Patent Publication Number: US-6217872-B1

Title: Non-A, non-B hepatitis virus genomic cDNA and antigen polypeptide

Description:
This application is a division of application Ser. No. 08/904,686, filed Aug. 1, 1997 now U.S. Pat. No. 5,998,130, which is a division of application Ser. No. 08/324,977 filed Oct. 18, 1994 now U.S. Pat. No. 5,747,339, which was a continuation of application Ser. No. 08/099,706, filed Jul. 30, 1993, now abandoned, which was a division of application Ser. No. 07/769,996 filed Oct. 2, 1991, now abandoned, which was a continuation-in-part of application Ser. No. 07/635,451, filed Dec. 28, 1990 now abandoned. 
    
    
     BACKGROUND OF THE INVENTION 
     1. Field of the Invention 
     The present invention relates to a non-A, non-B hepatitis virus genomic CDNA and a non-A, non-B hepatitis virus antigen polypeptide. More particularly, the present invention is concerned with a non-A, non-B hepatitis virus genomic cDNA which is useful for producing a non-A, non-B hepatitis virus antigen polypeptide and with a non-A, non-B hepatitis antigen polypeptide which is an expression product thereof. The non-A, non-B hepatitis virus genomic cDNA of the present invention is also useful for genetically diagnosing non-A, non-B hepatitis. Further, the non-A, non-B hepatitis antigen polypeptide of the present invention is useful for producing a vaccine for non-A, non-B hepatitis, an immunoglobulin, a polyclonal or monoclonal antibody, an immunological diagnostic reagent, an agent for screening blood for transfusion and an agent for use in affinity chromatography for removing non-A, non-B hepatitis virus from blood for transfusion. 
     2. Discussion of Related Art 
     Definition of non-A, non-B hepatitis virus: 
     The viral hepatitis is a liver disease caused by the infection of a hepatitis virus. Heretofore, hepatitis A virus, hepatitis B virus and hepatitis D (delta) virus have been isolated and identified. The hepatitis D virus (delta-hepatitis virus) is a deficient virus which cannot multiply by itself and requires for its multiplication the co-presence of hepatitis B virus as a helper virus. Therefore, the hepatitis D virus is present only in a patient having hepatitis B. In 1974, it was reported that there were many patients having hepatitis caused by a factor other than the infection with either hepatitis A virus or hepatitis B virus. Such a hepatitis was named “non-A, non-B hepatitis”, and researches on the non-A, non-B hepatitis virus have been made extensively and intensively throughout the world. Heretofore, it has been found that a plurality of types of non-A, non-B hepatitis viruses exist. Results of the researches up to now show that the non-A, non-B hepatitis virus is classified into two types according to the infection route, that is, an epidemic hepatitis virus, namely an enterically-transmitted non-A, non-B hepatitis virus, which is spread through water and food; and a blood transmitted non-A, non-B hepatitis virus which is spread through blood by transfusion, etc. Of the non-A, non-B hepatitis viruses, only an enterically-transmitted non-A, non-B hepatitis virus which spreads over the areas of Africa, India and Southeast Asia has been virologically identified, but the blood-transmitted non-A, non-B hepatitis virus has not yet been identified. 
     Hereinbelow, the blood-transmitted non-A, non-B hepatitis is often referred to simply as “NANB hepatitis”, and the blood-transmitted non-A, non-B hepatitis virus is often referred to simply as “NANBV”. Current situation of the studies on NANB hepatitis and problems: 
     With respect to the epidemiology, clinical examination, diagnosis, treatment and prevention of the NANB hepatitis, virological studies have been made in the world by the comparison of NANBV with the other hepatitis viruses, based on the knowledge of diagnostics, histopathology, immunology, molecular biology and the like [“Japan Medical Journal”, No. 3320, pp.3-10, 1987; “Igaku-no Ayumi (Progress of medicine)”, 151(13), pp.735-923, 1989; “Kan Tan Sui (Liver; Gallbladder, Pancreas)”, 21(1), pp.5-113, 1990; “Jikken Igaku (Experimental Medicine)”, 8(3), pp.201-233, 1990]. With respect to the NANB hepatitis, the following findings have been reported. 
     (1) Epidemiology: In Japan, according to the estimation by the Ministry of Health and Welfare, about 60% of chronic hepatitis patients (namely about 720 thousand patients), about 40% of hepatocirrhosis patients (namely about 100 thousand patients) and about 40% of liver cancer patients (namely about 7 thousand patients) are patients having NANB hepatitis. Further, the mortality attributed to the above-mentioned NANB hepatitis reaches 16 thousand per year. In U.S.A., the number of post-transfusion hepatitis patients reaches 150 to 300 thousand per year and 90% of the post-transfusion hepatitis patients are patients having NANB hepatitis. Further, it is considered that 1 to 6% of the blood donors are NANBV carriers. Further, it is estimated that in the other countries also, the incidence of NANB hepatitis and the ratio of the NANBV carrier are equal to or higher than those in U.S.A. and Japan. Therefore, prevention, early diagnosis and early treatment of the NANB hepatitis are of global importance. 
     (2) Virology: The NANBV heretofore reported comprises an envelope and assumes a viral particle having a spherical shape of about 50 nm in diameter. The taxonomic observations suggest that the known NANBV is a virus similar to a togavirus or a flavivirus, or a virus of new type different from the togavirus or flavivirus. Further, the results of pathological observations of the cytoplasm of hepatocytes of a plurality of chimpanzees injected with serum of a patient having NANBV hepatitis show that the formation of a tubular structure occurs in the cytoplasm of a hepatocyte of some of the chimpanzees, but does not occur in the cytoplasm of a hepatocyte of the other chimpanzees, and that an intranuclear particle is formed in the cytoplasm of a hepatocyte of some of the chimpanzees. These results and the results of the epidemiological observations, tests on the presence or absence of the chloroform sensitivity and immunological diagnosis suggest that a plurality of types of NANBV-sexist (see, for example, “Science”, Vol. 205, pp.197-200, 1979, “Journal of Infectious Disease”, Vol. 148, pp.254-265, 1983, and “Biseibutsu” (Microorganism), Vol. 5, No. 5, pp.463-475, 1989). The amount of the NANBV present in the blood of a patient having NANB hepatitis is extremely small as compared to either the amount of a hepatitis A virus present in the feces of a patient having hepatitis A or the amount of a hepatitis B virus present in the blood of a patient having hepatitis B. For example, the amount of hepatitis B virus in the blood of the patient is 10 8  to 10 9  per ml in terms of Chimpanzee Infectious dose (CID), whereas the amount of NANBV in the blood of the patient is only 10 4  to 10 5  per ml in terms of CID (Bradley, D. W.: Research perspectives in post-transfusion non-A, non-B hepatitis, in “Infection, Immunity and Blood Transfusion”, edited by Dodd, R. Y. &amp; Barker, L. F., published by Alan R. Liss, Inc., New York (1985) pp.81-97). Further, it is known that except for human, there are no animals except chimpanzee that are sensitive to NANBV and that in the cytoplasm of the hepatocyte, a typical tubular structure is occasionally formed by NANBV infection. Since only chimpanzee can be used as an animal for experiment of the NANBV infection, a large number of chimpanzees are required to be used for the study of NANBV. However, the chimpanzee is not easily available and expensive. Therefore, the study of NANBV by, for example, experimental infection by NANBV, identification of NANBV and search for a useful marker for NANBV, is necessarily restricted and delayed. In order to solve these problems, various attempts have been made for the study of NANBV. For example, in an attempt, an NANBV genomic cDNA [(referred to as “hepatitis C virus (HCV)”] was cloned from blood plasma of chimpanzees suffering from NANB hepatitis (Science, Vol. 244, pp.359-362, 1989), and it was confirmed that the antigen (referred to as “C-100”) obtained by expressing the cDNA exhibited an antigen-antibody reaction with the antibody in the blood of an NANB hepatitis patient (Science, Vol. 244, pp.362-364, 1989). Further, in another attempt, a chimpanzee was not used and an NANBV genomic CDNA was cloned from the blood plasma of NANB hepatitis patients, and it was confirmed that the antigen obtained by expressing the CDNA exhibited an antigen-antibody reaction with the antibody in the serum of an NANB hepatitis patient (Gastroenterologia Japonica, Vol. 24, pp.540-544 and pp.545-548, 1989). 
     (3) Clinical observations: Hepatitis is generally classified either into epidemic hepatitis and sporadic hepatitis according to the number and frequency of the occurrences of hepatitis, or into acute hepatitis, fulminant hepatitis, subacute hepatitis, persistent hepatitis and chronic hepatitis according to the severeness and stage of the hepatitis patients. The latent period of the NANB hepatitis is 2 to 26 weeks. The symptom of NANB hepatitis in the early stage is mild as compared to that of hepatitis B. For example, a patient having NANB hepatitis only becomes feverish and complains of languor. Further, 70% of the patients have anicteric symptom. Therefore, the NANB hepatitis is frequently overlooked. However, the NANB hepatitis is very dangerous because the NANB hepatitis is likely to become chronic and, then, to progress to liver cirrhosis. Illustratively stated, 40 to 50% of the patients having NANB hepatitis whose serum exhibits an increased aminotransferase activity develop chronic hepatitis. 10 to 20% of the cases of chronic hepatitis suffer from liver cirrhosis. Further, 0.5 to 1% of blood recipients per year becomes liver cirrhosis patients without subjective symptoms. More seriously, the liver cirrhosis may further progress to liver cancer or hepatoma. Therefore, for preventing biohazard caused by blood transfusion and bleeding, eradication of the NANB hepatitis is a matter of global importance from the viewpoint of public health. 
     (4) Diagnosis: As mentioned above, the NANBV (blood-transmitted type) has not yet been identified and a viral marker, such as an NANBV antigen, which is useful for the diagnosis of NANB hepatitis has not been known. Therefore, diagnosis of NANB hepatitis has been conducted by examining the titer of the antibody in serum of a patient, which is specific for each of the known pathogenic viruses, such as hepatitis A virus, hepatitis B virus, cytomegalovirus, EB virus, varicella virus and herpes simplex virus, and diagnosing the patient whose serum is negative with respect to the antibody specific for any of the above-mentioned viruses, as having NANB hepatitis, or by performing a histopathological examination through a biopsy of the liver (“Disease of the Liver and biliary system”, 8th edition, S. Shenlock, pp. 326-333, 1989, Blackwell Scientific Publications). At the same time, another diagnosis method has also been used. For example, there have been used a method in which the activity of an enzyme in serum, such as GPT [glutamic-pyruvic transaminase, also known as “ALT” (alanine aminotransaminase)], GOT [glutamic-oxalo-acetic transaminase, also known as “AST” (aspartate aminotransferase)], and guanine deaminase (also known as “guanase”) is determined (“Kan Tan Sui (Liver, Gallbladder, Pancreas)”, Vol. 14, pp. 519-522, 1987). With respect to the GPT or GOT in serum mentioned above, a standard for the diagnosis of NANB hepatitis in which lasting and abnormally high activities of GPT and GOT are utilized as a criterion for the diagnosis of NANB hepatitis, is employed in Japan (“Journal of Blood Transfusion Society in Japan”, Vol. 31, No. 4, pp. 316-320, 1985; and “Nippon Rinsho”, Vol. 46, p. 2635-2638, 1988). Regarding the immunological diagnosis, in the present situation n which the isolation and identification of NANBV are difficult, an antigen-antibody reaction between an antigen obtained by expression of NANBV cDNA clone (which has been isolated using the techniques of genetic engineering and the knowledge of immunology) and the serum of an NANB hepatitis patient is used as a criterion. Examples of known antigens include an expression product of an NANBV cDNA prepared from the plasma of an NANB hepatitis patient (European Patent Application Publication No. 363025), an expression product of “HCV” cDNA prepared from the plasma of a chimpanzee having the symptoms of NANB hepatitis (European Patent Application publication No. 318216 and Japanese Patent Application Laid-Open Specification No. 2-500880), an expression product of an NANBV CDNA derived from the liver of an NANBV-infected chimpanzee (European Patent Application Publication No. 293274, Japanese Patent Publication Specification No. 64-2576 and Japanese Patent Application Laid-Open Specification No. 1-124387). As a method for determining the antigen-antibody reaction, RIA (radioimmunoassay) and EIA (enzyme immunoassay) are generally used. However, these expression products are different in antigenicity. The antigen which is an expression product of HCV cDNA (that is, the C-100 antigen mentioned above) can be some criterion or yardstick for the diagnosis of chronic hepatitis caused by the HCV infection. However, since the region in which the antigen (C-100) exhibits its antigenicity is limited (“Biseibutsu (Microorganism)”, Vol. 5, pp. 463-475, 1989; “Kan Tan Sui (Liver, Gallbladder, Pancreas)”, Vol. 20, pp. 47-51, 1990; and “Igaku-no Ayumi (Progress of Medicine)”, Vol. 151, p. 871, 1989), this antigen is unsatisfactory from the viewpoint of accurate diagnosis of NANB hepatitis and NANBV infection and from the viewpoint of accurate determination of the progress of a patient suffering from chronic hepatitis and acute hepatitis for treatment thereof. Therefore, it has been desired to obtain a reliable method for the diagnosis and prognosis of the NANB hepatitis. 
     (5) Therapy and Prevention: Recently, the usefulness of α- and β-interferons in the treatment of chronic NANB hepatitis have been reported (“Kan Tan Sui (Liver, Gallbladder, Panceras)” vol.20, pp. 59-64, 1990; “Igaku-no Ayumi (Progress of Medicine)”, vol. 151, pp. 871-876, 1989). However, a suitable dose of α- and β-interferons and a suitable period for administration thereof have not yet been established. 
     On the other hand, for prevention of NANB hepatitis, various vaccines are used in which the above-mentioned conventional expression products of NANBV cDNAs (European Patent Application Publication No. 363025) or HCV cDNAs (European Patent Application Publication No. 318216) are used as an antigen. However, as is apparent from the fact that the NANBV itself has not yet been isolated and identified before completion of the present invention, it has been impossible to specify an antigen useful for NANBV vaccines from the above-mentioned expression products each having a variety of antigenic determinants (epitopes) and determine the effectiveness and safety of such a specific antigen so that the antigen can be clinically used. Accordingly, there is no NANBV vaccine which can be advantageously put into practical use. 
     SUMMARY OF THE INVENTION 
     The present inventors have made extensive and intensive studies with a view toward solving the above-mentioned problems by developing a novel NANBV genomic cDNA. As a result, the present inventors have surprisingly succeeded in cloning an NANBV genomic cDNA, which not only has excellent reliability as compared to the known NANBV cDNA but also is larger in length than any known NANBV cDNAs and contains the entire region of the open reading frame of the NANBV genome, and expressing this NANBV cDNA to thereby obtain an NANBV antigen peptide which can reliably exhibit an antigen-antibody reaction specific for not only sera from patients having chronic NANB hepatitis but also sera from patients having acute NANB hepatitis. This success is attributed to a unique technique of the present inventors such that in order to obtain an authentic NANBV genome, NANBV RNAs are extracted directly from NANBV particles contained in whole blood of a patient having NANB hepatitis or a resected liver of a patient having NANB hepatitis and liver cancer in combination, without multiplying the NANBV in a chimpanzee having unknown factors which are considered to have rendered difficult the isolation of NANBV, although the amount of NANBV in the blood or resected liver is extremely small, that is, as small as about {fraction (1/10,000)} that of a hepatitis A virus or a hepatitis B virus, but with paying minute care in the operating procedure so that the NANBV and its genome do not undergo cleavage and/or decomposition by the action of body fluids or blood enzymes during the storage of fresh materials for NANBV genome. RNAs thus prepared from fresh human materials are then converted to double-stranded cDNA by means of a reverse transcriptase to obtain a cDNA library. In order to screen an NANBV genome from the CDNA library, the cDNAs are individually inserted in lambda gt11 phage vectors and then expressed on the phage plaques at high concentration, followed by screening of NANBV genomic cDNAs by repeatedly conducting enzyme immunoassay (EIA) in which both serum from a convalescent patient having acute NANB hepatitis and serum from a patient having chronic NANB hepatitis are used. Thus, safe production of the NANBV antigen polypeptide with high purity on a large scale at low cost without biohazard, has for the first time been realized by expressing the cDNA of the present invention by recombinant DNA techniques. Based on the above, the present invention has been completed. 
     Therefore, it is an object of the present invention to provide an NANB hepatitis virus genomic cDNA. 
     It is another object of the present invention to provide an NANB hepatitis virus antigen polypeptide which is useful as an active ingredient for a diagnostic reagent and a vaccine for NANB hepatitis. 
     It is still another object of the present invention to provide a method for producing an NANBV antigen polypeptide. 
     It is a further object of the present invention to provide a diagnostic reagent for NANB hepatitis. 
     It is still a further object of the present invention to provide a vaccine for NANB hepatitis. 
     The foregoing and other objects, features and advantages of the present invention will be apparent from the following detailed description, appended claims taken in connection with the accompanying drawings. 
    
    
     BRIEF DESCRIPTION OF THE DRAWINGS 
     In the Drawings: 
     FIG.  1 ( 1 ) and FIG.  1 ( 2 ) are diagrams showing the relationships between the CDNA clones of the NANBV gene of the present invention, shown relative to the entire region of the NANBV genome; 
     FIG.  2 ( 1 ) through FIG.  2 ( 16 ) show the nucleotide sequence of the entire region of the NANBV genomic CDNA according to the present invention (SEQ ID NO: 1) and the amino acid sequence (SEQ ID NO: 2) coded for by the nucleotide sequence; and 
     FIG. 3 is a diagram showing the hydrophobicity profiles of both of the NANBV of the present invention and the Japanese encephalitis virus (JEV), in which the hydrophobicity index of the NANBV is compared with that of the JEV. 
    
