaaacca attttaaccc actctggtcc tccgctgact   1800 

acaacattac ctgaatggtg tggtccgatt tccaggctgc ttaccagtcc tcaagcctat   1860 

ggggaacagc taaaagagga tgatgtggaa tgcattgtaa accaggatga actagccata   1920 

aattaccagg agcaagcctc ctcaccctgc agtcctcctg caaggctagg tctggaccag   1980 

aaagcttcac cccagacgcc aggcaaggaa aacatttatg agggagacct cggccctggg   2040 

aggctatgaa ctcaagcttg agcaaacttt gggtcaatcc cagttgaatt aattggcatg   2100 

aagagtacag atgtaatcac aagtaatgca agactcactg aggaatacaa gccaagctga   2160 

tgaggcagta caggggagag gctggaaaac atattaagag cataaattgg agagaatcaa   2220 

agccttgtca catggatcct ctggtgcctg aagaaatgag attttattat ccctctctat   2280 

tatgcaaatg aatttagttt tttgacagca gccattctga ttactggatt ggctggggtg   2340 

gggatggagg tatcaggagt ctagctgctg gaggatggga cagctgtgct gggtcttcag   2400 

ggcatttctg ctgcgaatgc ggctctccag gcccttcact tctattctgg attttattcc   2460 

ctccattaag gagagtttaa aaataaaaga aagcttctga gagtaaacat tttgctccta   2520 

agctgaaggg aatgcccagc tatttagtaa gtgataagtt tcttattttg aggacttgac   2580 

tcccatttgc tctcagtgac cccagggcag agcccagaga agtgttccgt acccactgct   2640 

gatggtttcc cagagcccac actgagttga agaacctatt gttcttcttg gcatccttct   2700 

tatgctactt ctcccatcgc tcaaaggggt tgcctatggc tgggtgtgcc ctgccctaaa   2760 

tgcagcacca ctttcaagca gcttctagct atagctttcc accaggtatt tttaatccca   2820 

tttcacctcc tcccccagca attcaccagt caggagtgat ttttactgta aagatggttg   2880 

cttagtaaaa                                                          2890 

 
           
             46  
             3926  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 2944004CB1  
             
           
            46 

ctggaccttt aatccactgt aggtatggac agggaagaaa ggaagaccat caatcagggt     60 

caagaagatg aaatggagat ttatggttac aatttgagtc gctggaagct tgccatagtt    120 

tctttaggag tgatttgctc tggtggggtt tctcctcctc ctctctattg gatgcctgag    180 

tggcgggtga aagcgacctg tgtcagagct gcaattaaag actgtgaagt agtgctgctg    240 

aggactactg atgaattcaa aatgtggttt tgtgcaaaaa ttcgcgttct ttctttggaa    300 

acttacccag tttcaagtcc aaaatctatg tctaataagc tttcaaatgg ccatgcagtt    360 

tgtttaattg agaatcccac tgaagaaaat aggcacagga tcagtaaata ttcacagact    420 

gaatcacaac agattcgtta tttcacccac catagtgtaa aatatttctg gaatgatacc    480 

attcacaatt ttgatttctt aaagggactg gatgaaggtg tttcttgtac gtcaatttat    540 

gaaaagcata gtgcaggact gacaaagggg atgcatgcct acagaaaact gctttatgga    600 

gtaaatgaaa ttgctgtaaa agtgccttct gtttttaagc ttctaattaa agaggttctc    660 

aacccatttt acattttcca gctgttcagt gttatactgt ggagcactga tgaatactat    720 

tactatgctc tagctattgt ggttatgtcc atagtatcaa tcgtaagctc actatattcc    780 

attagaaagc aatatgttat gttgcatgac atggtggcaa ctcatagtac cgtaagagtt    840 

tcagtttgta gagtaaatga agaaatagaa gaaatctttt ctaccgacct tgtgccagga    900 

gatgtcatgg tcattccatt aaatgggaca ataatgcctt gtgatgctgt gcttattaat    960 

ggtacctgca ttgtaaacga aagcatgtta acaggagaaa gtgttccagt gacaaagact   1020 

aatttgccaa atccttcagt ggatgtgaaa ggaataggag atgaattata taatccagaa   1080 

acacataaac gacatacttt gttttgtggg acaactgtta ttcagactcg tttctacact   1140 

ggagaactcg tcaaagccat agttgttaga acaggattta gtacttccaa aggacagctt   1200 

gttcgttcca tattgtatcc caaaccaact gattttaaac tctacagaga tgcctacttg   1260 

tttctactat gtcttgtggc agttgctggc attgggttta tctacactat tattaatagc   1320 

attttaaatg aggtacaagt tggggtcata attatcgagt ctcttgatat tatcacaatt   1380 

actgtgcccc ctgcacttcc tgctgcaatg actgctggta ttgtgtatgc tcagagaaga   1440 

ctgaaaaaaa tcggtatttt ctgtatcagt cctcaaagaa taaatatttg tggacagctc   1500 

aatcttgttt gctttgacaa gactggaact ctaactgaag atggtttaga tctttggggg   1560 

attcaacgag tggaaaatgc acgatttctt tcaccagaag aaaatgtgtg caatgagatg   1620 

ttggtaaaat cccagtttgt tgcttgtatg gctacttgtc attcacttac aaaaattgaa   1680 

ggagtgctct ctggtgatcc acttgatctg aaaatgtttg aggctattgg atggattctg   1740 

gaagaagcaa ctgaagaaga aacagcactt cataatcgaa ttatgcccac agtggttcgt   1800 

cctcccaaac aactgcttcc tgaatctacc cctgcaggaa accaagaaat ggagctgttt   1860 

gaacttccag ctacttatga gataggaatt gttcgccagt tcccattttc ttctgctttg   1920 

caacgtatga gtgtggttgc cagggtgctg ggggatagga aaatggacgc ctacatgaaa   1980 

ggagcgcccg aggccattgc cggtctctgt aaacctgaaa cagttcctgt cgattttcaa   2040 

aacgttttgg aagacttcac taaacagggc ttccgtgtga ttgctcttgc acacagaaaa   2100 

ttggagtcaa aactgacatg gcataaagta cagaatatta gcagagatgc aattgagaac   2160 

aacatggatt ttatgggatt aattataatg cagaacaaat taaagcaaaa aacccctgca   2220 

gtacttgaag atttgcataa agccaacatt cgcaccgtca tggtcacagg tgacagtatg   2280 

ttgactgctg tctctgtggc cagagattgt ggaatgattc tacctcagga taaagtgatt   2340 

attgctgaag cattacctcc aaaggatggg aaagttgcca aaataaattg gcattatgca   2400 

gactccctca cgcagtgcag tcatccatca gcaattgacc cagaggctat tccggttaaa   2460 

ttggtccatg atagcttaga ggatcttcaa atgactcgtt atcattttgc aatgaatgga   2520 

aaatcattct cagtgatact ggagcatttt caagaccttg ttcctaagtt gatgttgcat   2580 

ggcaccgtgt ttgcccgtat ggcacctgat cagaagacac agttgataga agcattgcaa   2640 

aatgttgatt attttgttgg gatgtgtggt gatggcgcaa atgattgtgg tgctttgaag   2700 

agggcacacg gaggcatttc cttatcggag ctcgaagctt cagtggcatc tccctttacc   2760 

tctaagactc ctagtatttc ctgtgtgcca aaccttatca gggaaggccg tgctgcttta   2820 

ataacttcct tctgtgtgtt taaattcatg gcattgtaca gcattatcca gtacttcagt   2880 

gttactctgc tgtattctat cttaagtaac ctaggagact tccagtttct cttcattgat   2940 

ctggcaatca ttttggtagt ggtatttaca atgagtttaa atcctgcctg gaaagaactt   3000 

gtggcacaaa gaccaccttc gggtcttata tctggggccc ttctcttctc cgttttgtct   3060 

cagattatca tctgcattgg atttcaatct ttgggttttt tttgggtcaa acagcaacct   3120 

tggtatgaag tgtggcatcc aaaatcagat gcttgtaata caacaggaag cgggttttgg   3180 

aattcttcac acgtagacaa tgaaaccgaa cttgatgaac ataatataca aaattatgaa   3240 

aataccacag tgttttttat ttccagtttt cagtacctca tagtggcaat tgccttttca   3300 

aaaggaaaac ccttcaggca accttgctac aaaaattatt tttttgtttt ttctgtgatt   3360 

tttttatata tttttatatt attcatcatg ttgtatccag ttgcctctgt tgaccaggtt   3420 

cttcagatag tgtgtgtacc atatcagtgg cgtgtaacta tgctcatcat tgttcttgtc   3480 

aatgcctttg tgtctatcac agtggagaac ttcttccttg acatggtcct ttggaaagtt   3540 

gtgttcaacc gagacaaaca aggagagtat cggttcagca ccacacagcc accgcaggag   3600 

tcagtggatc ggtggggaaa atgctgctta ccctgggccc tgggctgtag aaagaagaca   3660 

ccaaaggcaa agtacatgta tctggcgcag gagctcttgg ttgatccaga atggccacca   3720 

aaacctcaga caaccacaga agctaaagct ttagttaagg agaatggatc atgtcaaatc   3780 

atcaccataa catagcagtg aatcagtctc agtggtattg ctgatagcag tattcaggaa   3840 

tatgtgattt taggagtttc tgatcctgtg tgtcagaatg gcactagttc agtttatgtc   3900 

ccttctgata tagtagctta tttgac                                        3926  
           
             47  
             2135  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3046849CB1  
             
           
            47 

cgctcaggcc cctctttcga atgctccacg ccctcctgcg atctagaacg attcagggca     60 

ggatcctgct cctgaccatc tgcgctgccg gcattggtgg gacttttcag tttggctata    120 

acctctctat catcaatgcc ccgaccttgc acattcagga attcaccaat gagacatggc    180 

aggcgcgtac tggagagcca ctgcccgatc acctagtcct gcttatgtgg tccctcatcg    240 

tgtctctgta tcccctggga ggcctctttg gagcactgct tgcaggtccc ttggccatca    300 

cgctgggaag gaagaagtcc ctcctggtga ataacatctt tgtggtgtca gcagcaatcc    360 

tgtttggatt cagccgcaaa gcaggctcct ttgagatgat catgctggga agactgctcg    420 

tgggagtcaa tgcaggtgtg agcatgaaca tccagcccat gtacctgggg gagagcgccc    480 

ctaaggagct ccgaggagct gtggccatga gctcagccat ctttacggct ctggggatcg    540 

tgatgggaca ggtggtcgga ctcagggagc tcctaggtgg ccctcaggcc tggcccctgc    600 

tgctggccag ctgcctggtg cccggggcgc tccagctcgc ctccctgcct ctgctccctg    660 

aaagcccgcg ctacctcctc attgactgtg gagacaccga ggcctgcctg gcagcactac    720 

ggcagctacg gggctccggg gacttggcag gggagctgga ggagctggag gaggagcgcg    780 

ctgcctgcca gggctgccgt gcccggcgcc catgggagct gttccagcat cgggccctga    840 

ggagacaggt gacaagcctc gtggttctgg gcagtgccat ggagctctgc gggaatgact    900 

cggtgtacgc ctacgcctcc tccgtgttcc ggaaggcagg agtgccggaa gcgaagatcc    960 

agtacgcgat catcgggact gggagctgcg agctgctcac ggcggttgtt agttgtgtgg   1020 

taatcgagag ggtgggtcgg cgcgtgctgc tcatcggtgg gtacagcctg atgacctgct   1080 

gggggagcat cttcactgtg gccctgtgcc tgcagagctc cttcccctgg acactctacc   1140 

tggccatggc ctgcatcttt gccttcatcc tcagctttgg cattggccct gccggagtga   1200 

cggggatcct ggccacagag ctgtttgacc agatggccag gcctgctgcc tgcatggtct   1260 

gcggggcgct catgtggatc atgctcatcc tggtcggcct gggatttccc tttatcatgg   1320 

aggccttgtc ccacttcctc tatgtccctt tccttggtgt ctgtgtctgt ggggccatct   1380 

acactggcct gttccttcct gagaccaaag gcaagacctt ccaagagatc tccaaggaat   1440 

tacacagact caacttcccc aggcgggccc agggccccac gtggaggagc ctggaggtta   1500 

tccagtcaac agaactctag tcccaaaggg gtggccagag ccaaagccag ctactgtcct   1560 

gtcctctgct tcctgccagg gccctggtcc tcactccctc ctgcattcct catttaagga   1620 

gtgtttattg agcacccttt gtgtgcagac atggctccag gtgcttagca atcaatggtg   1680 

agcgtggtat tccaggctaa aggtaattaa ctgacagaaa atcagtaaca acataattac   1740 

aggctggttg tggcagctca tgactgtaat cccagcactt tgggaggcca aggtgggagg   1800 

atcaattgag gccagagttt gaaaccagcc taggtaacat agtgagaccc cctatctcta   1860 

caaaaaattt taaacattag ctgggcatgg tggtatgtgc taacagctct agctactcag   1920 

gaggctgagg cagcaggatc acttgagtcc caagagttca aggtagcagt aagctaacaa   1980 

ttcacaccac tgcatgccca gactggggtg acagagggag acttcatctc tttaaaaaca   2040 

taataataat aattacggac tccggaaatg cgttgacaac gaaacatacc ggtggccccg   2100 

tgaggtggtg atcccgtatc ccagccttgg gaagc                              2135 

 
           
             48  
             2637  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 4538363CB1  
             