    
     DETAILED DESCRIPTION OF THE INVENTION 
     Essentially, according to the present invention, there is provided an isolated deoxyribonucleic acid comprising at least one nucleotide sequence selected from the group consisting of a nucleotide sequence comprising at least part of the non-A, non-B hepatitis virus entire nucleotide sequence (SEQ ID NO: 1) from the 1st to 9416th nucleotides shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ) hereof and a nucleotide sequence complementary to said nucleotide sequence, or comprising at least one nucleotide sequence obtained by substituting at least one nucleotide of said nucleotide sequence in accordance with the degeneracy of the genetic code. 
     In another aspect of the present invention, there is provided an isolated antigen polypeptide comprising at least one amino acid sequence comprising at least part of an amino acid sequence coded for by a deoxyribonucleic acid comprising a coding region from the 333rd to 9362nd nucleotides of the non-A, non-B hepatitis virus nucleotide sequence (SEQ ID NO: 1) shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ) hereof. 
     In the present invention, unless otherwise specified, the left end and right end of the sequence of deoxyribonucleotides are the 5′ end and 3′ end, respectively. Further, unless otherwise specified, the left end and right end of the amino acid sequences of peptides are the N-terminus and C-terminus, respectively. 
     The NANBV genomic cDNA of the present invention and the NANBV antigen polypeptide as an expression product thereof can be prepared and identified in accordance with the following steps (I) to (VII). 
     Step (I): Selection and collection of a material for extracting an NANBV RNA. 
     As a material for extracting the NANBV RNA, there may be used, for example, blood, lymph, ascites and hepatocyte of an NANBV carrier, or of a human or a chimpanzee suffering from NANB hepatitis, and hepatocyte of a patient suffering from NANB hepatitis and liver cancer or hepatoma in combination. Since the materials derived from a chimpanzee may contain NANBV in a relatively small amount as compared to the materials derived from a human and a chimpanzee has unknown factors which are considered to have rendered difficult the isolation of NANBV, the use of the materials derived from a human is preferred. Of blood, lymph, ascites and hepatocytes from a human, blood can most easily be obtained in a large amount. For example, blood which is not acceptable for use as blood for transfusion is available from a blood bank in a large amount. Such blood can advantageously be used as a material for extracting an NANBV RNA. When blood is used as a material, blood is separated into plasma and erythrocytes. The thus obtained plasma is examined to determine whether or not the plasma is negative to the surface antigen of hepatitis B virus (WHO expert committee on viral hepatitis: Advances in viral hepatitis, WHO Technical Report Series, 602, 28-33, 1977) and negative to a genomic DNA of hepatitis B virus (Brechot, C., Hadchouel, M., Scotto, J., Degos, F., Charnay, P., Trepo, C., Tiollais, P.: Detection of hepatitis B virus DNA in liver and serum: a direct appraisal of the chronic carrier state. Lancet 2: 765-768, 1981). Further, the plasma is examined with respect to the activities of enzymes, such as GPT (Wroblewski, F. &amp; LaDue, J. S.: Serum glutamic-pyruvic transaminase in cardiac and hepatic disease, Proc. Soc. Exp. Biol. Med., 91, 569, 1956), GOT, guanase and the like, which are employed as the criterion for the diagnosis of NANB hepatitis. The above-mentioned procedures of the separation of blood into plasma and erythrocytes and the examination of the plasma are conducted with respect to blood of different lots. The plasma which is negative to both surface antigen and genomic cDNA of hepatitis B virus and exhibits extremely high activities of the above-mentioned enzymes, for example, a GPT activity of 35 IU/ml or more, is pooled. 
     The number of the NANB hepatitis virus particles in blood is extremely small as compared to that of the hepatitis B virus particles as mentioned hereinbefore. From the results of the infection experiment, the number of the NANB hepatitis virus particles in blood is estimated to be about {fraction (1/10,000)} of the number of the hepatitis B virus particles (Bradley, D. W., (1985): Research perspectives in post-transfusion non-A, non-B hepatitis, in “Infection, Immunity and Blood Transfusion”, edited by Dodd, R. Y. &amp; Barker, L. F., published by Alan R. Liss, Inc., New York, pp. 81-97). Therefore, for the extraction of the RNA, it is preferred to use blood in a large amount, for example, in an amount as large as about 3 to 10 liters. Fresh whole blood to be used as a material for extracting an NANB RNA from NANBV particles is stored at 1 to 5° C. in order to prevent NANBV and its gene from being denatured and to prevent its gene from being cleaved or decomposed by the action of an enzyme. It is also desirable to complete the preparation of NANBV RNAs by Step (II) within 48 to 72 hours from the collection of the fresh whole blood. When a hepatocyte is used as a material, about 1 to 3 g of a non-cancerous or a cancerous portion of a liver tissue resected from a patient having hepatoma or liver cancer which is a complication of a chronic NANB hepatitis may advantageously be used. Hepatocyte to be used as a material is stored in a frozen state at −70° C. 
     Step (II): Preparation of the NANBV RNA 
     From the material obtained in Step (I), the RNA may be extracted and purified by conventional methods. For example, when fresh whole blood is used as the material, about 2 to 10 liters of fresh whole blood is subjected to low-speed centrifugation to collect a plasma fraction as a supernatant. The virus fraction is obtained from the plasma through purification for use in the subsequent procedure for the extraction and purification of the RNA. 
     On the-other hand, when hepatocyte is used as a material for extracting the NANBV RNA, about 5 to 30-fold volume of a diluent containing ribonuclease inhibitor is added to the liver tissue. Then, according to the conventional method using a homogenizer and the like, the liver tissue is crushed or disrupted to obtain a homogenate of hepatocyte. As a diluent, 10 to 150 mM of a conventional buffer may be used. Then, the homogenate is subjected to low-speed centrifugation to collect a supernatant. The collected supernatant is used as an original solution for the extraction and purification of the NANBV RNA. The extraction and purification of the NANBV RNA may be conducted by the conventional method, for example, an extraction method in which a mixture of a ribonuclease inhibitor, such as heparin, diethyl pyrocarbonate and guanidine thiocyanate, with a surfactant, a chelating agent, or a reducing agent capable of enhancing the denaturation of a protein, is used; a method in which fractionation is conducted by density gradient centrifugation using sucrose, cesium chloride, cesium trichloroacetate, Ficoll (Pharmacia Fine Chemicals AB, Sweden) or the like as a solute of a gradient; a method in which separation is conducted by affinity column utilizing the 3′-terminal poly A chain which an mRNA specifically has; a separation method in which an mRNA-bonded polysome is obtained by the immunoprecipitation using an antibody specific for a protein synthesized on the polysome; a phenol extraction method based on a principle of two-phase separation; a precipitation method by the use of a polyethylene glycol, a dextran sulfate, an alcohol or the like. The above-mentioned methods may be used individually or in combination. The above-mentioned procedure for extracting and purifying the NANBV RNA may preferably be conducted at pH 3 to 10 in order to prevent the irreversible denaturation of the RNA. 
     Step (III): Preparation of a double-stranded cDNA from the NANBV RNA 
     Using the above-obtained NANBV RNA as a template, a cDNA may be prepared by a customary method. That is, using an oligodeoxythymidine and a random hexanucleotide primer as primers and using a reverse transcriptase, a cDNA complementary to the NANBV RNA is synthesized using the NANBV RNA as a template to obtain a double-strand comprising the cDNA and the NANBV RNA which are complementarily bonded to each other. Then, the thus obtained double-strand is reacted with ribonuclease H so that the NANBV RNA is decomposed and removed from the cDNA. Thus, a single-stranded cDNA is obtained. Using the obtained single-stranded cDNA as a template, a double-stranded cDNA is synthesized by means of a DNA synthase. The double-stranded cDNA synthesis may easily be conducted using a commercially available kit for cDNA synthesis, for example, cDNA Synthesis System Plus® (manufactured and sold by Amersham, England), cDNA System Kit® (manufactured and sold by Pharmacia LKB, Sweden), cDNA Synthesis Kit® (manufactured and sold by Boehringer Mannheim GmbH, West Germany), and the like. When the quantity of the synthesized cDNA is small, the cDNA can be amplified using a conventional method, such as PCR (polymerase chain reaction) method (“PCR Technology”, edited by H. A. Erlich, published by Stockton Press, 1989) using a PCR kit, such as AmpliTaq (manufactured and sold by Perkin Elmer Cetus, U.S.A.). 
     Step (IV): Preparation of a CDNA library 
     Using the cDNA prepared in Step (III), a cDNA library is prepared by a customary method. That is, the cDNA prepared in Step (III) is cut into fragments having different lengths and the resultant various cDNA fragments are individually ligated to replicable cloning vectors, to thereby obtain a CDNA library. As a replicable cloning vector, any known or commercially available vectors, such as phage genes, cosmids, plasmids and animal virus genes may be used. When a phage gene or a cosmid is used as a replicable vector, in order to attain high stability and high transforming ability of the vector after each of the cDNA fragments has been individually inserted therein, the in vitro packaging of each of the cDNA-inserted vectors is conducted by a customary method. Thus, the cDNA-inserted vectors are obtained in the form of a recombinant phage particle. The obtained phage particles are used as a cDNA library for cDNA cloning. On the other hand, when a plasmid is used as a replicable vector, the above-mentioned cDNA fragments are individually inserted in the plasmid vectors and the resultant cDNA-inserted vectors are then individually introduced into host cells, such as cells of  Escherichia coli, Bacillus subtilis , yeast or the like, according to a customary method. The thus obtained transformants are used as a cDNA library for CDNA cloning. Further, when the animal virus gene is used as a replicable vector, the above-mentioned CDNA fragments are individually inserted in the virus gene vectors and the resultant recombinant viruses are then individually transfected into sensitive animal cells according to a standard method and multiplied in the cells. In the case of the recombinant virus, the obtained recombinant viruses as such are used as a CDNA library. 
     The preparation of the cDNA library may easily be conducted using a commercially available kit, for example; a cDNA cloning system lambda gt10 and lambda gt11 (manufactured and sold by Amersham, England; BRL Inc., U.S.A.; and Stratagene Inc., U.S.A.), an in vitro packaging system (manufactured and sold by Amersham, England; BRL Inc., U.S.A.; and Stratagene Inc., U.S.A.) and the like. 
     Step (V): Cloning of a cDNA containing an NANBV gene from the cDNA library 
     In this step, a CDNA clone containing an NANBV gene is obtained. When the cDNA library is comprised of transformants, the transformants are cultured on a standard agar medium to form colonies. On the other hand, when the CDNA library is comprised of recombinant phage particles or recombinant viruses, these phage particles or recombinant viruses are used to infect known sensitive host cells, such as  Escherichia coli, Bacillus subtilis , yeast, animal cell culture and the like, and cultured to form a plaque, or to multiply the infected cells. The above-obtained transformant colonies, plaques or infected cells are subjected to immunoassay by at least one of the standard methods individually using serum from a convalescent patient having acute NANB hepatitis, serum from a patient having chronic NANB hepatitis, and serum from chimpanzee infected with an NANBV irrespective of whether or not the NANBV is of the type which causes a tubular structure to be formed in the cytoplasm of the hepatocyte of the chimpanzee, so that colonies, plaques or infected cells which have produced an NANBV antigen specifically reacted with at least one of the above-mentioned sera are selected and isolated. For the strict selection of the colonies, plaques and infected cells, it is preferred that the above procedure be repeated. From each of the thus selected and isolated colonies, plaques or the infected cells, a cDNA clone containing an NANBV gene is isolated according to a standard method described in T. Maniatis et al., Molecular Cloning, A Laboratory Manual, published by Cold Spring Harbor Laboratory, U.S.A., pp. 309-433 (1982). The immunoassay may be conducted by, for example, an enzyme-labeled antibody technique in which an antibody labeled with an enzyme, such as peroxidase and alkaline phosphatase is used; and a fluorescent antibody technique in which an antibody labeled with fluorescein isothiocyanate, europium or the like is used. It is preferred that the immunoassay by the above-mentioned technique be conducted by an indirect method because with the indirect method, high sensitivity immunoassay can be attained even by the use of an extremely small amount of serum from a patient. As a primary antibody to be used in the indirect method, serum from a patient having NANB hepatitis or serum from a chimpanzee having NANB hepatitis may preferably be employed because these sera contain an antibody specific for an NANBV antigen in relatively large amount. As a secondary antibody to be used in the indirect method, a commercially. available anti-human Ig (immunoglobulin) antibody labeled with an enzyme, a fluorescent substance or the like may be used. 
     A specimen to be subjected to immunoassay may be prepared according to a conventional method, for example, a blotting method in which nucleic acids and proteins of the colonies, plaques and infected cells are adsorbed on a filter membrane, a method in which a microplate or a slide glass for microscopy is used, or the like. When the blotting method is used in combination with an indirect, enzyme-labeled antibody technique, the selection of the intended colonies, plaques or infected cells from an extremely large number of the original colonies, original plaques or original infected cells can be conducted easily and promptly. In this case, blotting is conducted by contacting a commercially available filter made of nitrocellulose, cellulose acetate, nylon or the like, with the colonies, plaques or infected cells. 
     The above-obtained cDNA clone is a part of the NANBV gene. Therefore, in order to obtain cDNA clones covering the entire region of the NANBV gene, it is requisite to extend the cNDA clone by a method in which CDNA fragments adjacent to the cDNA clone are isolated by using 3′- and 5′- terminals of the cDNA clone as a probe. In this case, the technique which is known as “gene walking” (also known as “genomic walking” or “chromosome walking”) may be employed (“DNA cloning volume III”, edited by D. M. Glover, pp.37-39, IRL Press, 1987; “Molecular Cloning—a laboratory manual” 2nd edit., T. Maniatis et al, 3.21-3.23, 1989). By the repetition of the cloning procedure and the gene walking, the entire region of the NANBV gene can be obtained in the form of cDNA clones. 
     In this step, it is preferred to determine the nucleotide sequence of each of the obtained CDNA clones. The determination of the nucleotide sequence of the cDNA clone may generally be conducted according to a conventional method, for example, the Maxam-Gilbert method, the dideoxy chain termination method (Analytical Biochemistry, 152, 232-238, 1986), or the like. 
     Based on the determined nucleotide sequence, the amino acid sequence can be determined. The sequencing of the amino acids is conducted from the location of the initiation codon (ATG on the cDNA or AUG on the MRNA). Important portions of the amino acid sequence, for example, a hydrophilic portion, which is considered to constitute an epitope, can be identified by synthesizing a peptide corresponding to each hydrophilic portion and purifying the synthesized polypeptide by high performance liquid chromatography (HPLC), followed by subjecting the purified peptide to enzyme immunoasssy (EIA) or radioimmunoassay (RIA). 
     The cDNA clones are preferably classified into groups according to the respective properties of the NANBV antigen polypeptides coded for by the cDNA clones in order to distinguishing clones from one another. In this connection, the location of each cDNA clone on the restriction map of the NANBV gene can be used as a yardstick for the classification [see FIG.  1 ( 1 ) and FIG.  1 ( 2 )]. Further, it has been found that some of NANBVs have the ability to cause a tubular structure to be formed in the cytoplasm of a hepatocyte of a chimpanzee, and some of NANBV do not have such ability (Science, 205, pp. 197-200, 1979). Therefore, the cDNA clones may be identified and classified by examining the serological reactivity of each cDNA clone with serum from a chimpanzee infected with an NANBV of the type which causes a tubular structure to be formed in the cytoplasm of the hepatocyte of the chimpanzee and with serum from a chimpanzee infected with an NANBV of the type which does not cause a tubular structure to be formed in the cytoplasm of the hepacyte of the chimpanzee. The examination of this serological reactivity may be conducted by immunoassay mentioned above. 
     In the present invention, as shown in FIGS.  1 ( 1 ) and  1 ( 2 ), the cDNA clones of the NANBV gene of the present invention are identified with prefix “BK”. 
     FIG.  1 ( 1 ) is a diagram showing the relationships between the cDNA clones of the NANBV gene of the present invention, shown relative to the entire region of the NANBV gene, and FIG.  1 ( 2 ) is a diagram showing the relationships between the CDNA clones obtained by gene walking, shown relative to the entire region of the NANBV gene. 
     These BK NANBV cDNA clones include, for example,  Escherichia coli  BK 108 (deposited at Fermentation Research Institute, Japan under the accession number FERM BP-2971),  Escherichia coli  BK 129 (deposited at Fermentation Research Institute, Japan under the accession number FERM BP-2972),  Escherichia coli  BK 138 (deposited at Fermentation Research Institute, Japan under the accession number FERM BP-2973),  Escherichia coli  BK 153 (deposited at Fermentation Research Institute, Japan under the accession number FERM BP-2974),  Escherichia coli  BK 157,  Escherichia coli  BK 166 (deposited at Fermentation Research Institute, Japan under the accession number FERM BP-2975), and  Escherichia coli  BK 172 (deposited at Fermentation Research Institute, Japan under accession number FERM BP-2976). These seven BK NANBV cDNA clones are considered to cover at least the entire region of the open reading frame of the NANBV gene and probably the entire region of the NANBV gene. 
     The nucleotide sequence (SEQ ID NO: 1) of the entire region of the NANBV gene which is covered by the above-mentioned BK NANBV cDNA clones and the amino acid sequence (SEQ ID NO: 2) which is coded for by this nucleotide sequence are shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ). Based on the entire NANBV nucleotide sequence (SEQ ID NO: 1) and the entire NANBV amino acid sequence (SEQ ID NO: 2) shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ), various studies and observations can be made with respect to the homology of the nucleotide sequence and amino acid sequence of the NANBV gene to those of other virus genes, the hydrophobicity index (hydrophobicity/hydrophilicity profile), the structure of the NANBV gene, the regions of epitopes (antigenic determinants) and the like. 
     With respect to the homology, studies can be made by comparison of the nucleotide sequence and amino acid sequence of the NANBV gene with those of various viruses whose genes are well known (Japanese Patent Application Laid-Open specification No. 62-286930 and “Virology”, Vol. 161, pp. 497-510, 1987) and those of other viruses, such as bovine virus diarrhea-mucosal disease virus (“Virology”, Vol. 165, pp. 497-510, 1988), swine cholera virus (“Virology”, Vol. 171, pp. 555-567, 1989), tobacco vein mottling virus (“Nucleic Acid Research, Vol. 165, pp. 5417-5430, 1986), etc. 
     With respect to the analysis of the hydrophobicity index, studies can be made by techniques using, for example, a genetic information processing software, SDC-Genetyx (manufactured and sold by SDC Software Co., Ltd., Japan), Doolittle&#39;s program (Journal of Molecular Biology, Vol. 157, pp. 105-132, 1982) and the like. 
     FIG. 3 is a diagram showing the hydrophobic profiles of both of the NANBV of the present invention and the Japanese encephalitis virus (JEV), in which the respective hydrophobic indexes of both viruses are compared with each other. A significant similarity is found between the gene structure of the NANBV gene and that of the JEV gene. As shown in FIG. 3, the polypeptide of the NANBV of the present invention contains three structural proteins, namely, core protein (C), pre-matrix protein (PreM) that is further processed to matrix protein (M) and envelope protein (E), and seven nonstructural proteins, NS1, NS2a, NS2b, NS3, NS4a, NS4b and NS5. These proteins are, respectively, coded for by the following nucleotide sequences. 
     C protein: from the 333rd to 677th nucleotides 
     M protein: from the 678th to 905th nucleotides 
     E protein: from the 906th to 1499th nucleotides 
     NS1 protein: from the 1500th to 2519th nucleotides 
     NS2 protein: from the 2520th to 3350th nucleotides 
     NS3 protein: from the 3351st to 5177th nucleotides 
     NS4a protein: from the 5178th to 5918th nucleotides 
     NS4b protein: from the 5919th to 6371th nucleotides 
     NS5 protein: from the 6372nd to 9362nd nucleotides 
     These nucleotide sequences are useful for the diagnosis of NANB hepatitis. Polypeptides respectively coded for by these nucleotide sequences are useful as antigens for not only vaccines but also diagnostic reagents for NANB hepatitis. 
     The above-mentioned three structural proteins are represented by the 1st(Met) to 389th(Gly) amino acids of SEQ ID NO: 2 shown in FIG.  2 ( 1 ) through FIG.  2 ( 3 ). The 1st methionine residue is the residue that is coded for by the initiation codon. 
     By further studies by the present inventors, it has been found that the following nucleotide sequences contain epitopes which are reactive to an anti-NANBV antibody: nucleotide sequences respectively of the 333rd to 422nd nucleotides, of the 333rd to 1499th nucleotides, of the 333rd to 6371st nucleotides, of the 474th to 563rd nucleotides, of the 906th to 953rd nucleotides, of the 1020th to 1046th nucleotides, of the 1020th to 1121st nucleotides, of the 1194th to 1232nd nucleotides, of the 1209th to 1322nd nucleotides, of the 4485th to 4574th nucleotides and of the 5544th to 5633rd nucleotides of SEQ ID NO: 1. 
     As described hereinbelow, the above-mentioned nucleotide sequences or nucleotide sequences containing such nucleotide sequences as part of the whole sequences, can be effectively used not only for producing NANBV antigen polypeptides by recombinant DNA technique or chemical synthesis but also for diagnosing NANB hepatitis by hybridization or polymerase chain reaction (PCR). 
     Further, it has been found that a first nucleotide sequence comprising at least six nucleotides of the entire region from the 1st to 9416th nucleotides of SEQ ID NO: 1 shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ) is useful as a probe for hybridization or as a primer for polymerase chain reaction in the diagnosis of NANB hepatitis and that a polypeptide comprising at least four amino acids, which is coded for by a nucleotide sequence of at least twelve nucleotides of the nucleotide sequence of the 333rd to 9362nd nucleotides of SEQ ID NO: 1 is effective as an antigen not only for a vaccine but also for a diagnostic reagent for NANB hepatitis. Further, as is well known in the art, a second nucleotide sequence complementary to the first nucleotide sequence is also useful as a probe for hybridization or as a primer for polymerase chain reaction in the diagnosis of NANB hepatitis. Further, a nucleotide sequence obtained by substituting at least one nucleotide of at least part of the coding region of the first nucleotide sequence of the NANBV in accordance with the degeneracy of the genetic code can also be used for producing the antigen polypeptide of the present invention by recombinant DNA technique. 
     Accordingly, the isolated deoxyribonucleic acid of the present invention comprises at least one nucleotide sequence selected from the group consisting of a first nucleotide sequence comprising at least part of the non-A, non-B hepatitis virus entire nucleotide sequence from the 1st to 9416th nucleotides of SEQ ID NO: 1 shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ) hereof and a second nucleotide sequence complementary to the first nucleotide sequence, or comprises at least one nucleotide sequence obtained by substituting at least one nucleotide of the first nucleotide sequence in accordance with the degeneracy of the genetic code. 
     In one preferred embodiment of the present invention with respect to the deoxyribonucleic acid, the first nucleotide sequence comprises at least six nucleotides of the non-A, non-B hepatitis virus entire nucleotide sequence from the 1st to 9416th nucleotides of SEQ ID NO: 1 shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ) hereof. 
     In another preferred embodiment of the present invention with respect to the deoxyribonucleic acid, the first nucleotide sequence comprises at least one nucleotide sequence selected from the group consisting of a nucleotide sequence of the 333rd to 422nd nucleotides, a nucleotide sequence of the 333rd to 677th nucleotides a nucleotide sequence of the 333rd to 1499th nucleotides, a nucleotide sequence of the 333rd to 6371st nucleotides, a nucleotide sequence of the 474th to 563rd nucleotides, a nucleotide sequence of the 678th to 905th nucleotides, a nucleotide sequence of the 906th to 953rd nucleotides, a nucleotide sequence of the 906th to 1499th nucleotides, a nucleotide sequence of the 1020th to 1046th nucleotides, a nucleotide sequence of the 1020th to 1121st nucleotides, a nucleotide sequence of the 1194th to 1232nd nucleotides, a nucleotide sequence of the 1209th to 1322nd nucleotides, a nucleotide sequence of the 1500th to 2519th nucleotides, a nucleotide sequence of the 2520th to 3350th nucleotides, a nucleotide sequence of the 3351st to 5177th nucleotides, a nucleotide sequence of the 4485th to 4574th nucleotides, a nucleotide sequence of the 5178th to 5918th nucleotides, a nucleotide sequence of the 5544th to 5633rd nucleotides, a nucleotide sequence of the 5919th to 6371st nucleotides, a nucleotide sequence of the 6372nd to 9362nd nucleotides and a nucleotide sequence from the 1st to 9416th nucleotides of SEQ ID NO: 1. 
     The isolated antigen polypeptide of the present invention comprises at least one amino acid sequence comprising at least part of an amino acid sequence coded for by a deoxyribonucleic acid comprising a coding region from the 333rd to 9362nd nucleotides of the non-A, non-B hepatitis virus nucleotide sequence (SEQ ID NO: 1) shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ) hereof. 
     In one preferred embodiment of the present invention with respect to the antigen polypeptide, the antigen polypeptide comprises at least one amino acid sequence of at least four amino acids, which is coded for by a nucleotide sequence of at least twelve nucleotides of the nucleotide sequence of the 333rd to 9362nd nucleotides of SEQ ID NO: 1. 
     In another preferred embodiment of the present invention with respect to the antigen polypeptide, the antigen polypeptide comprises an amino acid sequence coded for by a nucleotide sequence selected from the group consisting of a nucleotide sequence of the 333rd to 422nd nucleotides, a nucleotide sequence of the 333rd to 677th nucleotides, a nucleotide sequence of the 333rd to 1499th nucleotides, a nucleotide sequence of the 333rd to 6371st nucleotides, a nucleotide sequence of the 474th to 563rd nucleotides, a nucleotide sequence of the 678th to 905th nucleotides, a nucleotide sequence of the 906th to 953rd nucleotides, a nucleotide sequence of the 906th to 1499th nucleotides, a nucleotide sequence of the 1020th to 1046th nucleotides, a nucleotide sequence of the 1020th to 1121st nucleotides, a nucleotide sequence of the 1194th to 1232nd nucleotides, a nucleotide sequence of the 1209th to 1322n. nucleotides, a nucleotide sequence of the 1500th to 2519th nucleotides, a nucleotide sequence of the 2520th to 3350th nucleotides, a nucleotide sequence of the 3351st to 5177th nucleotides, a nucleotide sequence of the 4485th to 4574th nucleotides, a nucleotide sequence of the 5178th to 5918th nucleotides, a nucleotide sequence of the 5544th to 5633rd nucleotides, a nucleotide sequence of the 5919th to 6371st nucleotides, a nucleotide sequence of the 6372nd to 9362nd nucleotides and a nucleotide sequence of the 333rd to 9362nd nucleotides of SEQ ID NO: 1. 
     Furthermore, it should be noted that since a polypeptide coded for by the entire coding region of the NANBV (SEQ ID NO: 1) shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ), such a polypeptide has a broad antigen-antibody reaction spectrum and therefore can react to a wide variety of antibodies produced by infection with NANB hepatitis virus as compared to an antigen containing a single epitope, so that it has high sensitivity in detecting NANB hepatitis. 
     Step (VI): Expression of the NANBV genomic CDNA clone and a mass production of an NANBV antigen polypeptide. 
     In order to express the cloned cDNA of an NANBV antigen gene to produce an NANBV antigen polypeptide on a commercial scale, part or whole of the cloned CDNA present in the CDNA clone is taken out from the replicable cloning vector and recombined with a replicable expression vector. Illustratively stated, part or whole of the cDNA of each cDNA clone is cut off using a restriction enzyme to obtain a DNA fragment containing an NANBV antigen gene (hereafter referred to as “NANBV DNA fragment”). The NANBV DNA fragment is then inserted in a replicable expression vector by a customary method. When one DNA fragment is inserted in an expression vector, one type of antigen polypeptide can be produced by gene expression. When two or more of different DNA fragments are inserted in sequence in an expression vector, an antigen polypeptide can be produced by gene expression in the form of a fused polypeptide comprising polypeptides coded for by the inserted DNA fragments. 
     As the replicable expression vector which may be used in this step, any conventionally known or commercially available expression vector can be used. Examples of expression vectors include plasmid vector pSN508 for enterobacteria (U.S. Pat. No. 4,703,005), plasmid vector pBH103 for yeast, and its series (Japanese Patent Application Laid-Open Specification No. 63-22098), plasmid pJM105 (Japanese Patent application Laid-Open Specification No. 62-286930), an attenuated chicken pox virus gene (Japanese Patent Application Laid-Open Specification No. 53-41202), an attenuated Marek&#39;s disease virus (The Journal of Japanese Society of Veterinary, 27, 20-24 (1974), and Gan Monograph on Cancer Research, 10, 91-107 (1971)), plasmid pTTQ series (manufactured and sold by Amersham, England), plasmid pSLV series (manufactured and sold by Pharmacia LKB, Sweden), and the like. 
     The NANBV DNA-inserted expression vectors are individually introduced or transfected into host cells sensitive to the vector according to a conventional method, to obtain transformants. Then, from the transformants, the transformant(s) which has produced an NANBV antigen polypeptide or an NANBV particle is selected. The production of an NANBV antigen polypeptide (or an NANBV particle) may be detected by the immunoassay mentioned above in Step (V). When an animal virus gene is used as an expression vector, a recombinant virus having an NANBV antigen polypeptide on the surface thereof may be obtained. Such a recombinant virus may advantageously be used as a raw material for a multifunctional vaccine having not only an antigenicity inherent in the virus vector but also an antigenicity of the NANBV. 
     By culturing the transformant or recombinant virus obtained above according to a customary method, an NANBV antigen polypeptide can be produced in the culture of the transformant or recombinant virus on a commercial scale. With respect to the details of the method in which an animal virus gene is used as an expression vector, reference may be made to European patent Application Publication No. 0 334 530 Al. 
     Accordingly, in still another aspect of the present invention, there is provided a method for producing a non-A, non-B hepatitis virus antigen polypeptide, which comprises: 
     (a) inserting a deoxyribonucleic acid into a replicable expression vector selected from a plasmid and an animal virus gene to obtain a replicable recombinant DNA comprising the plasmid and the deoxyribonucleic acid inserted therein when the replicable expression vector is a plasmid or obtain a recombinant virus comprising the animal virus gene and the deoxyribonucleic acid inserted therein when the expression vector is an animal virus gene, the deoxyribonucleic acid comprising a nucleotide sequence selected from the group consisting of a first nucleotide sequence comprising at least part of a region from the 1st to 1499th nucleotides or at least part of a region from the 1500th to 9416th nucleotides of the non-A, non-B hepatitis virus entire nucleotide sequence (SEQ ID NO: 1) shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ) hereof and a nucleotide sequence obtained by substituting at least one nucleotide of the first nucleotide sequence in accordance with the degeneracy of the genetic code; 
     (b) transfecting cells of a microorganism or eukaryotic cell culture with the recombinant DNA when the replicable expression vector used in step (a) is a plasmid, to thereby form a transformant, followed by selection of the transformant from parent cells of the microorganism or eukaryotic cell culture; 
     (c) culturing the transformant obtained in step (b) to thereby express the deoxyribonucleic acid and produce a non-A, non-B hepatitis virus antigen peptide, or culturing the recombinant virus obtained in step (a) to thereby express the deoxyribonucleic acid and the animal virus gene and produce a non-A, non-B hepatitis virus antigen peptide in the form of a multiplied recombinant virus comprising an animal virus and a non-A, non-B hepatitis virus antigen peptide contained on the surface thereof; and 
     (d) isolating the non-A, non-B hepatitis virus antigen peptide alone or in the form of the multiplied recombinant virus. 
     Furthermore, by using part or whole of the CDNA of FIG.  2 ( 1 ) through FIG.  2 ( 16 ) (SEQ ID NO: 1) as a template, an RNA or mRNA corresponding thereto can be synthesized by in vitro transcription according to a standard method. For example, an RNA or mRNA corresponding to the entire region of the CDNA of FIG.  2 ( 1 ) through FIG.  2 ( 16 ) (SEQ ID NO: 1) can synthesized using as a template the entire region of the cDNA which is prepared by digesting plasmid pDM-18 (constructed in Example 2) with restriction enzyme HindIII, followed by in vitro transcription by means of T7 RNA polymerase and cap analog. The thus synthesized RNA or mRNA covers the entire region of NANBV gene, that is, the RNA or mRNA is substantially naked NANBV genome. Therefore, when the mRNA is transfected into animal cells, an infectious NANBV particle can be obtained. The above-mentioned mRNA can be synthesized by means of, for example, a commercially available m-RNA Capping Kit (manufactured and sold by Stratagene, U.S.A.) in a conventional manner. With respect to the details of the operating procedure for the synthesis, reference may be made to “Current Protocols in Molecular Biology”, 10.17.1-10.17.5, published by John Wiley &amp; Sons, 1989). The RNA which can be obtained using part or whole of the CDNA of FIG.  2 ( 1 ) through FIG.  2 ( 16 )(SEQ ID NO: 1), is part or whole of the NANBV genome and, therefore, it is useful for studying NANBV and infectious disease caused thereby. 
     Step (VII): Purification of an NANBV antigen polypeptide 
     The NANBV antigen polypeptide produced in the culture of the transformant or recombinant virus may be purified using an appropriate combination of customary techniques selected from, for example, salting-out; adsorption and desorption using a silica gel, an activated carbon or the like; precipitation by an organic solvent; fractionation by ultracentrifugation; separation by ion exchange chromatography or affinity column chromatography; fractionation by high-performance liquid chromatography or electrophoresis, and the like. 
     When the NANBV antigen polypeptide is purified from the culture of an  E. coli  transformant or a yeast transformant, from the viewpoint of effective removal of allergens derived from  E. coli  and yeast which cause the quality of the final product of the NANBV antigen polypeptide to be markedly lowered, it is preferred that the purification be conducted by, for example, the steps of (1) adsorption and desorption using a silica gel, removal of impurities by adsorption on an activated carbon and (2) fractionation by density gradient centrifugation in this order (Japanese Patent Application Laid-Open Specification No. 63-297). When the NANBV antigen polypeptide is purified from the culture of a recombinant virus, e.g., the culture of a recombinant virus-infected cells, a high purity NANBV antigen polypeptide can be obtained by subjecting a crude solution containing the antigen to purification by ultracentrifugation and density gradient centrifugation repeatedly. 
     Thus, a solution containing a purified NANBV antigen polypeptide of the present invention is obtained. If desired, the solution may be lyophilized to obtain a purified NANBV antigen polypeptide in a dry form. 
     The mixed antigen polypeptide of the present invention may be obtained by mixing at least two different types of the NANBV antigen polypeptides obtained by gene expression of at least two different types of CDNAs having different nucleotide sequences. 
     As described above, the core protein (C protein), matrix protein (M protein) and envelope protein (E protein) of the NANBV are included in the region from the 1st (Met) to 389th (Gly) amino acids of SEQ ID NO: 2 shown in FIG.  2 ( 1 ) through FIG.  2 ( 3 ). Therefore, the above-mentioned epitopes contained in this region, especially epitopes coded for by nucleotide sequences respectively of the 906th to 953rd nucleotides, of the 1020th to 1046th nucleotides and of the 1194th to 1232nd nucleotides of SEQ ID NO: 1, are extremely useful as antigens. The epitopes may be obtained by polypeptide synthesis. The polypeptide synthesis can be conducted by means of a commercially available polypeptide synthesizer, such as polypeptide synthesizer COUPLER 2100 (manufactured and sold by Du Pont, USA) and polypeptide synthesizer 430A (manufactured and sold by Applied Biosystems, USA). The synthesized antigen polypeptide may be used, for example, for producing a vaccine, a diagnostic reagent and an antibody. 
     In a further aspect of the present invention, there is provided a replicable recombinant comprising a replicable expression vector selected from a plasmid and an animal virus gene and a deoxyribonucleic acid comprising a nucleotide sequence selected from the group consisting of the first nucleotide sequence comprising at least part of a region from the 1st to 1499th nucleotides or at least part of a region from the 1500th to 9416th nucleotides of the non-A, non-B hepatitis virus nucleotide sequence (SEQ ID NO: 1) shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ) hereof and a nucleotide sequence obtained by substituting at least one nucleotide of the first nucleotide sequence in accordance with the degeneracy of the genetic code. 
     The replicable recombinant can be used not only for producing the NANBV antigen polypeptide of the present invention but also for amplifying the NANBV genomic CDNA of the present invention by replication. 
     In a preferred embodiment of the present invention with respect to the replicable recombinant for amplifying the NANBV genomic cDNA by replication, the first nucleotide sequence comprises at least six nucleotides of the nucleotide sequence of the 1st to 1499th nucleotides or at least six nucleotides of the nucleotide sequence of the 1500th to 9416th nucleotides of SEQ ID NO: 1. 
     In a preferred embodiment of the present invention with respect to the replicable recombinant for producing the NANB antigen polypeptide, the first nucleotide sequence comprises at least twelve nucleotides of the nucleotide sequence of the 333rd to 1499th nucleotides or at least twelve nucleotides of the nucleotide sequence of the 1500th to 9362nd nucleotides of SEQ ID NO: 1. 
     In another preferred embodiemnt of the present invention with respect to the replicable recombinant for producing the NANBV antigen polypeptide, the first nucleotide sequence is selected from the group consisting of a nucleotide sequence of the 333rd to 422nd nucleotides, a nucleotide sequence of the 333rd to 677th nucleotides, a nucleotide sequence of the 333rd to 1499th nucleotides, a nucleotide sequence of the 474th to 563rd nucleotides, a nucleotide sequence of the 678th to 905th nucleotides, a nucleotide sequence of the 906th to 953rd nucleotides, a nucleotide sequence of the 906th to 1499th nucleotides, a nucleotide sequence of the 1020th to 1046th nucleotides, a nucleotide sequence of the 1020th to 1121st nucleotides, a nucleotide sequence of the 1194th to 1232nd nucleotides a nucleotide sequence of the 1209th to 1322nd nucleotides, a nucleotide sequence of the 1500th to 2519th nucleotides, a nucleotide sequence of the 2520th to 3350th nucleotides, a nucleotide sequence of the 3351st to 5177th nucleotides, a nucleotide sequence of the 4485th to 4574th nucleotides, a nucleotide sequence of the 5178th to 5918th nucleotides, a nucleotide sequence of the 5544th to 5633rd nucleotides, a nucleotide sequence of the 5919th to 6371st nucleotides and a nucleotide sequence of the 6372nd to 9362nd nucleotides of SEQ ID NO: 1. 
     The purified NANBV antigen polypeptide of the present invention is useful as a diagnostic reagent for detecting NANB hepatitis. 
     The NANBV antigen polypeptide of the present invention can be formulated into a diagnostic reagent as follows. The purified NANBV antigen polypeptide solution obtained above is dispensed in a vessel, such as a vial and an ampul, and sealed. The antigen polypeptide solution put in a vessel may be lyophilized before the sealing, in the same manner as mentioned above. The amount of the NANBV antigen polypeptide put in a vessel is generally about 1 μg to about 10 mg. Alternatively, the NANBV antigen polypeptide may also be adsorbed on the surface of a customarily employed support, such as a microplate, polyethylene beads, filter paper or a membrane. 
     The determination of the reactivity of the serum with the NANBV antigen polypeptide may be conducted in substantially the same manner as described in Step (V) mentioned above. That is, the determination of the reactivity may be conducted by a conventional immunoassay method, such as radioimmunoassay (RIA), enzyme-linked immunosorbent assay (ELISA), fluorescent antibody technique (FA), passive haemagglutination (PHA), reversed passive haemagglutination (rPRA) and the like. The amount of the NANBV antigen polypeptide to be used for the above immunoassay is generally from about 0.1 to about 100 mg/ml of serum. Particularly, the amounts of the NANBV antigen polypeptide to be used for RIA, ELISA, FA, PHA and rPHA are generally from 0.1 to 1 mg/ml, from 0.1 to 1 mg/ml, from 1 to 100 mg/ml, from 1 to 50 mg/ml and from 1 to 50 mg/ml, respectively. 
     The NANBV antigen polypeptide of the present invention may also be used for screening blood for transfusion. The screening method consists in: 
     a) isolating serum from whole blood; 
     b) contacting serum of an unknown blood with an isolated NANBV antigen polypeptide comprising at least one amino acid sequence comprising at least part of an amino acid sequence coded for by a deoxyribonucleic acid comprising a coding region from the 333rd to 9362nd nucleotides of the NANBV nucleotide sequence (SEQ ID NO: 1) shown in FIG.  2 ( 1 ) through FIG.  2 ( 16 ); 
     c) determining whether the serum reacts with the NANBV antigen polypeptide; 
     d) classifying the serum as positive or negative to non-A, non-B hepatitis based on the reactivity; and 
     e) effecting separation of the blood in accordance with the identification. 
     The contact of serum of an unknown blood with the NANBV antigen polypeptide of the present invention, and the determination of the reactivity of the serum of the blood with the NANBV antigen polypeptide may be conducted in the same manner as mentioned above with respect to the method for diagnosing NANB hepatitis. By the above method, a blood for transfusion free from the NANBV can be selected. 
     The polyclonal antibody and monoclonal antibody specific for the NANBV antigen polypeptide of the present invention may be used as an agent for removing NANBV from blood for transfusion. That is, NANBV present in blood can efficiently be removed by the polyclonal antibody or the monoclonal antibody by antigen-antibody reaction. 
     Further, the NANBV antigen polypeptide of the present invention may advantageously be used as an active ingredient of a vaccine for NANB hepatitis. The vaccine for NANB hepatitis may be prepared as follows. The culturing of a transformant containing a recombinant phage or plasmid carrying the CDNA coding for the NANBV antigen polypeptide, or a cell infected with the recombinant virus carrying the CDNA coding for the NANBV antigen polypeptide is conducted in the same manner as described above to thereby produce the NANBV antigen polypeptide in the culture. For detoxifying the NANBV antigen polypeptide in the culture to secure the safety of the antigen polypeptide and for fixing the antigen polypeptide to stabilize the immunogenicity and the antigenicity of the antigen polypeptide, it is preferred to add a conventional inactivating agent to the culture of the transformant or recombinant virus-infected cell, or to a culture medium obtained by removing the transformant cells or the recombinant virus-infected cell. For example, an inactivating agent, such as formalin, may be added in an amount of from 0.0001 to 0.001 v/v%, followed by incubation at 4 to 37° C. for 5 to 90 days. Then, the resultant culture or culture medium is subjected to purification in the same manner as mentioned above. Thus, an original NANB hepatitis vaccine solution containing the purified NANBV antigen polypeptide is obtained. 
     The original NANB hepatitis vaccine solution is filtered using a microfilter by a standard method to sterilize the solution. The filtrate is diluted with physiological saline so that the protein concentration is about 1 to about 500 μg/ml as measured by the Lowry method. To the resultant solution is then added aluminum hydroxide gel as an adjuvant so that the concentration of the added gel becomes about 0.1 to about 1.0 mg/ml. As an adjuvant, there may also be employed precipitating depositary adjuvants such as calcium phosphate gel, aluminum phosphate gel, aluminum sulfate, alumina and bentonite, and antibody-production inducing adjuvants such as muramyl peptide derivatives, polynucleotides, Kresti® (manufactured and sold by Kureha Chemical Industry Co., Ltd., Japan) and picibanil (both of which are an antineoplastic agent). Further, to the mixture, at least one stabilizing agent may be added. As the stabilizing agent, any commercially available stabilizing agent may be used. Examples of stabilizing agents include gelatin and hydrolysates thereof, albumin, saccharides such as glucose, fructose, galactose, sucrose and lactose, and amino acids such as glycine, alanine, lysine, arginine and glutamine. 
     Then, the thus obtained NANB hepatitis vaccine solution containing a gel-adsorbed NANBV antigen-polypeptide is dispensed into a small vessel, such as an ampul and a vial, and sealed. Thus, there is obtained a purified adsorbed NANB hepatitis vaccine comprising an adsorbed NANBV antigen polypeptide. 
     The NANB hepatitis vaccine solution thus obtained may be lyophilized to obtain the NANB hepatitis vaccine in a dried form so that the product can be transported to and stored at a place of severe climate, for example, in an area in the tropics. The lyophilization may generally be conducted according to a standard method after the liquid adsorbed NANB hepatitis vaccine is dispensed in a vessel such as a vial and an ampul. After lyophilization, a nitrogen gas is introduced in the vessel containing the dried vaccine, followed by sealing. Incidentally, the quality of the vaccine produced is examined in accordance with “Adsorbed Hepatitis B Vaccine”, “Dried Japanese Encephalitis Vaccine”, and “Adsorbed Pertussis Vaccine” provided for in Notification No. 159 of the Ministry of Health and Welfare, Japan, “Minimum Requirements for Biological Products”. 
     The NANB hepatitis vaccine may be prepared in the form of a mixed vaccine which contains an adsorbed NANBV antigen polypeptide mentioned above and at least one antigen other than the present NANBV antigen polypeptide. As the antigen other than the present NANBV antigen polypeptide, there may be employed any antigens that are conventionally used as active ingredients of the corresponding vaccines insofar as the side effects and adverse reactions caused by such other antigens and the NANBV antigen polypeptide are not additively or synergistically increased by the use of the NANBV antigen polypeptide and such other antigens in combination and the antigenicities and immunogenicities of the NANBV antigen polypeptide and such other antigens are not reduced by the interference between the NANBV antigen polypeptide and other antigens. The number and the types of the antigens which may be mixed with the NANBV antigen polypeptide are not limited insofar as the side effects and adverse reactions are not increased additively or synergistically and the antigenicity and immunogenicity of each of the NANBV antigen polypeptide and such antigens are not reduced as mentioned above. Generally, two to six types of antigens may be mixed with the NANBV antigen polypeptide. Examples of antigens which may be mixed with the present NANBV antigen polypeptide, include detoxified antigens, inactivated antigens or toxoids which are derived from Japanese encephalitis virus, HFRS (hemorrhagic fever with renal syndrome) virus, influenza virus, parainfluenza virus, hepatitis B virus, dengue fever virus, AIDS virus,  Bordetella pertussis , diphtheria bacillus, tetanus bacillus, meningococcus, pneumococcus and the like. 
     Generally, the vaccine comprising the NANBV antigen polypeptide of the present invention may be contained and sealed in a vial, an ampul or the like. The vaccine of the present invention may generally be administered in the form of a liquid or suspension. In the case where the vaccine is in a dried form, the vaccine is dissolved or suspended in sterilized distilled water before administration, the amount of the distilled water being such that the volume becomes the original volume before being subjected to lyophilization. Generally, the vaccine may be administered subcutaneously. The dose of the vaccine per person may generally be about 0.5 ml. In general, the dose of the vaccine per child may be half as much as that of the vaccine per adult. The vaccine may generally be administered twice at an interval of about one week to one month and then, about half a year later, administered once more. 
     Further, the NANBV antigen polypeptide may be used for preparing an antibody, such as a polyclonal antibody and a monoclonal antibody, specific for the NANBV antigen polypeptide. For example, a polyclonal antibody specific for the NANBV antigen polypeptide may be prepared by a conventional method as follows. The purified NANBV antigen polypeptide of the present invention is inoculated subcutaneously, intramuscularly, intraperitoneally or intravenously to an animal, such as mouse, guinea pig and rabbit. The inoculation of the NANBV antigen polypeptide is generally conducted several times at intervals of 1 to 4 weeks, to thereby completely immunize the animal. In order to enhance the immunizing effect, a conventional and commercially available adjuvant may be used. Then, blood serum is collected from the immunized animal and an anti-NANBV antigen polypeptide polyclonal antibody is isolated and purified from the blood serum according to a standard method. 
     On the other hand, a monoclonal antibody specific for the NANBV antigen polypeptide may be prepared by a conventional method as described, for example, in Cell Technology, 1, 23-29 (1982). For example, splenic cells obtained from a mouse immunized with the purified NANBV antigen polypeptide are fused with commercially available mouse myeloma cells by cell fusion technique, to obtain hybridomas. The hybridomas are screened to obtain a hybridoma capable of producing an antibody reactive with the NANBV antigen polypeptide. The obtained hybridoma is cultured in a standard method. From the supernatant of the culture, an anti-NANBV antigen polypeptide monoclonal antibody is isolated and purified by a standard method. 
     The above-mentioned polyclonal antibody and monoclonal antibody may also be used as a diagnostic reagent for diagnosing NANB hepatitis. The diagnosis of NANB hepatitis using the antibody may be conducted by immunoassay in substantially the same manner as mentioned above with respect to the diagnosis of NANB hepatitis using the NANBV antigen polypeptide. By the use of the polyclonal antibody or the monoclonal antibody, the identification and quantification of the NANBV antigen polypeptide present in a liver tissue and blood can be conducted. 
     The NANBV genomic cDNA of the present invention can be prepared by digesting the NANBV genomic CDNA clone defined in the present invention with an appropriate restriction enzyme. Also, the NANBV genomic cDNA of the present invention can be prepared by the technique of DNA synthesis in accordance with the nucleotide sequence (SEQ ID NO: 1) shown in FIG.  2 ( 1 ) to FIG.  2 ( 16 ) of the present application. The preparation of the NANBV genomic cDNA by way of DNA synthesis can be performed by means of a customary DNA synthesizer, such as DNA synthesizer Model 380B (manufactured and sold by Applied Biosystem, U.S.A.) and DNA Synthesizer Model 8700 (manufactured and sold by Biosearch, U.S.A.). The NANBV genomic CDNA of the present invention can be used to conduct the genetic diagnosis of NANBV infection. That is, the NANBV genomic CDNA of the present invention can be used as a primer for polymerase chain reaction (PCR) in the detection of an NANBV gene in the body fluid or cells from a patient. For the diagnosis by polymerase chain reaction, the NANBV genomic cDNA is used in an amount of 10 to 100 ng. 
     The NANBV genomic cDNA of the present invention may also be used for diagnosing NANB hepatitis by hybridization technique. That is, the NANBV genomic cDNA is labeled with, for example, biotin, alkaline phosphatase, radioisotope  32 P or the like and used as a probe for hybridization. The cDNA to be used for the diagnosis by hybridization technique may be prepared by a standarad method, for example, as follows. The recombinant phage containing the NANBV cDNA obtained in Step (V) mentioned above is digested with an appropriate restriction enzyme to cut off the DNA fragment containing the NANBV cDNA. The obtained DNA fragment is ligated to a commercially available replicable cloning plasmid to obtain a recombinant plasmid containing the DNA fragment. The recombinant plasmid is introduced in a host cell to form a transformant and the transformant is cultured to multiply the recombinant plasmid. The multiplied recombinant plasmid is isolated from the transformant and digested with a restriction enzyme. The resultant digest is subjected to low-melting point agarose gel electrophoresis to isolate and purify the cDNA coding for the NANBV antigen polypeptide. The thus obtained CDNA is labeled with biotin, alkaline phosphatase, radioisotope 32p or the like. The labeling of the cDNA may be conducted by using a commercially available nick translation kit or multiprime DNA labeling system (manufactured and sold by, for example, Amersham, England; Nippon Gene Co., Ltd., Japan; and the like). The labeled cDNA is put in a vessel having a volume of about 5 to 20 ml, such as a vial or an ampul, and sealed. The amount of the labeled cDNA put in a vessel is generally 1 to 100 μg per vessel. The labeled cDNA may be contained in the vessel in the form of a solution. Alternatively, the labeled cDNA may be contained in the vessel in a lyophilized state. The diagnosis of NANB hepatitis by the use of the labeled cDNA is conducted by a standard hybridization method. That is, plasma, serum or leukocytes obtained from a patient is placed in contact with the labeled CDNA and an RNA hybridized with the labeled CDNA is detected. The detection of the RNA hybridized with the labeled cDNA may be conducted by a standard method. When the cDNA is labeled with an enzyme, the detection is conducted by enzyme immunoassay. When the CDNA is labeled with a radioisotope, the detection is conducted by, for example, scintillation counting. 
     The NANBV genomic CDNA of the present invention is excellent in reliability and contains the entire region of the open reading frame of the NANBV gene. 
     The NANBV antigen polypeptide of the present invention is specifically reactive with the NANBV. Therefore, when the NANBV antigen polypeptide is used as a diagnostic reagent, the diagnosis of NANB hepatitis can be conducted easily with high reliability. Further, when the NANBV antigen polypeptide of the present invention is used for screening blood for transfusion, blood which is infected by NANBV can be selected easily with high reliability and removed from blood not infected by NANBV. Therefore, the post-transfusion NANB hepatitis can be prevented. 
     Further, the NANBV antigen polypeptide of the present invention may advantageously be used as an active ingredient of a vaccine for preventing NANB hepatitis. 
     Further, by the use of the NANBV antigen polypeptide of the present invention, an antibody, particularly monoclonal antibody, specific for NANBV can easily be prepared. The antibody specific for NANBV can advantageously be used as not only a diagnostic reagent for detecting NANB hepatitis, but also an agent for removing NANBV from blood for transfusion. 
     Furthermore, it should be noted that the NANBV antigen polypeptide of the present invention is not produced by the infection of an animal with a virus, but produced by gene expression of the DNA coding for the present antigen polypeptide in a host cell. Hence, the possibility of infection during the steps for production of the present antigen polypeptide is substantially eliminated. Also, the production cost can be decreased. Moreover, since all of the materials used in the production process, e.g., medium for the incubation system, are well-known in respect of the composition thereof, purification is facile and an antigen polypeptide product having high purity can be obtained. 
     Preferred Embodiment of the Invention 
     The present invention will now be described in detail with reference to the following Examples, which should not be construed to be limiting the scope of the present invention. 
     EXAMPLE 1 
     Step 1 (Preparation of a plasma-derived RNA for producing cDNA, which is complementary to NANBV genome RNA) 
     In order to obtain NANBV from plasma, 4.8 liters of human plasma exhibiting a glutamic-pyruvic transaminase (GPT) activity of 35 IU/ or more (as measured by the method of Wroblewski, F &amp; J. S. LaDue: Serum glutamic-pyruvic transaminase in cardiac and hepatic disease. Proc. Soc. Exp. Biol. Med., 91:569, 1956) was superposed on a 30% (w/w) aqueous sucrose solution, and subjected to centrifugation under 48,000×g at 4° C. and for 13 hours to obtain a precipitate. The precipitate was suspended in an aqueous solution containing 50 mM Tris.HCl (pH 8.0) and 1 mM EDTA, and once more subjected to centrifugation under 250,000×g at 4° C. and for 3 hours to thereby obtain a precipitate. The obtained precipitate was dissolved in 75 ml of 5.5 M GTC solution containing 5.5 M quanidine thiocyanate, 20 mM sodium citrate (pH 7.0), 0.05% sarkosyl (sodium lauryl sarcosinate) and 0.1 M 2-mercaptoethanol. The resultant solution was superposed on 16 ml of CsTFA-0.1 M EDTA solution (ρ=1.51), and subjected to centrifugation under 140,000×g at 15° C. and for 20 hours to thereby obtain a precipitate of RNA. The supernatant containing proteins and DNA was removed by suction, and the precipitate was dissolved in 200 μl of TE 10 mM Tris.HCl, pH 8.0 and 1 mM EDTA solution. 20 μl of 3 M sodium chloride and ethanol were added to the solution, and allowed to stand still at −70° C. for 90 minutes. The mixture was centrifuged under 12,000×g at 4° C. and for 30 minutes to obtain a precipitate. The precipitate was dissolved in TE, and sodium chloride and ethanol were added in the same manner as mentioned above. The mixture was allowed to stand still at −70° C. to obtain a precipitate. The precipitate was dissolved in 10 al of TE to thereby obtain a purified RNA. 
     Step 2 (Preparation of a liver-derived RNA for producing a CDNA, which is complementary to NANBV genome RNA) 
     NANBV genome RNA was prepared from a liver tissue cut off from a NANBV hepatitis patient by the method of Okayama et al. (see H. Okayama, M. Kawaichi, M. Brownstein, F. Lee, T. Yokota, and K. Arai: High-Efficiency Cloning of Full-Length cDNA; Construction and Screening of cDNA Expression Libraries for Mammalian Cells, Methods in Enzymology 154.3-28, 1987). 
     Illustratively stated, 1 g of liver tissue was cut into small pieces. The small pieces were suspended in 100 ml of 5.5 M GTC solution as used in Step 1, and homogenized by means of a Teflon-glass homogenizer. Subsequently, the introduction of the homogenate into a syringe having #18 needle and the discharge of the homogenate from the syringe through the needle were repeated to thereby mechanically split DNA. The resultant homogenate was centrifuged under 1,500×g (lower centrifugal force) at 4° C. and for 15 minutes to thereby obtain a supernatant. Thee supernatant was superposed on CsTFA solution and centrifuged in substantially the same manner as described in Step 1 to thereby obtain a precipitate as an RNA fraction. The thus obtained precipitate was suspended in 0.4 ml of 4 M GTC solution. 10 μl of 1 M acetic acid and 300 μl of ethanol were added to the suspension, and allowed to stand still at a temperature of −20° C. for at least 3 hours to thereby obtain a precipitate of RNA. The precipitate was separated by centrifugation under 12,000×g at a temperature of 4° C. and for 10 minutes, and dissolved in 1 ml of TE solution. 100 μl of 2 M sodium chloride solution and 3 ml of ethanol were added to the solution, and the mixture was allowed to stand at −20° C. for 3 hours. The resultant precipitate was collected by centrifugation and dissolved in 10 μl of TE to thereby obtain a purified, liver-derived RNA. 
     Step 3 (Preparation of a double-stranded cDNA using a cDNA synthesis kit) 
     A double-stranded CDNA was prepared using a commercially available cDNA synthesis kit (manufactured and sold by Amersham International, England). 
     Illustratively stated, 0.75 μg of the purified RNA obtained in Step 1 and 2 μl of random hexanucleotide primer and 2 μl of reverse transcriptase taken from the reagents included in the kit were put in a reaction tube. Then, distilled water was added in an amount such that the total volume of the resultant mixture became 20 μl. The mixture was incubated at 42° C. for 40 minutes, thereby preparing a first strand of cDNA. Subsequently, a second strand of CDNA was synthesized while cooling the reaction mixture in ice water, as follows. To 20 μl of the reaction mixture were added 37.5 μl of buffer for second strand synthetic reaction, 1 μl of  E. coli  ribonuclease H and 6.6 μl of DNA polymerase I, which were taken from the reagents included in the kit, followed by addition of 34.9 μl of distilled water. The mixture was incubated at 12° C. for 60 minutes, 22° C. for 60 minutes and at 70° C. for 10 minutes. Then, the mixture was once more cooled with ice water. 1 μl of T4 DNA polymerase was added, incubated at a temperature of 37° C. for 10 minutes, and 4 μl of 0.25 M EDTA (pH 8.0) was added to thereby terminate the reaction. The reaction mixture was mixed well with a mixture of phenol and chloroform, and centrifuged under 12,000×g for one minute to thereby separate an aqueous layer. The aqueous layer was again subjected to the same extraction as mentioned above, and an equal amount of chloroform was added. The mixture was agitated well and centrifuged to Sepdrdte an aqueous layer. Subsequently, an equal amount of 4 M ammonium acetate and a two-fold amount of ethanol were added to the aqueous layer, and the mixture was cooled to −70° C., thereby obtaining a precipitate of purified double-stranded CDNA. The precipitate was dissolved in 50 μl of 2 M ammonium acetate. To the mixture, 100 μl of ethanol was added, and the resultant mixture was cooled to −70° C. to thereby obtain a precipitate. The precipitate was collected by centrifugation under −12,000×g for ten minutes. The collected precipitate was dried and then, dissolved in 20 μl of TE. 
     Step 4 (Preparation of a double-stranded cDNA by the Polymerase Chain Reaction (PCR) method) 
     The cDNAs which were prepared by means of a reverse transcriptase using as templates the RNAs prepared in Step 1 and Step 2, were individually amplified by the PCR method (see Saiki, R. K., Gelfand, D. H., Stoffer, S., Scharf, S. J., Higuchi, R., Horn, G. T., Mullis, K. B., and Erlich, H. A., Primer-directed enzymatic amplification of DNA with a thermostable DNA Polymerase, Science 239:487-491, 1988). That is, 5 to 1,000 ng of the RNA was incubated in 20 μl of a reverse transcriptase solution containing 50 mM Tris.HCl (pH 8.3), 40 mM KCl, 6 mM MgCl 2 , 1 μM 3′-primer [synthesized oligonucleotide comprised of 25 nucleotides of nucleotide numbers 7949 to 7973 in FIG.  2 ( 14 )], 10 mM dNTP, and 0.5 unit of reverse transcriptase (product of New England Bio Lab., U.S.A.) at 37° C. for 30 minutes. To the resultant mixture was added 80 μl of a PCR reaction solution containing 18 mM Tris.HCl (pH 8.3), 48 mM KCl, 1.5 mM MgCl 2 , 0.6 μM each of 5′-primer [synthesized oligonucleotide comprised of 25 nucleotides of nucleotide numbers 7612 to 7636 in FIG.  2 ( 13 )] and the above-mentioned 3′-primer, 10 mM dNTP and 2.5 units of Taq DNA polymerase (manufactured and sold by Perkin Elmer Cetus Co., Ltd., U.S.A.). The mixture was subjected to incubation at 94° C. for one minute, at 50° C. for 2 minutes and at 72° C. for 3 minutes. This incubation was repeated 40 times. The resultant mixture was subjected to electrophoresis using agarose gel, thereby obtaining amplified cDNA. The amplified cDNA was subjected to phenol treatment, ethanol precipitation and drying. The dried cDNA was dissolved in 10 μl of TE. 
     Step 5 (Preparation of a cDNA library using lambda gt11) 
     Using a commercially available cDNA cloning kit (manufactured and sold by Amersham International, England), a CDNA library was prepared. That is, to 130 ng of CDNA prepared in Step 3 were added 2 μl of L/K buffer, 2 μl of EcoRI adaptor and 2 μl of T4 DNA ligase, which were taken from the reagents included in the cloning kit. Distilled water was added to the solution in an amount such that the total volume of the resultant mixture became 20 μl. The mixture was incubated at a temperature of 15° C. for a period of from 16 to 20 hours, and 2 μl of 0.25 M EDTA was added thereto, to thereby terminate the reaction. Subsequently, the mixture was passed through a size fractionating column included in the kit, thereby removing EcoRI adaptors which were not ligated to the cDNA. To 700 μl of the cDNA having EcoRI adaptor ligated thereto were added 83 μl of LIK buffer and 8 μl of T4 polynucleotidekinase. The mixture was incubated at a temperature of 37° C. for 30 minutes. The resultant mixture was subjected to phenol extraction twice, concentration to 350 to 400 μl by means of butanol and then ethanol precipitation, thereby obtaining a precipitate. The precipitate was dissolved in 5 μl of TE. 
     Subsequently, in order to insert the cDNA having EcoRI adaptor ligated thereto to the EcoRI site of cloning vector lambda gt10, 1 μl of L/K buffer, 2 μl (1 μg) of lambda gt11 arm DNA and 2 μl of T4 DNA ligase were added to 1 μl (10 ng) of the above-mentioned CDNA having EcoRI adaptor ligated thereto. Distilled water was added to the mixture in an amount such that the total volume of the mixture became 10 μl. The mixture was incubated at a temperature of 15° C. for a period of from 16 to 20 hours. Thus, a recombinant lambda gt11 DNA solution was prepared. Further, a recombinant lambda phage was obtained by in vitro packaging using a commercially available in vitro packaging kit (manufactured and sold by Stratagene Co., Ltd., U.S.A.) including Gigapack II Gold solutions A and B, SM buffer and chloroform. That is, 10 μl of Gigapack II Gold solution A and 15 μl of Gigapack II Gold solution B were added to 4 μl of the above-mentioned recombinant lambda gt11 DNA solution. The mixture was incubated at 22° C. for 2 hours. After the incubation, 470 μl of SM buffer and 10 μl of chloroform were added to thereby obtain a recombinant phage, which was stored at 4° C. 
     Step 6 (Cloning of cDNA using  E. coli  plasmid pUC19) 
     Using a commercially available DNA ligation kit (manufactured and sold by Takara Shuzo Co., Ltd., Japan) including solutions A and B, the cDNA was inserted in  E. coli  plasmid pUC19 (C. Yanishi-Perron, J. Vieira, J. Messing, Gene 33, 103, 1985), and cloned in  E. coli . That is, 40 μl of solution A and 10 μl of solution B were added to 5 μl of the CDNA prepared by polymerase chain reaction (PCR) in Step 4 and 5 μl (50 ng) of plasmid pUC19 DNA which had been digested with restriction enzyme SmaI and dephosphorylated. The mixture was incubated at a temperature of 15° C. for 16 hours.  E. coli  strain JM 109 (see Messing, J., Crea, R., and Seeburg, P. H., Nucleic Acids Res. 9, 309, 1981) was transformed with the above-obtained plasmid DNA according to the calcium chloride method (see Mandel, M. and A. Higa, J. Mol. Biol., 53, 154,-1970). Thus, a transformed  E. coli  containing the plasmid having the CDNA ligated thereto was obtained. 
     Step 7 (Screening of clone having NANBV gene from a CDNA library) 
       E. coli  strain Y 1090 (see Richard A. Young and Ronald W. Davis, Science, 222, 778, 1983) was cultured in 50 ml of LBM medium containing 1% tryptone, 0.5% yeast extract, 1% sodium chloride, 50 μg/ml ampicillin and 0.4% maltose at a temperature of 37° C. The  E. coli  cells in a logarithmic growth phase were suspended in 15 ml of 10 mM magnesium sulfate cooled with ice. The phage solution obtained in Step 5 was diluted with SM buffer containing 0.1 M sodium chloride, 8 mM magnesium sulfate, 50 mM Tris.HCl (pH 7.5) and 0.01% gelatin. 0.1 ml of the diluted phage solution was mixed with an equal volume of the above-mentioned  E. coli  cell suspension, and the mixture was incubated at a temperature of 37° C. for 15 minutes. To the mixture was added 4 ml of soft agar medium heated to 45° C. and containing 1% tryptone, 0.5% yeast extract, 0.5% sodium chloride, 0.25% magnesium sulfate and 0.7% agar (pH 7.0). The mixture was spread on L-agar plate containing 1% tryptone, 0.5% yeast extract, 1% sodium chloride, 1.5% agar and 100 μg/ml ampicillin (pH 7.0), and incubated at a temperature of 42° C. for 3 hours. Subsequently, 10 mM IPTG (isopropyl β-D-thiogalactopyranoside) was infiltrated into a nitrocellulose filter, and the nitrocellulose filter was dried and closely contacted with the L-agar plate. The plate was incubated at a temperature of 37° C. for 3 hours. The filter was separated, and washed with TBS buffer three times. The washed filter was immersed in 2% bovine serum albumin solution, and incubated at room temperature for one hour. {fraction (1/20)} volume of  E. coli  lysate solution included in a commercially available immunoscreening kit (manufactured and sold by Amersham International, England) was added to pooled serum from NANB hepatitis patients, and incubated at room temperature for 30 minutes. Thereafter, the serum was diluted to 50-fold with 0.2% bovine serum albumin-added TBS buffer, and the filter was immersed in the diluted serum solution, and incubated at room temperature for one hour. 
     The resultant filter was washed four times with a TBS buffer containing 0.05% Tween. 20. The washed filter was immersed in an antibody solution which had been prepared by diluting a peroxidase-labeled anti-human IgG (manufactured and sold by Cappel Co., Ltd., Germany) 1,000-fold for one hour. The filter was washed with the above-mentioned Tween-TBS buffer, and immersed in a solution prepared by adding 0.4 ml of DAB (3,3′-diaminobenzidine tetrahydrochloride) and 15 μl of a 30% aqueous hydrogen peroxide solution to 50 ml of a TBS buffer, followed by incubation at room temperature for 5 to 30 minutes to allow color development. The resultant filter was completely washed with distilled water to terminate the reaction. 
     By the above-mentioned procedure, the obtained plaques were purified. As a result, 9 positive clones were isolated, which were, respectively, designated as BK 102, BK 103, BK 105, BK 106, BK 108, BK 109, BK 110, BK 111 and BK 112. All of these clones did not react with serum from a healthy human, but reacted with serum from a patient suffering from NANB hepatitis. See Table 1. 
     