           
            48 

atgggctgga gatgccactg tccgcttggt ttaatgatca atgagctccc tgccaggaaa     60 

ccctttctga cctggtttgc ccctcagtcc ctcgggctca tacctagtgc ctgcggcagg    120 

acagccatgg ccgccaactc caccagcgac ctccacactc ccgggacgca gctgagcgtg    180 

gctgacatca tcgtcatcac tgtgtatttt gctctgaacg tggccgtggg catatggtcc    240 

tcttgtcggg ccagtaggaa cacggtgaat ggctacttcc tggcaggccg ggacatgacg    300 

tggtggccga ttggagcctc cctcttcgcc agcagcgagg gctctggcct cttcattgga    360 

ctggcgggct caggcgcggc aggaggtctg gccgtggcag gcttcgagtg gaatgccacg    420 

tacgtgctgc tggcactggc atgggtgttc gtgcccatct acatctcctc agagatcgtc    480 

accttacctg agtacattca gaagcgctac gggggccagc ggatccgcat gtacctgtct    540 

gtcctgtccc tgctactgtc tgtcttcacc aagatatcgc tggacctgta cgcgggggct    600 

ctgtttgtgc acatctgcct gggctggaac ttctacctct ccaccatcct cacgctcggc    660 

atcacagccc tgtacaccat cgcagggggc ctggctgctg taatctacac ggacgccctg    720 

cagacgctca tcatggtggt gggggctgtc atcctgacaa tcaaagcttt tgaccagatc    780 

ggtggttacg ggcagctgga ggcagcctac gcccaggcca ttccctccag gaccattgcc    840 

aacaccacct gccacctgcc acgtacagac gccatgcaca tgtttcgaga cccccacaca    900 

ggggacctgc cgtggaccgg gatgaccttt ggcctgacca tcatggccac ctggtactgg    960 

tgcaccgacc aggtcatcgt gcagcgatca ctgtcagccc gggacctgaa ccatgccaag   1020 

gcgggctcca tcctggccag ctacctcaag atgctcccca tgggcctgat catcatgccg   1080 

ggcatgatca gccgcgcatt gttcccagat gatgtgggct gcgtggtgcc gtccgagtgc   1140 

ctgcgggcct gcggggccga ggtcggctgc tccaacatcg cctaccccaa gctggtcatg   1200 

gaactgatgc ccatcggtct gcgggggctg atgatcgcag tgatgctggc ggcgctcatg   1260 

tcgtcgctga cctccatctt caacagcagc agcaccctct tcactatgga catctggagg   1320 

cggctgcgtc cccgctccgg cgagcgggag ctcctgctgg tgggacggct ggtcatagtg   1380 

gcactcatcg gcgtgagtgt ggcctggatc cccgtcctgc aggactccaa cagcgggcaa   1440 

ctcttcatct acatgcagtc agtgaccagc tccctggccc caccagtgac tgcagtcttt   1500 

gtcctgggcg tcttctggcg acgtgccaac gagcaggggg ccttctgggg cctgatagca   1560 

gggctggtgg tgggggccac gaggctggtc ctggaattcc tgaacccagc cccaccgtgc   1620 

ggagagccag acacgcggcc agccgtcctg gggagcatcc actacctgca cttcgctgtc   1680 

gccctctttg cactcagtgg tgctgttgtg gtggctggaa gcctgctgac cccaccccca   1740 

cagagtgtcc agattgagaa ccttacctgg tggaccctgg ctcaggatgt gcccttggga   1800 

actaaagcag gtgatggcca aacaccccag aaacacgcct tctgggcccg tgtctgtggc   1860 

ttcaatgcca tcctcctcat gtgtgtcaac atattctttt atgcctactt cgcctgaaca   1920 

ctgccatcct ggacagaaag gcaggagctc tgagtcctca ggtccaccca tttccctcat   1980 

ggggatcccg aggccccaag aggggcagat tcccctcaca gctgcacagc agctcggtgc   2040 

ccaagaactg gccaagccag caaagcggga gcctgaaaac attagggggg aaactgggac   2100 

gaaacataag tgtgactttt tccaaacaac agcacccaaa gcaagtcaag catttggaac   2160 

gcgacaaact tagattttcc tgaccgggcc caccacaccc caacctcctc acctcccaaa   2220 

ctaccaacac agctcatcac catactcaca ccacccacag cggcccgccc ccactccaat   2280 

cagaaaggca cccccccact ctcaagacgc gacggcgcaa tcgactgcaa ctccataacg   2340 

atgccaaaac gacacaagcc aggacacggc actgtataca gcacgagggt gatctgcaac   2400 

gttgtggccg aatgcagaaa atacactggg tgctggcgta aggaagatcc gcgagtaaac   2460 

aacggtcttg taaacttact gcatccacca aggtacactt ccagaacgag accagacaac   2520 

tacactccac acaacctgca gccacaccct atttctgcta tcataaagag cccccgcacc   2580 

acataataat gccggcagac tcagtgcgcg aaacccttgt gctggacttc accacgg      2637 

 
           
             49  
             3783  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 6427460CB1  
             
           
            49 

gcactagtac cccggagccc atgggcgcgc cgagccgggc gcgggggcgc tgaacggcgg     60 

agcgggagcg gccggaggag ccatggactg cagcctcgtg cggacgctcg tgcacagata    120 

ctgtgcagga gaagagaatt gggtggacag caggaccatc tacgtgggac acagggagcc    180 

acctccgggc gcagaggcct acatcccaca gagataccca gacaacagga tcgtctcgtc    240 

caagtacaca ttttggaact ttatacccaa gaatttattt gaacaattca gaagagtagc    300 

caacttttat ttccttatca tatttctggt gcagttgatt attgatacac ccacaagtcc    360 

agtgacaagc ggacttccac tcttctttgt cattactgtg acggctatca aacagggtta    420 

tgaagactgg cttcgacata aagcagacaa tgccatgaac cagtgtcctg ttcatttcat    480 

tcagcacggc aagctcgttc ggaaacaaag tcgaaagctg cgagttgggg acattgtcat    540 

ggttaaggag gacgagacct ttccctgcga cttgatcttc ctttccagca accggggaga    600 

tgggacgtgc cacgtcacca ccgccagctt ggatggagaa tccagccata aaacgcatta    660 

cgcggtccag gacaccaaag gcttccacac agaggaggat atcggcggac ttcacgccac    720 

catcgagtgt gagcagcccc agcccgacct ctacaagttc gtgggtcgca tcaacgttta    780 

cagtgacctg aatgaccccg tggtgaggcc cttaggatcg gaaaacctgc tgcttagagg    840 

agctacactg aagaacactg agaaaatctt tggtgtggct atttacacgg gaatggaaac    900 

caagatggca ttaaattatc aatcaaaatc tcagaagcga tctgccgtgg aaaaatcgat    960 

gaatgcgttc ctcattgtgt atctctgcat tctgatcagc aaagccctga taaacactgt   1020 

gctgaaatac gtgtggcaga gtgagccctt tcgggatgag ccgtggtata atcagaaaac   1080 

ggagtcggaa aggcagagga atctgttcct caaggcattc acggacttcc tggccttcat   1140 

ggtcctcttt aactacatca tccctgtgtc catgtacgtc acggtcgaga tgcagaagtt   1200 

cctcggctct tacttcatca cctgggacga agacatgttt gacgaggaga ctggcgaggg   1260 

gcctctggtg aacacgtcgg acctcaatga agagctggga caggtggagt acatcttcac   1320 

agacaagacc ggcaccctca cggaaaacaa catggagttc aaggagtgct gcatcgaagg   1380 

ccatgtctac gtgccccacg tcatctgcaa cgggcaggtc ctcccagagt cgtcaggaat   1440 

cgacatgatt gactcgtccc ccagcgtcaa cgggagggag cgcgaggagc tgtttttccg   1500 

ggccctctgt ctctgccaca ccgtccaggt gaaagacgat gacagcgtag acggccccag   1560 

gaaatcgccg gacgggggga aatcctgtgt gtacatctca tcctcgcccg acgaggtggc   1620 

gctggtcgaa ggtgtccaga gacttggctt tacctaccta aggctgaagg acaattacat   1680 

ggagatatta aacagggaga accacatcga aaggtttgaa ttgctggaaa ttttgagttt   1740 

tgactcagtc agaaggagaa tgagtgtaat tgtaaaatct gctacaggag aaatttatct   1800 

gttttgcaaa ggagcagatt cttcgatatt cccccgagtg atagaaggca aagttgacca   1860 

gatccgagcc agagtggagc gtaacgcagt ggaggggctc cgaactttgt gtgttgctta   1920 

taaaaggctg atccaagaag aatatgaagg catttgtaag ctgctgcagg ctgccaaagt   1980 

ggcccttcaa gatcgagaga aaaagttagc agaagcctat gagcaaatag agaaagatct   2040 

tactctgctt ggtgctacag ctgttgagga ccggctgcag gagaaagctg cagacaccat   2100 

cgaggccctg cagaaggccg ggatcaaagt ctgggttctc acgggagaca agatggagac   2160 

ggccgcggcc acgtgctacg cctgcaagct cttccgcagg aacacgcagc tgctggagct   2220 

gaccaccaag aggatcgagg agcagagcct gcacgacgtc ctgttcgagc tgagcaagac   2280 

ggtcctgcgc cacagcggga gcctgaccag agacaacctc tccggacttt cagcagatat   2340 

gcaggactac ggtttaatta tcgacggagc tgcactgtct ctgataatga agcctcgaga   2400 

agacgggagt tccggcaact acagggagct cttcctggaa atctgccgga gctgcagcgc   2460 

ggtgctctgc tgccgcatgg cgcccttgca gaaggctcag attgttaaat taatcaaatt   2520 

ttcaaaagag cacccaatca cgttagcaat tggcgatggt gcaaatgatg tcagcatgat   2580 

tctggaagcg cacgtgggca taggtgtcat cggcaaggaa ggccgccagg ctgccaggaa   2640 

cagcgactat gcaatcccaa agtttaagca tttgaagaag atgctgcttg ttcacgggca   2700 

tttttattac attaggatct ctgagctcgt gcagtacttc ttctataaga acgtctgctt   2760 

catcttccct cagtttttat accagttctt ctgtgggttt tcacaacaga ctttgtacga   2820 

caccgcgtat ctgaccctct acaacatcag cttcacctcc ctccccatcc tcctgtacag   2880 

cctcatggag cagcatgttg gcattgacgt gctcaagaga gacccgaccc tgtacaggga   2940 

cgtcgccaag aatgccctgc tgcgctggcg cgtgttcatc tactggacgc tcctgggact   3000 

gtttgacgca ctggtgttct tctttggtgc ttatttcgtg tttgaaaata caactgtgac   3060 

aagcaacggg cagatatttg gaaactggac gtttggaacg ctggtattca ccgtgatggt   3120 

gttcacagtt acactaaagc ttgcattgga cacacactac tggacttgga tcaaccattt   3180 

tgtcatctgg gggtcgctgc tgttctacgt tgtcttttca cttctctggg gaggagtgat   3240 

ctggccgttc ctcaactacc agaggatgta ctacgtgttc atccagatgc tgtccagcgg   3300 

gcccgcctgg ctggccatcg tgctgctggt gaccatcagc ctccttcccg acgtcctcaa   3360 

gaaagtcctg tgccggcagc tgtggccaac agcaacagag agagtccagc agaatgggtg   3420 

cgcacagcct cgggaccgcg actcagaatt cacccctctt gcctctctgc agagcccagg   3480 

ctaccagagc acctgtccct cggccgcctg gtacagctcc cactctcagc aggtgacact   3540 

cgcggcctgg aaggagaagg tgtccacgga gcccccaccc atcctcggcg gttcccatca   3600 

ccactgcagt tccatcccaa gtcacagctg ccctaggtcc cgtgtgggaa tgctcgtgtg   3660 

atggatggtc ctaagcctgt ggagactgtg cacgtgcctc ttcctggccc ccagcaggca   3720 

aggagggggg tcacaggcct tgccctcgaa catggcaccc tggccgcctg gacccagcac   3780 

tgt                                                                 3783 

 
           
             50  
             2105  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7474127CB1  
             
           
            50 

ccagcgccca gggaagcggc tcaaccacct gaatccggaa aacgccaaca agtagtttct     60 

cgtcggagaa gggcggctca cctgggcgcc aagactcagt cccgctgccc agagaacctc    120 

gtccactcgg aaaccaaagc agaaccactt ttctctcggt ctcgttaagt catgtctgag    180 

tcacagagat gggcaagatc gagaacaacg agagggtgat cctcaatgtc gggggcaccc    240 

ggcacgaaac ctaccgcagc accctcaaga ccctgcctgg aacacgcctg gcccttcttg    300 

cctcctccga gcccccaggc gactgcttga ccacggcggg cgacaagctg cagccgtcgc    360 

cgcctccact gtcgccgccg ccgagagcgc ccccgctgtc ccccgggcca ggcggctgct    420 

tcgagggcgg cgcgggcaac tgcagttccc gcggcggcag ggccagcgac catcccggtg    480 

gcggccgcga gttcttcttc gaccggcacc cgggcgtctt cgcctatgtg ctcaattact    540 

accgcaccgg caagctgcac tgccccgcag acgtgtgcgg gccgctcttc gaggaggagc    600 

tggccttctg gggcatcgac gagaccgacg tggagccctg ctgctggatg acctaccggc    660 

agcaccgcga cgccgaggag gcgctggaca tcttcgagac ccccgacctc attggcggcg    720 

accccggcga cgacgaggac ctggcggcca agaggctggg catcgaggac gcggcggggc    780 

tcgggggccc cgacggcaaa tctggccgct ggaggaggct gcagccccgc atgtgggccc    840 

tcttcgaaga cccctactcg tccagagccg ccaggtttat tgcttttgct tctttattct    900 

tcatcctggt ttcaattaca actttttgcc tggaaacaca tgaagctttc aatattgtta    960 

aaaacaagac agaaccagtc atcaatggca caagtgttgt tctacaatat gaaattgaaa   1020 

cagatcctgc cttgacgtat gtagaaggag tgtgtgtggt gtggtttact tttgaatttt   1080 

tagtccgtat tgttttttca cccaataaac ttgaattcat caaaaatctc ttgaatatca   1140 

ttgactttgt ggccatccta cctttctact tagaggtggg actcagtggg ctgtcatcca   1200 

aagctgctaa agatgtgctt ggcttcctca gggtggtaag gtttgtgagg atcctgagaa   1260 

ttttcaagct cacccgccat tttgtaggtc tgagggtgct tggacatact cttcgagcta   1320 

gtactaatga atttttgctg ctgataattt tcctggctct aggagttttg atatttgcta   1380 

ccatgatcta ctatgccgag agagtgggag ctcaacctaa cgacccttca gctagtgagc   1440 

acacacagtt caaaaacatt cccattgggt tctggtgggc tgtagtgacc atgactaccc   1500 

tgggttatgg ggatatgtac ccccaaacat ggtcaggcat gctggtggga gccctgtgtg   1560 

ctctggctgg agtgctgaca atagccatgc cagtgcctgt cattgtcaat aattttggaa   1620 

tgtactactc cttggcaatg gcaaagcaga aacttccaag gaaaagaaag aagcacatcc   1680 

ctcctgctcc tcaggcaagc tcacctactt tttgcaagac agaattaaat atggcctgca   1740 

atagtacaca gagtgacaca tgtctgggca aagacaatcg acttctggaa cataacagat   1800 

cagtgttatc aggtgacgac agtacaggaa gtgagccgcc actatcaccc ccagaaaggc   1860 

tccccatcag acgctctagt accagagaca aaaacagaag aggggaaaca tgtttcctac   1920 

tgacgacagg tgattacacg tgtgcttctg atggagggat caggaaaggt tatgaaaaat   1980 

cccgaagctt aaacaacata gcgggcttgg caggcaatgc tctgaggctc tctccagtaa   2040 

catcacccta caactctcct tgtcctctga ggcgctctcg atctcccatc ccatctatct   2100 

tgtaa                                                               2105 

 
           
             51  
             2069  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7476949CB1  
             
           
            51 

atgagcaagg acctggcagc aatggggcct ggagcttcag gggacggggt caggactgag     60 

acagctccac acatagcact ggactccaga gttggtctgc acgcctacga catcagcgtg    120 

gtggtcatct actttgtctt cgtcattgct gtggggatct ggtcgtccat ccgtgcaagt    180 

cgagggacca ttggcggcta tttcctggcc gggaggtcca tgagctggtg gccaattgga    240 

gcatctctga tgtccagcaa tgtgggcagt ggcttgttca tcggcctggc tgggacaggg    300 

gctgccggag gccttgccgt aggtggcttc gagtggaacg caacctggct gctcctggcc    360 

cttggctggg tcttcgtccc tgtgtacatc gcagcaggtg tggtcacaat gccgcagtat    420 

ctgaagaagc gatttggggg ccagaggatc caggtgtaca tgtctgtcct gtctctcatc    480 

ctctacatct tcaccaagat ctcgactgac atcttctctg gagccctctt catccagatg    540 

gcattgggct ggaacctgta cctctccaca gggatcctgc tggtggtgac tgccgtctac    600 

accattgcag gtggcctcat ggccgtgatc tacacagatg ctctgcagac ggtgatcatg    660 

gtagggggag ccctggtcct catgtttctg ggctttcagg acgtgggctg gtacccaggc    720 

ctggagcagc ggtacaggca ggccatccct aatgtcacag tccccaacac cacctgtcac    780 

ctcccacggc ccgatgcttt ccacattctt cgggaccctg tgagcgggga catcccttgg    840 

ccaggtctca ttttcgggct cacagtgctg gccacctggt gttggtgcac agaccaggtc    900 

attgtgcagc ggtctctctc ggccaagagt ctgtctcatg ccaagggagg ctccgtgctg    960 

gggggctacc tgaagatcct ccccatgttc ttcatcgtca tgcctggcat gatcagccgg   1020 

gccctgttcc cagacgaggt gggctgcgtg gaccctgatg tctgccaaag aatctgtggg   1080 

gcccgagtgg gatgttccaa cattgcctac cctaagttgg tcatggccct catgcctgtt   1140 

ggtctgcggg ggctgatgat tgccgtgatc atggccgctc tcatgagctc actcacctcc   1200 

atcttcaaca gcagcagcac cctgttcacc attgatgtgt ggcagcgctt ccgcaggaag   1260 

tcaacagagc aggagctgat ggtggtgggc agagtgtttg tggtgttcct ggttgtcatc   1320 

agcatcctct ggatccccat catccaaagc tccaacagtg ggcagctctt cgactacatc   1380 

caggctgtca ccagttacct ggccccaccc atcaccgctc tcttcctgct ggccatcttc   1440 

tgcaagaggg tcacagagcc cggagctttc tggggcctcg tgtttggcct gggagtgggg   1500 

cttctgcgta tgatcctgga gttctcatac ccagcgccag cctgtgggga ggtggaccgg   1560 

aggccagcag tgctgaagga cttccactac ctgtactttg caatcctcct ctgcgggctc   1620 

actgccatcg tcattgtcat tgtcagcctc tgtacaactc ccatccctga ggaacagctc   1680 

acacgcctca catggtggac tcggaactgc cccctctctg agctggagaa ggaggcccac   1740 

gagagcacac cggagatatc cgagaggcca gccggggagt gccctgcagg aggtggagcg   1800 

gcagagaact cgagcctggg ccaggagcag cctgaagccc caagcaggtc ctggggaaag   1860 

ttgctctgga gctggttctg tgggctctct ggaacaccgg agcaggccct gagcccagca   1920 

gagaaggctg cgctagaaca gaagctgaca agcattgagg aggagccact ctggagacat   1980 

gtctgcaaca tcaatgctgt ccttttgctg gccatcaaca tcttcctctg gggctatttt   2040 

gcgtgattca aacctggctt cactgtaga                                     2069 

 
           
             52  
             4245  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477249CB1  
             
           
            52 

gcggcggcag gctcagctgc gccgggcggg ggcggcgctg gggccgcgcc tgtaggactc     60 

ggggccgacg ccgcgggatg gggacgcggc gcggggagtg aggcagtggc ggcggcggcg    120 

gtaagcggaa cttcggcccg aggggctcgc ccgctcccgc ctctgtcttg tcggcctcca    180 

cctgcagccc cgcggccccc gcgccccgcg ggacccggac ggcgacgacg ggggaatgtg    240 

gcgctggatc cggcagcagc tgggttttga cccaccacat cagagtgaca caagaaccat    300 

ctacgtagcc aacaggtttc ctcagaatgg cctttacaca cctcagaaat ttatagataa    360 

caggatcatt tcatctaagt acactgtgtg gaattttgtt ccaaaaaatt tatttgaaca    420 

gttcagaaga gtggcaaact tttattttct tattatattt ttggttcagc ttatgattga    480 

tacacctacc agtccagtta ccagtggact tccattattc tttgtgataa cagtaactgc    540 

cataaagcag ggatatgaag attggttacg gcataactca gataatgaag taaatggagc    600 

tcctgtttat gttgttcgaa gtggtggcct tgtaaaaact agatcaaaaa acattcgggt    660 

gggtgatatt gttcgaatag ccaaagatga aatttttcct gcagacttgg tgcttctgtc    720 

ctcagatcga ctggatggtt cctgtcacgt tacaactgct agtttggacg gagaaactaa    780 

cctgaagaca catgtggcag ttccagaaac agcattatta caaacagttg ccaatttgga    840 

cactctagta gctgtaatag aatgccagca accagaagca gacttataca gattcatggg    900 

acgaatgatc ataacccaac aaatggaaga aattgtaaga cctctggggc cggagagtct    960 

cctgcttcgt ggagccagat taaaaaacac aaaagaaatt tttggtgttg cggtatacac   1020 

tggaatggaa actaagatgg cattaaatta caagagcaaa tcacagaaac gatctgcagt   1080 

agaaaagtca atgaatacat ttttgataat ttatctagta attcttatat ctgaagctgt   1140 

catcagcact atcttgaagt atacatggca agctgaagaa aaatgggatg aaccttggta   1200 

taaccaaaaa acagaacatc aaagaaatag cagtaaggta gagtacgtgt ttacagataa   1260 

aactggtaca ctgacagaaa atgagatgca gtttcgggaa tgttcaatta atggcatgaa   1320 

ataccaagaa attaatggta gacttgtacc cgaaggacca acaccagact cttcagaagg   1380 

aaacttatct tatcttagta gtttatccca tcttaacaac ttatcccatc ttacaaccag   1440 

ttcctctttc agaaccagtc ctgaaaatga aactgaacta attaaagaac atgatctctt   1500 

ctttaaagca gtcagtctct gtcacactgt acagattagc aatgttcaaa ctgactgcac   1560 

tggtgatggt ccctggcaat ccaacctggc accatcgcag ttggagtact atgcatcttc   1620 

accagatgaa aaggctctag tagaagctgc tgcaaggatt ggtattgtgt ttattggcaa   1680 

ttctgaagaa actatggagg ttaaaactct tggaaaactg gaacggtaca aactgcttca   1740 

tattctggaa tttgattcag atcgtaggag aatgagtgta attgttcagg caccttcagg   1800 

tgagaagtta ttatttgcta aaggagctga gtcatcaatt ctccctaaat gtataggtgg   1860 

agaaatagaa aaaaccagaa ttcatgtaga tgaatttgct ttgaaagggc taagaactct   1920 

gtgtatagca tatagaaaat ttacatcaaa agagtatgag gaaatagata aacgcatatt   1980 

tgaagccagg actgccttgc agcagcggga agagaaattg gcagctgttt tccagttcat   2040 

agagaaagac ctgatattac ttggagccac agcagtagaa gacagactac aagataaagt   2100 

tcgagaaact attgaagcat tgagaatggc tggtatcaaa gtatgggtac ttactgggga   2160 

taaacatgaa acagctgtta gtgtgagttt atcatgtggc cattttcata gaaccatgaa   2220 

catccttgaa cttataaacc agaaatcaga cagcgagtgt gctgaacaat tgaggcagct   2280 

tgccagaaga attacagagg atcatgtgat tcagcatggg ctggtagtgg atgggaccag   2340 

cctatctctt gcactcaggg agcatgaaaa actatttatg gaagtttgca gaaattgttc   2400 

agctgtatta tgctgtcgta tggctccact gcagaaagca aaagtaataa gactaataaa   2460 

aatatcacct gagaaaccta taacattggc tgttggtgat ggtgctaatg acgtaagcat   2520 

gatacaagaa gcccatgttg gcataggaat catgggtaaa gaaggaagac aggctgcaag   2580 

aaacagtgac tatgcaatag ccagatttaa gttcctctcc aaattgcttt ttgttcatgg   2640 

tcatttttat tatattagaa tagctaccct tgtacagtat tttttttata agaatgtgtg   2700 

ctttatcaca ccccagtttt tatatcagtt ctactgtttg ttttctcagc aaacattgta   2760 

tgacagcgtg tacctgactt tatacaatat ttgttttact tccctaccta ttctgatata   2820 

tagtcttttg gaacagcatg tagaccctca tgtgttacaa aataagccca ccctttatcg   2880 

agacattagt aaaaaccgcc tcttaagtat taaaacattt ctttattgga ccatcctggg   2940 

cttcagtcat gcctttattt tcttttttgg atcctattta ctaataggga aagatacatc   3000 

tctgcttgga aatggccaga tgtttggaaa ctggacattt ggcactttgg tcttcacagt   3060 

catggttatt acagtcacag taaagatggc tctggaaact catttttgga cttggatcaa   3120 

ccatctcgtt acctggggat ctattatatt ttattttgta ttttccttgt tttatggagg   3180 

gattctctgg ccatttttgg gctcccagaa tatgtatttt gtgtttattc agctcctgtc   3240 

aagtggttct gcttggtttg ccataatcct catggttgtt acatgtctat ttcttgatat   3300 

cataaagaag gtctttgacc gacacctcca ccctacaagt actgaaaagg cacagcttac   3360 

tgaaacaaat gcaggtatca agtgcttgga ctccatgtgc tgtttcccgg aaggagaagc   3420 

agcgtgtgca tctgttggaa gaatgctgga acgagttata ggaagatgta gtccaaccca   3480 

catcagcagg tgtgaaatct ctctaagtag cctttgctgc agatgagtat cctatctgga   3540 

acaggatgaa cctgccgctc tagataccta ataaatcagc agctggtttt accaactgaa   3600 

gcaggaagtc tgctatttat tagcactctt tggtggtaga tttcactttg tggctttggg   3660 

gtaagggctt tttcactcac aaaggaagag aaagcacctt tgaagagact tcatctaatg   3720 

aacaaaaaat tttgtttcat aatctttcta aaatgtgctc agtaggagtg tgtttatggt   3780 

actcttttat ggtttgtata actttctttt ttaaattata catatactat ttccttttta   3840 

tttttttaaa atttttttgc tttttgtctt tacaaaataa tctcaacata acagtgaagt   3900 

caaaggcttt ccttttctta ctctgtatgt atattttcca gttggttatt tgaggctttg   3960 

aggtatttat aaacacaaaa ggctgtattt ctgctcccct acctcttctt atgtctgtaa   4020 

tgaagttttg aaatgagtca tgatttttaa gtttcttttg cttggtattt attgcctaat   4080 

taaaagtgta tgagttagaa caggcttttt aaattatgga gtaaaagaat cttagcattt   4140 

ttgtcccctc ctaaatctgt ttcttgaatg agatttatca ccatgcctgc tgttgtgcac   4200 

cataacgaaa aaaaacacct tttggtaaac accatttaaa attca                   4245 

 
           
             53  
             2124  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477720CB1  
             