       
         
           
               
             
               
                 TABLE 1 
               
             
            
               
                   
               
               
                 Reactivity between the serum obtained from 
               
               
                 a patient suffering from NANB hepatitis and 
               
               
                 the recombinant lambda gt11 phage clone 
               
            
           
           
               
               
               
               
            
               
                   
                   
                 Serum from 
                 Serum from NANB 
               
               
                   
                 Clone 
                 healthy person 
                 hepatitis patient 
               
               
                   
                   
               
               
                   
                 BK 102 
                  0/10* 
                 10/11  
               
               
                   
                 BK 103 
                 0/10 
                 9/11 
               
               
                   
                 BK 105 
                 0/10 
                 11/11  
               
               
                   
                 BK 106 
                 0/10 
                 11/11  
               
               
                   
                 BK 108 
                 0/10 
                 9/11 
               
               
                   
                 BK 109 
                 0/10 
                 9/11 
               
               
                   
                 BK 110 
                 0/10 
                 9/11 
               
               
                   
                 BK 111 
                 0/10 
                 9/11 
               
               
                   
                 BK 112 
                 0/10 
                 10/11  
               
               
                   
                   
               
               
                   
                 *the number of positive samples/the number of specimens.  
               
            
           
         
       
     
     Step 8 (Determination of the nucleotide sequence of the obtained clones) 
     Recombinant phage DNAs of clones BK 102 to BK 112 were collected, and the collected DNAs were digested with restriction enzyme EcoRI. Then, cDNA fragments of NANBV were isolated and the isolated cDNAs were individually inserted into plasmid pUC19 at EcoRI site. Using the plasmids,  E. coli  strain JM 109 was transformed in substantially the same manner as in Step 7. Plasmid DNAs were obtained from the transformed  E. coli  and purified. The nucleotide sequence of each of the NANBV cDNAs was determined using 7-DEAZA sequencing kit (manufactured and sold by Takara Shuzo Co., Ltd., Japan; see Mizusawa, S., Nishimura, S. and Seela, F. Nucleic Acids Res., 14, 1319, 1986). The relationship between the nucleotide sequences of the obtained CDNA clones is shown in FIG.  1 ( 1 ). 
     Step 9 (Cloning of NANBV cDNA clones from a cDNA library by Genomic Walking) 
     Probes were prepared by labeling with  32 P-dCTP the cDNA fragments of clone BK 102, clone BK 106 and clone BK 112 which were. obtained in Step 8. Using the probes, phage clones containing NANBV cDNAs were obtained by hybridization from the cDNA library of cloning vector lambda gt11 obtained in Step 5 and the above-mentioned probes. That is, plasmid DNAs were prepared from the transformed  E. coli  with clone BK 102, clone BK 106 and clone BK 112 obtained in Step 8 by the alkali method (see T. Maniatis, E. F. Fritsch, and J. Sambrook: Isolation of Bacteriophage λ and Plasmid DNA: “Molecular Cloning”, Cold Spring Harbor Lab., pp 75-96.). 
     Plasmid DNA of clone BK 102 was digested with restriction enzymes NcoI and HincII, and the resultant 0.7 kb fragments having been on the 5′-terminus side of the DNA were subjected to electrophoresis with agarose gel, and collected. Plasmid DNAs of clone PR 106 and clone BK 112 were digested with restriction enzyme NcoI. In the same manner as mentioned above, 1.1 kb DNA fragments were collected from clone BK 106, and 0.7 kb fragments having been on the 3′-terminus side were collected from clone BK 112. 25 ng to 1 μg of DNA fragments were incubated with [α- 32 P]dCTP (3000 Ci/mmol; manufactured by Amersham Co., Ltd., England) at a temperature of 37° C. for a period of from 3 to 5 hours, using commercially available DNA labeling kit (manufactured by Nippon Gene Co., Ltd.). Thus, probes for hybridization were prepared. 
     Subsequently, the cDNA library phage obtained in Step 5 was incubated at a temperature of 42° C. in L-agar medium for 3 hours, as described in Step 7. Further, the phage was incubated at a temperature of 37° C. for 3 hours, and was cooled. A nitrocellulose filter was disposed on the mixture, and was allowed to stand still for a period of from 30 to 60 seconds. Thus, the phage was adsorbed onto the filter. 
     The filter was subjected to alkali denaturation for a period of from 1 to 5 minutes using an aqueous solution containing 0.5 N sodium hydroxide and 1.5 M sodium chloride and to the neutralization with an aqueous solution containing 0.5 M Tris.HCl (pH 8.0) and 1.5 M sodium chloride for a period of from 1 to 5 minutes. The filter was washed with 2×SSC solution containing 0.3 M sodium chloride and 0.03 M sodium citrate, air dried, and baked at a temperature of 80° C. for 2 hours. 
     The filter was incubated at a temperature of 42° C. for 6 hours in a solution for hybridization containing 50% formamide, 5×SSC, 5×Denhart solution, 50 mM phosphoric acid-citric acid buffer (pH 6.5), 100 μg/ml trout sperm DNA and 0.1% SDS. Then, the filter was immersed in 300 ml of the hybridization solution having 1 ml of the above-mentioned probe of about 4×10 8  cpm/ml added thereto, and incubated at a temperature of 42° C. for 16 to 20 hours. The filter was washed with an SDS solution containing 0.1% 2×SSC four times and with an SDS solution containing 0.1% 0.1×SSC twice. After the washing, the filter was dried, and was subjected to autoradiography. Thus, hybridization positive clones were isolated. As a result, 27 clones being reactive with the probe derived from clone BK 102, 14 clones being reactive with the probe derived from clone BK 106 and 13 clones being reactive with the probe derived from clone BK 112, were obtained, which were respectively designated as BK 114 to BK 169. 
     The nucleotide sequence of each. of clones BK 114 to BK 169 was determined according to the method described in Step 8, followed by mapping for each of the clones. As a result, a map of nucleotide sequence having a length of about 9.5 kb considered to be the approximately total length of the NANBV genome was obtained [see FIG.  1 ( 2 )]. 
     Clone BK 157 located on the 5′ terminus side was digested with restriction enzyme KpnI to thereby collect a 0.55 kb fragment having been on the 5′-terminus side. Also, clone BK 116 located on the extreme 3′-terminus side was digested with restriction enzymes HpaI and EcoRI to thereby collect a 0.55 kb fragment having been on the 3′-terminus side. A probe labeled with  32 P was prepared in the same manner as described above, and the cDNA library phage obtained in Step 5 was subjected to plaque hybridization. As a result, three new additional clones were separated by the probe derived from the clone BK 157. These new clones were, respectively, designated as clones BK 170, BK 171 and BK 172. 
     Step 10 (Analysis of the nucleotide sequence of cDNA) The entire nucleotide sequence (SEQ ID NO: 1) of NANBV gene was determined from the nucleotide sequences of the clones obtained in Steps 8 and 9, and shown in FIGS.  2 ( 1 ) to  2 ( 16 ). From the Figures, it was assumed that the cloned genomic cDNAs of NANBV were composed of 9416 nucleotides, wherein there was an open reading frame composed of 9030 nucleotides coding for a protein composed of 3010 amino acid residues. The hydrophilicity/hydrophobicity pattern of this protein was similar to that of flavivirus as already reported (see H. Sumiyoshi, C. Mori, I. Fuke et al., Complete Nucleotide Sequence of the Japanese Encephalitis Virus Genome RNA. Virology, 161, 497-510, 1987). Clone BK 157 covers nucleotide numbers 1 to 1962 of FIGS.  2 ( 1 ) to  2 ( 16 ), clone BK 172 covers nucleotide numbers 5 to 366, clone BK 153 covers nucleotide numbers 338 to 1802, clone BK 138 covers nucleotide numbers 1755 to 5124, clone BK 129 covers nucleotide numbers 4104 to 6973, clone BK 108 covers nucleotide numbers 6886 to 8344 and clone BK 166 covers nucleotide numbers 8082 to 9416. They are preserved as  Escherichia coli  BK 108 (deposited at Fermentation Research Institute, Japan under accession number FERM BP-2971), BK 129 (deposited at Fermantation Research Institute, Japan under accession number FERM BP-2972), BK 138 (deposited at Fermentation Research Institute, Japan under accession number FERM BP-2973), BK 153 (deposited at Fermentation Research Institute, Japan under accession number FERM BP-2974), BK 157, BK 166 (deposited at Fermentation Research Institute, Japan under accession number FERM BP-2975), and BK 172 (deposited at Fermentation Research Institute, Japan under accession number FERM BP-2976), respectively. 
     Step 11 (Production of NANBV-related antigens in  E. coli , which antigens are related with the antibody-response accompanying NANBV infection) 
     Respective cDNAs of clone BK 106, clone BK 111 and clone BK 112 each obtained in Step 8 and cDNA of clone BK 147 obtained in Step 9 were individually inserted into plasmids, and the thus obtained plasmid DNAs were collected by the conventional alkali method. Subsequently, the collected DNA of clone BK 106 was digested with restriction enzymes EcoRI and ClaI to thereby obtain 0.5 μg of a DNA fragment of 0.34 kb in length. The thus obtained DNA fragment was incubated at 37° C. for 60 minutes in a T4 DNA polymerase solution containing 67 mM Tris.HCl (pH 8.8), 6.7 mM magnesium chloride, 16.6 mM ammonium sulfate, 10 mM 2-mercaptoethanol, 6.7 μM EDTA, 0.02% bovine serum albumin, 0.3 mM dNTP and 2-5 units of T4 DNA polymerase, thereby rendering both terminals blunt. The DNA of clone BK 102 was digested with restriction enzyme BamHI to thereby collect 0.5 μg of a DNA fragment of 0.7 kb in length, and the terminals of the DNA fragment were rendered blunt using T4 DNA polymerase in substantially the same manner as mentioned above. The DNA of clone BK 147 was digested with restriction enzyme Sau3AI to thereby obtain 0.5 μg of a DNA fragment of 1 kb in length and the terminals of the DNA fragment were rendered blunt in the same manner as mentioned above. Also, the DNA of clone BK 111 was digested with restriction enzyme EcoRI to thereby obtain 0.5 μg of a DNA fragment of 1 kb in length, and the terminals of the DNA fragment were rendered blunt in substantially the same manner as mentioned above. Subsequently, the DNA of expression vector pKK 233-2 (Amann, E. and J. Brosius. ATG vector for regulated high-level expression of cloned genes in  Escherichia coli . Gene, Vol. 40, 183, 1985) was digested with restriction enzyme HindIII. 2 μg of the resultant DNA was incubated at 37° C. for 20 minutes in a S1 nuclease solution containing 0.3 M sodium chloride, 50 mM sodium acetate (pH 4.5), 1 mM zinc sulfate and 100-200 units of Si nuclease, and the reaction was terminated by adding {fraction (1/10)} volume of each of 0.12 M EDTA and 1 M Tris.HCl solution (pH 9.0). Then, phenol 5 extraction was performed, and the vector DNA having blunt terminals was precipitated by ethanol and collected. On the other hand, the DNA of vector pKK 233-2 was digested with restriction enzyme PstI, and the digested DNA was purified by extraction with phenol and precipitation from ethanol. The terminals of 2 μg of the purified vector DNA which had been cleaved by restriction enzyme PstI were rendered blunt by the above-mentioned T4 DNA polymerase reaction. The thus obtained DNA fragments derived from clone BK 106 and clone BK 111 were each cleaved with restriction enzyme HindIII. 0.5 μg of each of the cleaved DNA fragments was mixed with 0.5 μg of a vector DNA having blunt terminals. The DNA fragments derived from clone BK 102 and clone BK 147 were each cleaved with restriction enzyme PstI. 0.5 μg of each of the claved DNA fragments was mixed with 0.5 μg of a vector DNA having terminals thereof rendered blunt. The volume of each of the mixtures was adjusted to 20 μl by adding 2 μl of 10× ligation solution containing 500 mM Tris.HCl (pH 7.5), 100 mM magnesium chloride, 100 mM DTT and 10 mM ATP, 300-400 units of T4 DNA ligase and distilled water. The mixtures were incubated at 14° C. for 12-18 hours, thereby obtaining plasmids, which were respectively designated as pCE-06, pE-11, pB-02 and pS-09. Using each of these plasmid DNAs,  E. coli  strain JM 109 was transformed in substantially the same manner as de scribed in Step 6, thereby obtaining transformed  E. coli . The transformed  E. coli  was cultured at 37° C. in LB medium (pH 7.5) containing 1 (w/v) % trypton, 0.5 (w/v) % yeast extract and 1 (w/v) % sodium chloride, and when it was in logarithmic growth phase, 1 mM IPTG (isopropyl-β-D-thiogalactopyranosidey was added to the medium. The culturing was further continued for 3 hours. Then,  E. coli  cells were collected by centrifugation (10,000×g for 15 minutes), and the collected cells were lysed in 50 mM Tris.HCl (pH 8.0). The mixture was subjected to ultrasonic treatment (20 KHz, 600 W, 5 minutes), and centrifuged at 10,000×g for 15 minutes to thereby obtain a supernatant fraction and a precipitate fraction. Each of the fractions was dissolved in a sample buffer containing of 20 (v/v)% glycerol, 0.1 M Tris.HCl (pH 6.8), 2 (w/v)% SDS, 2 (v/v)% 2-mercaptoethanol and 0.02% BPB, heated at 100° C. for 3 minutes, and subjected to electrophoresis using 0.1% SDS-7.5% polyacrylamide gel to separate protein. After the electrophoresis, the protein was transferred to a nitrocellulose filter by trans blot cell (manufactured and sold by BIO-RAD Co., Ltd., U.S.A.). The filter was immersed in 3% gelatin solution, and allowed to stand still for 60 minutes. The filter was incubated together with serum from a patient suffering from NANB hepatitis, which had been diluted 100-fold, for 2 to 3 hours at room temperature. The filter was washed with distilled water and then with TTBS solution containing 0.02 M Tris.HCl (pH 7.5), 0.5× sodium chloride and 0.05 (v/v)% Tween 20. Subsequently, the washed filter was immersed in a 2,000 fold-diluted solution of peroxidase-labeled anti-human IgG antibody, and incubated at room temperature for 90 minutes. The filter was washed with distilled water and then with TTBS solution. The washed filter was immersed in a buffer having, added thereto, coloring agent DAB and 30%, based on substrate, hydrogen peroxide as described in Step 7 for 5 to 30 minutes, following by washing with water, to terminate the reaction. 
     As a result, as shown in Table 2, all of the antigens produced by the plasmids specifically react with serum from a patient suffering from NANB hepatitis, thereby demonstrating that the proteins produced by the cDNAs inserted in the plasmids are clinically important. 
     
       
         
           
               
             
               
                 TABLE 2 
               
             
            
               
                   
               
               
                 Reactivity evaluated by the Western blot method between 
               
               
                 proteins produced by various plasmids and sera from a 
               
               
                 patient suffering from NANB hepatitis. 
               
            
           
           
               
               
               
               
               
            
               
                   
                   
                   
                 Serum from 
                 Serum from 
               
               
                   
                 origin of 
                   
                 NANB hepati- 
                 healthy 
               
               
                 Plasmid 
                 cDNA 
                 Extract 
                 titis patient 
                 human 
               
               
                   
               
               
                 pCE-066 
                 BK 106 
                 S 
                 ± 
                 − 
               
               
                   
                   
                 P 
                 + 
                 − 
               
               
                 pE-11-89 
                 BK 111 
                 S 
                 ± 
                 − 
               
               
                   
                   
                 P 
                 + 
                 − 
               
               
                 pB-02-10 
                 BK 102 
                 S 
                 + 
                 − 
               
               
                   
                   
                 P 
                 − 
                 − 
               
               
                 ps-09-07 
                 BK 109 
                 S 
                 ± 
                 − 
               
               
                   
                   
                 P 
                 + 
                 − 
               
               
                 pKK233-3 
                 — 
                 S 
                 − 
                 − 
               
               
                   
                   
                 P 
                 − 
                 − 
               
               
                   
               
               
                 S: Supernatant by centrifugation  
               
               
                 P: Precipitate by centrifugation  
               
               
                 +: positive  
               
               
                 ±: slightly positive  
               
               
                 −: negative  
               
            
           
         
       
     
     Step 12 (Purification of NANBV-related antigens produced by  E. coli  and reactivity thereof with serum from a patient suffering from hepatitis) 
     The usefulness of the protein produced by the cDNA which was inserted into an expression vector was demonstrated by purifying the protein and using the purified protein as an antigen for ELISA or radioimmunoassay. That is, the lysate of the transformed  E. coli  which was obtained in Step 11 was subjected to centrifugation at 10,000×g for 15 minutes, thereby obtaining a supernatant and a precipitate. For example, the precipitate obtained from transformant JM 109/pCE 066 was suspended in a solution of 100 mM Tris.HCl (pH 8.0) and 0.1% Triton X-100, and the resultant suspension was subjected to ultrasonic treatment at a frequency of 20 KHz (600 W) for one minute, followed by centrifugation at 21,000×g for 15 minutes, thereby obtaining a precipitate. The precipitate was re-suspended in a solution of 100 mM Tris.HCl (pH 8.0) and 6 M urea, and then subjected to ultrasonic treatment followed by centrifugation. 
     The resultant supernatant was dialyzed against a solution of 10 mM phosphoric acid buffer (pH 7.5) and 6 M urea to thereby obtain an antigen solution. 20 ml of the antigen solution was passed through a column (21.5×250 mm) packed with hydroxyapatite, which had been equilibrated with the above-mentioned buffer, to cause the antigen to be adsorbed onto the packing material. The column was subjected to high speed liquid chromatography (HPLC) wherein elution was performed with the above-mentioned buffer having, added thereto, sodium chloride, the concentration of which was varied from 0 to 2 M with a linear concentration gradient, thereby obtaining a fraction containing an antigen. The obtained fraction was dialyzed against a solution of 50 mM carbonate buffer (pH 9.6) and 0.05% sodium dodecyl sulfate (SDS). 
     Further, the supernatant obtained by centrifugation (at 10,000 g for 15 minutes) of the lysate of transformant JM 109/pB-02-10 was treated with 35% saturated ammonium sulfate, and the obtained precipitate was dissolved in a solution of 50 mM Tris.HCl (pH 8.5) and 100 mM 2-mercaptoethanol. The resultant solution was dialyzed against the above-mentioned buffer. Subsequently, 100 ml of the dialysed solution was passed through a column (22.0×200 mm) packed with DEAE cellulose, which had been equilibrated with the above-mentioned buffer, to cause the antigen to be adsorbed onto the packing material. The column was subjected to high performance liquid chromatography wherein elution was performed with a solution of 50 mM Tris.HCl (pH 8.5) and 100 mM 2-mercaptoethanol having, added thereto, sodium chloride, the concentration of which was varied from 0 to 2 M with a linear concentration gradient, thereby pooling a fraction containing the antigen. 
     The fraction was dialyzed against a solution of 10 mM phosphate buffer (pH 6.8) and 100 mM 2-mercaptoethanol. The dialyzed solution was passed through the column of hydroxyapatite for high performance liquid chromatography, which had been equilibrated by the above-mentioned buffer, to cause the antigen to be adsorbed onto the packing material. The column was subjected to high speed liquid chromatography wherein elution was performed with phosphoric acid, the concentration of which was varied with a linear concentration gradient from 10 to 400 mM, thereby pooling a fraction containing the antigen. The resultant fraction was dialyzed against a solution of 50 mM carbonate buffer (pH 9.6) and 0.05% SDS. 
     The precipitate obtained by centrifugation of the lysate of transformant JM 109/pE-11-89 was suspended in 10 mM phosphate buffer (pH−5.5). The suspension was subjected to the above-mentioned ultrasonic treatment for one minute, and then subjected to centrifugation at 21,000×g for 15 minutes. The resultant precipitate was suspended in a solution of 100 mM carbonate buffer (pH 10.5), 500 mM sodium chloride and 10 mM EDTA. The resultant suspension was again subjected to the ultrasonic treatment for one minute, followed by centrifugation. The resultant supernatant was dialyzed against a solution of 30 mM phosphate buffer and 6 M urea. Subsequently, 20 ml of the dialyzed solution was passed through a CM cellulose column (22×200 mm) for high performance liquid chromatography (HPLC), which had been equilibrated with the same buffer as used for the above-mentioned dialysis, to thereby cause the antigen to be adsorbed onto the packing material. The column was subjected to high performance liquid chromatography wherein elution was performed with the above-mentioned buffer having, added thereto, sodium chloride, the concentration of which was varied from 0 to 1.5 M with a linear concentration gradient, obtaining a fraction containing the antigen. The fraction was dialyzed against a solution containing 50 mM carbonate buffer (pH 9.6) and 0.05% SDS, thereby obtaining a solution containing the antigen. 
     The antigens prepared above were used as an antigen for ELISA for the clinical diagnosis of infection with non-A, non-B hepatitis virus. The protein concentration of each of the above-mentioned purified antigens was adjusted to 1 μg/ml, and put in each well of Microplate Immulone 600 (manufactured and sold by Greiner, Co., Ltd., Germany) in an amount of 100 ml for use in ELISA, which well was allowed to stand still at 4° C. overnight. The contents of the individual wells were washed well three times with PBS-T buffer containing 10 mM phosphate buffer (pH 7.2), 0.8% sodium chloride and 0.05% Tween 20, and sample serum diluted with the PBS-T buffer was added in an amount of 100 μl/well, followed by reaction at 37μC for one hour. The contents of the individual wells were washed three times with the PBS-T buffer, and a peroxidase-labeled anti-human IgG antibody (manufactured and sold by Cappel Co., Ltd., Germany) which had been diluted 8000-fold with PBS-T buffer containing 10% fetal calf serum was added in an amount of 100 μl/well. The individual well contents were reacted at 37° C. for one hour, and washed with the PBS-T buffer four times. A substrate coloring agent solution composed of 9 ml of 0.05 M citric acid-phosphate buffer and, contained therein, 0.5 μg of o-phenylenediamine and 20 μl of aqueous hydrogen peroxide, was added in an amount of 100 μl/well. The plate was light shielded, and allowed to stand still at room temperature for 60 minutes. 75 μl of 4 N sulfuric acid was added to each of the wells, and the absorbance at 490 nm was determined. The results are shown in Table 3. As apparent from the table, all of the antigens derived from the transformants specifically react with the serum from NANB hepatitis patient, thereby attesting to the usefulness in clinical diagnosis of the antigens produced by the transofrmants. 
     
       
         
           
               
             
               
                 TABLE 3 
               
             
            
               
                   
               
               
                 Reactivity in ELISA between the purified antigens from 
               
               
                 various transformed  Escherichia coli  and the serum 
               
               
                 from NANB hepatitis patient 
               
            
           
           
               
               
               
            
               
                 origin of 
                   
                   
               
               
                 antigen 
                 Serum from blood transfused 
                   
               
               
                 (transformed 
                 patient of hepatitis 
                 healthy 
               
            
           
           
               
               
               
               
               
               
            
               
                 
                   Escherichia 
                 
                   
                   
                 hepato- 
                   
                 human 
               
               
                 
                   coli 
                 
                 acute 
                 chronic 
                 cirrhosis 
                 hepatoma 
                 serum 
               
               
                   
               
               
                 JM109/pCE-066 
                  2/3* 
                 7/8 
                 3/4 
                 3/3 
                 0/10 
               
               
                 JM109/pB-02-10 
                 2/3 
                 8/8 
                 4/4 
                 3/3 
                 0/10 
               
               
                 JM109/pE-11-89 
                 2/3 
                 8/8 
                 2/4 
                 3/3 
                 0/10 
               
               
                   
               
               
                 *the number of positive samples/the number of samples examined  
               
            
           
         
       
     
     The same results as shown in Table 3 were also obtained by radioimmunoassay using the above-mentioned antigens. That is, a polystyrene ball of ¼ inch in diameter (manufactured and sold by Pesel Co., Ltd., Germany) was put in 0.2 ml of each of the above-mentioned purified antigen solutions of 1 μg/ml in concentration, and allowed to stand still at 4° C. overnight. Then, the polystyrene ball was washed five times with the same PBS-T buffer as used in the above-mentioned ELISA, and a sample serum diluted 20 to 2500-fold with the PBS-T buffer was added in an amount of 200 μl/ball. Reaction was performed at 37° C. for 60 min. The polystyrene ball was washed five times with the PBS-T buffer, and  125 I-labeled anti-human IgG antibody was added in an amount of 200 μl/ball. Reaction was performed at 37° C. for one hour and the ball was washed five times with the PBS-T buffer. The cpm of  125 I bound to the polystyrene ball was measured, thereby obtaining the same results as shown in Table 3. Thus, the usefulness of the purified antigens obtained above in the clinical diagnosis of infection with NANB hepatitis virus, was demonstrated. 
     APPLICATION EXAMPLE 1 
     (Assay of the reactivity of synthetic polypeptide) 
     The antibody molecule reacts with a specific region structure known as “epitope” which exists on the antigen molecule, to thereby form a bonding therebetween. Such a specific region can be found in the hydrophilic region of the antigen molecule. The antigen polypeptide having such a specific region is believed to be useful for easily preparing a valuable clinical diagnostic reagent with high reaction specificity. The NANBV epitope is presumed from the hydrophilicity/hydrophobicity pattern of the amino acid sequence coded for by the NANBV genomic cDNA shown in FIGS.  2 ( 1 ) to  2 ( 16 ) Namely, polypeptides BKP-106-1, BKP-106-2, BKP-102-1 and BKP-147-1 were prepared, which were respectively comprised of amino acid residues coded for by nucleotide numbers 333 to 422 shown in FIG.  2 ( 1 ), nucleotide numbers 474 to 563 shown in FIG.  2 ( 1 ) through FIG. 2 ( 2 ), nucleotide numbers 4485 to 4574 shown in FIG.  2 ( 8 ), and nucleotide numbers 5544 to 5633 shown in FIG.  2 ( 10 ) of SEQ ID NO: 1. The concentration of each of the prepared polypeptides was adjusted to 1 μg/ml, applied to a microplate for ELISA according to the same method as described in Step 12 to thereby form a solid phase, and examined with respect to the reactivity thereof with the serum from NANB hepatitis patient by the method of ELISA. The results are shown in Table 4. As apparent from the table, all of the prepared polypeptides specifically reacted with the serum from NANB hepatitis patient, thereby demonstrating the importance in clinical diagnosis of the particular regions of nucleotide sequences described above. 
     