           
            53 

atggctctgc agatgttcgt gacttacagt ccttggaatt gtttgctact gctagtggct     60 

cttgagtgtt ctgaagcatc ttctgatttg aatgaatctg caaattccac tgctcagtat    120 

gcatctaacg cttggtttgc tgctgccagc tcagagccag aggaagggat atctgttttt    180 

gaactggatt atgactatgt gcaaattcct tatgaggtca ctctctggat acttctagca    240 

tcccttgcaa aaataggctt ccacctctac cacaggctgc caggcctcat gccagaaagc    300 

tgcctcctca tcctggtggg ggcgctggtg ggcggcatca tcttcggcac cgaccacaaa    360 

tcgcctccgg tcatggactc cagcatctac ttcctgtatc tcctgccacc catcgttctg    420 

gagggcggct acttcatgcc cacccggccc ttctttgaga acatcggctc catcctgtgg    480 

tgggcagtat tgggggccct gatcaacgcc ttgggcattg gcctctccct ctacctcatc    540 

tgccaggtga aggcctttgg cctgggcgac gtcaacctgc tgcagaacct gctgttcggc    600 

agcctgatct ccgccgtgga cccagtggcc gtgctagccg tgtttgagga agcgcgcgtg    660 

aacgagcagc tctacatgat gatctttggg gaggccctgc tcaatgatgg cattactgtg    720 

gtcttataca atatgttaat tgcctttaca aagatgcata aatttgaaga catagaaact    780 

gtcgacattt tggctggatg tgcccgattc atcgttgtgg ggcttggagg ggtattgttt    840 

ggcatcgttt ttggatttat ttctgcattt atcacacgtt tcactcagaa tatctctgca    900 

attgagccac tcatcgtctt catgttcagc tatttgtctt acttagctgc tgaaaccctc    960 

tatctctccg gcatcctggc aatcacagcc tgcgcagtaa caatgaaaaa gtacgtggaa   1020 

gaaaacgtgt cccagacatc atacacgacc atcaagtact tcatgaagat gctgagcagc   1080 

gtcagcgaga ccttgatctt catcttcatg ggtgtgtcca ctgtgggcaa gaatcacgag   1140 

tggaactggg ccttcatctg cttcaccctg gccttctgcc aaatctggag agccatcagc   1200 

gtatttgctc tcttctatat cagtaaccag tttcggactt tccccttctc catcaaggac   1260 

cagtgcatca ttttctacag tggtgttcga ggagctggaa gtttttcact tgcatttttg   1320 

cttcctctgt ctctttttcc taggaagaaa atgtttgtca ctgctactct agtagttata   1380 

tactttactg tatttattca gggaatcaca gttggccctc tggtcaggta cctggatgtt   1440 

aaaaaaacca ataaaaaaga atccatcaat gaagagcttc atattcgtct gatggatcac   1500 

ttaaaggctg gaatcgaaga tgtgtgtggg cactggagtc actaccaagt gagagacaag   1560 

tttaagaagt ttgatcatag atacttacgg aaaatcctca tcagaaagaa cctacccaaa   1620 

tcaagcattg tttctttgta caagaagctg gaaatgaagc aagccatcga gatggtggag   1680 

actgggatac tgagctctac agctttctcc ataccccatc aggcccagag gatacaagga   1740 

atcaaaagac tttcccctga agatgtggag tccataaggg acattctgac atccaacatg   1800 

taccaagttc ggcaaaggac cctgtcctac aacaaataca acctcaaacc ccaaacaagt   1860 

gagaagcagg ctaaagagat tctgatccgc cgccagaaca ccttaaggga gagcatgagg   1920 

aaaggtcaca gcctgccctg gggaaagccg gctggcacca agaatatccg ctacctctcc   1980 

tacccctacg ggaatcctca gtctgcagga agagacacaa gggctgctgg gttctcaggt   2040 

aagctgccca cctggctgct ctgctgcttt tctgtagagt caggtggtaa atatctgggg   2100 

gtgtgggcca agaggcaaca ttaa                                          2124 

 
           
             54  
             2195  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477852CB1  
             
           
            54 

atggggggtt ttctacctaa ggcagaaggg cccgggagcc aactccagaa acttctgccc     60 

tcctttctgg tcagagaaca agactgggac cagcacctgg acaagcttca tatgctgcag    120 

cagaagagga ttctagagtc tccactgctt cgagcatcca aggaaaatga cctgtctgtt    180 

cttaggcaac ttctactgga ctgcacctgt gacgttcgac aaagaggagc cctgggggag    240 

acggcgctgc acatagcagc cctctatgac aacttggagg cggccttggt gctgatggag    300 

gctgccccag agctggtctt tgagcccacc acatgtgagg cttttgcagg tcagactgca    360 

ctgcacatcg ctgttgtgaa ccagaatgtg aacctggtgc gtgccctgct cacccgcagg    420 

gccagtgtct ctgccagagc cacaggcact gccttccgcc gtagtccccg caacctcatc    480 

tactttggtg agcacccttt gtcctttgct gcctgtgtga acagcgagga gatcgtgcgg    540 

ctgctcattg agcatggagc tgacatcagg gcccaggact ccctgggtaa cacagtatta    600 

cacatcctca tcctccagcc caacaaaacc tttgcctgcc agatgtacaa cctgctgctg    660 

tcctacgatg gacatgggga ccacctgcag cccctggacc ttgtgcccaa tcaccagggt    720 

ctcaccccct tcaagctggc tggagtggag ggtaacactg tgatgttcca gcacctgatg    780 

cagaagcgga ggcacatcca gtggacgtat ggacccctga cctccattct ctacgacctc    840 

acagagatcg actcctgggg agaggagctg tccttcctgg agcttgtggt ctcctctgat    900 

aaacgagagg ctcgccaaat tctggaacag accccagtga aggagctggt gagcttcaag    960 

tggaacaagt atggccggcc gtacttctgc atcctggctg ccttgtacct gctctacatg   1020 

atctgcttta ccacgtgctg cgtctaccgc ccccttaagt ttcgtggtgg caaccgcact   1080 

cattctcgag acatcaccat cctccagcaa aaactactac aggaggccta tgagacacgt   1140 

gaagatatca tcaggctggt gggggagctg gtgagcatcg ttggggctgt gatcatcctg   1200 

ctcctagaga ttccagacat cttcagggtt ggtgcctctc gctattttgg aaagacgatt   1260 

cttggggggc cattccatgt catcatgatc acctatgcct ccctggtgct ggtgaccatg   1320 

gtgatgcggc tcaccaacac caatggggag gtggtgccca tgtcctttgc cctggtgctg   1380 

ggctggtgca gtgtcatgta tttcactcga ggattccaga tgctgggtcc cttcaccatc   1440 

atgatccaga agatgatttt tggagaccta atgcgtttct gctggctgat ggctgtggtc   1500 

atcttgggat ttgcctccgc gttctatatc attttccaga cagaggaccc aaccagtctg   1560 

gggcaattct atgactaccc catggcactg ttcaccacct ttgagctttt tctcactgtt   1620 

attgatgcac ctgccaacta cgacgtggac ttgcccttca tgttcagcat tgtcaacttc   1680 

gccttcgcca tcattgccac actgctcatg ctcaacttgt tcatcgccat gatgggcgac   1740 

acccactgga gggtggccca ggagagggat gagctctgga gggcccaggt cgtggccacc   1800 

acagtgatgc tggagcggaa gctgcctcgc tgcctgtggc ctcgctccgg gatctgtggg   1860 

tgcgaattcg ggctggggga ccgctggttc ctgcgggttg agaaccacaa tgatcagaat   1920 

cctctgcgag tgcttcgcta tgtggaagtg ttcaagaact cagacaagga ggatgaccag   1980 

gagcatccat ctgagaaaca gccctctggg gctgagagtg ggactctagc cagagcctct   2040 

ttggctcttc caacttcctc cctgtcccgg accgcgtccc agagcagcag tcaccgaggc   2100 

tgggagatcc ttcgtcaaaa caccctgggg cacttgaatc ttggactgaa ccttagtgag   2160 

ggggatggag aggaggtcta ccatttttga ttaac                              2195 

 
           
             55  
             2055  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 1471717CB1  
             
           
            55 

cggctctggg ccctcagcct ggctcatgca caactgtctg aagtgctctg gactatggtg     60 

atgaacagcg gccttcagac gcgaggctgg ggaggaatcg tcggggtttt tattattttt    120 

gccgtatttg ctgtcctgac agtagccatc cttctgatca tggagggcct ctctgctttc    180 

ctgcacgccc tgcgactgca ctgggaagct gtttggggaa cttgagctat ttagaagatg    240 

gcaaccaagc caacagagcc tgtcacgatc ctcagccttc ggaaattgag cctggggacc    300 

gcagagccac aggttaaaga gccaaagacg ttcaccgtgg aagatgcagt ggagactatc    360 

ggcttcgggc gtttccacat tgccctcttt ctgatcatgg gcagtactgg ggtggttgag    420 

gccatggaga tcatgttgat agctgttgtg tctcctgtca tccgctgtga atggcaactg    480 

gagaattggc aggtggcatt agtaaccacg atggtgtttt ttggctacat ggttttcagt    540 

atcctctttg gcctcctggc tgacagatat ggccgctgga agattctgct catctcgttc    600 

ctgtggggag cctatttctc cttgctgacc tcgtttgctc cttcgtacat ctggtttgtc    660 

ttcctgcgga cgatggtggg ctgtggtgtg tccggccact cgcaagggtt aatcataaag    720 

actgaatttt tgcccacgaa ataccgaggc tatatgttac ccttgtctca ggtgttctgg    780 

cttgcgggct ccctgctcat cattggcttg gcctctgtga tcatccccac catcgggtgg    840 

cgctggctca ttcgcgtcgc ctccatcccg ggcatcatcc tcatcgtggc cttcaagttt    900 

attcctgaat ctgcccggtt caatgtctcc actgggaaca ctcgggctgc cctggccact    960 

ctggagcgcg ttgccaagat gaaccgctcg gtcatgccgg aggggaagct ggtggagccc   1020 

gtcctggaaa aaagaggaag atttgcagac ctattggatg ctaaatattt acggaccaca   1080 

ttacagatct gggtcatatg gcttggaatc tcttttgcct actatggggt tatcctggcc   1140 

agtgctgagc tgctggagcg ggacttggtc tgtggttcaa agtcagactc tgcggtggtg   1200 

gtgactgggg gggactcagg ggagagccag agcccctgct actgccacat gtttgcaccc   1260 

tctgactatc ggaccatgat catcagcacc atcggtgaaa ttgctttgaa tcctttaaat   1320 

atactgggca tcaatttcct gggaagacgg ctgagccttt ctattaccat gggatgcacg   1380 

gctttattct gccttctcct caacatttgc acttcaagtg ccggcctgat tggcttcctc   1440 

ttcatgctga gggctctggt agctgcaaac ttcaacaccg tctacattta cacagctgag   1500 

gtctacccca ccacgatgcg cgctttgggg atgggaacca gcggctccct gtgtcgcatt   1560 

ggtgcaatgg tggcgccatt tatatcccag gttcttatga gtgcatcaat actgggggcc   1620 

ctgtgtctct tctcatctgt ctgtgttgta tgcgccattt ctgcattcac tctccccatc   1680 

gaaaccaaag gacgggccct ccagcaaatt aaatgaagac ctgcaaagct atgtctacca   1740 

gatgagaaaa atgaattcta tcttcagaac tgcggtgcat ttttttaaaa cttggtttta   1800 

cttctgtatg ctactcggta attagtaaag tgattttttt ttaaaaggca tatatgggaa   1860 

tggggtaggt aactgtatat tgatctcttc cttgaggaac aatatataaa gtacttttat   1920 

aaaatataat ttaagctttc aaaggggtgt gagagggaga tggtgggggg gaagatggct   1980 

tttcttcgtt gaaatcaagt ctgtaaacct ttatatgaat aaatactaaa ttttaaactt   2040 

acaaaaaaaa aaaaa                                                    2055 

 
           
             56  
             4727  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 3874406CB1  
             