       
         
           
               
             
               
                 TABLE 4 
               
             
            
               
                   
               
               
                 Reactivity of synthetic polypeptides with the serum 
               
               
                 from NANB hepatitis patient 
               
            
           
           
               
               
               
               
            
               
                   
                 synthetic 
                 serum from NANB hepatitis patient 
                 healthy 
               
            
           
           
               
               
               
               
               
            
               
                   
                 polypeptides 
                 acute 
                 chronic 
                 human 
               
               
                   
                   
               
               
                   
                 BKP-106-1 
                 2/5 
                 5/5 
                 0/5 
               
               
                   
                 BKP-106-2 
                 2/5 
                 5/5 
                 0/5 
               
               
                   
                 BKP-102-1 
                 3/5 
                 5/5 
                 0/5 
               
               
                   
                 BKP-147-1 
                 2/5 
                 5/5 
                 0/5 
               
               
                   
                   
               
            
           
         
       
     
     Moreover, presuming the epitopes of the envelop protein of NANBV, three types of proteins were prepared. That is, proteins coded for by nucleotide numbers 906 to 953 shown in FIG.  2 ( 2 ), nucleotide numbers 1020 to 1046 shown in FIG.  2 ( 2 ) and nucleotide numbers 1194 to 1232 shown in FIG.  2 ( 2 ) through FIG.  2 ( 3 ) of SEQ ID NO: 1, were prepared. All of the thus prepared polypeptides correspond to the regions of the envelop where antigenic variation is believed to occur depending on the type of the NANBV strain, and the reactivity thereof in ELISA with the serum from a NANB hepatitis patient was confirmed. These attest to the importance and usefulness of the above-mentioned proteins in immunological survey, clinical diagnosis and vaccination. 
     APPLICATION EXAMPLE 2 
     [Detection of NANBV nucleic acid according to PCR (Polymerase Chain Reaction) method] 
     For preventing NANB hepatitis caused by blood transfusion, it is important to determine whether or not any NANBV infection exists in the blood supplied for transfusion. Further, for diagnosing hepatitis, it is extremely clinically important to study whether or not any NANBV infection exists in liver tissue. The NANBV cDNA of the present invention can be advantageously used for producing a primer for polymerase chain reaction (PCR) useful for detecting NANB hepatitis. That is, as described in Step 1, the purification of RNA and the preparation of cDNA were performed from 1 ml of serum. Likewise, cDNA was prepared from liver cells as described in Step 2. Subsequently, as described in Step 4, PCR and electrophoresis were conducted. According to the customary procedure, whether or not the amplified CDNA was derived from NANBV, was investigated by Southern hybridization using  32 P-labeled probe prepared from the cDNA derived from NANBV cDNA clone BK 108. 
     The results are shown in Table 5. From the table, it is apparent that the NANBV nucleic acid in serum can be detected and the serum infection with NANBV can be diagnosed by the use of the primer prepared from the nucleotide sequence of the NANBV CDNA obtained according to the present invention and the fragment of cloned NANBV CDNA as a probe. 
     
       
         
           
               
             
               
                 TABLE 5 
               
             
            
               
                   
               
               
                 Detection of NANBV nucleic acid by PCR 
               
            
           
           
               
               
               
               
            
               
                   
                   
                 antibody 
                   
               
               
                   
                   
                 against 
                   
               
               
                   
                 sample 
                 NANBV 
                 PCR 
               
               
                   
                   
               
               
                   
                 serum from chronic hepatitis patient 
                   
                   
               
            
           
           
               
               
               
               
               
            
               
                   
                 NANB 
                 1 
                 + 
                 + 
               
               
                   
                   
                 2 
                 + 
                 + 
               
               
                   
                 HBV carrier 
                 1 
                 − 
                 − 
               
               
                   
                   
                 2 
                 − 
                 − 
               
               
                   
                 healthy human 
                 1 
                 − 
                 − 
               
               
                   
                   
                 2 
                 − 
                 − 
               
            
           
           
               
               
               
               
            
               
                   
                 excised liver 
                 + 
                   
               
               
                   
                 from NANB hepatoma-1 
               
               
                   
                 cancerous site 
                   
                 + 
               
               
                   
                 non-cancerous site 
                   
                 + 
               
               
                   
                 excised liver 
                 + 
               
               
                   
                 from NANB hepatoma-2 
               
               
                   
                 cancerous site 
                   
                 + 
               
               
                   
                 non-cancerous site 
                   
                 + 
               
               
                   
                   
               
            
           
         
       
     
     
       
         
           
             50 
           
           
             
               9416 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               CDS 
                333..9362 
             
             1
CGATTGGGGG CGACACTCCA CCATAGATCA CTCCCCTGTG AGGAACTACT GTCTTCACGC     60
AGAAAGCGTC TAGCCATGGC GTTAGTATGA GTGTCGTGCA GCCTCCAGGA CCCCCCCTCC    120
CGGGAGAGCC ATAGTGGTCT GCGGAACCGG TGAGTACACC GGAATTGCCA GGACGACCGG    180
GTCCTTTCTT GGATCAACCC GCTCAATGCC TGGAGATTTG GGCGTGCCCC CGCGAGACTG    240
CTAGCCGAGT AGTGTTGGGT CGCGAAAGGC CTTGTGGTAC TGCCTGATAG GGTGCTTGCG    300
AGTGCCCCGG GAGGTCTCGT AGACCGTGCA CC ATG AGC ACG AAT CCT AAA CCT      353
                                    Met Ser Thr Asn Pro Lys Pro
                                      1               5
CAA AGA AAA ACC AAA CGT AAC ACC AAC CGC CGC CCA CAG GAC GTC AAG      401
Gln Arg Lys Thr Lys Arg Asn Thr Asn Arg Arg Pro Gln Asp Val Lys
         10                  15                  20
TTC CCG GGC GGT GGT CAG ATC GTT GGT GGA GTT TAC CTG TTG CCG CGC      449
Phe Pro Gly Gly Gly Gln Ile Val Gly Gly Val Tyr Leu Leu Pro Arg
     25                  30                  35
AGG GGC CCC AGG TTG GGT GTG CGC GCG CCC AGG AAG ACT TCC GAG CGG      497
Arg Gly Pro Arg Leu Gly Val Arg Ala Pro Arg Lys Thr Ser Glu Arg
 40                  45                  50                  55
TCG CAA CCT CGT GGA AGG CGA CAA CCT ATC CCC AAG GCT CGC CGG CCC      545
Ser Gln Pro Arg Gly Arg Arg Gln Pro Ile Pro Lys Ala Arg Arg Pro
                 60                  65                  70
GAG GGC AGG ACC TGG GCT CAG CCC GGG TAC CCT TGG CCT CTC TAT GGC      593
Glu Gly Arg Thr Trp Ala Gln Pro Gly Tyr Pro Trp Pro Leu Tyr Gly
             75                  80                  85
AAT GAG GGC TTA GGG TGG GCA GGA TGG CTC CTG TCA CCC CGC GGC TCC      641
Asn Glu Gly Leu Gly Trp Ala Gly Trp Leu Leu Ser Pro Arg Gly Ser
         90                  95                 100
CGG CCT AGT TGG GGC CCC ACG GAC CCC CGG CGT AGG TCG CGT AAT TTG      689
Arg Pro Ser Trp Gly Pro Thr Asp Pro Arg Arg Arg Ser Arg Asn Leu
    105                 110                 115
GGT AAG GTC ATC GAT ACC CTC ACA TGC GGC TTC GCC GAT CTC ATG GGG      737
Gly Lys Val Ile Asp Thr Leu Thr Cys Gly Phe Ala Asp Leu Met Gly
120                 125                 130                 135
TAC ATT CCG CTC GTC GGC GCC CCC CTG GGG GGC GCT GCC AGG GCC CTG      785
Tyr Ile Pro Leu Val Gly Ala Pro Leu Gly Gly Ala Ala Arg Ala Leu
                140                 145                 150
GCA CAT GGT GTC CGG GTT CTG GAG GAC GGC GTG AAC TAT GCA ACA GGG      833
Ala His Gly Val Arg Val Leu Glu Asp Gly Val Asn Tyr Ala Thr Gly
            155                 160                 165
AAT CTG CCC GGT TGC TCT TTT TCT ATC TTC CTC TTG GCT CTG CTG TCC      881
Asn Leu Pro Gly Cys Ser Phe Ser Ile Phe Leu Leu Ala Leu Leu Ser
        170                 175                 180
TGC CTG ACC ACC CCA GCT TCC GCT TAC GAA GTG CAC AAC GTG TCC GGG      929
Cys Leu Thr Thr Pro Ala Ser Ala Tyr Glu Val His Asn Val Ser Gly
    185                 190                 195
ATA TAT CAT GTC ACG AAC GAC TGC TCC AAC GCA AGC ATT GTG TAT GAG      977
Ile Tyr His Val Thr Asn Asp Cys Ser Asn Ala Ser Ile Val Tyr Glu
200                 205                 210                 215
GCA GCG GAC TTG ATC ATG CAT ACT CCT GGG TGC GTG CCC TGC GTT CGG     1025
Ala Ala Asp Leu Ile Met His Thr Pro Gly Cys Val Pro Cys Val Arg
                220                 225                 230
GAA GGC AAC TCC TCC CGC TGC TGG GTA GCG CTC ACT CCC ACG CTC GCA     1073
Glu Gly Asn Ser Ser Arg Cys Trp Val Ala Leu Thr Pro Thr Leu Ala
            235                 240                 245
GCC AGG AAC GTC ACC ATC CCC ACC ACG ACG ATA CGA CGC CAC GTC GAT     1121
Ala Arg Asn Val Thr Ile Pro Thr Thr Thr Ile Arg Arg His Val Asp
        250                 255                 260
CTG CTC GTT GGG GCG GCT GCT TTC TGT TCC GCT ATG TAC GTG GGG GAC     1169
Leu Leu Val Gly Ala Ala Ala Phe Cys Ser Ala Met Tyr Val Gly Asp
    265                 270                 275
CTC TGC GGA TCT GTT TTC CTC GTC TCT CAG CTG TTC ACC TTC TCG CCT     1217
Leu Cys Gly Ser Val Phe Leu Val Ser Gln Leu Phe Thr Phe Ser Pro
280                 285                 290                 295
CGC CGG CAT GTG ACA TTA CAG GAC TGT AAC TGC TCA ATT TAT CCC GGC     1265
Arg Arg His Val Thr Leu Gln Asp Cys Asn Cys Ser Ile Tyr Pro Gly
                300                 305                 310
CAT GTG TCG GGT CAC CGT ATG GCT TGG GAC ATG ATG ATG AAC TGG TCG     1313
His Val Ser Gly His Arg Met Ala Trp Asp Met Met Met Asn Trp Ser
            315                 320                 325
CCC ACA ACA GCC CTA GTG GTG TCG CAG TTA CTC CGG ATC CCA CAA GCC     1361
Pro Thr Thr Ala Leu Val Val Ser Gln Leu Leu Arg Ile Pro Gln Ala
        330                 335                 340
GTC GTG GAC ATG GTG GCG GGG GCC CAC TGG GGA GTC CTG GCG GGC CTT     1409
Val Val Asp Met Val Ala Gly Ala His Trp Gly Val Leu Ala Gly Leu
    345                 350                 355
GCC TAC TAT TCC ATG GCG GGG AAC TGG GCT AAG GTT CTG ATT GTG ATG     1457
Ala Tyr Tyr Ser Met Ala Gly Asn Trp Ala Lys Val Leu Ile Val Met
360                 365                 370                 375
CTA CTT TTT GCT GGC GTT GAC GGG GAT ACC CAC GTG ACA GGG GGG GCG     1505
Leu Leu Phe Ala Gly Val Asp Gly Asp Thr His Val Thr Gly Gly Ala
                380                 385                 390
CAA GCC AAA ACC ACC AAC AGG CTC GTG TCC ATG TTC GCA AGT GGG CCG     1553
Gln Ala Lys Thr Thr Asn Arg Leu Val Ser Met Phe Ala Ser Gly Pro
            395                 400                 405
TCT CAG AAA ATC CAG CTT ATA AAC ACC AAT GGG AGT TGG CAC ATC AAC     1601
Ser Gln Lys Ile Gln Leu Ile Asn Thr Asn Gly Ser Trp His Ile Asn
        410                 415                 420
AGG ACT GCC CTG AAC TGC AAT GAC TCT CTC CAG ACT GGG TTT CTT GCC     1649
Arg Thr Ala Leu Asn Cys Asn Asp Ser Leu Gln Thr Gly Phe Leu Ala
    425                 430                 435
GCG CTG TTC TAC ACA CAT AGT TTC AAC TCG TCC GGG TGC CCA GAG CGC     1697
Ala Leu Phe Tyr Thr His Ser Phe Asn Ser Ser Gly Cys Pro Glu Arg
440                 445                 450                 455
ATG GCC CAG TGC CGC ACC ATT GAC AAG TTC GAC CAG GGA TGG GGT CCC     1745
Met Ala Gln Cys Arg Thr Ile Asp Lys Phe Asp Gln Gly Trp Gly Pro
                460                 465                 470
ATT ACT TAT GCT GAG TCT AGC AGA TCA GAC CAG AGG CCA TAT TGC TGG     1793
Ile Thr Tyr Ala Glu Ser Ser Arg Ser Asp Gln Arg Pro Tyr Cys Trp
            475                 480                 485
CAC TAC CCA CCT CCA CAA TGT ACC ATC GTA CCT GCG TCG GAG GTG TGC     1841
His Tyr Pro Pro Pro Gln Cys Thr Ile Val Pro Ala Ser Glu Val Cys
        490                 495                 500
GGC CCA GTG TAC TGC TTC ACC CCA AGC CCT GTC GTC GTG GGG ACG ACC     1889
Gly Pro Val Tyr Cys Phe Thr Pro Ser Pro Val Val Val Gly Thr Thr
    505                 510                 515
GAT CGT TTC GGT GTC CCT ACG TAT AGA TGG GGG GAG AAC GAG ACT GAC     1937
Asp Arg Phe Gly Val Pro Thr Tyr Arg Trp Gly Glu Asn Glu Thr Asp
520                 525                 530                 535
GTG CTG CTG CTC AAC AAC ACG CGG CCG CCG CAA GGC AAC TGG TTC GGC     1985
Val Leu Leu Leu Asn Asn Thr Arg Pro Pro Gln Gly Asn Trp Phe Gly
                540                 545                 550
TGC ACA TGG ATG AAT AGC ACC GGG TTC ACC AAG ACA TGT GGG GGG CCC     2033
Cys Thr Trp Met Asn Ser Thr Gly Phe Thr Lys Thr Cys Gly Gly Pro
            555                 560                 565
CCG TGT AAC ATC GGG GGG GTC GGC AAC AAC ACC CTG ACC TGC CCC ACG     2081
Pro Cys Asn Ile Gly Gly Val Gly Asn Asn Thr Leu Thr Cys Pro Thr
        570                 575                 580
GAC TGC TTC CGG AAG CAC CCC GAG GCT ACC TAC ACA AAA TGT GGT TCG     2129
Asp Cys Phe Arg Lys His Pro Glu Ala Thr Tyr Thr Lys Cys Gly Ser
    585                 590                 595
GGG CCT TGG CTG ACA CCT AGG TGC ATG GTT GAC TAT CCA TAC AGG CTC     2177
Gly Pro Trp Leu Thr Pro Arg Cys Met Val Asp Tyr Pro Tyr Arg Leu
600                 605                 610                 615
TGG CAT TAC CCC TGC ACT GTT AAC TTT ACC ATC TTC AAG GTT AGG ATG     2225
Trp His Tyr Pro Cys Thr Val Asn Phe Thr Ile Phe Lys Val Arg Met
                620                 625                 630
TAT GTG GGG GGG GTG GAG CAC AGG CTC AAT GCT GCA TGC AAT TGG ACC     2273
Tyr Val Gly Gly Val Glu His Arg Leu Asn Ala Ala Cys Asn Trp Thr
            635                 640                 645
CGA GGA GAG CGT TGT GAC TTG GAG GAC AGG GAT AGG CCG GAG CTC AGC     2321
Arg Gly Glu Arg Cys Asp Leu Glu Asp Arg Asp Arg Pro Glu Leu Ser
        650                 655                 660
CCG CTG CTG CTG TCT ACA ACA GAG TGG CAG GTA CTG CCC TGT TCC TTC     2369
Pro Leu Leu Leu Ser Thr Thr Glu Trp Gln Val Leu Pro Cys Ser Phe
    665                 670                 675
ACC ACC CTA CCA GCT CTG TCC ACT GGC TTG ATT CAC CTC CAT CAG AAC     2417
Thr Thr Leu Pro Ala Leu Ser Thr Gly Leu Ile His Leu His Gln Asn
680                 685                 690                 695
ATC GTG GAC GTG CAA TAC CTA TAC GGT ATA GGG TCA GCG GTT GTC TCC     2465
Ile Val Asp Val Gln Tyr Leu Tyr Gly Ile Gly Ser Ala Val Val Ser
                700                 705                 710
TTT GCA ATC AAA TGG GAG TAT GTC CTG TTG CTT TTC CTT CTC CTA GCG     2513
Phe Ala Ile Lys Trp Glu Tyr Val Leu Leu Leu Phe Leu Leu Leu Ala
            715                 720                 725
GAC GCA CGT GTC TGT GCC TGC TTG TGG ATG ATG CTG CTG ATA GCC CAG     2561
Asp Ala Arg Val Cys Ala Cys Leu Trp Met Met Leu Leu Ile Ala Gln
        730                 735                 740
GCC GAG GCC GCC TTG GAG AAC CTG GTG GTC CTC AAT TCG GCG TCT GTG     2609
Ala Glu Ala Ala Leu Glu Asn Leu Val Val Leu Asn Ser Ala Ser Val
    745                 750                 755
GCC GGC GCA CAT GGC ATC CTC TCC TTC CTT GTG TTC TTC TGT GCC GCC     2657
Ala Gly Ala His Gly Ile Leu Ser Phe Leu Val Phe Phe Cys Ala Ala
760                 765                 770                 775
TGG TAC ATC AAA GGC AGG CTG GTC CCT GGG GCG ACA TAT GCT CTT TAT     2705
Trp Tyr Ile Lys Gly Arg Leu Val Pro Gly Ala Thr Tyr Ala Leu Tyr
                780                 785                 790
GGC GTG TGG CCG CTG CTC CTG CTC TTG CTG GCA TTA CCA CCG CGA GCT     2753
Gly Val Trp Pro Leu Leu Leu Leu Leu Leu Ala Leu Pro Pro Arg Ala
            795                 800                 805
TAC GCC ATG GAC CGG GAG ATG GCT GCA TCG TGC GGA GGC GCG GTT TTT     2801
Tyr Ala Met Asp Arg Glu Met Ala Ala Ser Cys Gly Gly Ala Val Phe
        810                 815                 820
GTG GGT CTG GTA CTC CTG ACT TTG TCA CCA TAC TAC AAG GTG TTC CTC     2849
Val Gly Leu Val Leu Leu Thr Leu Ser Pro Tyr Tyr Lys Val Phe Leu
    825                 830                 835
GCT AGG CTC ATA TGG TGG TTA CAA TAT TTT ACC ACC AGA GCC GAG GCG     2897
Ala Arg Leu Ile Trp Trp Leu Gln Tyr Phe Thr Thr Arg Ala Glu Ala
840                 845                 850                 855
GAC TTA CAT GTG TGG ATC CCC CCC CTC AAC GCT CGG GGA GGC CGC GAT     2945
Asp Leu His Val Trp Ile Pro Pro Leu Asn Ala Arg Gly Gly Arg Asp
                860                 865                 870
GCC ATC ATC CTC CTC ATG TGC GCA GTC CAT CCA GAG CTA ATC TTT GAC     2993
Ala Ile Ile Leu Leu Met Cys Ala Val His Pro Glu Leu Ile Phe Asp
            875                 880                 885
ATC ACC AAA CTT CTA ATT GCC ATA CTC GGT CCG CTC ATG GTG CTC CAA     3041
Ile Thr Lys Leu Leu Ile Ala Ile Leu Gly Pro Leu Met Val Leu Gln
        890                 895                 900
GCT GGC ATA ACC AGA GTG CCG TAC TTC GTG CGC GCT CAA GGG CTC ATT     3089
Ala Gly Ile Thr Arg Val Pro Tyr Phe Val Arg Ala Gln Gly Leu Ile
    905                 910                 915
CAT GCA TGC ATG TTA GTG CGG AAG GTC GCT GGG GGT CAT TAT GTC CAA     3137
His Ala Cys Met Leu Val Arg Lys Val Ala Gly Gly His Tyr Val Gln
920                 925                 930                 935
ATG GCC TTC ATG AAG CTG GGC GCG CTG ACA GGC ACG TAC ATT TAC AAC     3185
Met Ala Phe Met Lys Leu Gly Ala Leu Thr Gly Thr Tyr Ile Tyr Asn
                940                 945                 950
CAT CTT ACC CCG CTA CGG GAT TGG CCA CGC GCG GGC CTA CGA GAC CTT     3233
His Leu Thr Pro Leu Arg Asp Trp Pro Arg Ala Gly Leu Arg Asp Leu
            955                 960                 965
GCG GTG GCA GTG GAG CCC GTC GTC TTC TCC GAC ATG GAG ACC AAG ATC     3281
Ala Val Ala Val Glu Pro Val Val Phe Ser Asp Met Glu Thr Lys Ile
        970                 975                 980
ATC ACC TGG GGA GCA GAC ACC GCG GCG TGT GGG GAC ATC ATC TTG GGT     3329
Ile Thr Trp Gly Ala Asp Thr Ala Ala Cys Gly Asp Ile Ile Leu Gly
    985                 990                 995
CTG CCC GTC TCC GCC CGA AGG GGA AAG GAG ATA CTC CTG GGC CCG GCC     3377
Leu Pro Val Ser Ala Arg Arg Gly Lys Glu Ile Leu Leu Gly Pro Ala
1000                1005                1010                1015
GAT AGT CTT GAA GGG CGG GGG TTG CGA CTC CTC GCG CCC ATC ACG GCC     3425
Asp Ser Leu Glu Gly Arg Gly Leu Arg Leu Leu Ala Pro Ile Thr Ala
                1020                1025                1030
TAC TCC CAA CAG ACG CGG GGC CTA CTT GGT TGC ATC ATC ACT AGC CTT     3473
Tyr Ser Gln Gln Thr Arg Gly Leu Leu Gly Cys Ile Ile Thr Ser Leu
            1035                1040                1045
ACA GGC CGG GAC AAG AAC CAG GTC GAG GGA GAG GTT CAG GTG GTT TCC     3521
Thr Gly Arg Asp Lys Asn Gln Val Glu Gly Glu Val Gln Val Val Ser
        1050                1055                1060
ACC GCA ACA CAA TCC TTC CTG GCG ACC TGC GTC AAC GGC GTG TGT TGG     3569
Thr Ala Thr Gln Ser Phe Leu Ala Thr Cys Val Asn Gly Val Cys Trp
    1065                1070                1075
ACC GTT TAC CAT GGT GCT GGC TCA AAG ACC TTA GCC GCG CCA AAG GGG     3617
Thr Val Tyr His Gly Ala Gly Ser Lys Thr Leu Ala Ala Pro Lys Gly
1080                1085                1090                1095
CCA ATC ACC CAG ATG TAC ACT AAT GTG GAC CAG GAC CTC GTC GGC TGG     3665
Pro Ile Thr Gln Met Tyr Thr Asn Val Asp Gln Asp Leu Val Gly Trp
                1100                1105                1110
CCC AAG CCC CCC GGG GCG CGT TCC TTG ACA CCA TGC ACC TGT GGC AGC     3713
Pro Lys Pro Pro Gly Ala Arg Ser Leu Thr Pro Cys Thr Cys Gly Ser
            1115                1120                1125
TCA GAC CTT TAC TTG GTC ACG AGA CAT GCT GAC GTC ATT CCG GTG CGC     3761
Ser Asp Leu Tyr Leu Val Thr Arg His Ala Asp Val Ile Pro Val Arg
        1130                1135                1140
CGG CGG GGC GAC AGT AGG GGG AGC CTG CTC TCC CCC AGG CCT GTC TCC     3809
Arg Arg Gly Asp Ser Arg Gly Ser Leu Leu Ser Pro Arg Pro Val Ser
    1145                1150                1155
TAC TTG AAG GGC TCT TCG GGT GGT CCA CTG CTC TGC CCC TTC GGG CAC     3857
Tyr Leu Lys Gly Ser Ser Gly Gly Pro Leu Leu Cys Pro Phe Gly His
1160                1165                1170                1175
GCT GTG GGC ATC TTC CGG GCT GCC GTA TGC ACC CGG GGG GTT GCG AAG     3905
Ala Val Gly Ile Phe Arg Ala Ala Val Cys Thr Arg Gly Val Ala Lys
                1180                1185                1190
GCG GTG GAC TTT GTG CCC GTA GAG TCC ATG GAA ACT ACT ATG CGG TCT     3953
Ala Val Asp Phe Val Pro Val Glu Ser Met Glu Thr Thr Met Arg Ser
            1195                1200                1205
CCG GTC TTC ACG GAC AAC TCA TCC CCC CCG GCC GTA CCG CAG TCA TTT     4001
Pro Val Phe Thr Asp Asn Ser Ser Pro Pro Ala Val Pro Gln Ser Phe
        1210                1215                1220
CAA GTG GCC CAC CTA CAC GCT CCC ACT GGC AGC GGC AAG AGT ACT AAA     4049
Gln Val Ala His Leu His Ala Pro Thr Gly Ser Gly Lys Ser Thr Lys
    1225                1230                1235
GTG CCG GCT GCA TAT GCA GCC CAA GGG TAC AAG GTG CTC GTC CTC AAT     4097
Val Pro Ala Ala Tyr Ala Ala Gln Gly Tyr Lys Val Leu Val Leu Asn
1240                1245                1250                1255
CCG TCC GTT GCC GCT ACC TTA GGG TTT GGG GCG TAT ATG TCT AAG GCA     4145
Pro Ser Val Ala Ala Thr Leu Gly Phe Gly Ala Tyr Met Ser Lys Ala
                1260                1265                1270
CAC GGT ATT GAC CCC AAC ATC AGA ACT GGG GTA AGG ACC ATT ACC ACA     4193
His Gly Ile Asp Pro Asn Ile Arg Thr Gly Val Arg Thr Ile Thr Thr
            1275                1280                1285
GGC GCC CCC GTC ACA TAC TCT ACC TAT GGC AAG TTT CTT GCC GAT GGT     4241
Gly Ala Pro Val Thr Tyr Ser Thr Tyr Gly Lys Phe Leu Ala Asp Gly
        1290                1295                1300
GGT TGC TCT GGG GGC GCT TAT GAC ATC ATA ATA TGT GAT GAG TGC CAT     4289
Gly Cys Ser Gly Gly Ala Tyr Asp Ile Ile Ile Cys Asp Glu Cys His
    1305                1310                1315
TCA ACT GAC TCG ACT ACA ATC TTG GGC ATC GGC ACA GTC CTG GAC CAA     4337
Ser Thr Asp Ser Thr Thr Ile Leu Gly Ile Gly Thr Val Leu Asp Gln
1320                1325                1330                1335
GCG GAG ACG GCT GGA GCG CGG CTT GTC GTG CTC GCC ACC GCT ACG CCT     4385
Ala Glu Thr Ala Gly Ala Arg Leu Val Val Leu Ala Thr Ala Thr Pro
                1340                1345                1350
CCG GGA TCG GTC ACC GTG CCA CAC CCA AAC ATC GAG GAG GTG GCC CTG     4433
Pro Gly Ser Val Thr Val Pro His Pro Asn Ile Glu Glu Val Ala Leu
            1355                1360                1365
TCT AAT ACT GGA GAG ATC CCC TTC TAT GGC AAA GCC ATC CCC ATT GAA     4481
Ser Asn Thr Gly Glu Ile Pro Phe Tyr Gly Lys Ala Ile Pro Ile Glu
        1370                1375                1380
GCC ATC AGG GGG GGA AGG CAT CTC ATT TTC TGT CAT TCC AAG AAG AAG     4529
Ala Ile Arg Gly Gly Arg His Leu Ile Phe Cys His Ser Lys Lys Lys
    1385                1390                1395
TGC GAC GAG CTC GCC GCA AAG CTG TCA GGC CTC GGA ATC AAC GCT GTG     4577
Cys Asp Glu Leu Ala Ala Lys Leu Ser Gly Leu Gly Ile Asn Ala Val
1400                1405                1410                1415
GCG TAT TAC CGG GGG CTC GAT GTG TCC GTC ATA CCA ACT ATC GGA GAC     4625
Ala Tyr Tyr Arg Gly Leu Asp Val Ser Val Ile Pro Thr Ile Gly Asp
                1420                1425                1430
GTC GTT GTC GTG GCA ACA GAC GCT CTG ATG ACG GGC TAT ACG GGC GAC     4673
Val Val Val Val Ala Thr Asp Ala Leu Met Thr Gly Tyr Thr Gly Asp
            1435                1440                1445
TTT GAC TCA GTG ATC GAC TGT AAC ACA TGT GTC ACC CAG ACA GTC GAC     4721
Phe Asp Ser Val Ile Asp Cys Asn Thr Cys Val Thr Gln Thr Val Asp
        1450                1455                1460
TTC AGC TTG GAT CCC ACC TTC ACC ATT GAG ACG ACG ACC GTG CCT CAA     4769
Phe Ser Leu Asp Pro Thr Phe Thr Ile Glu Thr Thr Thr Val Pro Gln
    1465                1470                1475
GAC GCA GTG TCG CGC TCG CAG CGG CGG GGT AGG ACT GGC AGG GGT AGG     4817
Asp Ala Val Ser Arg Ser Gln Arg Arg Gly Arg Thr Gly Arg Gly Arg
1480                1485                1490                1495
AGA GGC ATC TAC AGG TTT GTG ACT CCG GGA GAA CGG CCC TCG GGC ATG     4865
Arg Gly Ile Tyr Arg Phe Val Thr Pro Gly Glu Arg Pro Ser Gly Met
                1500                1505                1510
TTC GAT TCC TCG GTC CTG TGT GAG TGC TAT GAC GCG GGC TGT GCT TGG     4913
Phe Asp Ser Ser Val Leu Cys Glu Cys Tyr Asp Ala Gly Cys Ala Trp
            1515                1520                1525
TAC GAG CTC ACC CCG GCC GAG ACC TCG GTT AGG TTG CGG GCC TAC CTG     4961
Tyr Glu Leu Thr Pro Ala Glu Thr Ser Val Arg Leu Arg Ala Tyr Leu
        1530                1535                1540
AAC ACA CCA GGG TTG CCC GTT TGC CAG GAC CAC CTG GAG TTC TGG GAG     5009
Asn Thr Pro Gly Leu Pro Val Cys Gln Asp His Leu Glu Phe Trp Glu
    1545                1550                1555
AGT GTC TTC ACA GGC CTC ACC CAT ATA GAT GCA CAC TTC TTG TCC CAG     5057
Ser Val Phe Thr Gly Leu Thr His Ile Asp Ala His Phe Leu Ser Gln
1560                1565                1570                1575
ACC AAG CAG GCA GGA GAC AAC TTC CCC TAC CTG GTA GCA TAC CAA GCC     5105
Thr Lys Gln Ala Gly Asp Asn Phe Pro Tyr Leu Val Ala Tyr Gln Ala
                1580                1585                1590
ACG GTG TGC GCC AGG GCT CAG GCC CCA CCT CCA TCA TGG GAT CAA ATG     5153
Thr Val Cys Ala Arg Ala Gln Ala Pro Pro Pro Ser Trp Asp Gln Met
            1595                1600                1605
TGG AAG TGT CTC ATA CGG CTG AAA CCT ACG CTG CAC GGG CCA ACA CCC     5201
Trp Lys Cys Leu Ile Arg Leu Lys Pro Thr Leu His Gly Pro Thr Pro
        1610                1615                1620
TTG CTG TAC AGG CTG GGA GCC GTC CAG AAT GAG GTC ACC CTC ACC CAC     5249
Leu Leu Tyr Arg Leu Gly Ala Val Gln Asn Glu Val Thr Leu Thr His
    1625                1630                1635
CCC ATA ACC AAA TAC ATC ATG GCA TGC ATG TCG GCT GAC CTG GAG GTC     5297
Pro Ile Thr Lys Tyr Ile Met Ala Cys Met Ser Ala Asp Leu Glu Val
1640                1645                1650                1655
GTC ACT AGC ACC TGG GTG CTG GTG GGC GGA GTC CTT GCA GCT CTG GCC     5345
Val Thr Ser Thr Trp Val Leu Val Gly Gly Val Leu Ala Ala Leu Ala
                1660                1665                1670
GCG TAT TGC CTG ACA ACA GGC AGT GTG GTC ATT GTG GGT AGG ATT ATC     5393
Ala Tyr Cys Leu Thr Thr Gly Ser Val Val Ile Val Gly Arg Ile Ile
            1675                1680                1685
TTG TCC GGG AGG CCG GCC ATT GTT CCC GAC AGG GAG CTT CTC TAC CAG     5441
Leu Ser Gly Arg Pro Ala Ile Val Pro Asp Arg Glu Leu Leu Tyr Gln
        1690                1695                1700
GAG TTC GAT GAA ATG GAA GAG TGC GCC TCG CAC CTC CCT TAC ATC GAG     5489
Glu Phe Asp Glu Met Glu Glu Cys Ala Ser His Leu Pro Tyr Ile Glu
    1705                1710                1715
CAG GGA ATG CAG CTC GCC GAG CAA TTC AAG CAG AAA GCG CTC GGG TTA     5537
Gln Gly Met Gln Leu Ala Glu Gln Phe Lys Gln Lys Ala Leu Gly Leu
1720                1725                1730                1735
CTG CAA ACA GCC ACC AAA CAA GCG GAG GCT GCT GCT CCC GTG GTG GAG     5585
Leu Gln Thr Ala Thr Lys Gln Ala Glu Ala Ala Ala Pro Val Val Glu
                1740                1745                1750
TCC AAG TGG CGA GCC CTT GAG ACA TTC TGG GCG AAG CAC ATG TGG AAT     5633
Ser Lys Trp Arg Ala Leu Glu Thr Phe Trp Ala Lys His Met Trp Asn
            1755                1760                1765
TTC ATC AGC GGG ATA CAG TAC TTA GCA GGC TTA TCC ACT CTG CCT GGG     5681
Phe Ile Ser Gly Ile Gln Tyr Leu Ala Gly Leu Ser Thr Leu Pro Gly
        1770                1775                1780
AAC CCC GCA ATA GCA TCA TTG ATG GCA TTC ACA GCC TCT ATC ACC AGC     5729
Asn Pro Ala Ile Ala Ser Leu Met Ala Phe Thr Ala Ser Ile Thr Ser
    1785                1790                1795
CCG CTC ACC ACC CAA AGT ACC CTC CTG TTT AAC ATC TTG GGG GGG TGG     5777
Pro Leu Thr Thr Gln Ser Thr Leu Leu Phe Asn Ile Leu Gly Gly Trp
1800                1805                1810                1815
GTG GCT GCC CAA CTC GCC CCC CCC AGC GCC GCT TCG GCT TTC GTG GGC     5825
Val Ala Ala Gln Leu Ala Pro Pro Ser Ala Ala Ser Ala Phe Val Gly
                1820                1825                1830
GCC GGC ATC GCC GGT GCG GCT GTT GGC AGC ATA GGC CTT GGG AAG GTG     5873
Ala Gly Ile Ala Gly Ala Ala Val Gly Ser Ile Gly Leu Gly Lys Val
            1835                1840                1845
CTT GTG GAC ATT CTG GCG GGT TAT GGA GCA GGA GTG GCC GGC GCG CTC     5921
Leu Val Asp Ile Leu Ala Gly Tyr Gly Ala Gly Val Ala Gly Ala Leu
        1850                1855                1860
GTG GCC TTT AAG GTC ATG AGC GGC GAG ATG CCC TCC ACC GAG GAC CTG     5969
Val Ala Phe Lys Val Met Ser Gly Glu Met Pro Ser Thr Glu Asp Leu
    1865                1870                1875
GTC AAT CTA CTT CCT GCC ATC CTC TCT CCT GGC GCC CTG GTC GTC GGG     6017
Val Asn Leu Leu Pro Ala Ile Leu Ser Pro Gly Ala Leu Val Val Gly
1880                1885                1890                1895
GTC GTG TGT GCA GCA ATA CTG CGT CGA CAC GTG GGT CCG GGA GAG GGG     6065
Val Val Cys Ala Ala Ile Leu Arg Arg His Val Gly Pro Gly Glu Gly
                1900                1905                1910
GCT GTG CAG TGG ATG AAC CGG CTG ATA GCG TTC GCC TCG CGG GGT AAT     6113
Ala Val Gln Trp Met Asn Arg Leu Ile Ala Phe Ala Ser Arg Gly Asn
            1915                1920                1925
CAT GTT TCC CCC ACG CAC TAT GTG CCT GAG AGC GAC GCC GCA GCG CGT     6161
His Val Ser Pro Thr His Tyr Val Pro Glu Ser Asp Ala Ala Ala Arg
        1930                1935                1940
GTT ACT CAG ATC CTC TCC AGC CTT ACC ATC ACT CAG CTG CTG AAA AGG     6209
Val Thr Gln Ile Leu Ser Ser Leu Thr Ile Thr Gln Leu Leu Lys Arg
    1945                1950                1955
CTC CAC CAG TGG ATT AAT GAA GAC TGC TCC ACA CCG TGT TCC GGC TCG     6257
Leu His Gln Trp Ile Asn Glu Asp Cys Ser Thr Pro Cys Ser Gly Ser
1960                1965                1970                1975
TGG CTA AGG GAT GTT TGG GAC TGG ATA TGC ACG GTG TTG ACT GAC TTC     6305
Trp Leu Arg Asp Val Trp Asp Trp Ile Cys Thr Val Leu Thr Asp Phe
                1980                1985                1990
AAG ACC TGG CTC CAG TCC AAG CTC CTG CCG CAG CTA CCT GGA GTC CCT     6353
Lys Thr Trp Leu Gln Ser Lys Leu Leu Pro Gln Leu Pro Gly Val Pro
            1995                2000                2005
TTT TTC TCG TGC CAA CGC GGG TAC AAG GGA GTC TGG CGG GGA GAC GGC     6401
Phe Phe Ser Cys Gln Arg Gly Tyr Lys Gly Val Trp Arg Gly Asp Gly
        2010                2015                2020
ATC ATG CAA ACC ACC TGC CCA TGT GGA GCA CAG ATC ACC GGA CAT GTC     6449
Ile Met Gln Thr Thr Cys Pro Cys Gly Ala Gln Ile Thr Gly His Val
    2025                2030                2035
AAA AAC GGT TCC ATG AGG ATC GTC GGG CCT AAG ACC TGC AGC AAC ACG     6497
Lys Asn Gly Ser Met Arg Ile Val Gly Pro Lys Thr Cys Ser Asn Thr
2040                2045                2050                2055
TGG CAT GGA ACA TTC CCC ATC AAC GCA TAC ACC ACG GGC CCC TGC ACA     6545
Trp His Gly Thr Phe Pro Ile Asn Ala Tyr Thr Thr Gly Pro Cys Thr
                2060                2065                2070
CCC TCT CCA GCG CCA AAC TAT TCT AGG GCG CTG TGG CGG GTG GCC GCT     6593
Pro Ser Pro Ala Pro Asn Tyr Ser Arg Ala Leu Trp Arg Val Ala Ala
            2075                2080                2085
GAG GAG TAC GTG GAG GTC ACG CGG GTG GGG GAT TTC CAC TAC GTG ACG     6641
Glu Glu Tyr Val Glu Val Thr Arg Val Gly Asp Phe His Tyr Val Thr
        2090                2095                2100
GGC ATG ACC ACT GAC AAC GTA AAG TGC CCA TGC CAG GTT CCG GCT CCT     6689
Gly Met Thr Thr Asp Asn Val Lys Cys Pro Cys Gln Val Pro Ala Pro
    2105                2110                2115
GAA TTC TTC TCG GAG GTG GAC GGA GTG CGG TTG CAC AGG TAC GCT CCG     6737
Glu Phe Phe Ser Glu Val Asp Gly Val Arg Leu His Arg Tyr Ala Pro
2120                2125                2130                2135
GCG TGC AGG CCT CTC CTA CGG GAG GAG GTT ACA TTC CAG GTC GGG CTC     6785
Ala Cys Arg Pro Leu Leu Arg Glu Glu Val Thr Phe Gln Val Gly Leu
                2140                2145                2150
AAC CAA TAC CTG GTT GGG TCA CAG CTA CCA TGC GAG CCC GAA CCG GAT     6833
Asn Gln Tyr Leu Val Gly Ser Gln Leu Pro Cys Glu Pro Glu Pro Asp
            2155                2160                2165
GTA GCA GTG CTC ACT TCC ATG CTC ACC GAC CCC TCC CAC ATC ACA GCA     6881
Val Ala Val Leu Thr Ser Met Leu Thr Asp Pro Ser His Ile Thr Ala
        2170                2175                2180
GAA ACG GCT AAG CGT AGG TTG GCC AGG GGG TCT CCC CCC TCC TTG GCC     6929
Glu Thr Ala Lys Arg Arg Leu Ala Arg Gly Ser Pro Pro Ser Leu Ala
    2185                2190                2195
AGC TCT TCA GCT AGC CAG TTG TCT GCG CCT TCC TTG AAG GCG ACA TGC     6977
Ser Ser Ser Ala Ser Gln Leu Ser Ala Pro Ser Leu Lys Ala Thr Cys
2200                2205                2210                2215
ACT ACC CAC CAT GTC TCT CCG GAC GCT GAC CTC ATC GAG GCC AAC CTC     7025
Thr Thr His His Val Ser Pro Asp Ala Asp Leu Ile Glu Ala Asn Leu
                2220                2225                2230
CTG TGG CGG CAG GAG ATG GGC GGG AAC ATC ACC CGC GTG GAG TCG GAG     7073
Leu Trp Arg Gln Glu Met Gly Gly Asn Ile Thr Arg Val Glu Ser Glu
            2235                2240                2245
AAC AAG GTG GTA GTC CTG GAC TCT TTC GAC CCG CTT CGA GCG GAG GAG     7121
Asn Lys Val Val Val Leu Asp Ser Phe Asp Pro Leu Arg Ala Glu Glu
        2250                2255                2260
GAT GAG AGG GAA GTA TCC GTT CCG GCG GAG ATC CTG CGG AAA TCC AAG     7169
Asp Glu Arg Glu Val Ser Val Pro Ala Glu Ile Leu Arg Lys Ser Lys
    2265                2270                2275
AAG TTC CCC GCA GCG ATG CCC ATC TGG GCG CGC CCG GAT TAC AAC CCT     7217
Lys Phe Pro Ala Ala Met Pro Ile Trp Ala Arg Pro Asp Tyr Asn Pro
2280                2285                2290                2295
CCA CTG TTA GAG TCC TGG AAG GAC CCG GAC TAC GTC CCT CCG GTG GTG     7265
Pro Leu Leu Glu Ser Trp Lys Asp Pro Asp Tyr Val Pro Pro Val Val
                2300                2305                2310
CAC GGG TGC CCG TTG CCA CCT ATC AAG GCC CCT CCA ATA CCA CCT CCA     7313
His Gly Cys Pro Leu Pro Pro Ile Lys Ala Pro Pro Ile Pro Pro Pro
            2315                2320                2325
CGG AGA AAG AGG ACG GTT GTC CTA ACA GAG TCC TCC GTG TCT TCT GCC     7361
Arg Arg Lys Arg Thr Val Val Leu Thr Glu Ser Ser Val Ser Ser Ala
        2330                2335                2340
TTA GCG GAG CTC GCT ACT AAG ACC TTC GGC AGC TCC GAA TCA TCG GCC     7409
Leu Ala Glu Leu Ala Thr Lys Thr Phe Gly Ser Ser Glu Ser Ser Ala
    2345                2350                2355
GTC GAC AGC GGC ACG GCG ACC GCC CTT CCT GAC CAG GCC TCC GAC GAC     7457
Val Asp Ser Gly Thr Ala Thr Ala Leu Pro Asp Gln Ala Ser Asp Asp
2360                2365                2370                2375
GGT GAC AAA GGA TCC GAC GTT GAG TCG TAC TCC TCC ATG CCC CCC CTT     7505
Gly Asp Lys Gly Ser Asp Val Glu Ser Tyr Ser Ser Met Pro Pro Leu
                2380                2385                2390
GAG GGG GAA CCG GGG GAC CCC GAT CTC AGT GAC GGG TCT TGG TCT ACC     7553
Glu Gly Glu Pro Gly Asp Pro Asp Leu Ser Asp Gly Ser Trp Ser Thr
            2395                2400                2405
GTG AGC GAG GAA GCT AGT GAG GAT GTC GTC TGC TGC TCA ATG TCC TAC     7601
Val Ser Glu Glu Ala Ser Glu Asp Val Val Cys Cys Ser Met Ser Tyr
        2410                2415                2420
ACA TGG ACA GGC GCC TTG ATC ACG CCA TGC GCT GCG GAG GAA AGC AAG     7649
Thr Trp Thr Gly Ala Leu Ile Thr Pro Cys Ala Ala Glu Glu Ser Lys
    2425                2430                2435
CTG CCC ATC AAC GCG TTG AGC AAC TCT TTG CTG CGC CAC CAT AAC ATG     7697
Leu Pro Ile Asn Ala Leu Ser Asn Ser Leu Leu Arg His His Asn Met
2440                2445                2450                2455
GTT TAT GCC ACA ACA TCT CGC AGC GCA GGC CTG CGG CAG AAG AAG GTC     7745
Val Tyr Ala Thr Thr Ser Arg Ser Ala Gly Leu Arg Gln Lys Lys Val
                2460                2465                2470
ACC TTT GAC AGA CTG CAA GTC CTG GAC GAC CAC TAC CGG GAC GTG CTC     7793
Thr Phe Asp Arg Leu Gln Val Leu Asp Asp His Tyr Arg Asp Val Leu
            2475                2480                2485
AAG GAG ATG AAG GCG AAG GCG TCC ACA GTT AAG GCT AAA CTC CTA TCC     7841
Lys Glu Met Lys Ala Lys Ala Ser Thr Val Lys Ala Lys Leu Leu Ser
        2490                2495                2500
GTA GAG GAA GCC TGC AAG CTG ACG CCC CCA CAT TCG GCC AAA TCC AAG     7889
Val Glu Glu Ala Cys Lys Leu Thr Pro Pro His Ser Ala Lys Ser Lys
    2505                2510                2515
TTT GGC TAT GGG GCA AAG GAC GTC CGG AAC CTA TCC AGC AAG GCC GTT     7937
Phe Gly Tyr Gly Ala Lys Asp Val Arg Asn Leu Ser Ser Lys Ala Val
2520                2525                2530                2535
AAC CAC ATC CAC TCC GTG TGG AAG GAC TTG CTG GAA GAC ACT GTG ACA     7985
Asn His Ile His Ser Val Trp Lys Asp Leu Leu Glu Asp Thr Val Thr
                2540                2545                2550
CCA ATT GAC ACC ACC ATC ATG GCA AAA AAT GAG GTT TTC TGT GTC CAA     8033
Pro Ile Asp Thr Thr Ile Met Ala Lys Asn Glu Val Phe Cys Val Gln
            2555                2560                2565
CCA GAG AAA GGA GGC CGT AAG CCA GCC CGC CTT ATC GTA TTC CCA GAT     8081
Pro Glu Lys Gly Gly Arg Lys Pro Ala Arg Leu Ile Val Phe Pro Asp
        2570                2575                2580
CTG GGA GTC CGT GTA TGC GAG AAG ATG GCC CTC TAT GAT GTG GTC TCC     8129
Leu Gly Val Arg Val Cys Glu Lys Met Ala Leu Tyr Asp Val Val Ser
    2585                2590                2595
ACC CTT CCT CAG GTC GTG ATG GGC TCC TCA TAC GGA TTC CAG TAC TCT     8177
Thr Leu Pro Gln Val Val Met Gly Ser Ser Tyr Gly Phe Gln Tyr Ser
2600                2605                2610                2615
CCT GGG CAG CGA GTC GAG TTC CTG GTG AAT ACC TGG AAA TCA AAG AAA     8225
Pro Gly Gln Arg Val Glu Phe Leu Val Asn Thr Trp Lys Ser Lys Lys
                2620                2625                2630
AAC CCC ATG GGC TTT TCA TAT GAC ACT CGC TGT TTC GAC TCA ACG GTC     8273
Asn Pro Met Gly Phe Ser Tyr Asp Thr Arg Cys Phe Asp Ser Thr Val
            2635                2640                2645
ACC GAG AAC GAC ATC CGT GTT GAG GAG TCA ATT TAC CAA TGT TGT GAC     8321
Thr Glu Asn Asp Ile Arg Val Glu Glu Ser Ile Tyr Gln Cys Cys Asp
        2650                2655                2660
TTG GCC CCC GAA GCC AGA CAG GCC ATA AAA TCG CTC ACA GAG CGG CTT     8369
Leu Ala Pro Glu Ala Arg Gln Ala Ile Lys Ser Leu Thr Glu Arg Leu
    2665                2670                2675
TAT ATC GGG GGT CCT CTG ACT AAT TCA AAA GGG CAG AAC TGC GGT TAT     8417
Tyr Ile Gly Gly Pro Leu Thr Asn Ser Lys Gly Gln Asn Cys Gly Tyr
2680                2685                2690                2695
CGC CGG TGC CGC GCG AGC GGC GTG CTG ACG ACT AGC TGC GGT AAC ACC     8465
Arg Arg Cys Arg Ala Ser Gly Val Leu Thr Thr Ser Cys Gly Asn Thr
                2700                2705                2710
CTC ACA TGT TAC TTG AAG GCC TCT GCA GCC TGT CGA GCT GCG AAG CTC     8513
Leu Thr Cys Tyr Leu Lys Ala Ser Ala Ala Cys Arg Ala Ala Lys Leu
            2715                2720                2725
CAG GAC TGC ACG ATG CTC GTG AAC GGA GAC GAC CTC GTC GTT ATC TGT     8561
Gln Asp Cys Thr Met Leu Val Asn Gly Asp Asp Leu Val Val Ile Cys
        2730                2735                2740
GAA AGC GCG GGA ACC CAA GAG GAC GCG GCG AGC CTA CGA GTC TTC ACG     8609
Glu Ser Ala Gly Thr Gln Glu Asp Ala Ala Ser Leu Arg Val Phe Thr
    2745                2750                2755
GAG GCT ATG ACT AGG TAC TCC GCC CCC CCC GGG GAC CCG CCC CAA CCA     8657
Glu Ala Met Thr Arg Tyr Ser Ala Pro Pro Gly Asp Pro Pro Gln Pro
2760                2765                2770                2775
GAA TAC GAC TTG GAG CTG ATA ACA TCA TGT TCC TCC AAT GTG TCG GTC     8705
Glu Tyr Asp Leu Glu Leu Ile Thr Ser Cys Ser Ser Asn Val Ser Val
                2780                2785                2790
GCC CAC GAT GCA TCA GGC AAA AGG GTG TAC TAC CTC ACC CGT GAT CCC     8753
Ala His Asp Ala Ser Gly Lys Arg Val Tyr Tyr Leu Thr Arg Asp Pro
            2795                2800                2805
ACC ACC CCC CTA GCA CGG GCT GCG TGG GAG ACA GCT AGA CAC ACT CCA     8801
Thr Thr Pro Leu Ala Arg Ala Ala Trp Glu Thr Ala Arg His Thr Pro
        2810                2815                2820
GTT AAC TCC TGG CTA GGC AAC ATT ATT ATG TAT GCG CCC ACT TTG TGG     8849
Val Asn Ser Trp Leu Gly Asn Ile Ile Met Tyr Ala Pro Thr Leu Trp
    2825                2830                2835
GCA AGG ATG ATT CTG ATG ACT CAC TTC TTC TCC ATC CTT CTA GCG CAG     8897
Ala Arg Met Ile Leu Met Thr His Phe Phe Ser Ile Leu Leu Ala Gln
2840                2845                2850                2855
GAG CAA CTT GAA AAA GCC CTG GAC TGC CAG ATC TAC GGG GCC TGT TAC     8945
Glu Gln Leu Glu Lys Ala Leu Asp Cys Gln Ile Tyr Gly Ala Cys Tyr
                2860                2865                2870
TCC ATT GAG CCA CTT GAC CTA CCT CAG ATC ATT GAA CGA CTC CAT GGC     8993
Ser Ile Glu Pro Leu Asp Leu Pro Gln Ile Ile Glu Arg Leu His Gly
            2875                2880                2885
CTT AGC GCA TTT TCA CTC CAT AGT TAC TCT CCA GGT GAG ATC AAT AGG     9041
Leu Ser Ala Phe Ser Leu His Ser Tyr Ser Pro Gly Glu Ile Asn Arg
        2890                2895                2900
GTG GCT TCA TGC CTC AGG AAA CTT GGG GTA CCA CCC TTG CGA GTC TGG     9089
Val Ala Ser Cys Leu Arg Lys Leu Gly Val Pro Pro Leu Arg Val Trp
    2905                2910                2915
AGA CAT CGG GCC AGG AGC GTC CGC GCT AGG CTA CTG TCC CAG GGA GGG     9137
Arg His Arg Ala Arg Ser Val Arg Ala Arg Leu Leu Ser Gln Gly Gly
2920                2925                2930                2935
AGG GCC GCC ACT TGT GGC AAA TAC CTC TTC AAC TGG GCA GTA AAA ACC     9185
Arg Ala Ala Thr Cys Gly Lys Tyr Leu Phe Asn Trp Ala Val Lys Thr
                2940                2945                2950
AAA CTT AAA CTC ACT CCA ATC CCG GCT GCG TCC CGG CTG GAC TTG TCC     9233
Lys Leu Lys Leu Thr Pro Ile Pro Ala Ala Ser Arg Leu Asp Leu Ser
            2955                2960                2965
GGC TGG TTC GTT GCT GGT TAC AGC GGG GGA GAC ATA TAT CAC AGC CTG     9281
Gly Trp Phe Val Ala Gly Tyr Ser Gly Gly Asp Ile Tyr His Ser Leu
        2970                2975                2980
TCT CGT GCC CGA CCC CGT TGG TTC ATG CTG TGC CTA CTC CTA CTT TCT     9329
Ser Arg Ala Arg Pro Arg Trp Phe Met Leu Cys Leu Leu Leu Leu Ser
    2985                2990                2995
GTA GGG GTA GGC ATC TAC CTG CTC CCC AAC CGA TGAACGGGGA GATAAACACT   9382
Val Gly Val Gly Ile Tyr Leu Leu Pro Asn Arg
3000                3005                3010
CCAGGCCAAT AGGCCATCCC CCTTTTTTTT TTTT                               9416 
           
           
             
               3010 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             2
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile Val Gly
             20                  25                  30
Gly Val Tyr Leu Leu Pro Arg Arg Gly Pro Arg Leu Gly Val Arg Ala
         35                  40                  45
Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln Pro
     50                  55                  60
Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala Gln Pro Gly
 65                  70                  75                  80
Tyr Pro Trp Pro Leu Tyr Gly Asn Glu Gly Leu Gly Trp Ala Gly Trp
                 85                  90                  95
Leu Leu Ser Pro Arg Gly Ser Arg Pro Ser Trp Gly Pro Thr Asp Pro
            100                 105                 110
Arg Arg Arg Ser Arg Asn Leu Gly Lys Val Ile Asp Thr Leu Thr Cys
        115                 120                 125
Gly Phe Ala Asp Leu Met Gly Tyr Ile Pro Leu Val Gly Ala Pro Leu
    130                 135                 140
Gly Gly Ala Ala Arg Ala Leu Ala His Gly Val Arg Val Leu Glu Asp
145                 150                 155                 160
Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly Cys Ser Phe Ser Ile
                165                 170                 175
Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Thr Pro Ala Ser Ala Tyr
            180                 185                 190
Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys Ser
        195                 200                 205
Asn Ala Ser Ile Val Tyr Glu Ala Ala Asp Leu Ile Met His Thr Pro
    210                 215                 220
Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ser Ser Arg Cys Trp Val
225                 230                 235                 240
Ala Leu Thr Pro Thr Leu Ala Ala Arg Asn Val Thr Ile Pro Thr Thr
                245                 250                 255
Thr Ile Arg Arg His Val Asp Leu Leu Val Gly Ala Ala Ala Phe Cys
            260                 265                 270
Ser Ala Met Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val Ser
        275                 280                 285
Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp Cys
    290                 295                 300
Asn Cys Ser Ile Tyr Pro Gly His Val Ser Gly His Arg Met Ala Trp
305                 310                 315                 320
Asp Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ser Gln
                325                 330                 335
Leu Leu Arg Ile Pro Gln Ala Val Val Asp Met Val Ala Gly Ala His
            340                 345                 350
Trp Gly Val Leu Ala Gly Leu Ala Tyr Tyr Ser Met Ala Gly Asn Trp
        355                 360                 365
Ala Lys Val Leu Ile Val Met Leu Leu Phe Ala Gly Val Asp Gly Asp
    370                 375                 380
Thr His Val Thr Gly Gly Ala Gln Ala Lys Thr Thr Asn Arg Leu Val
385                 390                 395                 400
Ser Met Phe Ala Ser Gly Pro Ser Gln Lys Ile Gln Leu Ile Asn Thr
                405                 410                 415
Asn Gly Ser Trp His Ile Asn Arg Thr Ala Leu Asn Cys Asn Asp Ser
            420                 425                 430
Leu Gln Thr Gly Phe Leu Ala Ala Leu Phe Tyr Thr His Ser Phe Asn
        435                 440                 445
Ser Ser Gly Cys Pro Glu Arg Met Ala Gln Cys Arg Thr Ile Asp Lys
    450                 455                 460
Phe Asp Gln Gly Trp Gly Pro Ile Thr Tyr Ala Glu Ser Ser Arg Ser
465                 470                 475                 480
Asp Gln Arg Pro Tyr Cys Trp His Tyr Pro Pro Pro Gln Cys Thr Ile
                485                 490                 495
Val Pro Ala Ser Glu Val Cys Gly Pro Val Tyr Cys Phe Thr Pro Ser
            500                 505                 510
Pro Val Val Val Gly Thr Thr Asp Arg Phe Gly Val Pro Thr Tyr Arg
        515                 520                 525
Trp Gly Glu Asn Glu Thr Asp Val Leu Leu Leu Asn Asn Thr Arg Pro
    530                 535                 540
Pro Gln Gly Asn Trp Phe Gly Cys Thr Trp Met Asn Ser Thr Gly Phe
545                 550                 555                 560
Thr Lys Thr Cys Gly Gly Pro Pro Cys Asn Ile Gly Gly Val Gly Asn
                565                 570                 575
Asn Thr Leu Thr Cys Pro Thr Asp Cys Phe Arg Lys His Pro Glu Ala
            580                 585                 590
Thr Tyr Thr Lys Cys Gly Ser Gly Pro Trp Leu Thr Pro Arg Cys Met
        595                 600                 605
Val Asp Tyr Pro Tyr Arg Leu Trp His Tyr Pro Cys Thr Val Asn Phe
    610                 615                 620
Thr Ile Phe Lys Val Arg Met Tyr Val Gly Gly Val Glu His Arg Leu
625                 630                 635                 640
Asn Ala Ala Cys Asn Trp Thr Arg Gly Glu Arg Cys Asp Leu Glu Asp
                645                 650                 655
Arg Asp Arg Pro Glu Leu Ser Pro Leu Leu Leu Ser Thr Thr Glu Trp
            660                 665                 670
Gln Val Leu Pro Cys Ser Phe Thr Thr Leu Pro Ala Leu Ser Thr Gly
        675                 680                 685
Leu Ile His Leu His Gln Asn Ile Val Asp Val Gln Tyr Leu Tyr Gly
    690                 695                 700
Ile Gly Ser Ala Val Val Ser Phe Ala Ile Lys Trp Glu Tyr Val Leu
705                 710                 715                 720
Leu Leu Phe Leu Leu Leu Ala Asp Ala Arg Val Cys Ala Cys Leu Trp
                725                 730                 735
Met Met Leu Leu Ile Ala Gln Ala Glu Ala Ala Leu Glu Asn Leu Val
            740                 745                 750
Val Leu Asn Ser Ala Ser Val Ala Gly Ala His Gly Ile Leu Ser Phe
        755                 760                 765
Leu Val Phe Phe Cys Ala Ala Trp Tyr Ile Lys Gly Arg Leu Val Pro
    770                 775                 780
Gly Ala Thr Tyr Ala Leu Tyr Gly Val Trp Pro Leu Leu Leu Leu Leu
785                 790                 795                 800
Leu Ala Leu Pro Pro Arg Ala Tyr Ala Met Asp Arg Glu Met Ala Ala
                805                 810                 815
Ser Cys Gly Gly Ala Val Phe Val Gly Leu Val Leu Leu Thr Leu Ser
            820                 825                 830
Pro Tyr Tyr Lys Val Phe Leu Ala Arg Leu Ile Trp Trp Leu Gln Tyr
        835                 840                 845
Phe Thr Thr Arg Ala Glu Ala Asp Leu His Val Trp Ile Pro Pro Leu
    850                 855                 860
Asn Ala Arg Gly Gly Arg Asp Ala Ile Ile Leu Leu Met Cys Ala Val
865                 870                 875                 880
His Pro Glu Leu Ile Phe Asp Ile Thr Lys Leu Leu Ile Ala Ile Leu
                885                 890                 895
Gly Pro Leu Met Val Leu Gln Ala Gly Ile Thr Arg Val Pro Tyr Phe
            900                 905                 910
Val Arg Ala Gln Gly Leu Ile His Ala Cys Met Leu Val Arg Lys Val
        915                 920                 925
Ala Gly Gly His Tyr Val Gln Met Ala Phe Met Lys Leu Gly Ala Leu
    930                 935                 940
Thr Gly Thr Tyr Ile Tyr Asn His Leu Thr Pro Leu Arg Asp Trp Pro
945                 950                 955                 960
Arg Ala Gly Leu Arg Asp Leu Ala Val Ala Val Glu Pro Val Val Phe
                965                 970                 975
Ser Asp Met Glu Thr Lys Ile Ile Thr Trp Gly Ala Asp Thr Ala Ala
            980                 985                 990
Cys Gly Asp Ile Ile Leu Gly Leu Pro Val Ser Ala Arg Arg Gly Lys
        995                 1000                1005
Glu Ile Leu Leu Gly Pro Ala Asp Ser Leu Glu Gly Arg Gly Leu Arg
    1010                1015                1020
Leu Leu Ala Pro Ile Thr Ala Tyr Ser Gln Gln Thr Arg Gly Leu Leu
1025                1030                1035                1040
Gly Cys Ile Ile Thr Ser Leu Thr Gly Arg Asp Lys Asn Gln Val Glu
                1045                1050                1055
Gly Glu Val Gln Val Val Ser Thr Ala Thr Gln Ser Phe Leu Ala Thr
            1060                1065                1070
Cys Val Asn Gly Val Cys Trp Thr Val Tyr His Gly Ala Gly Ser Lys
        1075                1080                1085
Thr Leu Ala Ala Pro Lys Gly Pro Ile Thr Gln Met Tyr Thr Asn Val
    1090                1095                1100
Asp Gln Asp Leu Val Gly Trp Pro Lys Pro Pro Gly Ala Arg Ser Leu
1105                1110                1115                1120
Thr Pro Cys Thr Cys Gly Ser Ser Asp Leu Tyr Leu Val Thr Arg His
                1125                1130                1135
Ala Asp Val Ile Pro Val Arg Arg Arg Gly Asp Ser Arg Gly Ser Leu
            1140                1145                1150
Leu Ser Pro Arg Pro Val Ser Tyr Leu Lys Gly Ser Ser Gly Gly Pro
        1155                1160                1165
Leu Leu Cys Pro Phe Gly His Ala Val Gly Ile Phe Arg Ala Ala Val
    1170                1175                1180
Cys Thr Arg Gly Val Ala Lys Ala Val Asp Phe Val Pro Val Glu Ser
1185                1190                1195                1200
Met Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro
                1205                1210                1215
Pro Ala Val Pro Gln Ser Phe Gln Val Ala His Leu His Ala Pro Thr
            1220                1225                1230
Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala Ala Gln Gly
        1235                1240                1245
Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe
    1250                1255                1260
Gly Ala Tyr Met Ser Lys Ala His Gly Ile Asp Pro Asn Ile Arg Thr
1265                1270                1275                1280
Gly Val Arg Thr Ile Thr Thr Gly Ala Pro Val Thr Tyr Ser Thr Tyr
                1285                1290                1295
Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp Ile
            1300                1305                1310
Ile Ile Cys Asp Glu Cys His Ser Thr Asp Ser Thr Thr Ile Leu Gly
        1315                1320                1325
Ile Gly Thr Val Leu Asp Gln Ala Glu Thr Ala Gly Ala Arg Leu Val
    1330                1335                1340
Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro His Pro
1345                1350                1355                1360
Asn Ile Glu Glu Val Ala Leu Ser Asn Thr Gly Glu Ile Pro Phe Tyr
                1365                1370                1375
Gly Lys Ala Ile Pro Ile Glu Ala Ile Arg Gly Gly Arg His Leu Ile
            1380                1385                1390
Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Ser
        1395                1400                1405
Gly Leu Gly Ile Asn Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser
    1410                1415                1420
Val Ile Pro Thr Ile Gly Asp Val Val Val Val Ala Thr Asp Ala Leu
1425                1430                1435                1440
Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val Ile Asp Cys Asn Thr
                1445                1450                1455
Cys Val Thr Gln Thr Val Asp Phe Ser Leu Asp Pro Thr Phe Thr Ile
            1460                1465                1470
Glu Thr Thr Thr Val Pro Gln Asp Ala Val Ser Arg Ser Gln Arg Arg
        1475                1480                1485
Gly Arg Thr Gly Arg Gly Arg Arg Gly Ile Tyr Arg Phe Val Thr Pro
    1490                1495                1500
Gly Glu Arg Pro Ser Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys
1505                1510                1515                1520
Tyr Asp Ala Gly Cys Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Ser
                1525                1530                1535
Val Arg Leu Arg Ala Tyr Leu Asn Thr Pro Gly Leu Pro Val Cys Gln
            1540                1545                1550
Asp His Leu Glu Phe Trp Glu Ser Val Phe Thr Gly Leu Thr His Ile
        1555                1560                1565
Asp Ala His Phe Leu Ser Gln Thr Lys Gln Ala Gly Asp Asn Phe Pro
    1570                1575                1580
Tyr Leu Val Ala Tyr Gln Ala Thr Val Cys Ala Arg Ala Gln Ala Pro
1585                1590                1595                1600
Pro Pro Ser Trp Asp Gln Met Trp Lys Cys Leu Ile Arg Leu Lys Pro
                1605                1610                1615
Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gln
            1620                1625                1630
Asn Glu Val Thr Leu Thr His Pro Ile Thr Lys Tyr Ile Met Ala Cys
        1635                1640                1645
Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly
    1650                1655                1660
Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Thr Thr Gly Ser Val
1665                1670                1675                1680
Val Ile Val Gly Arg Ile Ile Leu Ser Gly Arg Pro Ala Ile Val Pro
                1685                1690                1695
Asp Arg Glu Leu Leu Tyr Gln Glu Phe Asp Glu Met Glu Glu Cys Ala
            1700                1705                1710
Ser His Leu Pro Tyr Ile Glu Gln Gly Met Gln Leu Ala Glu Gln Phe
        1715                1720                1725
Lys Gln Lys Ala Leu Gly Leu Leu Gln Thr Ala Thr Lys Gln Ala Glu
    1730                1735                1740
Ala Ala Ala Pro Val Val Glu Ser Lys Trp Arg Ala Leu Glu Thr Phe
1745                1750                1755                1760
Trp Ala Lys His Met Trp Asn Phe Ile Ser Gly Ile Gln Tyr Leu Ala
                1765                1770                1775
Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala Ile Ala Ser Leu Met Ala
            1780                1785                1790
Phe Thr Ala Ser Ile Thr Ser Pro Leu Thr Thr Gln Ser Thr Leu Leu
        1795                1800                1805
Phe Asn Ile Leu Gly Gly Trp Val Ala Ala Gln Leu Ala Pro Pro Ser
    1810                1815                1820
Ala Ala Ser Ala Phe Val Gly Ala Gly Ile Ala Gly Ala Ala Val Gly
1825                1830                1835                1840
Ser Ile Gly Leu Gly Lys Val Leu Val Asp Ile Leu Ala Gly Tyr Gly
                1845                1850                1855
Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys Val Met Ser Gly Glu
            1860                1865                1870
Met Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Ala Ile Leu Ser
        1875                1880                1885
Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala Ile Leu Arg Arg
    1890                1895                1900
His Val Gly Pro Gly Glu Gly Ala Val Gln Trp Met Asn Arg Leu Ile
1905                1910                1915                1920
Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Thr His Tyr Val Pro
                1925                1930                1935
Glu Ser Asp Ala Ala Ala Arg Val Thr Gln Ile Leu Ser Ser Leu Thr
            1940                1945                1950
Ile Thr Gln Leu Leu Lys Arg Leu His Gln Trp Ile Asn Glu Asp Cys
        1955                1960                1965
Ser Thr Pro Cys Ser Gly Ser Trp Leu Arg Asp Val Trp Asp Trp Ile
    1970                1975                1980
Cys Thr Val Leu Thr Asp Phe Lys Thr Trp Leu Gln Ser Lys Leu Leu
1985                1990                1995                2000
Pro Gln Leu Pro Gly Val Pro Phe Phe Ser Cys Gln Arg Gly Tyr Lys
                2005                2010                2015
Gly Val Trp Arg Gly Asp Gly Ile Met Gln Thr Thr Cys Pro Cys Gly
            2020                2025                2030
Ala Gln Ile Thr Gly His Val Lys Asn Gly Ser Met Arg Ile Val Gly
        2035                2040                2045
Pro Lys Thr Cys Ser Asn Thr Trp His Gly Thr Phe Pro Ile Asn Ala
    2050                2055                2060
Tyr Thr Thr Gly Pro Cys Thr Pro Ser Pro Ala Pro Asn Tyr Ser Arg
2065                2070                2075                2080
Ala Leu Trp Arg Val Ala Ala Glu Glu Tyr Val Glu Val Thr Arg Val
                2085                2090                2095
Gly Asp Phe His Tyr Val Thr Gly Met Thr Thr Asp Asn Val Lys Cys
            2100                2105                2110
Pro Cys Gln Val Pro Ala Pro Glu Phe Phe Ser Glu Val Asp Gly Val
        2115                2120                2125
Arg Leu His Arg Tyr Ala Pro Ala Cys Arg Pro Leu Leu Arg Glu Glu
    2130                2135                2140
Val Thr Phe Gln Val Gly Leu Asn Gln Tyr Leu Val Gly Ser Gln Leu
2145                2150                2155                2160
Pro Cys Glu Pro Glu Pro Asp Val Ala Val Leu Thr Ser Met Leu Thr
                2165                2170                2175
Asp Pro Ser His Ile Thr Ala Glu Thr Ala Lys Arg Arg Leu Ala Arg
            2180                2185                2190
Gly Ser Pro Pro Ser Leu Ala Ser Ser Ser Ala Ser Gln Leu Ser Ala
        2195                2200                2205
Pro Ser Leu Lys Ala Thr Cys Thr Thr His His Val Ser Pro Asp Ala
    2210                2215                2220
Asp Leu Ile Glu Ala Asn Leu Leu Trp Arg Gln Glu Met Gly Gly Asn
2225                2230                2235                2240
Ile Thr Arg Val Glu Ser Glu Asn Lys Val Val Val Leu Asp Ser Phe
                2245                2250                2255
Asp Pro Leu Arg Ala Glu Glu Asp Glu Arg Glu Val Ser Val Pro Ala
            2260                2265                2270
Glu Ile Leu Arg Lys Ser Lys Lys Phe Pro Ala Ala Met Pro Ile Trp
        2275                2280                2285
Ala Arg Pro Asp Tyr Asn Pro Pro Leu Leu Glu Ser Trp Lys Asp Pro
    2290                2295                2300
Asp Tyr Val Pro Pro Val Val His Gly Cys Pro Leu Pro Pro Ile Lys
2305                2310                2315                2320
Ala Pro Pro Ile Pro Pro Pro Arg Arg Lys Arg Thr Val Val Leu Thr
                2325                2330                2335
Glu Ser Ser Val Ser Ser Ala Leu Ala Glu Leu Ala Thr Lys Thr Phe
            2340                2345                2350
Gly Ser Ser Glu Ser Ser Ala Val Asp Ser Gly Thr Ala Thr Ala Leu
        2355                2360                2365
Pro Asp Gln Ala Ser Asp Asp Gly Asp Lys Gly Ser Asp Val Glu Ser
    2370                2375                2380
Tyr Ser Ser Met Pro Pro Leu Glu Gly Glu Pro Gly Asp Pro Asp Leu
2385                2390                2395                2400
Ser Asp Gly Ser Trp Ser Thr Val Ser Glu Glu Ala Ser Glu Asp Val
                2405                2410                2415
Val Cys Cys Ser Met Ser Tyr Thr Trp Thr Gly Ala Leu Ile Thr Pro
            2420                2425                2430
Cys Ala Ala Glu Glu Ser Lys Leu Pro Ile Asn Ala Leu Ser Asn Ser
        2435                2440                2445
Leu Leu Arg His His Asn Met Val Tyr Ala Thr Thr Ser Arg Ser Ala
    2450                2455                2460
Gly Leu Arg Gln Lys Lys Val Thr Phe Asp Arg Leu Gln Val Leu Asp
2465                2470                2475                2480
Asp His Tyr Arg Asp Val Leu Lys Glu Met Lys Ala Lys Ala Ser Thr
                2485                2490                2495
Val Lys Ala Lys Leu Leu Ser Val Glu Glu Ala Cys Lys Leu Thr Pro
            2500                2505                2510
Pro His Ser Ala Lys Ser Lys Phe Gly Tyr Gly Ala Lys Asp Val Arg
        2515                2520                2525
Asn Leu Ser Ser Lys Ala Val Asn His Ile His Ser Val Trp Lys Asp
    2530                2535                2540
Leu Leu Glu Asp Thr Val Thr Pro Ile Asp Thr Thr Ile Met Ala Lys
2545                2550                2555                2560
Asn Glu Val Phe Cys Val Gln Pro Glu Lys Gly Gly Arg Lys Pro Ala
                2565                2570                2575
Arg Leu Ile Val Phe Pro Asp Leu Gly Val Arg Val Cys Glu Lys Met
            2580                2585                2590
Ala Leu Tyr Asp Val Val Ser Thr Leu Pro Gln Val Val Met Gly Ser
        2595                2600                2605
Ser Tyr Gly Phe Gln Tyr Ser Pro Gly Gln Arg Val Glu Phe Leu Val
    2610                2615                2620
Asn Thr Trp Lys Ser Lys Lys Asn Pro Met Gly Phe Ser Tyr Asp Thr
2625                2630                2635                2640
Arg Cys Phe Asp Ser Thr Val Thr Glu Asn Asp Ile Arg Val Glu Glu
                2645                2650                2655
Ser Ile Tyr Gln Cys Cys Asp Leu Ala Pro Glu Ala Arg Gln Ala Ile
            2660                2665                2670
Lys Ser Leu Thr Glu Arg Leu Tyr Ile Gly Gly Pro Leu Thr Asn Ser
        2675                2680                2685
Lys Gly Gln Asn Cys Gly Tyr Arg Arg Cys Arg Ala Ser Gly Val Leu
    2690                2695                2700
Thr Thr Ser Cys Gly Asn Thr Leu Thr Cys Tyr Leu Lys Ala Ser Ala
2705                2710                2715                2720
Ala Cys Arg Ala Ala Lys Leu Gln Asp Cys Thr Met Leu Val Asn Gly
                2725                2730                2735
Asp Asp Leu Val Val Ile Cys Glu Ser Ala Gly Thr Gln Glu Asp Ala
            2740                2745                2750
Ala Ser Leu Arg Val Phe Thr Glu Ala Met Thr Arg Tyr Ser Ala Pro
        2755                2760                2765
Pro Gly Asp Pro Pro Gln Pro Glu Tyr Asp Leu Glu Leu Ile Thr Ser
    2770                2775                2780
Cys Ser Ser Asn Val Ser Val Ala His Asp Ala Ser Gly Lys Arg Val
2785                2790                2795                2800
Tyr Tyr Leu Thr Arg Asp Pro Thr Thr Pro Leu Ala Arg Ala Ala Trp
                2805                2810                2815
Glu Thr Ala Arg His Thr Pro Val Asn Ser Trp Leu Gly Asn Ile Ile
            2820                2825                2830
Met Tyr Ala Pro Thr Leu Trp Ala Arg Met Ile Leu Met Thr His Phe
        2835                2840                2845
Phe Ser Ile Leu Leu Ala Gln Glu Gln Leu Glu Lys Ala Leu Asp Cys
    2850                2855                2860
Gln Ile Tyr Gly Ala Cys Tyr Ser Ile Glu Pro Leu Asp Leu Pro Gln
2865                2870                2875                2880
Ile Ile Glu Arg Leu His Gly Leu Ser Ala Phe Ser Leu His Ser Tyr
                2885                2890                2895
Ser Pro Gly Glu Ile Asn Arg Val Ala Ser Cys Leu Arg Lys Leu Gly
            2900                2905                2910
Val Pro Pro Leu Arg Val Trp Arg His Arg Ala Arg Ser Val Arg Ala
        2915                2920                2925
Arg Leu Leu Ser Gln Gly Gly Arg Ala Ala Thr Cys Gly Lys Tyr Leu
    2930                2935                2940
Phe Asn Trp Ala Val Lys Thr Lys Leu Lys Leu Thr Pro Ile Pro Ala
2945                2950                2955                2960
Ala Ser Arg Leu Asp Leu Ser Gly Trp Phe Val Ala Gly Tyr Ser Gly
                2965                2970                2975
Gly Asp Ile Tyr His Ser Leu Ser Arg Ala Arg Pro Arg Trp Phe Met
            2980                2985                2990
Leu Cys Leu Leu Leu Leu Ser Val Gly Val Gly Ile Tyr Leu Leu Pro
        2995                3000                3005
Asn Arg
    3010 
           