           
            56 

aagagctgct ggagtaggca cccatttaaa gaaaaaatga agaagcagca ataaagaagt     60 

tgtaatcgtt acctagacaa acagagaact ggttttgaca gtgtttctag agtgcttttt    120 

attattttcc tgacagttgt gttccaccat gattactttc tccttcagcg aataggctaa    180 

atgaatatga aacagaaaag cgtgtatcag caaaccaaag cacttctgtg caagaatttt    240 

cttaagaaat ggaggatgaa aagagagagc ttattggaat ggggcctctc aatacttcta    300 

ggactgtgta ttgctctgtt ttccagttcc atgagaaatg tccagtttcc tggaatggct    360 

cctcagaatc tgggaagggt agataaattt aatagctctt ctttaatggt tgtgtataca    420 

ccaatatcta atttaaccca gcagataatg aataaaacag cacttgctcc tcttttgaaa    480 

ggaacaagtg tcattggggc accaaataaa acacacatgg acgaaatact tctggaaaat    540 

ttaccatatg ctatgggaat catctttaat gaaactttct cttataagtt aatatttttc    600 

cagggatata acagtccact ttggaaagaa gatttctcag ctcattgctg ggatggatat    660 

ggtgagtttt catgtacatt gaccaaatac tggaatagag gatttgtggc tttacaaaca    720 

gctattaata ctgccattat agaagtagct ttggtgttcc tgatgagtgt gctgttaaag    780 

aaagctgtcc tcaccaattt ggttgtgttt ctccttaccc tcttttgggg atgtctggga    840 

ttcactgtat tttatgaaca acttccttca tctctggagt ggattttgaa tatttgtagc    900 

ccttttgcct ttactactgg aatgattcag attatcaaac tggattataa cttgaatggt    960 

gtaatttttc ctgacccttc aggagactca tatacaatga tagcaacttt ttctatgttg   1020 

cttttggatg gtctcatcta cttgctattg gcattatact ttgacaaaat tttaccctat   1080 

ggagatgagc gccattattc tcctttattt ttcttgaatt catcatcttg tttccaacac   1140 

caaaggacta atgctaaggt tattgagaaa gaaatcgatg ctgagcatcc ctctgatgat   1200 

tattttgaac cagtagctcc tgaattccaa ggaaaagaag ccatcagaat cagaaatgtt   1260 

aagaaggaat ataaaggaaa atctggaaaa gtggaagcat tgaaaggctt gctctttgac   1320 

atatatgaag gtcaaatcac ggcaatcctg ggtcacagtg gagctggcaa atcttcactg   1380 

ctaaatattc ttaatggatt gtctgttcca acagaaggat cagttaccat ctataataaa   1440 

aatctctctg aaatgcaaga cttggaggaa atcagaaaga taactggcgt ctgtcctcaa   1500 

ttcaatgttc aatttgacat actcaccgtg aaggaaaacc tcagcctgtt tgctaaaata   1560 

aaagggattc atctaaagga agtggaacaa gaggtacaac gaatattatt ggaattggac   1620 

atgcaaaaca ttcaagataa ccttgctaaa catttaagtg aaggacagaa aagaaagctg   1680 

acttttggga ttaccatttt aggagatcct caaattttgc tcttagatga accaactact   1740 

ggattggatc ccttttccag agatcaagtg tggagcctcc tgagagagcg tagagcagat   1800 

catgtgatcc ttttcagtac ccagtccatg gatgaggctg acatcctggc tgatagaaaa   1860 

gtgatcatgt ccaatgggag actgaagtgt gcaggttctt ctatcttttt gaaaagaagg   1920 

tggggtcttg gatatcacct aagtttacat aggaatgaaa tatgtaaccc agaacaaata   1980 

acatccttca ttactcatca catccccgat gctaaattaa aaacagaaaa caaagaaaag   2040 

cttgtatata ctttgccact ggaaaggaca aatacatttc cagatctttt cagtgatctg   2100 

gataagtgtt ctgaccaggg agtgacaggt tatgacattt ccatgtcaac tctaaatgaa   2160 

gtctttatga aactggaagg acagtcaact atcgaacaag atttcgaaca agtggagatg   2220 

ataagagact cagaaagcct caatgaaatg gagctggctc actcttcctt ctctgaaatg   2280 

cagacagctg tgagtgacat gggcctctgg agaatgcaag tctttgccat ggcacggctc   2340 

cgtttcttaa agttaaaacg tcaaactaaa gtgttattga ccctattatt ggtatttgga   2400 

atcgcaatat tccctttgat tgttgaaaat ataatatatg ctatgttaaa tgaaaagatc   2460 

gattgggaat ttaaaaacga attgtatttt ctctctcctg gacaacttcc ccaggaaccc   2520 

cgtaccagcc tgttgatcat caataacaca gaatcaaata ttgaagattt tataaaatca   2580 

ctgaagcatc aaaatatact tttggaagta gatgactttg aaaacagaaa tggtactgat   2640 

ggcctctcat acaatggagc tatcatagtt tctggtaaac aaaaggatta tagattttca   2700 

gttgtgtgta ataccaagag attgcactgt tttccaattc ttatgaatat tatcagcaat   2760 

gggctacttc aaatgtttaa tcacacacaa catattcgaa ttgagtcaag cccatttcct   2820 

cttagccaca taggactctg gactgggttg ccggatggtt cctttttctt atttttggtt   2880 

ctatgtagca tttctcctta tatcaccatg ggcagcatca gtgattacaa gaaaaatgct   2940 

aagtcccagc tatggatttc aggcctctac acttctgctt actggtgtgg gcaggcacta   3000 

gtggacgtca gcttcttcat tttaattctc cttttaatgt atttaatttt ctacatagaa   3060 

aacatgcagt accttcttat tacaagccaa attgtgtttg ctttggttat agttactcct   3120 

ggttatgcag cttctcttgt cttcttcata tatatgatat catttatttt tcgcaaaagg   3180 

agaaaaaaca gtggcctttg gtcattttac ttcttttttg cctccaccat catgttttcc   3240 

atcactttaa tcaatcattt tgacctaagt atattgatta ccaccatggt attggttcct   3300 

tcatatacct tgcttggatt taaaactttt ttggaagtga gagaccagga gcactacaga   3360 

gaatttccag aggcaaattt tgaattgagt gccactgatt ttctagtctg cttcataccc   3420 

tactttcaga ctttgctatt cgtttttgtt ctaagatgca tggaactaaa atgtggaaag   3480 

aaaagaatgc gaaaagatcc tgttttcaga atttcccccc aaagtagaga tgctaagcca   3540 

aatccagaag aacccataga tgaagatgaa gatattcaaa cagaaagaat aagaacagtc   3600 

actgctctga ccacttcaat cttagatgag aaacctgtta taattgccag ctgtctacac   3660 

aaagaatatg caggccagaa gaaaagttgc ttttcaaaga ggaagaagaa aatagcagca   3720 

agaaatatct ctttctgtgt tcaagaaggt gagattttgg gattgctagg acccagtggt   3780 

gctggaaaaa gttcatctat tagaatgata tctgggatca caaagccaac tgctggagag   3840 

gtggaactga aaggctgcag ttcagttttg ggccacctgg ggtactgccc tcaagagaac   3900 

gtgctgtggc ccatgctgac gttgagggaa cacctggagg tgtatgctgc cgtcaagggg   3960 

ctcagggaag cggacgcgag gctcgccatc gcaagattag tgagtgcttt caaactgcat   4020 

gagcagctga atgttcctgt gcagaaatta acagcaggaa tcacgagaaa gttgtgtttt   4080 

gtgctgagcc tcctgggaaa ctcacctgtc ttgctcctgg atgaaccatc tacgggcata   4140 

gaccccacag ggcagcagca aatgtggcag gcaatccagg cagtcgttaa aaacacagag   4200 

agaggtgtcc tcctgaccac ccataacctg gctgaggcgg aagccttgtg tgaccgtgtg   4260 

gccatcatgg tgtctggaag gcttagatgc attggctcca tccaacacct gaaaaacaaa   4320 

cttggcaagg attacattct agagctaaaa gtgaaggaaa cgtctcaagt gactttggtc   4380 

cacactgaga ttctgaagct tttcccacag gctgcagggc agcaaaggta ttcctctttg   4440 

ttaacctata agctgcccgt ggcagacgtt taccctctat cacagacctt tcacaaatta   4500 

gaagcagtga agcataactt taacctggaa gaatacagcc tttctcagtg cacactggag   4560 

aaggtattct tagagctttc taaagaacag gaagtaggaa attttgatga agaaattgat   4620 

acaacaatga gatggaaact cctccctcat tcagatgaac cttaaaacct caaacctagt   4680 

aattttcttg cttgatctcc tataaactta tgttttatgt aataatt                 4727 

 
           
             57  
             3852  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 4599654CB1  
             
           
            57 

cgccggcgat tccgagccta cgacgcctcc gctagagccc gcggggctgc gccgactcct     60 

gctctggagg ggttgcgggt acctgatggc cacagagggc tctaggaggc cgagcgtgta    120 

agcggggtgg gcgccatgga ggcagagcag cggccggcgg cgggggccag cgaaggggcg    180 

acccctggac tggaggcggt gcctcccgtt gctcccccgc ctgcgaccgc ggcctcaggt    240 

ccgatcccca aatctgggcc tgagcctaag aggaggcacc ttgggacgct gctccagcct    300 

acggtcaaca agttctccct tcgggtgttc ggcagccaca aagcagtgga aatcgagcag    360 

gagcgggtga agtcagcggg ggcctggatc atccacccct acagcgactt ccggttttac    420 

tgggacctga tcatgctgct gctgatggtg gggaacctca tcgtcctgcc tgtgggcatc    480 

accttcttca aggaggagaa ctccccgcct tggatcgtct tcaacgtatt gtctgatact    540 

ttcttcctac tggatctggt gctcaacttc cgaacgggca tcgtggtgga ggagggtgct    600 

gagatcctgc tggcaccgcg ggccatccgc acgcgctacc tgcgcacctg gttcctggtt    660 

gacctcatct cttctatccc tgtggattac atcttcctag tggtggagct ggagccacgg    720 

ttggacgctg aggtctacaa aacggcacgg gccctacgca tcgttcgctt caccaagatc    780 

ctaagcctgc tgaggctgct ccgcctctcc cgcctcatcc gctacataca ccagtgggag    840 

gagatcttcc acatgaccta tgacctggcc agtgctgtgg ttcgcatctt caacctcatt    900 

gggatgatgc tgctgctatg tcactgggat ggctgtctgc agttcctggt gcccatgctg    960 

caggacttcc ctcccgactg ctgggtctcc atcaaccaca tggtgaacca ctcgtggggc   1020 

cgccagtatt cccatgccct gttcaaggcc atgagccaca tgctgtgcat tggctatggg   1080 

cagcaggcac ctgtaggcat gcccgacgtc tggctcacca tgctcagcat gatcgtaggt   1140 

gccacatgct acgccatgtt catcggccat gccacggcac tcatccagtc cctggactct   1200 

tcccggcgtc agtaccagga gaagtacaag caggtggagc agtacatgtc cttccacaag   1260 

ctgccagcag acacgcggca gcgcatccac gagtactatg agcaccgcta ccagggcaag   1320 

atgttcgatg aggaaagcat cctgggcgag ctgagcgagc cgcttcgcga ggagatcatt   1380 

aacttcacct gtcggggcct ggtggcccac atgccgctgt ttgcccatgc cgaccccagc   1440 

ttcgtcactg cagttctcac caagctgcgc tttgaggtct tccagccggg ggatctcgtg   1500 

gtgcgtgagg gctccgtggg gaggaagatg tacttcatcc agcatgggct gctcagtgtg   1560 

ctggcccgcg gcgcccggga cacacgcctc accgatggat cctactttgg ggagatctgc   1620 

ctgctaacta ggggccggcg cacagccagt gttcgggctg acacctactg ccgcctttac   1680 

tcactcagcg tggaccattt caatgctgtg cttgaggagt tccccatgat gcgccgggcc   1740 

tttgagactg tggccatgga tcggctgctc cgcatcggca agaagaattc catactgcag   1800 

cggaagcgct ccgagccaag tccaggcagc agtggtggca tcatggagca gcatttggtg   1860 

caacatgaca gagacatggc tcggggtgtt cggggtcggg ccccgagcac aggagctcag   1920 

cttagtggaa agccagtact gtgggagcca ctggtacatg cgccccttca ggcagctgct   1980 

gtgacctcca atgtggccat tgccctgact catcagcggg gccctctgcc cctctcccct   2040 

gactctccag ccaccctcct tgctcgctct gcttggcgct cagcaggctc tccagcttcc   2100 

ccgctggtgc ccgtccgagc tggcccatgg gcatccacct cccgcctgcc cgccccacct   2160 

gcccgaaccc tgcacgccag cctatcccgg gcagggcgct cccaggtctc cctgctgggt   2220 

ccccctccag gaggaggtgg acggcggcta ggacctcggg gccgcccact ctcagcctcc   2280 

caaccctctc tgcctcagcg ggcaacaggc gatggctctc ctgggcgtaa gggatcagga   2340 

agtgagcggc tgcctccctc agggctcctg gccaaacctc caaggacagc ccagcccccc   2400 

aggccaccag tgcctgagcc agccacaccc cggggtctcc agctttctgc caacatgtaa   2460 

aacctttgag tacatccagc cttagttctt ggggtgcagt agtatgtacc caagggcaga   2520 

tgcctcttgg ggaaggccat ggggacctga aacattgccc catggaaatg tcgaccctgt   2580 

gcggacattc cgcatactgc catgaagacg gtctctgtgt cctcagctca agaatcctgt   2640 

agcttgtccc atcataatcc attcacccgt tcatcatgtg tactgagcag ctaccatgtt   2700 

caaggtaata tgccaggcgc tgtatgtctc cactgccaag tagaagtgac tcaaaaccct   2760 

ctgacaagga tattcccttg gctatggtcc tgccaggtgc aggcccaggc ccatgacccc   2820 

acctttacta agcacaagta cttgccactg ccatcactgc caagtaacta gatgtctctg   2880 

tttccctgcc aatgatcctg caggttctgc ccggtctggt tatcttcctg tttcctgtag   2940 

catagccagg cactgccagt cacctgtgcc cccattgctg tcagcagatg tcttgggtcc   3000 

tgagtgtggg tatccacttt tacccgctca ctgccacctg tggacactct gtgtctaccc   3060 

tctgagtggg aacatacttc taagttccct gcagtctctg tcctgtggta gaccatcttt   3120 

ttgtaaactg cgagcttcct cttccctgta ccctctgccc cagtcgtgac cccctaaaag   3180 

ttaaggggta gttggcacct ccttattaat atgccagcct agatcccccc cggtggaggg   3240 

gcaaatggct gaatccttgt gtgatatttt tttcttcgct tgtttattta ttcatttatt   3300 

taattgtatt tattcattta ctaactttat gtgttaccaa ttaattttgt ttacccattc   3360 

ctttatccat ccctcccctc cttttcaggt aaggagacag gaggagtagg aggaggcagg   3420 

gcctctccat gccagcctct gtggtccttg cccaaaccca tcagcgcaat acttgaacct   3480 

tctcccaggt aggggcagga ggagccacat gagagaggga gaaggaccgc gtttaccttt   3540 

agagttttgt tttgtttttt ccttctgagt ttgctgttgg tgcaggaata agggaaaggc   3600 

ccaaggtatc caagcctggg gaagggcagg ccagccagca cctctgcctt ctcagggaca   3660 

agagtagtcc tttaccaccc tcactctgcc tgtcccctct cctactctac agcattaaag   3720 

actgtgggac caggacccta agtctccttt ccttctgggt ggggagttct aggggttctt   3780 

ggtgtgtggg agaagtttta taattgcttc caaacagctg ggtttaaata taaaatagac   3840 

acactcaaaa aa                                                       3852 

 
           
             58  
             1917  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 5047435CB1  
             