           
             
               1499 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               CDS 
                333..1499 
             
             
               misc_feature 
                1..1499 
                /note= “sequence = 1 - 1499 of
              SEQ ID NO 1” 
             
             3
CGATTGGGGG CGACACTCCA CCATAGATCA CTCCCCTGTG AGGAACTACT GTCTTCACGC     60
AGAAAGCGTC TAGCCATGGC GTTAGTATGA GTGTCGTGCA GCCTCCAGGA CCCCCCCTCC    120
CGGGAGAGCC ATAGTGGTCT GCGGAACCGG TGAGTACACC GGAATTGCCA GGACGACCGG    180
GTCCTTTCTT GGATCAACCC GCTCAATGCC TGGAGATTTG GGCGTGCCCC CGCGAGACTG    240
CTAGCCGAGT AGTGTTGGGT CGCGAAAGGC CTTGTGGTAC TGCCTGATAG GGTGCTTGCG    300
AGTGCCCCGG GAGGTCTCGT AGACCGTGCA CC ATG AGC ACG AAT CCT AAA CCT      353
                                    Met Ser Thr Asn Pro Lys Pro
                                      1               5
CAA AGA AAA ACC AAA CGT AAC ACC AAC CGC CGC CCA CAG GAC GTC AAG      401
Gln Arg Lys Thr Lys Arg Asn Thr Asn Arg Arg Pro Gln Asp Val Lys
         10                  15                  20
TTC CCG GGC GGT GGT CAG ATC GTT GGT GGA GTT TAC CTG TTG CCG CGC      449
Phe Pro Gly Gly Gly Gln Ile Val Gly Gly Val Tyr Leu Leu Pro Arg
     25                  30                  35
AGG GGC CCC AGG TTG GGT GTG CGC GCG CCC AGG AAG ACT TCC GAG CGG      497
Arg Gly Pro Arg Leu Gly Val Arg Ala Pro Arg Lys Thr Ser Glu Arg
 40                  45                  50                  55
TCG CAA CCT CGT GGA AGG CGA CAA CCT ATC CCC AAG GCT CGC CGG CCC      545
Ser Gln Pro Arg Gly Arg Arg Gln Pro Ile Pro Lys Ala Arg Arg Pro
                 60                  65                  70
GAG GGC AGG ACC TGG GCT CAG CCC GGG TAC CCT TGG CCT CTC TAT GGC      593
Glu Gly Arg Thr Trp Ala Gln Pro Gly Tyr Pro Trp Pro Leu Tyr Gly
             75                  80                  85
AAT GAG GGC TTA GGG TGG GCA GGA TGG CTC CTG TCA CCC CGC GGC TCC      641
Asn Glu Gly Leu Gly Trp Ala Gly Trp Leu Leu Ser Pro Arg Gly Ser
         90                  95                 100
CGG CCT AGT TGG GGC CCC ACG GAC CCC CGG CGT AGG TCG CGT AAT TTG      689
Arg Pro Ser Trp Gly Pro Thr Asp Pro Arg Arg Arg Ser Arg Asn Leu
    105                 110                 115
GGT AAG GTC ATC GAT ACC CTC ACA TGC GGC TTC GCC GAT CTC ATG GGG      737
Gly Lys Val Ile Asp Thr Leu Thr Cys Gly Phe Ala Asp Leu Met Gly
120                 125                 130                 135
TAC ATT CCG CTC GTC GGC GCC CCC CTG GGG GGC GCT GCC AGG GCC CTG      785
Tyr Ile Pro Leu Val Gly Ala Pro Leu Gly Gly Ala Ala Arg Ala Leu
                140                 145                 150
GCA CAT GGT GTC CGG GTT CTG GAG GAC GGC GTG AAC TAT GCA ACA GGG      833
Ala His Gly Val Arg Val Leu Glu Asp Gly Val Asn Tyr Ala Thr Gly
            155                 160                 165
AAT CTG CCC GGT TGC TCT TTT TCT ATC TTC CTC TTG GCT CTG CTG TCC      881
Asn Leu Pro Gly Cys Ser Phe Ser Ile Phe Leu Leu Ala Leu Leu Ser
        170                 175                 180
TGC CTG ACC ACC CCA GCT TCC GCT TAC GAA GTG CAC AAC GTG TCC GGG      929
Cys Leu Thr Thr Pro Ala Ser Ala Tyr Glu Val His Asn Val Ser Gly
    185                 190                 195
ATA TAT CAT GTC ACG AAC GAC TGC TCC AAC GCA AGC ATT GTG TAT GAG      977
Ile Tyr His Val Thr Asn Asp Cys Ser Asn Ala Ser Ile Val Tyr Glu
200                 205                 210                 215
GCA GCG GAC TTG ATC ATG CAT ACT CCT GGG TGC GTG CCC TGC GTT CGG     1025
Ala Ala Asp Leu Ile Met His Thr Pro Gly Cys Val Pro Cys Val Arg
                220                 225                 230
GAA GGC AAC TCC TCC CGC TGC TGG GTA GCG CTC ACT CCC ACG CTC GCA     1073
Glu Gly Asn Ser Ser Arg Cys Trp Val Ala Leu Thr Pro Thr Leu Ala
            235                 240                 245
GCC AGG AAC GTC ACC ATC CCC ACC ACG ACG ATA CGA CGC CAC GTC GAT     1121
Ala Arg Asn Val Thr Ile Pro Thr Thr Thr Ile Arg Arg His Val Asp
        250                 255                 260
CTG CTC GTT GGG GCG GCT GCT TTC TGT TCC GCT ATG TAC GTG GGG GAC     1169
Leu Leu Val Gly Ala Ala Ala Phe Cys Ser Ala Met Tyr Val Gly Asp
    265                 270                 275
CTC TGC GGA TCT GTT TTC CTC GTC TCT CAG CTG TTC ACC TTC TCG CCT     1217
Leu Cys Gly Ser Val Phe Leu Val Ser Gln Leu Phe Thr Phe Ser Pro
280                 285                 290                 295
CGC CGG CAT GTG ACA TTA CAG GAC TGT AAC TGC TCA ATT TAT CCC GGC     1265
Arg Arg His Val Thr Leu Gln Asp Cys Asn Cys Ser Ile Tyr Pro Gly
                300                 305                 310
CAT GTG TCG GGT CAC CGT ATG GCT TGG GAC ATG ATG ATG AAC TGG TCG     1313
His Val Ser Gly His Arg Met Ala Trp Asp Met Met Met Asn Trp Ser
            315                 320                 325
CCC ACA ACA GCC CTA GTG GTG TCG CAG TTA CTC CGG ATC CCA CAA GCC     1361
Pro Thr Thr Ala Leu Val Val Ser Gln Leu Leu Arg Ile Pro Gln Ala
        330                 335                 340
GTC GTG GAC ATG GTG GCG GGG GCC CAC TGG GGA GTC CTG GCG GGC CTT     1409
Val Val Asp Met Val Ala Gly Ala His Trp Gly Val Leu Ala Gly Leu
    345                 350                 355
GCC TAC TAT TCC ATG GCG GGG AAC TGG GCT AAG GTT CTG ATT GTG ATG     1457
Ala Tyr Tyr Ser Met Ala Gly Asn Trp Ala Lys Val Leu Ile Val Met
360                 365                 370                 375
CTA CTT TTT GCT GGC GTT GAC GGG GAT ACC CAC GTG ACA GGG             1499
Leu Leu Phe Ala Gly Val Asp Gly Asp Thr His Val Thr Gly
                380                 385 
           
           
             
               389 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             4
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile Val Gly
             20                  25                  30
Gly Val Tyr Leu Leu Pro Arg Arg Gly Pro Arg Leu Gly Val Arg Ala
         35                  40                  45
Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln Pro
     50                  55                  60
Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala Gln Pro Gly
 65                  70                  75                  80
Tyr Pro Trp Pro Leu Tyr Gly Asn Glu Gly Leu Gly Trp Ala Gly Trp
                 85                  90                  95
Leu Leu Ser Pro Arg Gly Ser Arg Pro Ser Trp Gly Pro Thr Asp Pro
            100                 105                 110
Arg Arg Arg Ser Arg Asn Leu Gly Lys Val Ile Asp Thr Leu Thr Cys
        115                 120                 125
Gly Phe Ala Asp Leu Met Gly Tyr Ile Pro Leu Val Gly Ala Pro Leu
    130                 135                 140
Gly Gly Ala Ala Arg Ala Leu Ala His Gly Val Arg Val Leu Glu Asp
145                 150                 155                 160
Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly Cys Ser Phe Ser Ile
                165                 170                 175
Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Thr Pro Ala Ser Ala Tyr
            180                 185                 190
Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys Ser
        195                 200                 205
Asn Ala Ser Ile Val Tyr Glu Ala Ala Asp Leu Ile Met His Thr Pro
    210                 215                 220
Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ser Ser Arg Cys Trp Val
225                 230                 235                 240
Ala Leu Thr Pro Thr Leu Ala Ala Arg Asn Val Thr Ile Pro Thr Thr
                245                 250                 255
Thr Ile Arg Arg His Val Asp Leu Leu Val Gly Ala Ala Ala Phe Cys
            260                 265                 270
Ser Ala Met Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val Ser
        275                 280                 285
Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp Cys
    290                 295                 300
Asn Cys Ser Ile Tyr Pro Gly His Val Ser Gly His Arg Met Ala Trp
305                 310                 315                 320
Asp Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ser Gln
                325                 330                 335
Leu Leu Arg Ile Pro Gln Ala Val Val Asp Met Val Ala Gly Ala His
            340                 345                 350
Trp Gly Val Leu Ala Gly Leu Ala Tyr Tyr Ser Met Ala Gly Asn Trp
        355                 360                 365
Ala Lys Val Leu Ile Val Met Leu Leu Phe Ala Gly Val Asp Gly Asp
    370                 375                 380
Thr His Val Thr Gly
385 
           
           
             
               90 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..90 
                /note “sequence = 333 - 422 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..90 
             
             5
ATG AGC ACG AAT CCT AAA CCT CAA AGA AAA ACC AAA CGT AAC ACC AAC       48
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
CGC CGC CCA CAG GAC GTC AAG TTC CCG GGC GGT GGT CAG ATC               90
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile
             20                  25                  30 
           
           
             
               30 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             6
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile
             20                  25                  30 
           
           
             
               345 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..345 
                /note “sequence = 333 - 677 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..345 
             
             7
ATG AGC ACG AAT CCT AAA CCT CAA AGA AAA ACC AAA CGT AAC ACC AAC       48
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
CGC CGC CCA CAG GAC GTC AAG TTC CCG GGC GGT GGT CAG ATC GTT GGT       96
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile Val Gly
             20                  25                  30
GGA GTT TAC CTG TTG CCG CGC AGG GGC CCC AGG TTG GGT GTG CGC GCG      144
Gly Val Tyr Leu Leu Pro Arg Arg Gly Pro Arg Leu Gly Val Arg Ala
         35                  40                  45
CCC AGG AAG ACT TCC GAG CGG TCG CAA CCT CGT GGA AGG CGA CAA CCT      192
Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln Pro
     50                  55                  60
ATC CCC AAG GCT CGC CGG CCC GAG GGC AGG ACC TGG GCT CAG CCC GGG      240
Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala Gln Pro Gly
 65                  70                  75                  80
TAC CCT TGG CCT CTC TAT GGC AAT GAG GGC TTA GGG TGG GCA GGA TGG      288
Tyr Pro Trp Pro Leu Tyr Gly Asn Glu Gly Leu Gly Trp Ala Gly Trp
                 85                  90                  95
CTC CTG TCA CCC CGC GGC TCC CGG CCT AGT TGG GGC CCC ACG GAC CCC      336
Leu Leu Ser Pro Arg Gly Ser Arg Pro Ser Trp Gly Pro Thr Asp Pro
            100                 105                 110
CGG CGT AGG                                                          345
Arg Arg Arg
        115 
           
           
             
               115 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             8
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile Val Gly
             20                  25                  30
Gly Val Tyr Leu Leu Pro Arg Arg Gly Pro Arg Leu Gly Val Arg Ala
         35                  40                  45
Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln Pro
     50                  55                  60
Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala Gln Pro Gly
 65                  70                  75                  80
Tyr Pro Trp Pro Leu Tyr Gly Asn Glu Gly Leu Gly Trp Ala Gly Trp
                 85                  90                  95
Leu Leu Ser Pro Arg Gly Ser Arg Pro Ser Trp Gly Pro Thr Asp Pro
            100                 105                 110
Arg Arg Arg
        115 
           
           
             
               1167 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..1167 
                /note “sequence = 333 - 1499 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..1167 
             
             9
ATG AGC ACG AAT CCT AAA CCT CAA AGA AAA ACC AAA CGT AAC ACC AAC       48
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
CGC CGC CCA CAG GAC GTC AAG TTC CCG GGC GGT GGT CAG ATC GTT GGT       96
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile Val Gly
             20                  25                  30
GGA GTT TAC CTG TTG CCG CGC AGG GGC CCC AGG TTG GGT GTG CGC GCG      144
Gly Val Tyr Leu Leu Pro Arg Arg Gly Pro Arg Leu Gly Val Arg Ala
         35                  40                  45
CCC AGG AAG ACT TCC GAG CGG TCG CAA CCT CGT GGA AGG CGA CAA CCT      192
Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln Pro
     50                  55                  60
ATC CCC AAG GCT CGC CGG CCC GAG GGC AGG ACC TGG GCT CAG CCC GGG      240
Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala Gln Pro Gly
 65                  70                  75                  80
TAC CCT TGG CCT CTC TAT GGC AAT GAG GGC TTA GGG TGG GCA GGA TGG      288
Tyr Pro Trp Pro Leu Tyr Gly Asn Glu Gly Leu Gly Trp Ala Gly Trp
                 85                  90                  95
CTC CTG TCA CCC CGC GGC TCC CGG CCT AGT TGG GGC CCC ACG GAC CCC      336
Leu Leu Ser Pro Arg Gly Ser Arg Pro Ser Trp Gly Pro Thr Asp Pro
            100                 105                 110
CGG CGT AGG TCG CGT AAT TTG GGT AAG GTC ATC GAT ACC CTC ACA TGC      384
Arg Arg Arg Ser Arg Asn Leu Gly Lys Val Ile Asp Thr Leu Thr Cys
        115                 120                 125
GGC TTC GCC GAT CTC ATG GGG TAC ATT CCG CTC GTC GGC GCC CCC CTG      432
Gly Phe Ala Asp Leu Met Gly Tyr Ile Pro Leu Val Gly Ala Pro Leu
    130                 135                 140
GGG GGC GCT GCC AGG GCC CTG GCA CAT GGT GTC CGG GTT CTG GAG GAC      480
Gly Gly Ala Ala Arg Ala Leu Ala His Gly Val Arg Val Leu Glu Asp
145                 150                 155                 160
GGC GTG AAC TAT GCA ACA GGG AAT CTG CCC GGT TGC TCT TTT TCT ATC      528
Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly Cys Ser Phe Ser Ile
                165                 170                 175
TTC CTC TTG GCT CTG CTG TCC TGC CTG ACC ACC CCA GCT TCC GCT TAC      576
Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Thr Pro Ala Ser Ala Tyr
            180                 185                 190
GAA GTG CAC AAC GTG TCC GGG ATA TAT CAT GTC ACG AAC GAC TGC TCC      624
Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys Ser
        195                 200                 205
AAC GCA AGC ATT GTG TAT GAG GCA GCG GAC TTG ATC ATG CAT ACT CCT      672
Asn Ala Ser Ile Val Tyr Glu Ala Ala Asp Leu Ile Met His Thr Pro
    210                 215                 220
GGG TGC GTG CCC TGC GTT CGG GAA GGC AAC TCC TCC CGC TGC TGG GTA      720
Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ser Ser Arg Cys Trp Val
225                 230                 235                 240
GCG CTC ACT CCC ACG CTC GCA GCC AGG AAC GTC ACC ATC CCC ACC ACG      768
Ala Leu Thr Pro Thr Leu Ala Ala Arg Asn Val Thr Ile Pro Thr Thr
                245                 250                 255
ACG ATA CGA CGC CAC GTC GAT CTG CTC GTT GGG GCG GCT GCT TTC TGT      816
Thr Ile Arg Arg His Val Asp Leu Leu Val Gly Ala Ala Ala Phe Cys
            260                 265                 270
TCC GCT ATG TAC GTG GGG GAC CTC TGC GGA TCT GTT TTC CTC GTC TCT      864
Ser Ala Met Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val Ser
        275                 280                 285
CAG CTG TTC ACC TTC TCG CCT CGC CGG CAT GTG ACA TTA CAG GAC TGT      912
Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp Cys
    290                 295                 300
AAC TGC TCA ATT TAT CCC GGC CAT GTG TCG GGT CAC CGT ATG GCT TGG      960
Asn Cys Ser Ile Tyr Pro Gly His Val Ser Gly His Arg Met Ala Trp
305                 310                 315                 320
GAC ATG ATG ATG AAC TGG TCG CCC ACA ACA GCC CTA GTG GTG TCG CAG     1008
Asp Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ser Gln
                325                 330                 335
TTA CTC CGG ATC CCA CAA GCC GTC GTG GAC ATG GTG GCG GGG GCC CAC     1056
Leu Leu Arg Ile Pro Gln Ala Val Val Asp Met Val Ala Gly Ala His
            340                 345                 350
TGG GGA GTC CTG GCG GGC CTT GCC TAC TAT TCC ATG GCG GGG AAC TGG     1104
Trp Gly Val Leu Ala Gly Leu Ala Tyr Tyr Ser Met Ala Gly Asn Trp
        355                 360                 365
GCT AAG GTT CTG ATT GTG ATG CTA CTT TTT GCT GGC GTT GAC GGG GAT     1152
Ala Lys Val Leu Ile Val Met Leu Leu Phe Ala Gly Val Asp Gly Asp
    370                 375                 380
ACC CAC GTG ACA GGG                                                 1167
Thr His Val Thr Gly
385 
           
           
             
               389 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             10
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile Val Gly
             20                  25                  30
Gly Val Tyr Leu Leu Pro Arg Arg Gly Pro Arg Leu Gly Val Arg Ala
         35                  40                  45
Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln Pro
     50                  55                  60
Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala Gln Pro Gly
 65                  70                  75                  80
Tyr Pro Trp Pro Leu Tyr Gly Asn Glu Gly Leu Gly Trp Ala Gly Trp
                 85                  90                  95
Leu Leu Ser Pro Arg Gly Ser Arg Pro Ser Trp Gly Pro Thr Asp Pro
            100                 105                 110
Arg Arg Arg Ser Arg Asn Leu Gly Lys Val Ile Asp Thr Leu Thr Cys
        115                 120                 125
Gly Phe Ala Asp Leu Met Gly Tyr Ile Pro Leu Val Gly Ala Pro Leu
    130                 135                 140
Gly Gly Ala Ala Arg Ala Leu Ala His Gly Val Arg Val Leu Glu Asp
145                 150                 155                 160
Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly Cys Ser Phe Ser Ile
                165                 170                 175
Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Thr Pro Ala Ser Ala Tyr
            180                 185                 190
Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys Ser
        195                 200                 205
Asn Ala Ser Ile Val Tyr Glu Ala Ala Asp Leu Ile Met His Thr Pro
    210                 215                 220
Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ser Ser Arg Cys Trp Val
225                 230                 235                 240
Ala Leu Thr Pro Thr Leu Ala Ala Arg Asn Val Thr Ile Pro Thr Thr
                245                 250                 255
Thr Ile Arg Arg His Val Asp Leu Leu Val Gly Ala Ala Ala Phe Cys
            260                 265                 270
Ser Ala Met Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val Ser
        275                 280                 285
Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp Cys
    290                 295                 300
Asn Cys Ser Ile Tyr Pro Gly His Val Ser Gly His Arg Met Ala Trp
305                 310                 315                 320
Asp Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ser Gln
                325                 330                 335
Leu Leu Arg Ile Pro Gln Ala Val Val Asp Met Val Ala Gly Ala His
            340                 345                 350
Trp Gly Val Leu Ala Gly Leu Ala Tyr Tyr Ser Met Ala Gly Asn Trp
        355                 360                 365
Ala Lys Val Leu Ile Val Met Leu Leu Phe Ala Gly Val Asp Gly Asp
    370                 375                 380
Thr His Val Thr Gly
385 
           
           
             
               6039 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..6039 
                /note “sequence = 333 - 6371 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..6039 
             