           
            58 

atggcagaag gtgaaagggg agcagacgtg ccacatggcc tcggggcctg gctggccgac     60 

gtggcgttgg cggcgctgcg cgcgggaggg cagggcagga gggacagagg cgggggcggg    120 

ccggaaagtt tgtccggcgg cagcggcgtt ggggactccg gcgggggatg cgcgcccggc    180 

ccctcagcgc ccccagcacg ccgccgagtc ccgctcgcca tgggccactc cccacctgtc    240 

ctgcctttgt gtgcctctgt gtctttgctg ggtggcctga cctttggtta tgaactggca    300 

gtcatatcag gtgccctgct gccactgcag cttgactttg ggctaagctg cttggagcag    360 

gagttcctgg tgggcagcct gctcctgggg gctctcctcg cctccctggt tggtggcttc    420 

ctcattgact gctatggcag gaagcaagcc atcctcggga gcaacttggt gctgctggca    480 

ggcagcctga ccctgggcct ggctggttcc ctggcctggc tggtcctggg ccgcgctgtg    540 

gttggcttcg ccatttccct ctcctccatg gcttgctgta tctacgtgtc agagctggtg    600 

gggccacggc agcggggagt gctggtgtcc ctctatgagg caggcatcac cgtgggcatc    660 

ctgctctcct atgccctcaa ctatgcactg gctggtaccc cctggggatg gaggcacatg    720 

ttcggctggg ccactgcacc tgctgtcctg caatccctca gcctcctctt cctccctgct    780 

ggtacagatg agactgcaac acacaaggac ctcatcccac tccagggagg tgaggccccc    840 

aagctgggcc cggggaggcc acggtactcc tttctggacc tcttcagggc acgcgataac    900 

atgcgaggcc ggaccacagt gggcctgggg ctggtgctct tccagcaact aacagggcag    960 

cccaacgtgc tgtgctatgc ctccaccatc ttcagctccg ttggtttcca tgggggatcc   1020 

tcagccgtgc tggcctctgt ggggcttggc gcagtgaagg tggcagctac cctgaccgcc   1080 

atggggctgg tggaccgtgc aggccgcagg gctctgttgc tagctggctg tgccctcatg   1140 

gccctgtccg tcagtggcat aggcctcgtc agctttgccg tgcccatgga ctcaggccca   1200 

agctgtctgg ctgtgcccaa tgccaccggg cagacaggcc tccctggaga ctctggcctg   1260 

ctgcaggact cctctctacc tcccattcca aggaccaatg aggaccaaag ggagccaatc   1320 

ttgtccactg ctaagaaaac caagccccat cccagatctg gagacccctc agcccctcct   1380 

cggctggccc tgagctctgc cctccctggg ccccctctgc ccgctcgggg gcatgcactg   1440 

ctgcgctgga ccgcactgct gtgcctgatg gtctttgtca gtgccttctc ctttgggttt   1500 

gggccagtga cctggcttgt cctcagcgag atctaccctg tggagatacg aggaagagcc   1560 

ttcgccttct gcaacagctt caactgggcg gccaacctct tcatcagcct ctccttcctc   1620 

gatctcattg gcaccatcgg cttgtcctgg accttcctgc tctacggact gaccgctgtc   1680 

ctcggcctgg gcttcatcta tttatttgtt cctgaaacaa aaggccagtc gttggcagag   1740 

atagaccagc agttccagaa gagacggttc accctgagct ttggccacag gcagaactcc   1800 

actggcatcc cgtacagccg catcgagatc tctgcggcct cctgaggaat ccgtctgcct   1860 

ggaaattctg gaactgtggc tttggcagac catctccagc atcctgcttc ctaggcc      1917 

 
           
             59  
             6791  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7475603CB1  
             
           
            59 

cgcgctccct gcctgctgct gggcggaggg aaggcggcaa gagctgcgga gcccctggaa     60 

gagcttccag gaaccctgcg ctgtgggata aaggaatgag gttcagaaag gggcaggagt    120 

tgcccgcagc cgcaccgcac gtcttcagcc cgaccgttgt cctgacctct ctgtcccgtc    180 

ccctgcccag tctcaccatg gccttctgga cacagctgat gctgctgctc tggaagaatt    240 

tcatgtatcg ccggagacag ccggtccagc tcctggtcga attgctgtgg cctctcttcc    300 

tcttcttcat cctggtggct gttcgccact cccacccgcc cctggagcac catgaatgcc    360 

acttcccaaa caagccactg ccatcggcgg gcaccgtgcc ctggctccag ggtctcatct    420 

gtaatgtgaa caacacctgc tttccgcagc tgacaccggg cgaggagccc gggcgcctga    480 

gcaacttcaa cgactccctg gtctcccggc tgctagccga tgcccgcact gtgctgggag    540 

gggccagtgc ccacaggacg ctggctggcc tagggaagct gatcgccacg ctgagggctg    600 

cacgcagcac ggcccagcct caaccaacca agcagtctcc actggaacca cccatgctgg    660 

atgtcgcgga gctgctgacg tcactgctgc gcacggaatc cctggggttg gcactgggcc    720 

aagcccagga gcccttgcac agcttgttgg aggccgctga ggacctggcc caggagctcc    780 

tggcgctgcg cagcctggtg gagcttcggg cactgctgca gagaccccga gggaccagcg    840 

gccccctgga gttgctgtca gaggccctct gcagtgtcag gggacctagc agcacagtgg    900 

gcccctccct caactggtac gaggctagtg acctgatgga gctggtgggg caggagccag    960 

aatccgccct gccagacagc agcctgagcc ccgcctgctc ggagctgatt ggagccctgg   1020 

acagccaccc gctgtcccgc ctgctctgga gacgcctgaa gcctctgatc ctcgggaagc   1080 

tactctttgc accagataca ccttttaccc ggaagctcat ggcccaggtg aaccggacct   1140 

tcgaggagct caccctgctg agggatgtcc gggaggtgtg ggagatgctg ggaccccgga   1200 

tcttcacctt catgaacgac agttccaatg tggccatgct gcagcggctc ctgcagatgc   1260 

aggatgaagg aagaaggcag cccagacctg gaggccggga ccacatggag gccctgcgat   1320 

cctttctgga ccctgggagc ggtggctaca gctggcagga cgcacacgct gatgtggggc   1380 

acctggtggg cacgctgggc cgagtgacgg agtgcctgtc cttggacaag ctggaggcgg   1440 

caccctcaga ggcagccctg gtgtcgcggg ccctgcaact gctcgcggaa catcgattct   1500 

gggccggcgt cgtcttcttg ggacctgagg actcttcaga ccccacagag cacccaaccc   1560 

cagacctggg ccccggccac gtgcgcatca aaatccgcat ggacattgac gtggtcacga   1620 

ggaccaataa gatcagggac aggttttggg accctggccc agccgcggac cccctgaccg   1680 

acctgcgcta cgtgtggggc ggcttcgtgt acctgcaaga cctggtggag cgtgcagccg   1740 

tccgcgtgct cagcggcgcc aacccccggg ccggcctcta cctgcagcag atgccctatc   1800 

cgtgctatgt ggacgacgtg ttcctgcgtg tgctgagccg gtcgctgccg ctcttcctga   1860 

cgctggcctg gatctactcc gtgacactga cagtgaaggc cgtggtgcgg gagaaggaga   1920 

cgcggctgcg ggacaccatg cgcgccatgg ggctcagccg cgcggtgctc tggctaggct   1980 

ggttcctcag ctgcctcggg cccttcctgc tcagcgccgc gctgctggtt ctggtgctca   2040 

agctggggga catcctcccc tacagccacc cgggcgtggt cttcctgttc ttggcagcct   2100 

tcgcggtggc cacggtgacc cagagcttcc tgctcagcgc cttcttctcc cgcgccaacc   2160 

tggctgcggc ctgcggcggc ctggcctact tctccctcta cctgccctac gtgctgtgtg   2220 

tggcttggcg ggaccggctg cccgcgggtg gccgcgtggc cgcgagcctg ctgtcgcccg   2280 

tggccttcgg cttcggctgc gagagcctgg ctctgctgga ggagcagggc gagggcgcgc   2340 

agtggcacaa cgtgggcacc cggcctacgg cagacgtctt cagcctggcc caggtctctg   2400 

gccttctgct gctggacgcg gcgctctacg gcctcgccac ctggtacctg gaagctgtgt   2460 

gcccaggcca gtacgggatc cctgaaccat ggaattttcc ttttcggagg agctactggt   2520 

gcggacctcg gccccccaag agtccagccc cttgccccac cccgctggac ccaaaggtgc   2580 

tggtagaaga ggcaccgccc ggcctgagtc ctggcgtctc cgttcgcagc ctggagaagc   2640 

gctttcctgg aagcccgcag ccagccctgc gggggctcag cctggacttc taccagggcc   2700 

acatcaccgc cttcctgggc cacaacgggg ccggcaagac caccaccctg tccatcttga   2760 

gtggcctctt cccacccagt ggtggctctg ccttcatcct gggccacgac gtccgctcca   2820 

gcatggccgc catccggccc cacctgggcg tctgtcctca gtacaacgtg ctgtttgaca   2880 

tgctgaccgt ggacgagcac gtctggttct atgggcggct gaagggtctg agtgccgctg   2940 

tagtgggccc cgagcaggac cgtctgctgc aggatgtggg gctggtctcc aagcagagtg   3000 

tgcagactcg ccacctctct ggtgggatgc aacggaagct gtccgtggcc attgcctttg   3060 

tgggcggctc ccaagttgtt atcctggacg agcctacggc tggcgtggat cctgcttccc   3120 

gccgcggtat ttgggagctg ctgctcaaat accgagaagg tcgcacgctg atcctctcca   3180 

cccaccacct ggatgaggca gagctgctgg gagaccgtgt ggccgtggtg gcaggtggcc   3240 

gcttgtgctg ctgtggatcc ccactcttcc tgcgccgtca cctgggctcc ggctactacc   3300 

tgacgctggt gaaggcccgc ctgcccctga ccaccaatga gaaggctgac actgacatgg   3360 

agggcagtgt ggacaccagg caggaaaaga agaatggcag ccagggcagc agagtcggca   3420 

ctcctcagct gctggccctg gtacagcact gggtgcccgg ggcacggctg gtggaggagc   3480 

tgccacacga gctggtgctg gtgctgccct acacgggtgc ccatgacggc agcttcgcca   3540 

cactcttccg agagctagac acgcggctgg cggagctgag gctcactggc tacgggatct   3600 

ccgacaccag cctcgaggag atcttcctga aggtggtgga ggagtgtgct gcggacacag   3660 

atatggagga tggcagctgc gggcagcacc tatgcacagg cattgctggc ctagacgtaa   3720 

ccctacggct caagatgccg ccacaggaga cagcgctgga gaacggggaa ccagctgggt   3780 

cagccccaga gactgaccag ggctctgggc cagacgccgt gggccgggta cagggctggg   3840 

cactgacccg ccagcagctc caggccctgc ttctcaagcg ctttctgctt gcccgccgca   3900 

gccgccgcgg cctgttcgcc cagatcgtgc tgcctgccct ctttgtgggc ctggccctcg   3960 

tgttcagcct catcgtgcct cctttcgggc actacccggc tctgcggctc agtcccacca   4020 

tgtacggtgc tcaggtgtcc ttcttcagtg aggacgcccc aggggaccct ggacgtgccc   4080 

ggctgctcga ggcgctgctg caggaggcag gactggagga gcccccagtg cagcatagct   4140 

cccacaggtt ctcggcacca gaagttcctg ctgaagtggc caaggtcttg gccagtggca   4200 

actggacccc agagtctcca tccccagcct gccagtgtag ccggcccggt gcccggcgcc   4260 

tgctgcccga ctgcccggct gcagctggtg gtccccctcc gccccaggca gtgaccggct   4320 

ctggggaagt ggttcagaac cagacaggcc ggaacctgtc tgacttcctg gtcaagacct   4380 

acccgcgcct ggtgcgccag ggcctgaaga ctaagaagtg ggtgaatgag gtcagatacg   4440 

gaggcttctc gctggggggc cgagacccag gcctgccctc gggccaagag ttgggccgct   4500 

cagtggagga gttgtgggcg ctgctgagtc ccctgcctgg cggggccctc gaccgtgtcc   4560 

tgaaaaacct cacagcctgg gctcacagcc tggatgctca ggacagtctc aagatctggt   4620 

tcaacaacaa aggctggcac tccatggtgg cctttgtcaa ccgagccagc aacgcaatcc   4680 

tccgtgctca cctgccccca ggcccggccc gccacgccca cagcatcacc acactcaacc   4740 

accccttgaa cctcaccaag gagcagctgt ctgaggctgc actgatggcc tcctcggtgg   4800 

acgtcctcgt ctccatctgt gtggtctttg ccatgtcctt tgtcccggcc agcttcactc   4860 

ttgtcctcat tgaggagcga gtcacccgag ccaagcacct gcagctcatg gggggcctgt   4920 

cccccaccct ctactggctt ggcaactttc tctgggacat gtgtaactac ttggtgccag   4980 

catgcatcgt ggtgctcatc tttctggcct tccagcagag ggcatatgtg gcccctgcca   5040 

acctgcctgc tctcctgctg ttgctactac tgtatggctg gtcgatcaca ccgctcatgt   5100 

acccagcctc cttcttcttc tccgtgccca gcacagccta tgtggtgctc acctgcataa   5160 

acctctttat tggcatcaat ggaagcatgg ccacctttgt gcttgagctc ttctctgatc   5220 

agaagctgca ggaggtgagc cggatcttga aacaggtctt ccttatcttc ccccacttct   5280 

gcttgggccg ggggctcatt gacatggtgc ggaaccaggc catggctgat gcctttgagc   5340 

gcttgggaga caggcagttc cagtcacccc tgcgctggga ggtggtcggc aagaacctct   5400 

tggccatggt gatacagggg cccctcttcc ttctcttcac actactgctg cagcaccgaa   5460 

gccaactcct gccacagccc agggtgaggt ctctgccact cctgggagag gaggacgagg   5520 

atgtagcccg tgaacgggag cgggtggtcc aaggagccac ccagggggat gtgttggtgc   5580 

tgaggaactt gaccaaggta taccgtgggc agaggatgcc agctgttgac cgcttgtgcc   5640 

tggggattcc ccctggtgag tgttttgggc tgctgggtgt gaatggagca gggaagacgt   5700 

ccacgtttcg catggtgacg ggggacacat tggccagcag gggcgaggct gtgctggcag   5760 

gccacagcgt ggcccgggaa cccagtgctg cgcacctcag catgggatac tgccctcaat   5820 

ccgatgccat ctttgagctg ctgacgggcc gcgagcacct ggagctgctt gcgcgcctgc   5880 

gcggtgtccc ggaggcccag gttgcccaga ccgctggctc gggcctggcg cgtctgggac   5940 

tctcatggta cgcagaccgg cctgcaggca cctacagcgg agggaacaaa cgcaagctgg   6000 

cgacggccct ggcgctggtt ggggacccag ccgtggtgtt tctggacgag ccgaccacag   6060 

gcatggaccc cagcgcgcgg cgcttccttt ggaacagcct tttggccgtg gtgcgggagg   6120 

gccgttcagt gatgctcacc tcccatagca tggaggagtg tgaagcgctc tgctcgcgcc   6180 

tagccatcat ggtgaatggg cggttccgct gcctgggcag cccgcaacat ctcaagggca   6240 

gattcgcggc gggtcacaca ctgaccctgc gggtgcccgc cgcaaggtcc cagccggcag   6300 

cggccttcgt ggcggccgag ttccctgggg cggagctgcg cgaggcacat ggaggccgcc   6360 

tgcgcttcca gctgccgccg ggagggcgct gcgccctggc gcgcgtcttt ggagagctgg   6420 

cggtgcacgg cgcagagcac ggcgtggagg acttttccgt gagccagacg atgctggagg   6480 

aggtattctt gtacttctcc aaggaccagg ggaaggacga ggacaccgaa gagcagaagg   6540 

aggcaggagt gggagtggac cccgcgccag gcctgcagca ccccaaacgc gtcagccagt   6600 

tcctcgatga ccctagcact gccgagactg tgctctgagc ctccctcccc tgcggggccg   6660 

cggggaggcc ctgggaatgg caagggcaag gtagagtgcc taggagccct ggactcaggc   6720 

tggcagaggg gctggtgccc tggagaaaat aaagagaagg ctggagagaa gccgtggtgg   6780 

tgaaaaaaaa a                                                        6791 

 
           