             11
ATG AGC ACG AAT CCT AAA CCT CAA AGA AAA ACC AAA CGT AAC ACC AAC       48
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
CGC CGC CCA CAG GAC GTC AAG TTC CCG GGC GGT GGT CAG ATC GTT GGT       96
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile Val Gly
             20                  25                  30
GGA GTT TAC CTG TTG CCG CGC AGG GGC CCC AGG TTG GGT GTG CGC GCG      144
Gly Val Tyr Leu Leu Pro Arg Arg Gly Pro Arg Leu Gly Val Arg Ala
         35                  40                  45
CCC AGG AAG ACT TCC GAG CGG TCG CAA CCT CGT GGA AGG CGA CAA CCT      192
Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln Pro
     50                  55                  60
ATC CCC AAG GCT CGC CGG CCC GAG GGC AGG ACC TGG GCT CAG CCC GGG      240
Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala Gln Pro Gly
 65                  70                  75                  80
TAC CCT TGG CCT CTC TAT GGC AAT GAG GGC TTA GGG TGG GCA GGA TGG      288
Tyr Pro Trp Pro Leu Tyr Gly Asn Glu Gly Leu Gly Trp Ala Gly Trp
                 85                  90                  95
CTC CTG TCA CCC CGC GGC TCC CGG CCT AGT TGG GGC CCC ACG GAC CCC      336
Leu Leu Ser Pro Arg Gly Ser Arg Pro Ser Trp Gly Pro Thr Asp Pro
            100                 105                 110
CGG CGT AGG TCG CGT AAT TTG GGT AAG GTC ATC GAT ACC CTC ACA TGC      384
Arg Arg Arg Ser Arg Asn Leu Gly Lys Val Ile Asp Thr Leu Thr Cys
        115                 120                 125
GGC TTC GCC GAT CTC ATG GGG TAC ATT CCG CTC GTC GGC GCC CCC CTG      432
Gly Phe Ala Asp Leu Met Gly Tyr Ile Pro Leu Val Gly Ala Pro Leu
    130                 135                 140
GGG GGC GCT GCC AGG GCC CTG GCA CAT GGT GTC CGG GTT CTG GAG GAC      480
Gly Gly Ala Ala Arg Ala Leu Ala His Gly Val Arg Val Leu Glu Asp
145                 150                 155                 160
GGC GTG AAC TAT GCA ACA GGG AAT CTG CCC GGT TGC TCT TTT TCT ATC      528
Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly Cys Ser Phe Ser Ile
                165                 170                 175
TTC CTC TTG GCT CTG CTG TCC TGC CTG ACC ACC CCA GCT TCC GCT TAC      576
Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Thr Pro Ala Ser Ala Tyr
            180                 185                 190
GAA GTG CAC AAC GTG TCC GGG ATA TAT CAT GTC ACG AAC GAC TGC TCC      624
Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys Ser
        195                 200                 205
AAC GCA AGC ATT GTG TAT GAG GCA GCG GAC TTG ATC ATG CAT ACT CCT      672
Asn Ala Ser Ile Val Tyr Glu Ala Ala Asp Leu Ile Met His Thr Pro
    210                 215                 220
GGG TGC GTG CCC TGC GTT CGG GAA GGC AAC TCC TCC CGC TGC TGG GTA      720
Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ser Ser Arg Cys Trp Val
225                 230                 235                 240
GCG CTC ACT CCC ACG CTC GCA GCC AGG AAC GTC ACC ATC CCC ACC ACG      768
Ala Leu Thr Pro Thr Leu Ala Ala Arg Asn Val Thr Ile Pro Thr Thr
                245                 250                 255
ACG ATA CGA CGC CAC GTC GAT CTG CTC GTT GGG GCG GCT GCT TTC TGT      816
Thr Ile Arg Arg His Val Asp Leu Leu Val Gly Ala Ala Ala Phe Cys
            260                 265                 270
TCC GCT ATG TAC GTG GGG GAC CTC TGC GGA TCT GTT TTC CTC GTC TCT      864
Ser Ala Met Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val Ser
        275                 280                 285
CAG CTG TTC ACC TTC TCG CCT CGC CGG CAT GTG ACA TTA CAG GAC TGT      912
Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp Cys
    290                 295                 300
AAC TGC TCA ATT TAT CCC GGC CAT GTG TCG GGT CAC CGT ATG GCT TGG      960
Asn Cys Ser Ile Tyr Pro Gly His Val Ser Gly His Arg Met Ala Trp
305                 310                 315                 320
GAC ATG ATG ATG AAC TGG TCG CCC ACA ACA GCC CTA GTG GTG TCG CAG     1008
Asp Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ser Gln
                325                 330                 335
TTA CTC CGG ATC CCA CAA GCC GTC GTG GAC ATG GTG GCG GGG GCC CAC     1056
Leu Leu Arg Ile Pro Gln Ala Val Val Asp Met Val Ala Gly Ala His
            340                 345                 350
TGG GGA GTC CTG GCG GGC CTT GCC TAC TAT TCC ATG GCG GGG AAC TGG     1104
Trp Gly Val Leu Ala Gly Leu Ala Tyr Tyr Ser Met Ala Gly Asn Trp
        355                 360                 365
GCT AAG GTT CTG ATT GTG ATG CTA CTT TTT GCT GGC GTT GAC GGG GAT     1152
Ala Lys Val Leu Ile Val Met Leu Leu Phe Ala Gly Val Asp Gly Asp
    370                 375                 380
ACC CAC GTG ACA GGG GGG GCG CAA GCC AAA ACC ACC AAC AGG CTC GTG     1200
Thr His Val Thr Gly Gly Ala Gln Ala Lys Thr Thr Asn Arg Leu Val
385                 390                 395                 400
TCC ATG TTC GCA AGT GGG CCG TCT CAG AAA ATC CAG CTT ATA AAC ACC     1248
Ser Met Phe Ala Ser Gly Pro Ser Gln Lys Ile Gln Leu Ile Asn Thr
                405                 410                 415
AAT GGG AGT TGG CAC ATC AAC AGG ACT GCC CTG AAC TGC AAT GAC TCT     1296
Asn Gly Ser Trp His Ile Asn Arg Thr Ala Leu Asn Cys Asn Asp Ser
            420                 425                 430
CTC CAG ACT GGG TTT CTT GCC GCG CTG TTC TAC ACA CAT AGT TTC AAC     1344
Leu Gln Thr Gly Phe Leu Ala Ala Leu Phe Tyr Thr His Ser Phe Asn
        435                 440                 445
TCG TCC GGG TGC CCA GAG CGC ATG GCC CAG TGC CGC ACC ATT GAC AAG     1392
Ser Ser Gly Cys Pro Glu Arg Met Ala Gln Cys Arg Thr Ile Asp Lys
    450                 455                 460
TTC GAC CAG GGA TGG GGT CCC ATT ACT TAT GCT GAG TCT AGC AGA TCA     1440
Phe Asp Gln Gly Trp Gly Pro Ile Thr Tyr Ala Glu Ser Ser Arg Ser
465                 470                 475                 480
GAC CAG AGG CCA TAT TGC TGG CAC TAC CCA CCT CCA CAA TGT ACC ATC     1488
Asp Gln Arg Pro Tyr Cys Trp His Tyr Pro Pro Pro Gln Cys Thr Ile
                485                 490                 495
GTA CCT GCG TCG GAG GTG TGC GGC CCA GTG TAC TGC TTC ACC CCA AGC     1536
Val Pro Ala Ser Glu Val Cys Gly Pro Val Tyr Cys Phe Thr Pro Ser
            500                 505                 510
CCT GTC GTC GTG GGG ACG ACC GAT CGT TTC GGT GTC CCT ACG TAT AGA     1584
Pro Val Val Val Gly Thr Thr Asp Arg Phe Gly Val Pro Thr Tyr Arg
        515                 520                 525
TGG GGG GAG AAC GAG ACT GAC GTG CTG CTG CTC AAC AAC ACG CGG CCG     1632
Trp Gly Glu Asn Glu Thr Asp Val Leu Leu Leu Asn Asn Thr Arg Pro
    530                 535                 540
CCG CAA GGC AAC TGG TTC GGC TGC ACA TGG ATG AAT AGC ACC GGG TTC     1680
Pro Gln Gly Asn Trp Phe Gly Cys Thr Trp Met Asn Ser Thr Gly Phe
545                 550                 555                 560
ACC AAG ACA TGT GGG GGG CCC CCG TGT AAC ATC GGG GGG GTC GGC AAC     1728
Thr Lys Thr Cys Gly Gly Pro Pro Cys Asn Ile Gly Gly Val Gly Asn
                565                 570                 575
AAC ACC CTG ACC TGC CCC ACG GAC TGC TTC CGG AAG CAC CCC GAG GCT     1776
Asn Thr Leu Thr Cys Pro Thr Asp Cys Phe Arg Lys His Pro Glu Ala
            580                 585                 590
ACC TAC ACA AAA TGT GGT TCG GGG CCT TGG CTG ACA CCT AGG TGC ATG     1824
Thr Tyr Thr Lys Cys Gly Ser Gly Pro Trp Leu Thr Pro Arg Cys Met
        595                 600                 605
GTT GAC TAT CCA TAC AGG CTC TGG CAT TAC CCC TGC ACT GTT AAC TTT     1872
Val Asp Tyr Pro Tyr Arg Leu Trp His Tyr Pro Cys Thr Val Asn Phe
    610                 615                 620
ACC ATC TTC AAG GTT AGG ATG TAT GTG GGG GGG GTG GAG CAC AGG CTC     1920
Thr Ile Phe Lys Val Arg Met Tyr Val Gly Gly Val Glu His Arg Leu
625                 630                 635                 640
AAT GCT GCA TGC AAT TGG ACC CGA GGA GAG CGT TGT GAC TTG GAG GAC     1968
Asn Ala Ala Cys Asn Trp Thr Arg Gly Glu Arg Cys Asp Leu Glu Asp
                645                 650                 655
AGG GAT AGG CCG GAG CTC AGC CCG CTG CTG CTG TCT ACA ACA GAG TGG     2016
Arg Asp Arg Pro Glu Leu Ser Pro Leu Leu Leu Ser Thr Thr Glu Trp
            660                 665                 670
CAG GTA CTG CCC TGT TCC TTC ACC ACC CTA CCA GCT CTG TCC ACT GGC     2064
Gln Val Leu Pro Cys Ser Phe Thr Thr Leu Pro Ala Leu Ser Thr Gly
        675                 680                 685
TTG ATT CAC CTC CAT CAG AAC ATC GTG GAC GTG CAA TAC CTA TAC GGT     2112
Leu Ile His Leu His Gln Asn Ile Val Asp Val Gln Tyr Leu Tyr Gly
    690                 695                 700
ATA GGG TCA GCG GTT GTC TCC TTT GCA ATC AAA TGG GAG TAT GTC CTG     2160
Ile Gly Ser Ala Val Val Ser Phe Ala Ile Lys Trp Glu Tyr Val Leu
705                 710                 715                 720
TTG CTT TTC CTT CTC CTA GCG GAC GCA CGT GTC TGT GCC TGC TTG TGG     2208
Leu Leu Phe Leu Leu Leu Ala Asp Ala Arg Val Cys Ala Cys Leu Trp
                725                 730                 735
ATG ATG CTG CTG ATA GCC CAG GCC GAG GCC GCC TTG GAG AAC CTG GTG     2256
Met Met Leu Leu Ile Ala Gln Ala Glu Ala Ala Leu Glu Asn Leu Val
            740                 745                 750
GTC CTC AAT TCG GCG TCT GTG GCC GGC GCA CAT GGC ATC CTC TCC TTC     2304
Val Leu Asn Ser Ala Ser Val Ala Gly Ala His Gly Ile Leu Ser Phe
        755                 760                 765
CTT GTG TTC TTC TGT GCC GCC TGG TAC ATC AAA GGC AGG CTG GTC CCT     2352
Leu Val Phe Phe Cys Ala Ala Trp Tyr Ile Lys Gly Arg Leu Val Pro
    770                 775                 780
GGG GCG ACA TAT GCT CTT TAT GGC GTG TGG CCG CTG CTC CTG CTC TTG     2400
Gly Ala Thr Tyr Ala Leu Tyr Gly Val Trp Pro Leu Leu Leu Leu Leu
785                 790                 795                 800
CTG GCA TTA CCA CCG CGA GCT TAC GCC ATG GAC CGG GAG ATG GCT GCA     2448
Leu Ala Leu Pro Pro Arg Ala Tyr Ala Met Asp Arg Glu Met Ala Ala
                805                 810                 815
TCG TGC GGA GGC GCG GTT TTT GTG GGT CTG GTA CTC CTG ACT TTG TCA     2496
Ser Cys Gly Gly Ala Val Phe Val Gly Leu Val Leu Leu Thr Leu Ser
            820                 825                 830
CCA TAC TAC AAG GTG TTC CTC GCT AGG CTC ATA TGG TGG TTA CAA TAT     2544
Pro Tyr Tyr Lys Val Phe Leu Ala Arg Leu Ile Trp Trp Leu Gln Tyr
        835                 840                 845
TTT ACC ACC AGA GCC GAG GCG GAC TTA CAT GTG TGG ATC CCC CCC CTC     2592
Phe Thr Thr Arg Ala Glu Ala Asp Leu His Val Trp Ile Pro Pro Leu
    850                 855                 860
AAC GCT CGG GGA GGC CGC GAT GCC ATC ATC CTC CTC ATG TGC GCA GTC     2640
Asn Ala Arg Gly Gly Arg Asp Ala Ile Ile Leu Leu Met Cys Ala Val
865                 870                 875                 880
CAT CCA GAG CTA ATC TTT GAC ATC ACC AAA CTT CTA ATT GCC ATA CTC     2688
His Pro Glu Leu Ile Phe Asp Ile Thr Lys Leu Leu Ile Ala Ile Leu
                885                 890                 895
GGT CCG CTC ATG GTG CTC CAA GCT GGC ATA ACC AGA GTG CCG TAC TTC     2736
Gly Pro Leu Met Val Leu Gln Ala Gly Ile Thr Arg Val Pro Tyr Phe
            900                 905                 910
GTG CGC GCT CAA GGG CTC ATT CAT GCA TGC ATG TTA GTG CGG AAG GTC     2784
Val Arg Ala Gln Gly Leu Ile His Ala Cys Met Leu Val Arg Lys Val
        915                 920                 925
GCT GGG GGT CAT TAT GTC CAA ATG GCC TTC ATG AAG CTG GGC GCG CTG     2832
Ala Gly Gly His Tyr Val Gln Met Ala Phe Met Lys Leu Gly Ala Leu
    930                 935                 940
ACA GGC ACG TAC ATT TAC AAC CAT CTT ACC CCG CTA CGG GAT TGG CCA     2880
Thr Gly Thr Tyr Ile Tyr Asn His Leu Thr Pro Leu Arg Asp Trp Pro
945                 950                 955                 960
CGC GCG GGC CTA CGA GAC CTT GCG GTG GCA GTG GAG CCC GTC GTC TTC     2928
Arg Ala Gly Leu Arg Asp Leu Ala Val Ala Val Glu Pro Val Val Phe
                965                 970                 975
TCC GAC ATG GAG ACC AAG ATC ATC ACC TGG GGA GCA GAC ACC GCG GCG     2976
Ser Asp Met Glu Thr Lys Ile Ile Thr Trp Gly Ala Asp Thr Ala Ala
            980                 985                 990
TGT GGG GAC ATC ATC TTG GGT CTG CCC GTC TCC GCC CGA AGG GGA AAG     3024
Cys Gly Asp Ile Ile Leu Gly Leu Pro Val Ser Ala Arg Arg Gly Lys
        995                 1000                1005
GAG ATA CTC CTG GGC CCG GCC GAT AGT CTT GAA GGG CGG GGG TTG CGA     3072
Glu Ile Leu Leu Gly Pro Ala Asp Ser Leu Glu Gly Arg Gly Leu Arg
    1010                1015                1020
CTC CTC GCG CCC ATC ACG GCC TAC TCC CAA CAG ACG CGG GGC CTA CTT     3120
Leu Leu Ala Pro Ile Thr Ala Tyr Ser Gln Gln Thr Arg Gly Leu Leu
1025                1030                1035                1040
GGT TGC ATC ATC ACT AGC CTT ACA GGC CGG GAC AAG AAC CAG GTC GAG     3168
Gly Cys Ile Ile Thr Ser Leu Thr Gly Arg Asp Lys Asn Gln Val Glu
                1045                1050                1055
GGA GAG GTT CAG GTG GTT TCC ACC GCA ACA CAA TCC TTC CTG GCG ACC     3216
Gly Glu Val Gln Val Val Ser Thr Ala Thr Gln Ser Phe Leu Ala Thr
            1060                1065                1070
TGC GTC AAC GGC GTG TGT TGG ACC GTT TAC CAT GGT GCT GGC TCA AAG     3264
Cys Val Asn Gly Val Cys Trp Thr Val Tyr His Gly Ala Gly Ser Lys
        1075                1080                1085
ACC TTA GCC GCG CCA AAG GGG CCA ATC ACC CAG ATG TAC ACT AAT GTG     3312
Thr Leu Ala Ala Pro Lys Gly Pro Ile Thr Gln Met Tyr Thr Asn Val
    1090                1095                1100
GAC CAG GAC CTC GTC GGC TGG CCC AAG CCC CCC GGG GCG CGT TCC TTG     3360
Asp Gln Asp Leu Val Gly Trp Pro Lys Pro Pro Gly Ala Arg Ser Leu
1105                1110                1115                1120
ACA CCA TGC ACC TGT GGC AGC TCA GAC CTT TAC TTG GTC ACG AGA CAT     3408
Thr Pro Cys Thr Cys Gly Ser Ser Asp Leu Tyr Leu Val Thr Arg His
                1125                1130                1135
GCT GAC GTC ATT CCG GTG CGC CGG CGG GGC GAC AGT AGG GGG AGC CTG     3456
Ala Asp Val Ile Pro Val Arg Arg Arg Gly Asp Ser Arg Gly Ser Leu
            1140                1145                1150
CTC TCC CCC AGG CCT GTC TCC TAC TTG AAG GGC TCT TCG GGT GGT CCA     3504
Leu Ser Pro Arg Pro Val Ser Tyr Leu Lys Gly Ser Ser Gly Gly Pro
        1155                1160                1165
CTG CTC TGC CCC TTC GGG CAC GCT GTG GGC ATC TTC CGG GCT GCC GTA     3552
Leu Leu Cys Pro Phe Gly His Ala Val Gly Ile Phe Arg Ala Ala Val
    1170                1175                1180
TGC ACC CGG GGG GTT GCG AAG GCG GTG GAC TTT GTG CCC GTA GAG TCC     3600
Cys Thr Arg Gly Val Ala Lys Ala Val Asp Phe Val Pro Val Glu Ser
1185                1190                1195                1200
ATG GAA ACT ACT ATG CGG TCT CCG GTC TTC ACG GAC AAC TCA TCC CCC     3648
Met Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro
                1205                1210                1215
CCG GCC GTA CCG CAG TCA TTT CAA GTG GCC CAC CTA CAC GCT CCC ACT     3696
Pro Ala Val Pro Gln Ser Phe Gln Val Ala His Leu His Ala Pro Thr
            1220                1225                1230
GGC AGC GGC AAG AGT ACT AAA GTG CCG GCT GCA TAT GCA GCC CAA GGG     3744
Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala Ala Gln Gly
        1235                1240                1245
TAC AAG GTG CTC GTC CTC AAT CCG TCC GTT GCC GCT ACC TTA GGG TTT     3792
Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe
    1250                1255                1260
GGG GCG TAT ATG TCT AAG GCA CAC GGT ATT GAC CCC AAC ATC AGA ACT     3840
Gly Ala Tyr Met Ser Lys Ala His Gly Ile Asp Pro Asn Ile Arg Thr
1265                1270                1275                1280
GGG GTA AGG ACC ATT ACC ACA GGC GCC CCC GTC ACA TAC TCT ACC TAT     3888
Gly Val Arg Thr Ile Thr Thr Gly Ala Pro Val Thr Tyr Ser Thr Tyr
                1285                1290                1295
GGC AAG TTT CTT GCC GAT GGT GGT TGC TCT GGG GGC GCT TAT GAC ATC     3936
Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp Ile
            1300                1305                1310
ATA ATA TGT GAT GAG TGC CAT TCA ACT GAC TCG ACT ACA ATC TTG GGC     3984
Ile Ile Cys Asp Glu Cys His Ser Thr Asp Ser Thr Thr Ile Leu Gly
        1315                1320                1325
ATC GGC ACA GTC CTG GAC CAA GCG GAG ACG GCT GGA GCG CGG CTT GTC     4032
Ile Gly Thr Val Leu Asp Gln Ala Glu Thr Ala Gly Ala Arg Leu Val
    1330                1335                1340
GTG CTC GCC ACC GCT ACG CCT CCG GGA TCG GTC ACC GTG CCA CAC CCA     4080
Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro His Pro
1345                1350                1355                1360
AAC ATC GAG GAG GTG GCC CTG TCT AAT ACT GGA GAG ATC CCC TTC TAT     4128
Asn Ile Glu Glu Val Ala Leu Ser Asn Thr Gly Glu Ile Pro Phe Tyr
                1365                1370                1375
GGC AAA GCC ATC CCC ATT GAA GCC ATC AGG GGG GGA AGG CAT CTC ATT     4176
Gly Lys Ala Ile Pro Ile Glu Ala Ile Arg Gly Gly Arg His Leu Ile
            1380                1385                1390
TTC TGT CAT TCC AAG AAG AAG TGC GAC GAG CTC GCC GCA AAG CTG TCA     4224
Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Ser
        1395                1400                1405
GGC CTC GGA ATC AAC GCT GTG GCG TAT TAC CGG GGG CTC GAT GTG TCC     4272
Gly Leu Gly Ile Asn Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser
    1410                1415                1420
GTC ATA CCA ACT ATC GGA GAC GTC GTT GTC GTG GCA ACA GAC GCT CTG     4320
Val Ile Pro Thr Ile Gly Asp Val Val Val Val Ala Thr Asp Ala Leu
1425                1430                1435                1440
ATG ACG GGC TAT ACG GGC GAC TTT GAC TCA GTG ATC GAC TGT AAC ACA     4368
Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val Ile Asp Cys Asn Thr
                1445                1450                1455
TGT GTC ACC CAG ACA GTC GAC TTC AGC TTG GAT CCC ACC TTC ACC ATT     4416
Cys Val Thr Gln Thr Val Asp Phe Ser Leu Asp Pro Thr Phe Thr Ile
            1460                1465                1470
GAG ACG ACG ACC GTG CCT CAA GAC GCA GTG TCG CGC TCG CAG CGG CGG     4464
Glu Thr Thr Thr Val Pro Gln Asp Ala Val Ser Arg Ser Gln Arg Arg
        1475                1480                1485
GGT AGG ACT GGC AGG GGT AGG AGA GGC ATC TAC AGG TTT GTG ACT CCG     4512
Gly Arg Thr Gly Arg Gly Arg Arg Gly Ile Tyr Arg Phe Val Thr Pro
    1490                1495                1500
GGA GAA CGG CCC TCG GGC ATG TTC GAT TCC TCG GTC CTG TGT GAG TGC     4560
Gly Glu Arg Pro Ser Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys
1505                1510                1515                1520
TAT GAC GCG GGC TGT GCT TGG TAC GAG CTC ACC CCG GCC GAG ACC TCG     4608
Tyr Asp Ala Gly Cys Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Ser
                1525                1530                1535
GTT AGG TTG CGG GCC TAC CTG AAC ACA CCA GGG TTG CCC GTT TGC CAG     4656
Val Arg Leu Arg Ala Tyr Leu Asn Thr Pro Gly Leu Pro Val Cys Gln
            1540                1545                1550
GAC CAC CTG GAG TTC TGG GAG AGT GTC TTC ACA GGC CTC ACC CAT ATA     4704
Asp His Leu Glu Phe Trp Glu Ser Val Phe Thr Gly Leu Thr His Ile
        1555                1560                1565
GAT GCA CAC TTC TTG TCC CAG ACC AAG CAG GCA GGA GAC AAC TTC CCC     4752
Asp Ala His Phe Leu Ser Gln Thr Lys Gln Ala Gly Asp Asn Phe Pro
    1570                1575                1580
TAC CTG GTA GCA TAC CAA GCC ACG GTG TGC GCC AGG GCT CAG GCC CCA     4800
Tyr Leu Val Ala Tyr Gln Ala Thr Val Cys Ala Arg Ala Gln Ala Pro
1585                1590                1595                1600
CCT CCA TCA TGG GAT CAA ATG TGG AAG TGT CTC ATA CGG CTG AAA CCT     4848
Pro Pro Ser Trp Asp Gln Met Trp Lys Cys Leu Ile Arg Leu Lys Pro
                1605                1610                1615
ACG CTG CAC GGG CCA ACA CCC TTG CTG TAC AGG CTG GGA GCC GTC CAG     4896
Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gln
            1620                1625                1630
AAT GAG GTC ACC CTC ACC CAC CCC ATA ACC AAA TAC ATC ATG GCA TGC     4944
Asn Glu Val Thr Leu Thr His Pro Ile Thr Lys Tyr Ile Met Ala Cys
        1635                1640                1645
ATG TCG GCT GAC CTG GAG GTC GTC ACT AGC ACC TGG GTG CTG GTG GGC     4992
Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly
    1650                1655                1660
GGA GTC CTT GCA GCT CTG GCC GCG TAT TGC CTG ACA ACA GGC AGT GTG     5040
Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Thr Thr Gly Ser Val
1665                1670                1675                1680
GTC ATT GTG GGT AGG ATT ATC TTG TCC GGG AGG CCG GCC ATT GTT CCC     5088
Val Ile Val Gly Arg Ile Ile Leu Ser Gly Arg Pro Ala Ile Val Pro
                1685                1690                1695
GAC AGG GAG CTT CTC TAC CAG GAG TTC GAT GAA ATG GAA GAG TGC GCC     5136
Asp Arg Glu Leu Leu Tyr Gln Glu Phe Asp Glu Met Glu Glu Cys Ala
            1700                1705                1710
TCG CAC CTC CCT TAC ATC GAG CAG GGA ATG CAG CTC GCC GAG CAA TTC     5184
Ser His Leu Pro Tyr Ile Glu Gln Gly Met Gln Leu Ala Glu Gln Phe
        1715                1720                1725
AAG CAG AAA GCG CTC GGG TTA CTG CAA ACA GCC ACC AAA CAA GCG GAG     5232
Lys Gln Lys Ala Leu Gly Leu Leu Gln Thr Ala Thr Lys Gln Ala Glu
    1730                1735                1740
GCT GCT GCT CCC GTG GTG GAG TCC AAG TGG CGA GCC CTT GAG ACA TTC     5280
Ala Ala Ala Pro Val Val Glu Ser Lys Trp Arg Ala Leu Glu Thr Phe
1745                1750                1755                1760
TGG GCG AAG CAC ATG TGG AAT TTC ATC AGC GGG ATA CAG TAC TTA GCA     5328
Trp Ala Lys His Met Trp Asn Phe Ile Ser Gly Ile Gln Tyr Leu Ala
                1765                1770                1775
GGC TTA TCC ACT CTG CCT GGG AAC CCC GCA ATA GCA TCA TTG ATG GCA     5376
Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala Ile Ala Ser Leu Met Ala
            1780                1785                1790
TTC ACA GCC TCT ATC ACC AGC CCG CTC ACC ACC CAA AGT ACC CTC CTG     5424
Phe Thr Ala Ser Ile Thr Ser Pro Leu Thr Thr Gln Ser Thr Leu Leu
        1795                1800                1805
TTT AAC ATC TTG GGG GGG TGG GTG GCT GCC CAA CTC GCC CCC CCC AGC     5472
Phe Asn Ile Leu Gly Gly Trp Val Ala Ala Gln Leu Ala Pro Pro Ser
    1810                1815                1820
GCC GCT TCG GCT TTC GTG GGC GCC GGC ATC GCC GGT GCG GCT GTT GGC     5520
Ala Ala Ser Ala Phe Val Gly Ala Gly Ile Ala Gly Ala Ala Val Gly
1825                1830                1835                1840
AGC ATA GGC CTT GGG AAG GTG CTT GTG GAC ATT CTG GCG GGT TAT GGA     5568
Ser Ile Gly Leu Gly Lys Val Leu Val Asp Ile Leu Ala Gly Tyr Gly
                1845                1850                1855
GCA GGA GTG GCC GGC GCG CTC GTG GCC TTT AAG GTC ATG AGC GGC GAG     5616
Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys Val Met Ser Gly Glu
            1860                1865                1870
ATG CCC TCC ACC GAG GAC CTG GTC AAT CTA CTT CCT GCC ATC CTC TCT     5664
Met Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Ala Ile Leu Ser
        1875                1880                1885
CCT GGC GCC CTG GTC GTC GGG GTC GTG TGT GCA GCA ATA CTG CGT CGA     5712
Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala Ile Leu Arg Arg
    1890                1895                1900
CAC GTG GGT CCG GGA GAG GGG GCT GTG CAG TGG ATG AAC CGG CTG ATA     5760
His Val Gly Pro Gly Glu Gly Ala Val Gln Trp Met Asn Arg Leu Ile
1905                1910                1915                1920
GCG TTC GCC TCG CGG GGT AAT CAT GTT TCC CCC ACG CAC TAT GTG CCT     5808
Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Thr His Tyr Val Pro
                1925                1930                1935
GAG AGC GAC GCC GCA GCG CGT GTT ACT CAG ATC CTC TCC AGC CTT ACC     5856
Glu Ser Asp Ala Ala Ala Arg Val Thr Gln Ile Leu Ser Ser Leu Thr
            1940                1945                1950
ATC ACT CAG CTG CTG AAA AGG CTC CAC CAG TGG ATT AAT GAA GAC TGC     5904
Ile Thr Gln Leu Leu Lys Arg Leu His Gln Trp Ile Asn Glu Asp Cys
        1955                1960                1965
TCC ACA CCG TGT TCC GGC TCG TGG CTA AGG GAT GTT TGG GAC TGG ATA     5952
Ser Thr Pro Cys Ser Gly Ser Trp Leu Arg Asp Val Trp Asp Trp Ile
    1970                1975                1980
TGC ACG GTG TTG ACT GAC TTC AAG ACC TGG CTC CAG TCC AAG CTC CTG     6000
Cys Thr Val Leu Thr Asp Phe Lys Thr Trp Leu Gln Ser Lys Leu Leu
1985                1990                1995                2000
CCG CAG CTA CCT GGA GTC CCT TTT TTC TCG TGC CAA CGC                 6039
Pro Gln Leu Pro Gly Val Pro Phe Phe Ser Cys Gln Arg
                2005                2010 
           
           
             
               2013 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             12
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile Val Gly
             20                  25                  30
Gly Val Tyr Leu Leu Pro Arg Arg Gly Pro Arg Leu Gly Val Arg Ala
         35                  40                  45
Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln Pro
     50                  55                  60
Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala Gln Pro Gly
 65                  70                  75                  80
Tyr Pro Trp Pro Leu Tyr Gly Asn Glu Gly Leu Gly Trp Ala Gly Trp
                 85                  90                  95
Leu Leu Ser Pro Arg Gly Ser Arg Pro Ser Trp Gly Pro Thr Asp Pro
            100                 105                 110
Arg Arg Arg Ser Arg Asn Leu Gly Lys Val Ile Asp Thr Leu Thr Cys
        115                 120                 125
Gly Phe Ala Asp Leu Met Gly Tyr Ile Pro Leu Val Gly Ala Pro Leu
    130                 135                 140
Gly Gly Ala Ala Arg Ala Leu Ala His Gly Val Arg Val Leu Glu Asp
145                 150                 155                 160
Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly Cys Ser Phe Ser Ile
                165                 170                 175
Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Thr Pro Ala Ser Ala Tyr
            180                 185                 190
Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys Ser
        195                 200                 205
Asn Ala Ser Ile Val Tyr Glu Ala Ala Asp Leu Ile Met His Thr Pro
    210                 215                 220
Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ser Ser Arg Cys Trp Val
225                 230                 235                 240
Ala Leu Thr Pro Thr Leu Ala Ala Arg Asn Val Thr Ile Pro Thr Thr
                245                 250                 255
Thr Ile Arg Arg His Val Asp Leu Leu Val Gly Ala Ala Ala Phe Cys
            260                 265                 270
Ser Ala Met Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val Ser
        275                 280                 285
Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp Cys
    290                 295                 300
Asn Cys Ser Ile Tyr Pro Gly His Val Ser Gly His Arg Met Ala Trp
305                 310                 315                 320
Asp Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ser Gln
                325                 330                 335
Leu Leu Arg Ile Pro Gln Ala Val Val Asp Met Val Ala Gly Ala His
            340                 345                 350
Trp Gly Val Leu Ala Gly Leu Ala Tyr Tyr Ser Met Ala Gly Asn Trp
        355                 360                 365
Ala Lys Val Leu Ile Val Met Leu Leu Phe Ala Gly Val Asp Gly Asp
    370                 375                 380
Thr His Val Thr Gly Gly Ala Gln Ala Lys Thr Thr Asn Arg Leu Val
385                 390                 395                 400
Ser Met Phe Ala Ser Gly Pro Ser Gln Lys Ile Gln Leu Ile Asn Thr
                405                 410                 415
Asn Gly Ser Trp His Ile Asn Arg Thr Ala Leu Asn Cys Asn Asp Ser
            420                 425                 430
Leu Gln Thr Gly Phe Leu Ala Ala Leu Phe Tyr Thr His Ser Phe Asn
        435                 440                 445
Ser Ser Gly Cys Pro Glu Arg Met Ala Gln Cys Arg Thr Ile Asp Lys
    450                 455                 460
Phe Asp Gln Gly Trp Gly Pro Ile Thr Tyr Ala Glu Ser Ser Arg Ser
465                 470                 475                 480
Asp Gln Arg Pro Tyr Cys Trp His Tyr Pro Pro Pro Gln Cys Thr Ile
                485                 490                 495
Val Pro Ala Ser Glu Val Cys Gly Pro Val Tyr Cys Phe Thr Pro Ser
            500                 505                 510
Pro Val Val Val Gly Thr Thr Asp Arg Phe Gly Val Pro Thr Tyr Arg
        515                 520                 525
Trp Gly Glu Asn Glu Thr Asp Val Leu Leu Leu Asn Asn Thr Arg Pro
    530                 535                 540
Pro Gln Gly Asn Trp Phe Gly Cys Thr Trp Met Asn Ser Thr Gly Phe
545                 550                 555                 560
Thr Lys Thr Cys Gly Gly Pro Pro Cys Asn Ile Gly Gly Val Gly Asn
                565                 570                 575
Asn Thr Leu Thr Cys Pro Thr Asp Cys Phe Arg Lys His Pro Glu Ala
            580                 585                 590
Thr Tyr Thr Lys Cys Gly Ser Gly Pro Trp Leu Thr Pro Arg Cys Met
        595                 600                 605
Val Asp Tyr Pro Tyr Arg Leu Trp His Tyr Pro Cys Thr Val Asn Phe
    610                 615                 620
Thr Ile Phe Lys Val Arg Met Tyr Val Gly Gly Val Glu His Arg Leu
625                 630                 635                 640
Asn Ala Ala Cys Asn Trp Thr Arg Gly Glu Arg Cys Asp Leu Glu Asp
                645                 650                 655
Arg Asp Arg Pro Glu Leu Ser Pro Leu Leu Leu Ser Thr Thr Glu Trp
            660                 665                 670
Gln Val Leu Pro Cys Ser Phe Thr Thr Leu Pro Ala Leu Ser Thr Gly
        675                 680                 685
Leu Ile His Leu His Gln Asn Ile Val Asp Val Gln Tyr Leu Tyr Gly
    690                 695                 700
Ile Gly Ser Ala Val Val Ser Phe Ala Ile Lys Trp Glu Tyr Val Leu
705                 710                 715                 720
Leu Leu Phe Leu Leu Leu Ala Asp Ala Arg Val Cys Ala Cys Leu Trp
                725                 730                 735
Met Met Leu Leu Ile Ala Gln Ala Glu Ala Ala Leu Glu Asn Leu Val
            740                 745                 750
Val Leu Asn Ser Ala Ser Val Ala Gly Ala His Gly Ile Leu Ser Phe
        755                 760                 765
Leu Val Phe Phe Cys Ala Ala Trp Tyr Ile Lys Gly Arg Leu Val Pro
    770                 775                 780
Gly Ala Thr Tyr Ala Leu Tyr Gly Val Trp Pro Leu Leu Leu Leu Leu
785                 790                 795                 800
Leu Ala Leu Pro Pro Arg Ala Tyr Ala Met Asp Arg Glu Met Ala Ala
                805                 810                 815
Ser Cys Gly Gly Ala Val Phe Val Gly Leu Val Leu Leu Thr Leu Ser
            820                 825                 830
Pro Tyr Tyr Lys Val Phe Leu Ala Arg Leu Ile Trp Trp Leu Gln Tyr
        835                 840                 845
Phe Thr Thr Arg Ala Glu Ala Asp Leu His Val Trp Ile Pro Pro Leu
    850                 855                 860
Asn Ala Arg Gly Gly Arg Asp Ala Ile Ile Leu Leu Met Cys Ala Val
865                 870                 875                 880
His Pro Glu Leu Ile Phe Asp Ile Thr Lys Leu Leu Ile Ala Ile Leu
                885                 890                 895
Gly Pro Leu Met Val Leu Gln Ala Gly Ile Thr Arg Val Pro Tyr Phe
            900                 905                 910
Val Arg Ala Gln Gly Leu Ile His Ala Cys Met Leu Val Arg Lys Val
        915                 920                 925
Ala Gly Gly His Tyr Val Gln Met Ala Phe Met Lys Leu Gly Ala Leu
    930                 935                 940
Thr Gly Thr Tyr Ile Tyr Asn His Leu Thr Pro Leu Arg Asp Trp Pro
945                 950                 955                 960
Arg Ala Gly Leu Arg Asp Leu Ala Val Ala Val Glu Pro Val Val Phe
                965                 970                 975
Ser Asp Met Glu Thr Lys Ile Ile Thr Trp Gly Ala Asp Thr Ala Ala
            980                 985                 990
Cys Gly Asp Ile Ile Leu Gly Leu Pro Val Ser Ala Arg Arg Gly Lys
        995                 1000                1005
Glu Ile Leu Leu Gly Pro Ala Asp Ser Leu Glu Gly Arg Gly Leu Arg
    1010                1015                1020
Leu Leu Ala Pro Ile Thr Ala Tyr Ser Gln Gln Thr Arg Gly Leu Leu
1025                1030                1035                1040
Gly Cys Ile Ile Thr Ser Leu Thr Gly Arg Asp Lys Asn Gln Val Glu
                1045                1050                1055
Gly Glu Val Gln Val Val Ser Thr Ala Thr Gln Ser Phe Leu Ala Thr
            1060                1065                1070
Cys Val Asn Gly Val Cys Trp Thr Val Tyr His Gly Ala Gly Ser Lys
        1075                1080                1085
Thr Leu Ala Ala Pro Lys Gly Pro Ile Thr Gln Met Tyr Thr Asn Val
    1090                1095                1100
Asp Gln Asp Leu Val Gly Trp Pro Lys Pro Pro Gly Ala Arg Ser Leu
1105                1110                1115                1120
Thr Pro Cys Thr Cys Gly Ser Ser Asp Leu Tyr Leu Val Thr Arg His
                1125                1130                1135
Ala Asp Val Ile Pro Val Arg Arg Arg Gly Asp Ser Arg Gly Ser Leu
            1140                1145                1150
Leu Ser Pro Arg Pro Val Ser Tyr Leu Lys Gly Ser Ser Gly Gly Pro
        1155                1160                1165
Leu Leu Cys Pro Phe Gly His Ala Val Gly Ile Phe Arg Ala Ala Val
    1170                1175                1180
Cys Thr Arg Gly Val Ala Lys Ala Val Asp Phe Val Pro Val Glu Ser
1185                1190                1195                1200
Met Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro
                1205                1210                1215
Pro Ala Val Pro Gln Ser Phe Gln Val Ala His Leu His Ala Pro Thr
            1220                1225                1230
Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala Ala Gln Gly
        1235                1240                1245
Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe
    1250                1255                1260
Gly Ala Tyr Met Ser Lys Ala His Gly Ile Asp Pro Asn Ile Arg Thr
1265                1270                1275                1280
Gly Val Arg Thr Ile Thr Thr Gly Ala Pro Val Thr Tyr Ser Thr Tyr
                1285                1290                1295
Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp Ile
            1300                1305                1310
Ile Ile Cys Asp Glu Cys His Ser Thr Asp Ser Thr Thr Ile Leu Gly
        1315                1320                1325
Ile Gly Thr Val Leu Asp Gln Ala Glu Thr Ala Gly Ala Arg Leu Val
    1330                1335                1340
Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro His Pro
1345                1350                1355                1360
Asn Ile Glu Glu Val Ala Leu Ser Asn Thr Gly Glu Ile Pro Phe Tyr
                1365                1370                1375
Gly Lys Ala Ile Pro Ile Glu Ala Ile Arg Gly Gly Arg His Leu Ile
            1380                1385                1390
Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Ser
        1395                1400                1405
Gly Leu Gly Ile Asn Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser
    1410                1415                1420
Val Ile Pro Thr Ile Gly Asp Val Val Val Val Ala Thr Asp Ala Leu
1425                1430                1435                1440
Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val Ile Asp Cys Asn Thr
                1445                1450                1455
Cys Val Thr Gln Thr Val Asp Phe Ser Leu Asp Pro Thr Phe Thr Ile
            1460                1465                1470
Glu Thr Thr Thr Val Pro Gln Asp Ala Val Ser Arg Ser Gln Arg Arg
        1475                1480                1485
Gly Arg Thr Gly Arg Gly Arg Arg Gly Ile Tyr Arg Phe Val Thr Pro
    1490                1495                1500
Gly Glu Arg Pro Ser Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys
1505                1510                1515                1520
Tyr Asp Ala Gly Cys Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Ser
                1525                1530                1535
Val Arg Leu Arg Ala Tyr Leu Asn Thr Pro Gly Leu Pro Val Cys Gln
            1540                1545                1550
Asp His Leu Glu Phe Trp Glu Ser Val Phe Thr Gly Leu Thr His Ile
        1555                1560                1565
Asp Ala His Phe Leu Ser Gln Thr Lys Gln Ala Gly Asp Asn Phe Pro
    1570                1575                1580
Tyr Leu Val Ala Tyr Gln Ala Thr Val Cys Ala Arg Ala Gln Ala Pro
1585                1590                1595                1600
Pro Pro Ser Trp Asp Gln Met Trp Lys Cys Leu Ile Arg Leu Lys Pro
                1605                1610                1615
Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gln
            1620                1625                1630
Asn Glu Val Thr Leu Thr His Pro Ile Thr Lys Tyr Ile Met Ala Cys
        1635                1640                1645
Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly
    1650                1655                1660
Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Thr Thr Gly Ser Val
1665                1670                1675                1680
Val Ile Val Gly Arg Ile Ile Leu Ser Gly Arg Pro Ala Ile Val Pro
                1685                1690                1695
Asp Arg Glu Leu Leu Tyr Gln Glu Phe Asp Glu Met Glu Glu Cys Ala
            1700                1705                1710
Ser His Leu Pro Tyr Ile Glu Gln Gly Met Gln Leu Ala Glu Gln Phe
        1715                1720                1725
Lys Gln Lys Ala Leu Gly Leu Leu Gln Thr Ala Thr Lys Gln Ala Glu
    1730                1735                1740
Ala Ala Ala Pro Val Val Glu Ser Lys Trp Arg Ala Leu Glu Thr Phe
1745                1750                1755                1760
Trp Ala Lys His Met Trp Asn Phe Ile Ser Gly Ile Gln Tyr Leu Ala
                1765                1770                1775
Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala Ile Ala Ser Leu Met Ala
            1780                1785                1790
Phe Thr Ala Ser Ile Thr Ser Pro Leu Thr Thr Gln Ser Thr Leu Leu
        1795                1800                1805
Phe Asn Ile Leu Gly Gly Trp Val Ala Ala Gln Leu Ala Pro Pro Ser
    1810                1815                1820
Ala Ala Ser Ala Phe Val Gly Ala Gly Ile Ala Gly Ala Ala Val Gly
1825                1830                1835                1840
Ser Ile Gly Leu Gly Lys Val Leu Val Asp Ile Leu Ala Gly Tyr Gly
                1845                1850                1855
Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys Val Met Ser Gly Glu
            1860                1865                1870
Met Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Ala Ile Leu Ser
        1875                1880                1885
Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala Ile Leu Arg Arg
    1890                1895                1900
His Val Gly Pro Gly Glu Gly Ala Val Gln Trp Met Asn Arg Leu Ile
1905                1910                1915                1920
Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Thr His Tyr Val Pro
                1925                1930                1935
Glu Ser Asp Ala Ala Ala Arg Val Thr Gln Ile Leu Ser Ser Leu Thr
            1940                1945                1950
Ile Thr Gln Leu Leu Lys Arg Leu His Gln Trp Ile Asn Glu Asp Cys
        1955                1960                1965
Ser Thr Pro Cys Ser Gly Ser Trp Leu Arg Asp Val Trp Asp Trp Ile
    1970                1975                1980
Cys Thr Val Leu Thr Asp Phe Lys Thr Trp Leu Gln Ser Lys Leu Leu
1985                1990                1995                2000
Pro Gln Leu Pro Gly Val Pro Phe Phe Ser Cys Gln Arg
                2005                2010 
           
           
             
               9030 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..9030 
                /note “sequence = 333 - 9362 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..9030 
             