             60  
             5214  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477845CB1  
             
           
            60 

atgctcaaaa ggaagcagag ttccagggtg gaagcccagc cagtcactga ctttggtcct     60 

gatgagtctc tgtcggataa tgctgacatc ctctggatta acaaaccatg ggttcactct    120 

ttgctgcgca tctgtgccat catcagcgtc atttctgttt gtatgaatac gccaatgacc    180 

ttcgagcact atcctccact tcagtatgtg accttcactt tggatacatt attgatgttt    240 

ctctacacgg cagagatgat agcaaaaatg cacatccggg gcattgtcaa gggggatagt    300 

tcctatgtga aagatcgctg gtgtgttttt gatggattta tggtcttttg cctttgggtt    360 

tctttggtgc tacaggtgtt tgaaattgct gatatagttg atcagatgtc accttggggc    420 

atgttgcgga ttccacggcc actgattatg atccgagcat tccggattta tttccgattt    480 

gaactgccaa ggaccagaat tacaaatatt ttaaagcgat cgggagaaca aatatggagt    540 

gtttccattt ttctactttt ctttctactt ctttatggaa ttttaggagt tcagatgttt    600 

ggaacattta cttatcactg tgttgtaaat gacacaaagc cagggaatgt aacctggaat    660 

agtttagcta ttccagacac acactgctca ccagagctag aagaaggcta ccagtgccca    720 

cctggattta aatgcatgga ccttgaagat ctgggactta gcaggcaaga gctgggctac    780 

agtggcttta atgagatagg aactagtata ttcaccgtct atgaggccgc ctcacaggaa    840 

ggctgggtgt tcctcatgta cagagcaatt gacagctttc cccgttggcg ttcctacttc    900 

tatttcatca ctctcatttt cttcctcgcc tggcttgtga agaacgtgtt tattgctgtt    960 

atcattgaaa catttgcaga aatcagagta cagtttcaac aaatgtgggg atcgagaagc   1020 

agcactacct caacagccac cacccagatg tttcatgaag atgctgctgg aggttggcag   1080 

ctggtagctg tggatgtcaa caagccccag ggacgcgccc cagcctgcct ccagaaaatg   1140 

atgcggtcat ccgttttcca catgttcatc ctgagcatgg tgaccgtgga cgtgatcgtg   1200 

gcggctagca actactacaa aggagaaaac ttcaggaggc agtacgacga gttctacctg   1260 

gcggaggtgg cttttacagt actttttgat ttggaagcac ttctgaagat atggtgtttg   1320 

ggatttactg gatatattag ctcatctctc cacaaattcg aactactact cgtaattgga   1380 

actactcttc atgtataccc agatctttat cattcacaat tcacgtactt tcaggtactc   1440 

cgagtagttc ggctgattaa gatttcacct gcattagaag actttgtgta caagatattt   1500 

ggtcctggaa aaaagcttgg gagtttggtt gtatttactg ccagcctctt gattgttatg   1560 

tcagcaatta gtttgcagat gttctgcttt gtcgaagaac tggacagatt tactacgttt   1620 

ccgagggcat ttatgtccat gttccagatc ctcacccagg aaggatgggt ggacgtaatg   1680 

gaccaaactc taaatgctgt gggacatatg tgggcacccg tggttgccat ctatttcatt   1740 

ctctatcatc tttttgccac tctgatcctc ctgagtttgt ttgttgctgt tattttggac   1800 

aacttagaac ttgatgaaga cctaaagaag cttaaacaat taaagcaaag tgaagcaaat   1860 

gcggacacca aagaaaagct ccctttacgc ctgcgaatct ttgaaaaatt tccaaacaga   1920 

cctcaaatgg tgaaaatctc aaagcttcct tcagatttta cagttcctaa aatcagggag   1980 

agttttatga agcagtttat tgaccgccag caacaggaca catgttgcct tctgagaagc   2040 

ctcccgacca cctcttcctc ctcctgcgac cactccaaac gctcagcaat tgaggacaac   2100 

aaatacatcg accaaaaact tcgcaagtct gttttcagca tcagggcaag gaaccttctg   2160 

gaaaaggaga ccgcagtcac taaaatctta agggcttgca cccgacagcg catgctgagc   2220 

ggatcatttg aggggcagcc cgcaaaggag aggtcaatcc tcagcgtgca gcatcatatc   2280 

cgccaagagc gcaggtcact aagacatgga tcaaacagcc agaggatcag caggggaaaa   2340 

tctcttgaaa ctttgactca agatcattgc aatacagtga tatatagaaa tgctcaaaga   2400 

gaagtcagtg aaataaagat gattcaggaa aaaaaggagc tagcagagat gcttcaagga   2460 

aagtgcaaaa aggaactcag agagagccac ccatacttcg ataagccact gttcattgtc   2520 

gggcgagaac acaggttcag aaacttttgc cgggtggtgg tccgagcacg cttcaacgcg   2580 

tctaaaacag accctgtcac aggagctgtg aaaaatacaa agtaccatct tctttatgat   2640 

ttgctgggat tggtcactta cctggactgg gtcatgatca tcgtaacctc tgactcttgc   2700 

atttccatga tgtttgagtc cccgtttcga agagtcatgc atgcacctac tttgcagatt   2760 

gctgagtatg tgtttgtgat attcatgagc attgagctta atctgaagat tatggcagat   2820 

ggcttatttt tcactccaac tgctgtcatc agggacttcg gtggagtaat ggacatattt   2880 

atatatcttg tgagcttgat atttctttgt tggatgcctc aaaatgtacc tgctgaatcg   2940 

ggagctcagc ttctaatggt ccttcggtgc ctgagacctc tgcgcatatt caaactggtg   3000 

ccccagatga ggaaagttgt tcgagaactt ttcagcggct tcaaggaaat ttttttggtc   3060 

tccattcttt tgctgacatt aatgctcgtt tttgcaagct ttggagttca gctttttgct   3120 

ggaaaactgg ccaagtgcaa tgatcccaac attattagaa gggaagattg caatggcata   3180 

ttcagaatta atgtcagtgt gtcaaagaac ttaaatttaa aattgaggcc tggagagaaa   3240 

aaacctggat tttgggtgcc ccgtgtttgg gcgaatcctc ggaactttaa tttcgacaat   3300 

gtgggaaacg ctatgctggc gttgtttgaa gttctctcct tgaaaggctg ggtggaagtg   3360 

agagatgtta ttattcatcg tgtggggccg atccatggaa tctatattca tgtttttgta   3420 

ttcctgggtt gcatgattgg actgaccctt tttgttggag tagttattgc taatttcaat   3480 

gaaaacaagg ggacggcttt gctgaccgtc gatcagagaa gatgggaaga cctgaagagc   3540 

cgactgaaga tcgcacagcc tcttcatctt ccgcctcgcc cggataatga tggttttaga   3600 

gctaaaatgt atgacataac ccagcatcca ttttttaaga ggacaatcgc attactcgtc   3660 

ctggcccagt cggtgttgct ctctgtcaag tgggacgtcg aggacccggt gaccgtacct   3720 

ttggcaacaa tgtcagttgt tttcaccttc atctttgttc tggaggtaac catgaagatc   3780 

atagcaatgt cgcctgctgg cttctggcaa agcagaagaa accgatacga tctcctggtg   3840 

acgtcgcttg gcgttgtatg ggtggtgctt cactttgccc tcctgaatgc atatacttac   3900 

atgatgggcg cttgtgtgat tgtatttagg tttttctcca tctgtggaaa acatgtaacg   3960 

ctaaagatgc tcctcttgac agtggtcgtc agcatgtaca agagcttctt tatcatagta   4020 

ggcatgtttc tcttgctgct gtgttacgct tttgctggag ttgttttatt tggtactgtg   4080 

aaatatgggg agaatattaa caggcatgca aatttttctt cggctggaaa agctattacc   4140 

gtactgttcc gaattgtcac aggtgaagac tggaacaaga ttatgcatga ctgtatggta   4200 

cagcctccgt tttgtactcc agatgaattt acatactggg caacagactg tggaaattat   4260 

gctggggcac ttatgtattt ctgttcattt tatgtcatca ttgcctacat catgctaaat   4320 

ctgcttgtag ccataattgt ggagaatttc tccttgattt attccactga ggaggaccag   4380 

cttttaagtt acaatgatct tcgccacttt caaataatat ggaacatggt ggatgataaa   4440 

agagaggtat tccccacgtt ccgcgtcaag ttcctgctgc ggctactgcg tgggaggctg   4500 

gaggtggacc tggacaagga caagctcctg tttaagcaca tgtgctacga aatggagagg   4560 

ctccacaatg gcggcgacgt caccttccat gatgtcctga gcatgctttc ataccggtcc   4620 

gtggacatcc ggaagagctt gcagctggag gaactcctgg cgagggagca gctggagtac   4680 

accatagagg aggaggtggc caagcagacc atccgcatgt ggctcaagaa gtgcctgaag   4740 

cgcatcagag ctaaacagca gcagtcgtgc agtatcatcc acagcctgag agagagtcag   4800 

cagcaagagc tgagccggtt tctgaacccg cccagcatcg agaccaccca gcccagtgag   4860 

gacacgaatg ccaacagtca ggacaacagc atgcaacctg agacaagcag ccagcagcag   4920 

ctcctgagcc ccacgctgtc ggatcgagga ggaagtcggc aagatgcagc cgacgcaggg   4980 

aaaccccaga ggaaatttgg gcagtggcgt ctgccctcag ccccaaaacc aataagccat   5040 

tcagtgtcct cagtcaactt acggtttgga ggaaggacaa ccatgaaatc tgtcgtgtgc   5100 

aaaatgaacc ccatgactga cgcggcttcc tgcggttctg aagttaagaa gtggtggacc   5160 

cggcagctga ctgtggagag cgacgaaagt ggggatgacc ttctggatat ttag         5214 

 
           
             61  
             1818  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 168827CB1  
             
           
            61 

ggaaattgct tccgtgaccc tgctgcagat gggagagagg gcccattaag aagagagtgg     60 

ggtcaggatc aacacacaca cttagtgtga tttaaggaaa ggaaatattt tctctttgaa    120 

cttatctgga tacagtcatt ttgtctcctc ttggggatca cttgtccagc ctcaatggcc    180 

tttcaggacc tcctagatca agttggaggc ctggggagat tccagatcct tcagatggtt    240 

ttccttataa tgttcaacgt catagtatac catcaaactc agctggagaa cttcgcagca    300 

ttcatacttg atcatcgctg ctgggttcat atactggaca atgacactat ccctgacaat    360 

gaccctggga ccctcagcca ggatgccctc ctgagaatct ccatcccatt cgactcaaat    420 

ctgaggccag agaagtgtcg tcgctttgtc catccccagt ggaagctcat tcatctgaat    480 

gggaccttcc ccaacacgag tgagccagat acagagccct gtgtggatgg ctgggtatat    540 

gaccaaagct ccttcccttc caccattgtg actaagtggg atctggtatg cgaatctcaa    600 

ccactgaatt cagtagctaa atttctattc atggctggaa tgatggtggg aggcaaccta    660 

tatggccatt tgtcagacag gtttgggaga aagttcgtgc tcagatggtc ttacctccag    720 

ctcgccattg taggcacctg tgcggccttt gctcccacca tcctcgtata ctgctccctg    780 

cgcttcttgg ctggggctgc tacatttagc atcattgtaa atactgtttt gttaattgta    840 

gagtggataa ctcaccaatt ctgtgccatg gcattgacat tgacactttg tgctgctagt    900 

attggacata taaccctggg aagcctggct tttgtcattc gagaccagtg catcctccag    960 

ttggtgatgt ctgcaccatg ctttgtcttc tttctgttct caaggtggct ggcagagtct   1020 

gctcggtggc tcattatcaa caacaaacca gaagagggct taaaggaact tacaaaagct   1080 

gcacacagga atggaatgaa gaatgctgaa gacatcctaa ccatggaggt tttgaaatcc   1140 

accatgaagc aagaactgga ggcagcacag aaaaagcatt ctctttgtga attgctccgc   1200 

atacccaaca tatgtaaaag aatctgtttc ctgtcctttg tgagatttgc aagtaccatc   1260 

cctttttggg gccttacttt gcacctccag catctgggaa acaatgtttt cctgttgcag   1320 

actctctttg gtgcagtcac cctcctggcc aattgtgttg caccttgggc actgaatcac   1380 

atgagccgtc gactaagcca gatgcttctc atgttcctac tggcaacctg ccttctggcc   1440 

atcatatttg tgcctcaaga aatgcagacc ctgcgtgtgg ttttggcaac cctgggtgtg   1500 

ggagctgctt ctcttggcat tacctgttct actgcccaag aaaatgaact aattccttcc   1560 

ataatcaggg gaagagctac tggaatcact ggaaactttg ctaatattgg gggagccctg   1620 

gcttccctca tgatgatcct aagcatatat tctcgacccc tgccctggat catctatgga   1680 

gtctttgcca tcctctctgg ccttgttgtc ctcctccttc ctgaaaccag gaaccagcct   1740 

cttcttgaca gcatccagga tgtggaaaat gagggagtaa atagcctagc tgcccctcag   1800 

aggagctctg tgctatag                                                 1818 

 
           
             62  
             2245  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7472734CB1  
             
           
            62 

cccttggaac agtaggatgt tggtgatgca aaagtcaatg tttaaactca acattccact     60 

ttcctttaac taagaatagt ttttattaac ttttagtaaa actcagtcct agtccaaaaa    120 

aagccctgct ctctgatctt tgtacaagaa catcataaag caattcactt tggattttct    180 

aatatcccat ttctgagaag aatggcagac tattgaacag gtgtatttta ggtcacgtgg    240 

ggactgcatc cacctgaaaa tccaccgttg acttatcagg aaactcagag atcaggatct    300 

ttcacagagt agtcttttaa gaagattcag ttgtcaacag ctagcagtct ctttgccaaa    360 

taattatatc tgtgacttct gaaactattt ggctgcctaa agttaaagga cttggggaaa    420 

gtccctccac tgctcttctg cagtagtgtc acaccactca gtgcagggcc caccaagaag    480 

aaagcagtgt caggatccac atggcactat ggtaactttg tgaaagggga cattttctcc    540 

ctctgaactt ctcttcataa agtcattgtg cttcctcttg gggatcacct gttcagtctc    600 

aatgggcttt gatgtgctcc tggatcaagt gggtggcatg gggagattcc agatttgtct    660 

gatagctttc ttttgcatca ccaacatcct actgttccct aatattgtgt tggagaactt    720 

cactgcattc acccctagtc atcgctgctg ggtccccctc ctggacaatg acactgtgtc    780 

tgacaatgat accgggaccc tcagcaagga tgacctcctg agaatctcca tcccactgga    840 

ctcaaacctg aggccacaga agtgtcagcg ctttatccat ccccagtggc agctccttca    900 

cctgaacggg accttcccca acacaaatga gccagacacg gagccctgtg tggatggctg    960 

ggtgtacgac agaagctctt tcctctccac catcgtgact gagtgggacc tggtatgtga   1020 

atctcagtca ctaaaatcaa tggttcaatc cctatttatg gctgggtcac ttctgggagg   1080 

tctaatatat ggccatcttt cagacaggtt tgggagaaag ttcgtgctca gatggtctta   1140 

cctccagctc gccattgtag gcacctgtgc ggcctttgct cccaccatcc tcgtatactg   1200 

ctccctgcgc ttcttggctg gggctgctac atttagcatc attgtaaata ctgttttgtt   1260 

aattgtagag tggataactc accaattctg tgccatggca ttgacattga cactttgtgc   1320 

tgctagtatt ggacatataa ccctgggaag cctggctttt gtcattcgag accagtgcat   1380 

cctccagttg gtgatgtctg caccatgctt tgtcttcttt ctgttctcaa ggtggctggc   1440 

agagtctgct cggtggctca ttatcaacaa caaaccagaa gagggcttaa aggaacttag   1500 

aaaagctgca cacaggaatg gaatgaagaa tgctgaagac atcctaacca tggaggtttt   1560 

gaaatccacc atgaagcaag aactggaggc agcacagaaa aagcattctc tttgtgaatt   1620 

gctccgcata cccaacatat gtaaaagaat ctgtttcctg tcctttgtga gatttgcaag   1680 

taccatccct ttttggggcc ttactttgca cctccagcat ctgggaaaca atgttttcct   1740 

gttgcagact ctctttggtg cagtcaccct cctggccaat tgtgttgcac cttgggcact   1800 

gaatcacatg agccgtcgac taagccagat gcttctcatg ttcctactgg caacctgcct   1860 

tctggccatc atatttgtgc ctcaagaaat gcagaccctg cgtgtggttt tggcaaccct   1920 

gggtgtggga gctgcttctc ttggcattac ctgttctact gcccaagaaa atgaactaat   1980 

tccttccata atcaggggaa gagctactgg aatcactgga aactttgcta atattggggg   2040 

agccctggct tccctcatga tgatcctaag catatattct cgacccctgc cctggatcat   2100 

ctatggagtc tttgccatcc tctctggcct tgttgtcctc ctccttcctg aaaccaggaa   2160 

ccagcctctt cttgacagca tccaggatgt ggaaaatgag ggagtaaata gcctagctgc   2220 

ccctcagagg agctctgtgc tatag                                         2245 

 
           
             63  
             3196  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7473473CB1  
             
           
            63 

gcggcggccg ggggagcgct actaccatga actgcctggt cctcctcccc agagctgctc     60 

atccgggtcg ggctggagac acagtcaggg gaccccgtcg ccgccgccgc gccccctctt    120 

ctttcggctc aatcttctct tccacctttt cctcctcttc ctccaccttc tttgcctgca    180 

tccccccctc ccccgccgcg gatcctggcc gctgctctcc agacccagga tgccgggggg    240 

caagagaggg ctggtggcac cgcagaacac atttttggag aacatcgtca ggcgctccag    300 

tgaatcaagt ttcttactgg gaaatgccca gattgtggat tggcctgtag tttatagtaa    360 

tgacggtttt tgtaaactct ctggatatca tcgagctgac gtcatgcaga aaagcagcac    420 

ttgcagtttt atgtatgggg aattgactga caagaagacc attgagaaag tcaggcaaac    480 

ttttgacaac tacgaatcaa actgctttga agttcttctg tacaagaaaa acagaacccc    540 

tgtttggttt tatatgcaaa ttgcaccaat aagaaatgaa catgaaaagg tggtcttgtt    600 

cctgtgtact ttcaaggata ttacgttgtt caaacagcca atagaggatg attcaacaaa    660 

aggttggacg aaatttgccc gattgacacg ggctttgaca aatagccgaa gtgttttgca    720 

gcagctcacg ccaatgaata aaacagaggt ggtccataaa cattcaagac tagctgaagt    780 

tcttcagctg ggatcagata tccttcctca gtataaacaa gaagcgccaa agacgccacc    840 

acacattatt ttacattatt gtgcttttaa aactacttgg gattgggtga ttttaattct    900 

taccttctac accgccatta tggttcctta taatgtttcc ttcaaaacaa agcagaacaa    960 

catagcctgg ctggtactgg atagtgtggt ggacgttatt tttctggttg acatcgtttt   1020 

aaattttcac acgactttcg tggggcccgg tggagaggtc atttctgacc ctaagctcat   1080 

aaggatgaac tatctgaaaa cttggtttgt gatcgatctg ctgtcttgtt taccttatga   1140 

catcatcaat gcctttgaaa atgtggatga gggaatcagc agtctcttca gttctttaaa   1200 

agtggtgcgt ctcttacgac tgggccgtgt ggctaggaaa ctggaccatt acctagaata   1260 

tggagcagca gtcctcgtgc tcctggtgtg tgtgtttgga ctggtggccc actggctggc   1320 

ctgcatatgg tatagcatcg gagactacga ggtcattgat gaagtcacta acaccatcca   1380 

aatagacagt tggctctacc agctggcttt gagcattggg actccatatc gctacaatac   1440 

cagtgctggg atatgggaag gaggacccag caaggattca ttgtacgtgt cctctctcta   1500 

ctttaccatg acaagcctta caaccatagg atttggaaac atagctccta ccacagatgt   1560 

ggagaagatg ttttcggtgg ctatgatgat ggttggcgct cttctttatg caactatttt   1620 

tggaaatgtt acaacaattt tccagcaaat gtatgccaac accaaccgat accatgagat   1680 

gctgaataat gtacgggact tcctaaaact ctatcaggtc ccaaaaggcc ttagtgagcg   1740 

agtcatggat tatattgtct caacatggtc catgtcaaaa ggcattgata cagaaaaggt   1800 

cctctccatc tgtcccaagg acatgagagc tgatatctgt gttcatctaa accggaaggt   1860 

ttttaatgaa catcctgctt ttcgattggc cagcgatggg tgtctgcgcg ccttggcggt   1920 

agagttccaa accattcact gtgctcccgg ggacctcatt taccatgctg gagaaagtgt   1980 

ggatgccctc tgctttgtgg tgtcaggatc cttggaagtc atccaggatg atgaggtggt   2040 

ggctatttta gggaagggtg atgtatttgg agacatcttc tggaaggaaa ccacccttgc   2100 

ccatgcatgt gcgaacgtcc gggcactgac gtactgtgac ctacacatca tcaagcggga   2160 

agccttgctc aaagtcctgg acttttatac agcttttgca aactccttct caaggaatct   2220 

cactcttact tgcaatctga ggaaacggat catctttcgt aagatcagtg atgtgaagaa   2280 

agaggaggag gagcgcctcc ggcagaagaa tgaggtgacc ctcagcattc ccgtggacca   2340 

cccagtcaga aagctcttcc agaagttcaa gcagcagaag gagctgcgga atcagggctc   2400 

aacacagggt gaccctgaga ggaaccaact ccaggtagag agccgctcct tacagaatgg   2460 

agcctccatc accggaacca gcgtggtgac tgtgtcacag attactccca ttcagacgtc   2520 

tctggcctat gtgaaaacca gtgaatccct taagcagaac aaccgtgatg ccatggaact   2580 

caagcccaac ggcggtgctg accaaaaatg tctcaaagtc aacagcccaa taagaatgaa   2640 

gaatggaaat ggaaaagggt ggctgcgact caagaataat atgggagccc atgaggagaa   2700 

aaaggaagac tggaataatg tcactaaagc tgagtcaatg gggctattgt ctgaggaccc   2760 

caagagcagt gattcagaga acagtgtgac caaaaaccca ctaagaaaaa cagattcttg   2820 

tgacagtgga attacaaaaa gtgaccttcg tttggataag gctggggagg cccgaagtcc   2880 

gctagagcac agtcccatcc aggctgatgc caagcacccc ttttatccca tccccgagca   2940 

ggccttacag accacactgc aggaagtcaa acacgaactc aaagaggaca tccagctgct   3000 

cagctgcaga atgactgccc tagaaaagca ggtggcagaa attttaaaaa tactgtcgga   3060 

aaaaagcgta ccccaggcct catctcccaa atcccaaatg ccactccaag taccccccca   3120 

gataccatgt caggatattt ttagtgtctc aaggcctgaa tcacctgaat ctgacaaaga   3180 

tgaaatccac ttttaa                                                   3196 

 
           
             64  
             1602  
             DNA  
             Homo sapiens  
             
               misc_feature  
               Incyte ID No 7477725CB1  
             
           
            64 

atggcctttg aggagctctt gagtcaagtt ggaggccttg ggagatttca gatgcttcat     60 

ctggttttta ttcttccctc tctcatgtta ttaatccctc atatactgct agagaacttt    120 

gctgcagcca ttcctggtca tcgttgctgg gtccacatgc tggacaataa tactggatct    180 

ggtaatgaaa ctggaatcct cagtgaagat gccctcttga gaatctctat cccactagac    240 

tcaaatctga ggccagagaa gtgtcgtcgc tttgtccatc cccagtggca gcttcttcac    300 

ctgaatggga ctatccacag cacaagtgag gcagacacag aaccctgtgt ggatggctgg    360 

gtatatgatc aaagctactt cccttcgacc attgtgacta agtgggacct ggtatgtgat    420 

tatcagtcac tgaaatcagt ggttcaattc ctacttctga ctggaatgct ggtgggaggc    480 

atcataggtg gccatgtctc agacaggttt gggcgaagat ttattctcag atggtgtttg    540 

ctccagcttg ccattactga cacctgcgct gccttcgctc ccaccttccc tgtttactgt    600 

gtactacgct tcttggcagg tttttcttcc atgatcatta tatcaaataa ttctttgccc    660 

attactgagt ggataaggcc caactctaaa gccctggtag taatattgtc atctggtgcc    720 

cttagtattg gacagataat cctgggaggc ttggcttatg tcttccgaga ctggcaaacc    780 

ctgcacgtgg tggcgtctgt acctttcttt gtcttctttc ttctttcaag gtggctggtg    840 

gaatctgctc ggtggttgat aatcaccaat aaactagatg agggcttaaa ggcacttaga    900 

aaagttgcac gcacaaatgg aataaagaat gctgaagaaa ccctgaacat agaggttgta    960 

agatccacca tgcaggagga gctggatgca gcacagacca aaactactgt gtgtgacttg   1020 

ttccgcaacc ccagtatgcg taaaaggatc tgtatcctgg tatttttgag atttgcaaac   1080 

acaatacctt tttatggtac catggtcaat cttcagcatg tggggagcaa cattttcctg   1140 

ttgcaggtac tttatggagc tgtcgctctc atagttcgat gtcttgctct tttgacacta   1200 

aatcatatgg gccgtcgaat aagccagata ttgttcatgt tcctggtggg cctttccatt   1260 

ttggccaaca cgtttgtgcc caaagaaatg cagaccctgc gtgtggcttt ggcatgtctg   1320 

ggaatcggct gttctgctgc tactttttcc agtgttgctg ttcacttcat tgaactcatc   1380 

cccactgttc tcagggcaag agcttcagga atagatttaa cggctagtag gattggagca   1440 

gcactggctc ccctcttgat gaccttaacg gtatttttta ccactttgcc atggatcatt   1500 

tatggaatct tccccatcat tggtggcctt attgtcttcc tcctaccaga aaccaagaat   1560 

ctgcctttgc ctgacaccat caaggatgtg gaaaatcagt ga                      1602