             13
ATG AGC ACG AAT CCT AAA CCT CAA AGA AAA ACC AAA CGT AAC ACC AAC       48
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
CGC CGC CCA CAG GAC GTC AAG TTC CCG GGC GGT GGT CAG ATC GTT GGT       96
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile Val Gly
             20                  25                  30
GGA GTT TAC CTG TTG CCG CGC AGG GGC CCC AGG TTG GGT GTG CGC GCG      144
Gly Val Tyr Leu Leu Pro Arg Arg Gly Pro Arg Leu Gly Val Arg Ala
         35                  40                  45
CCC AGG AAG ACT TCC GAG CGG TCG CAA CCT CGT GGA AGG CGA CAA CCT      192
Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln Pro
     50                  55                  60
ATC CCC AAG GCT CGC CGG CCC GAG GGC AGG ACC TGG GCT CAG CCC GGG      240
Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala Gln Pro Gly
 65                  70                  75                  80
TAC CCT TGG CCT CTC TAT GGC AAT GAG GGC TTA GGG TGG GCA GGA TGG      288
Tyr Pro Trp Pro Leu Tyr Gly Asn Glu Gly Leu Gly Trp Ala Gly Trp
                 85                  90                  95
CTC CTG TCA CCC CGC GGC TCC CGG CCT AGT TGG GGC CCC ACG GAC CCC      336
Leu Leu Ser Pro Arg Gly Ser Arg Pro Ser Trp Gly Pro Thr Asp Pro
            100                 105                 110
CGG CGT AGG TCG CGT AAT TTG GGT AAG GTC ATC GAT ACC CTC ACA TGC      384
Arg Arg Arg Ser Arg Asn Leu Gly Lys Val Ile Asp Thr Leu Thr Cys
        115                 120                 125
GGC TTC GCC GAT CTC ATG GGG TAC ATT CCG CTC GTC GGC GCC CCC CTG      432
Gly Phe Ala Asp Leu Met Gly Tyr Ile Pro Leu Val Gly Ala Pro Leu
    130                 135                 140
GGG GGC GCT GCC AGG GCC CTG GCA CAT GGT GTC CGG GTT CTG GAG GAC      480
Gly Gly Ala Ala Arg Ala Leu Ala His Gly Val Arg Val Leu Glu Asp
145                 150                 155                 160
GGC GTG AAC TAT GCA ACA GGG AAT CTG CCC GGT TGC TCT TTT TCT ATC      528
Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly Cys Ser Phe Ser Ile
                165                 170                 175
TTC CTC TTG GCT CTG CTG TCC TGC CTG ACC ACC CCA GCT TCC GCT TAC      576
Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Thr Pro Ala Ser Ala Tyr
            180                 185                 190
GAA GTG CAC AAC GTG TCC GGG ATA TAT CAT GTC ACG AAC GAC TGC TCC      624
Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys Ser
        195                 200                 205
AAC GCA AGC ATT GTG TAT GAG GCA GCG GAC TTG ATC ATG CAT ACT CCT      672
Asn Ala Ser Ile Val Tyr Glu Ala Ala Asp Leu Ile Met His Thr Pro
    210                 215                 220
GGG TGC GTG CCC TGC GTT CGG GAA GGC AAC TCC TCC CGC TGC TGG GTA      720
Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ser Ser Arg Cys Trp Val
225                 230                 235                 240
GCG CTC ACT CCC ACG CTC GCA GCC AGG AAC GTC ACC ATC CCC ACC ACG      768
Ala Leu Thr Pro Thr Leu Ala Ala Arg Asn Val Thr Ile Pro Thr Thr
                245                 250                 255
ACG ATA CGA CGC CAC GTC GAT CTG CTC GTT GGG GCG GCT GCT TTC TGT      816
Thr Ile Arg Arg His Val Asp Leu Leu Val Gly Ala Ala Ala Phe Cys
            260                 265                 270
TCC GCT ATG TAC GTG GGG GAC CTC TGC GGA TCT GTT TTC CTC GTC TCT      864
Ser Ala Met Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val Ser
        275                 280                 285
CAG CTG TTC ACC TTC TCG CCT CGC CGG CAT GTG ACA TTA CAG GAC TGT      912
Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp Cys
    290                 295                 300
AAC TGC TCA ATT TAT CCC GGC CAT GTG TCG GGT CAC CGT ATG GCT TGG      960
Asn Cys Ser Ile Tyr Pro Gly His Val Ser Gly His Arg Met Ala Trp
305                 310                 315                 320
GAC ATG ATG ATG AAC TGG TCG CCC ACA ACA GCC CTA GTG GTG TCG CAG     1008
Asp Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ser Gln
                325                 330                 335
TTA CTC CGG ATC CCA CAA GCC GTC GTG GAC ATG GTG GCG GGG GCC CAC     1056
Leu Leu Arg Ile Pro Gln Ala Val Val Asp Met Val Ala Gly Ala His
            340                 345                 350
TGG GGA GTC CTG GCG GGC CTT GCC TAC TAT TCC ATG GCG GGG AAC TGG     1104
Trp Gly Val Leu Ala Gly Leu Ala Tyr Tyr Ser Met Ala Gly Asn Trp
        355                 360                 365
GCT AAG GTT CTG ATT GTG ATG CTA CTT TTT GCT GGC GTT GAC GGG GAT     1152
Ala Lys Val Leu Ile Val Met Leu Leu Phe Ala Gly Val Asp Gly Asp
    370                 375                 380
ACC CAC GTG ACA GGG GGG GCG CAA GCC AAA ACC ACC AAC AGG CTC GTG     1200
Thr His Val Thr Gly Gly Ala Gln Ala Lys Thr Thr Asn Arg Leu Val
385                 390                 395                 400
TCC ATG TTC GCA AGT GGG CCG TCT CAG AAA ATC CAG CTT ATA AAC ACC     1248
Ser Met Phe Ala Ser Gly Pro Ser Gln Lys Ile Gln Leu Ile Asn Thr
                405                 410                 415
AAT GGG AGT TGG CAC ATC AAC AGG ACT GCC CTG AAC TGC AAT GAC TCT     1296
Asn Gly Ser Trp His Ile Asn Arg Thr Ala Leu Asn Cys Asn Asp Ser
            420                 425                 430
CTC CAG ACT GGG TTT CTT GCC GCG CTG TTC TAC ACA CAT AGT TTC AAC     1344
Leu Gln Thr Gly Phe Leu Ala Ala Leu Phe Tyr Thr His Ser Phe Asn
        435                 440                 445
TCG TCC GGG TGC CCA GAG CGC ATG GCC CAG TGC CGC ACC ATT GAC AAG     1392
Ser Ser Gly Cys Pro Glu Arg Met Ala Gln Cys Arg Thr Ile Asp Lys
    450                 455                 460
TTC GAC CAG GGA TGG GGT CCC ATT ACT TAT GCT GAG TCT AGC AGA TCA     1440
Phe Asp Gln Gly Trp Gly Pro Ile Thr Tyr Ala Glu Ser Ser Arg Ser
465                 470                 475                 480
GAC CAG AGG CCA TAT TGC TGG CAC TAC CCA CCT CCA CAA TGT ACC ATC     1488
Asp Gln Arg Pro Tyr Cys Trp His Tyr Pro Pro Pro Gln Cys Thr Ile
                485                 490                 495
GTA CCT GCG TCG GAG GTG TGC GGC CCA GTG TAC TGC TTC ACC CCA AGC     1536
Val Pro Ala Ser Glu Val Cys Gly Pro Val Tyr Cys Phe Thr Pro Ser
            500                 505                 510
CCT GTC GTC GTG GGG ACG ACC GAT CGT TTC GGT GTC CCT ACG TAT AGA     1584
Pro Val Val Val Gly Thr Thr Asp Arg Phe Gly Val Pro Thr Tyr Arg
        515                 520                 525
TGG GGG GAG AAC GAG ACT GAC GTG CTG CTG CTC AAC AAC ACG CGG CCG     1632
Trp Gly Glu Asn Glu Thr Asp Val Leu Leu Leu Asn Asn Thr Arg Pro
    530                 535                 540
CCG CAA GGC AAC TGG TTC GGC TGC ACA TGG ATG AAT AGC ACC GGG TTC     1680
Pro Gln Gly Asn Trp Phe Gly Cys Thr Trp Met Asn Ser Thr Gly Phe
545                 550                 555                 560
ACC AAG ACA TGT GGG GGG CCC CCG TGT AAC ATC GGG GGG GTC GGC AAC     1728
Thr Lys Thr Cys Gly Gly Pro Pro Cys Asn Ile Gly Gly Val Gly Asn
                565                 570                 575
AAC ACC CTG ACC TGC CCC ACG GAC TGC TTC CGG AAG CAC CCC GAG GCT     1776
Asn Thr Leu Thr Cys Pro Thr Asp Cys Phe Arg Lys His Pro Glu Ala
            580                 585                 590
ACC TAC ACA AAA TGT GGT TCG GGG CCT TGG CTG ACA CCT AGG TGC ATG     1824
Thr Tyr Thr Lys Cys Gly Ser Gly Pro Trp Leu Thr Pro Arg Cys Met
        595                 600                 605
GTT GAC TAT CCA TAC AGG CTC TGG CAT TAC CCC TGC ACT GTT AAC TTT     1872
Val Asp Tyr Pro Tyr Arg Leu Trp His Tyr Pro Cys Thr Val Asn Phe
    610                 615                 620
ACC ATC TTC AAG GTT AGG ATG TAT GTG GGG GGG GTG GAG CAC AGG CTC     1920
Thr Ile Phe Lys Val Arg Met Tyr Val Gly Gly Val Glu His Arg Leu
625                 630                 635                 640
AAT GCT GCA TGC AAT TGG ACC CGA GGA GAG CGT TGT GAC TTG GAG GAC     1968
Asn Ala Ala Cys Asn Trp Thr Arg Gly Glu Arg Cys Asp Leu Glu Asp
                645                 650                 655
AGG GAT AGG CCG GAG CTC AGC CCG CTG CTG CTG TCT ACA ACA GAG TGG     2016
Arg Asp Arg Pro Glu Leu Ser Pro Leu Leu Leu Ser Thr Thr Glu Trp
            660                 665                 670
CAG GTA CTG CCC TGT TCC TTC ACC ACC CTA CCA GCT CTG TCC ACT GGC     2064
Gln Val Leu Pro Cys Ser Phe Thr Thr Leu Pro Ala Leu Ser Thr Gly
        675                 680                 685
TTG ATT CAC CTC CAT CAG AAC ATC GTG GAC GTG CAA TAC CTA TAC GGT     2112
Leu Ile His Leu His Gln Asn Ile Val Asp Val Gln Tyr Leu Tyr Gly
    690                 695                 700
ATA GGG TCA GCG GTT GTC TCC TTT GCA ATC AAA TGG GAG TAT GTC CTG     2160
Ile Gly Ser Ala Val Val Ser Phe Ala Ile Lys Trp Glu Tyr Val Leu
705                 710                 715                 720
TTG CTT TTC CTT CTC CTA GCG GAC GCA CGT GTC TGT GCC TGC TTG TGG     2208
Leu Leu Phe Leu Leu Leu Ala Asp Ala Arg Val Cys Ala Cys Leu Trp
                725                 730                 735
ATG ATG CTG CTG ATA GCC CAG GCC GAG GCC GCC TTG GAG AAC CTG GTG     2256
Met Met Leu Leu Ile Ala Gln Ala Glu Ala Ala Leu Glu Asn Leu Val
            740                 745                 750
GTC CTC AAT TCG GCG TCT GTG GCC GGC GCA CAT GGC ATC CTC TCC TTC     2304
Val Leu Asn Ser Ala Ser Val Ala Gly Ala His Gly Ile Leu Ser Phe
        755                 760                 765
CTT GTG TTC TTC TGT GCC GCC TGG TAC ATC AAA GGC AGG CTG GTC CCT     2352
Leu Val Phe Phe Cys Ala Ala Trp Tyr Ile Lys Gly Arg Leu Val Pro
    770                 775                 780
GGG GCG ACA TAT GCT CTT TAT GGC GTG TGG CCG CTG CTC CTG CTC TTG     2400
Gly Ala Thr Tyr Ala Leu Tyr Gly Val Trp Pro Leu Leu Leu Leu Leu
785                 790                 795                 800
CTG GCA TTA CCA CCG CGA GCT TAC GCC ATG GAC CGG GAG ATG GCT GCA     2448
Leu Ala Leu Pro Pro Arg Ala Tyr Ala Met Asp Arg Glu Met Ala Ala
                805                 810                 815
TCG TGC GGA GGC GCG GTT TTT GTG GGT CTG GTA CTC CTG ACT TTG TCA     2496
Ser Cys Gly Gly Ala Val Phe Val Gly Leu Val Leu Leu Thr Leu Ser
            820                 825                 830
CCA TAC TAC AAG GTG TTC CTC GCT AGG CTC ATA TGG TGG TTA CAA TAT     2544
Pro Tyr Tyr Lys Val Phe Leu Ala Arg Leu Ile Trp Trp Leu Gln Tyr
        835                 840                 845
TTT ACC ACC AGA GCC GAG GCG GAC TTA CAT GTG TGG ATC CCC CCC CTC     2592
Phe Thr Thr Arg Ala Glu Ala Asp Leu His Val Trp Ile Pro Pro Leu
    850                 855                 860
AAC GCT CGG GGA GGC CGC GAT GCC ATC ATC CTC CTC ATG TGC GCA GTC     2640
Asn Ala Arg Gly Gly Arg Asp Ala Ile Ile Leu Leu Met Cys Ala Val
865                 870                 875                 880
CAT CCA GAG CTA ATC TTT GAC ATC ACC AAA CTT CTA ATT GCC ATA CTC     2688
His Pro Glu Leu Ile Phe Asp Ile Thr Lys Leu Leu Ile Ala Ile Leu
                885                 890                 895
GGT CCG CTC ATG GTG CTC CAA GCT GGC ATA ACC AGA GTG CCG TAC TTC     2736
Gly Pro Leu Met Val Leu Gln Ala Gly Ile Thr Arg Val Pro Tyr Phe
            900                 905                 910
GTG CGC GCT CAA GGG CTC ATT CAT GCA TGC ATG TTA GTG CGG AAG GTC     2784
Val Arg Ala Gln Gly Leu Ile His Ala Cys Met Leu Val Arg Lys Val
        915                 920                 925
GCT GGG GGT CAT TAT GTC CAA ATG GCC TTC ATG AAG CTG GGC GCG CTG     2832
Ala Gly Gly His Tyr Val Gln Met Ala Phe Met Lys Leu Gly Ala Leu
    930                 935                 940
ACA GGC ACG TAC ATT TAC AAC CAT CTT ACC CCG CTA CGG GAT TGG CCA     2880
Thr Gly Thr Tyr Ile Tyr Asn His Leu Thr Pro Leu Arg Asp Trp Pro
945                 950                 955                 960
CGC GCG GGC CTA CGA GAC CTT GCG GTG GCA GTG GAG CCC GTC GTC TTC     2928
Arg Ala Gly Leu Arg Asp Leu Ala Val Ala Val Glu Pro Val Val Phe
                965                 970                 975
TCC GAC ATG GAG ACC AAG ATC ATC ACC TGG GGA GCA GAC ACC GCG GCG     2976
Ser Asp Met Glu Thr Lys Ile Ile Thr Trp Gly Ala Asp Thr Ala Ala
            980                 985                 990
TGT GGG GAC ATC ATC TTG GGT CTG CCC GTC TCC GCC CGA AGG GGA AAG     3024
Cys Gly Asp Ile Ile Leu Gly Leu Pro Val Ser Ala Arg Arg Gly Lys
        995                 1000                1005
GAG ATA CTC CTG GGC CCG GCC GAT AGT CTT GAA GGG CGG GGG TTG CGA     3072
Glu Ile Leu Leu Gly Pro Ala Asp Ser Leu Glu Gly Arg Gly Leu Arg
    1010                1015                1020
CTC CTC GCG CCC ATC ACG GCC TAC TCC CAA CAG ACG CGG GGC CTA CTT     3120
Leu Leu Ala Pro Ile Thr Ala Tyr Ser Gln Gln Thr Arg Gly Leu Leu
1025                1030                1035                1040
GGT TGC ATC ATC ACT AGC CTT ACA GGC CGG GAC AAG AAC CAG GTC GAG     3168
Gly Cys Ile Ile Thr Ser Leu Thr Gly Arg Asp Lys Asn Gln Val Glu
                1045                1050                1055
GGA GAG GTT CAG GTG GTT TCC ACC GCA ACA CAA TCC TTC CTG GCG ACC     3216
Gly Glu Val Gln Val Val Ser Thr Ala Thr Gln Ser Phe Leu Ala Thr
            1060                1065                1070
TGC GTC AAC GGC GTG TGT TGG ACC GTT TAC CAT GGT GCT GGC TCA AAG     3264
Cys Val Asn Gly Val Cys Trp Thr Val Tyr His Gly Ala Gly Ser Lys
        1075                1080                1085
ACC TTA GCC GCG CCA AAG GGG CCA ATC ACC CAG ATG TAC ACT AAT GTG     3312
Thr Leu Ala Ala Pro Lys Gly Pro Ile Thr Gln Met Tyr Thr Asn Val
    1090                1095                1100
GAC CAG GAC CTC GTC GGC TGG CCC AAG CCC CCC GGG GCG CGT TCC TTG     3360
Asp Gln Asp Leu Val Gly Trp Pro Lys Pro Pro Gly Ala Arg Ser Leu
1105                1110                1115                1120
ACA CCA TGC ACC TGT GGC AGC TCA GAC CTT TAC TTG GTC ACG AGA CAT     3408
Thr Pro Cys Thr Cys Gly Ser Ser Asp Leu Tyr Leu Val Thr Arg His
                1125                1130                1135
GCT GAC GTC ATT CCG GTG CGC CGG CGG GGC GAC AGT AGG GGG AGC CTG     3456
Ala Asp Val Ile Pro Val Arg Arg Arg Gly Asp Ser Arg Gly Ser Leu
            1140                1145                1150
CTC TCC CCC AGG CCT GTC TCC TAC TTG AAG GGC TCT TCG GGT GGT CCA     3504
Leu Ser Pro Arg Pro Val Ser Tyr Leu Lys Gly Ser Ser Gly Gly Pro
        1155                1160                1165
CTG CTC TGC CCC TTC GGG CAC GCT GTG GGC ATC TTC CGG GCT GCC GTA     3552
Leu Leu Cys Pro Phe Gly His Ala Val Gly Ile Phe Arg Ala Ala Val
    1170                1175                1180
TGC ACC CGG GGG GTT GCG AAG GCG GTG GAC TTT GTG CCC GTA GAG TCC     3600
Cys Thr Arg Gly Val Ala Lys Ala Val Asp Phe Val Pro Val Glu Ser
1185                1190                1195                1200
ATG GAA ACT ACT ATG CGG TCT CCG GTC TTC ACG GAC AAC TCA TCC CCC     3648
Met Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro
                1205                1210                1215
CCG GCC GTA CCG CAG TCA TTT CAA GTG GCC CAC CTA CAC GCT CCC ACT     3696
Pro Ala Val Pro Gln Ser Phe Gln Val Ala His Leu His Ala Pro Thr
            1220                1225                1230
GGC AGC GGC AAG AGT ACT AAA GTG CCG GCT GCA TAT GCA GCC CAA GGG     3744
Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala Ala Gln Gly
        1235                1240                1245
TAC AAG GTG CTC GTC CTC AAT CCG TCC GTT GCC GCT ACC TTA GGG TTT     3792
Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe
    1250                1255                1260
GGG GCG TAT ATG TCT AAG GCA CAC GGT ATT GAC CCC AAC ATC AGA ACT     3840
Gly Ala Tyr Met Ser Lys Ala His Gly Ile Asp Pro Asn Ile Arg Thr
1265                1270                1275                1280
GGG GTA AGG ACC ATT ACC ACA GGC GCC CCC GTC ACA TAC TCT ACC TAT     3888
Gly Val Arg Thr Ile Thr Thr Gly Ala Pro Val Thr Tyr Ser Thr Tyr
                1285                1290                1295
GGC AAG TTT CTT GCC GAT GGT GGT TGC TCT GGG GGC GCT TAT GAC ATC     3936
Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp Ile
            1300                1305                1310
ATA ATA TGT GAT GAG TGC CAT TCA ACT GAC TCG ACT ACA ATC TTG GGC     3984
Ile Ile Cys Asp Glu Cys His Ser Thr Asp Ser Thr Thr Ile Leu Gly
        1315                1320                1325
ATC GGC ACA GTC CTG GAC CAA GCG GAG ACG GCT GGA GCG CGG CTT GTC     4032
Ile Gly Thr Val Leu Asp Gln Ala Glu Thr Ala Gly Ala Arg Leu Val
    1330                1335                1340
GTG CTC GCC ACC GCT ACG CCT CCG GGA TCG GTC ACC GTG CCA CAC CCA     4080
Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro His Pro
1345                1350                1355                1360
AAC ATC GAG GAG GTG GCC CTG TCT AAT ACT GGA GAG ATC CCC TTC TAT     4128
Asn Ile Glu Glu Val Ala Leu Ser Asn Thr Gly Glu Ile Pro Phe Tyr
                1365                1370                1375
GGC AAA GCC ATC CCC ATT GAA GCC ATC AGG GGG GGA AGG CAT CTC ATT     4176
Gly Lys Ala Ile Pro Ile Glu Ala Ile Arg Gly Gly Arg His Leu Ile
            1380                1385                1390
TTC TGT CAT TCC AAG AAG AAG TGC GAC GAG CTC GCC GCA AAG CTG TCA     4224
Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Ser
        1395                1400                1405
GGC CTC GGA ATC AAC GCT GTG GCG TAT TAC CGG GGG CTC GAT GTG TCC     4272
Gly Leu Gly Ile Asn Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser
    1410                1415                1420
GTC ATA CCA ACT ATC GGA GAC GTC GTT GTC GTG GCA ACA GAC GCT CTG     4320
Val Ile Pro Thr Ile Gly Asp Val Val Val Val Ala Thr Asp Ala Leu
1425                1430                1435                1440
ATG ACG GGC TAT ACG GGC GAC TTT GAC TCA GTG ATC GAC TGT AAC ACA     4368
Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val Ile Asp Cys Asn Thr
                1445                1450                1455
TGT GTC ACC CAG ACA GTC GAC TTC AGC TTG GAT CCC ACC TTC ACC ATT     4416
Cys Val Thr Gln Thr Val Asp Phe Ser Leu Asp Pro Thr Phe Thr Ile
            1460                1465                1470
GAG ACG ACG ACC GTG CCT CAA GAC GCA GTG TCG CGC TCG CAG CGG CGG     4464
Glu Thr Thr Thr Val Pro Gln Asp Ala Val Ser Arg Ser Gln Arg Arg
        1475                1480                1485
GGT AGG ACT GGC AGG GGT AGG AGA GGC ATC TAC AGG TTT GTG ACT CCG     4512
Gly Arg Thr Gly Arg Gly Arg Arg Gly Ile Tyr Arg Phe Val Thr Pro
    1490                1495                1500
GGA GAA CGG CCC TCG GGC ATG TTC GAT TCC TCG GTC CTG TGT GAG TGC     4560
Gly Glu Arg Pro Ser Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys
1505                1510                1515                1520
TAT GAC GCG GGC TGT GCT TGG TAC GAG CTC ACC CCG GCC GAG ACC TCG     4608
Tyr Asp Ala Gly Cys Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Ser
                1525                1530                1535
GTT AGG TTG CGG GCC TAC CTG AAC ACA CCA GGG TTG CCC GTT TGC CAG     4656
Val Arg Leu Arg Ala Tyr Leu Asn Thr Pro Gly Leu Pro Val Cys Gln
            1540                1545                1550
GAC CAC CTG GAG TTC TGG GAG AGT GTC TTC ACA GGC CTC ACC CAT ATA     4704
Asp His Leu Glu Phe Trp Glu Ser Val Phe Thr Gly Leu Thr His Ile
        1555                1560                1565
GAT GCA CAC TTC TTG TCC CAG ACC AAG CAG GCA GGA GAC AAC TTC CCC     4752
Asp Ala His Phe Leu Ser Gln Thr Lys Gln Ala Gly Asp Asn Phe Pro
    1570                1575                1580
TAC CTG GTA GCA TAC CAA GCC ACG GTG TGC GCC AGG GCT CAG GCC CCA     4800
Tyr Leu Val Ala Tyr Gln Ala Thr Val Cys Ala Arg Ala Gln Ala Pro
1585                1590                1595                1600
CCT CCA TCA TGG GAT CAA ATG TGG AAG TGT CTC ATA CGG CTG AAA CCT     4848
Pro Pro Ser Trp Asp Gln Met Trp Lys Cys Leu Ile Arg Leu Lys Pro
                1605                1610                1615
ACG CTG CAC GGG CCA ACA CCC TTG CTG TAC AGG CTG GGA GCC GTC CAG     4896
Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gln
            1620                1625                1630
AAT GAG GTC ACC CTC ACC CAC CCC ATA ACC AAA TAC ATC ATG GCA TGC     4944
Asn Glu Val Thr Leu Thr His Pro Ile Thr Lys Tyr Ile Met Ala Cys
        1635                1640                1645
ATG TCG GCT GAC CTG GAG GTC GTC ACT AGC ACC TGG GTG CTG GTG GGC     4992
Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly
    1650                1655                1660
GGA GTC CTT GCA GCT CTG GCC GCG TAT TGC CTG ACA ACA GGC AGT GTG     5040
Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Thr Thr Gly Ser Val
1665                1670                1675                1680
GTC ATT GTG GGT AGG ATT ATC TTG TCC GGG AGG CCG GCC ATT GTT CCC     5088
Val Ile Val Gly Arg Ile Ile Leu Ser Gly Arg Pro Ala Ile Val Pro
                1685                1690                1695
GAC AGG GAG CTT CTC TAC CAG GAG TTC GAT GAA ATG GAA GAG TGC GCC     5136
Asp Arg Glu Leu Leu Tyr Gln Glu Phe Asp Glu Met Glu Glu Cys Ala
            1700                1705                1710
TCG CAC CTC CCT TAC ATC GAG CAG GGA ATG CAG CTC GCC GAG CAA TTC     5184
Ser His Leu Pro Tyr Ile Glu Gln Gly Met Gln Leu Ala Glu Gln Phe
        1715                1720                1725
AAG CAG AAA GCG CTC GGG TTA CTG CAA ACA GCC ACC AAA CAA GCG GAG     5232
Lys Gln Lys Ala Leu Gly Leu Leu Gln Thr Ala Thr Lys Gln Ala Glu
    1730                1735                1740
GCT GCT GCT CCC GTG GTG GAG TCC AAG TGG CGA GCC CTT GAG ACA TTC     5280
Ala Ala Ala Pro Val Val Glu Ser Lys Trp Arg Ala Leu Glu Thr Phe
1745                1750                1755                1760
TGG GCG AAG CAC ATG TGG AAT TTC ATC AGC GGG ATA CAG TAC TTA GCA     5328
Trp Ala Lys His Met Trp Asn Phe Ile Ser Gly Ile Gln Tyr Leu Ala
                1765                1770                1775
GGC TTA TCC ACT CTG CCT GGG AAC CCC GCA ATA GCA TCA TTG ATG GCA     5376
Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala Ile Ala Ser Leu Met Ala
            1780                1785                1790
TTC ACA GCC TCT ATC ACC AGC CCG CTC ACC ACC CAA AGT ACC CTC CTG     5424
Phe Thr Ala Ser Ile Thr Ser Pro Leu Thr Thr Gln Ser Thr Leu Leu
        1795                1800                1805
TTT AAC ATC TTG GGG GGG TGG GTG GCT GCC CAA CTC GCC CCC CCC AGC     5472
Phe Asn Ile Leu Gly Gly Trp Val Ala Ala Gln Leu Ala Pro Pro Ser
    1810                1815                1820
GCC GCT TCG GCT TTC GTG GGC GCC GGC ATC GCC GGT GCG GCT GTT GGC     5520
Ala Ala Ser Ala Phe Val Gly Ala Gly Ile Ala Gly Ala Ala Val Gly
1825                1830                1835                1840
AGC ATA GGC CTT GGG AAG GTG CTT GTG GAC ATT CTG GCG GGT TAT GGA     5568
Ser Ile Gly Leu Gly Lys Val Leu Val Asp Ile Leu Ala Gly Tyr Gly
                1845                1850                1855
GCA GGA GTG GCC GGC GCG CTC GTG GCC TTT AAG GTC ATG AGC GGC GAG     5616
Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys Val Met Ser Gly Glu
            1860                1865                1870
ATG CCC TCC ACC GAG GAC CTG GTC AAT CTA CTT CCT GCC ATC CTC TCT     5664
Met Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Ala Ile Leu Ser
        1875                1880                1885
CCT GGC GCC CTG GTC GTC GGG GTC GTG TGT GCA GCA ATA CTG CGT CGA     5712
Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala Ile Leu Arg Arg
    1890                1895                1900
CAC GTG GGT CCG GGA GAG GGG GCT GTG CAG TGG ATG AAC CGG CTG ATA     5760
His Val Gly Pro Gly Glu Gly Ala Val Gln Trp Met Asn Arg Leu Ile
1905                1910                1915                1920
GCG TTC GCC TCG CGG GGT AAT CAT GTT TCC CCC ACG CAC TAT GTG CCT     5808
Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Thr His Tyr Val Pro
                1925                1930                1935
GAG AGC GAC GCC GCA GCG CGT GTT ACT CAG ATC CTC TCC AGC CTT ACC     5856
Glu Ser Asp Ala Ala Ala Arg Val Thr Gln Ile Leu Ser Ser Leu Thr
            1940                1945                1950
ATC ACT CAG CTG CTG AAA AGG CTC CAC CAG TGG ATT AAT GAA GAC TGC     5904
Ile Thr Gln Leu Leu Lys Arg Leu His Gln Trp Ile Asn Glu Asp Cys
        1955                1960                1965
TCC ACA CCG TGT TCC GGC TCG TGG CTA AGG GAT GTT TGG GAC TGG ATA     5952
Ser Thr Pro Cys Ser Gly Ser Trp Leu Arg Asp Val Trp Asp Trp Ile
    1970                1975                1980
TGC ACG GTG TTG ACT GAC TTC AAG ACC TGG CTC CAG TCC AAG CTC CTG     6000
Cys Thr Val Leu Thr Asp Phe Lys Thr Trp Leu Gln Ser Lys Leu Leu
1985                1990                1995                2000
CCG CAG CTA CCT GGA GTC CCT TTT TTC TCG TGC CAA CGC GGG TAC AAG     6048
Pro Gln Leu Pro Gly Val Pro Phe Phe Ser Cys Gln Arg Gly Tyr Lys
                2005                2010                2015
GGA GTC TGG CGG GGA GAC GGC ATC ATG CAA ACC ACC TGC CCA TGT GGA     6096
Gly Val Trp Arg Gly Asp Gly Ile Met Gln Thr Thr Cys Pro Cys Gly
            2020                2025                2030
GCA CAG ATC ACC GGA CAT GTC AAA AAC GGT TCC ATG AGG ATC GTC GGG     6144
Ala Gln Ile Thr Gly His Val Lys Asn Gly Ser Met Arg Ile Val Gly
        2035                2040                2045
CCT AAG ACC TGC AGC AAC ACG TGG CAT GGA ACA TTC CCC ATC AAC GCA     6192
Pro Lys Thr Cys Ser Asn Thr Trp His Gly Thr Phe Pro Ile Asn Ala
    2050                2055                2060
TAC ACC ACG GGC CCC TGC ACA CCC TCT CCA GCG CCA AAC TAT TCT AGG     6240
Tyr Thr Thr Gly Pro Cys Thr Pro Ser Pro Ala Pro Asn Tyr Ser Arg
2065                2070                2075                2080
GCG CTG TGG CGG GTG GCC GCT GAG GAG TAC GTG GAG GTC ACG CGG GTG     6288
Ala Leu Trp Arg Val Ala Ala Glu Glu Tyr Val Glu Val Thr Arg Val
                2085                2090                2095
GGG GAT TTC CAC TAC GTG ACG GGC ATG ACC ACT GAC AAC GTA AAG TGC     6336
Gly Asp Phe His Tyr Val Thr Gly Met Thr Thr Asp Asn Val Lys Cys
            2100                2105                2110
CCA TGC CAG GTT CCG GCT CCT GAA TTC TTC TCG GAG GTG GAC GGA GTG     6384
Pro Cys Gln Val Pro Ala Pro Glu Phe Phe Ser Glu Val Asp Gly Val
        2115                2120                2125
CGG TTG CAC AGG TAC GCT CCG GCG TGC AGG CCT CTC CTA CGG GAG GAG     6432
Arg Leu His Arg Tyr Ala Pro Ala Cys Arg Pro Leu Leu Arg Glu Glu
    2130                2135                2140
GTT ACA TTC CAG GTC GGG CTC AAC CAA TAC CTG GTT GGG TCA CAG CTA     6480
Val Thr Phe Gln Val Gly Leu Asn Gln Tyr Leu Val Gly Ser Gln Leu
2145                2150                2155                2160
CCA TGC GAG CCC GAA CCG GAT GTA GCA GTG CTC ACT TCC ATG CTC ACC     6528
Pro Cys Glu Pro Glu Pro Asp Val Ala Val Leu Thr Ser Met Leu Thr
                2165                2170                2175
GAC CCC TCC CAC ATC ACA GCA GAA ACG GCT AAG CGT AGG TTG GCC AGG     6576
Asp Pro Ser His Ile Thr Ala Glu Thr Ala Lys Arg Arg Leu Ala Arg
            2180                2185                2190
GGG TCT CCC CCC TCC TTG GCC AGC TCT TCA GCT AGC CAG TTG TCT GCG     6624
Gly Ser Pro Pro Ser Leu Ala Ser Ser Ser Ala Ser Gln Leu Ser Ala
        2195                2200                2205
CCT TCC TTG AAG GCG ACA TGC ACT ACC CAC CAT GTC TCT CCG GAC GCT     6672
Pro Ser Leu Lys Ala Thr Cys Thr Thr His His Val Ser Pro Asp Ala
    2210                2215                2220
GAC CTC ATC GAG GCC AAC CTC CTG TGG CGG CAG GAG ATG GGC GGG AAC     6720
Asp Leu Ile Glu Ala Asn Leu Leu Trp Arg Gln Glu Met Gly Gly Asn
2225                2230                2235                2240
ATC ACC CGC GTG GAG TCG GAG AAC AAG GTG GTA GTC CTG GAC TCT TTC     6768
Ile Thr Arg Val Glu Ser Glu Asn Lys Val Val Val Leu Asp Ser Phe
                2245                2250                2255
GAC CCG CTT CGA GCG GAG GAG GAT GAG AGG GAA GTA TCC GTT CCG GCG     6816
Asp Pro Leu Arg Ala Glu Glu Asp Glu Arg Glu Val Ser Val Pro Ala
            2260                2265                2270
GAG ATC CTG CGG AAA TCC AAG AAG TTC CCC GCA GCG ATG CCC ATC TGG     6864
Glu Ile Leu Arg Lys Ser Lys Lys Phe Pro Ala Ala Met Pro Ile Trp
        2275                2280                2285
GCG CGC CCG GAT TAC AAC CCT CCA CTG TTA GAG TCC TGG AAG GAC CCG     6912
Ala Arg Pro Asp Tyr Asn Pro Pro Leu Leu Glu Ser Trp Lys Asp Pro
    2290                2295                2300
GAC TAC GTC CCT CCG GTG GTG CAC GGG TGC CCG TTG CCA CCT ATC AAG     6960
Asp Tyr Val Pro Pro Val Val His Gly Cys Pro Leu Pro Pro Ile Lys
2305                2310                2315                2320
GCC CCT CCA ATA CCA CCT CCA CGG AGA AAG AGG ACG GTT GTC CTA ACA     7008
Ala Pro Pro Ile Pro Pro Pro Arg Arg Lys Arg Thr Val Val Leu Thr
                2325                2330                2335
GAG TCC TCC GTG TCT TCT GCC TTA GCG GAG CTC GCT ACT AAG ACC TTC     7056
Glu Ser Ser Val Ser Ser Ala Leu Ala Glu Leu Ala Thr Lys Thr Phe
            2340                2345                2350
GGC AGC TCC GAA TCA TCG GCC GTC GAC AGC GGC ACG GCG ACC GCC CTT     7104
Gly Ser Ser Glu Ser Ser Ala Val Asp Ser Gly Thr Ala Thr Ala Leu
        2355                2360                2365
CCT GAC CAG GCC TCC GAC GAC GGT GAC AAA GGA TCC GAC GTT GAG TCG     7152
Pro Asp Gln Ala Ser Asp Asp Gly Asp Lys Gly Ser Asp Val Glu Ser
    2370                2375                2380
TAC TCC TCC ATG CCC CCC CTT GAG GGG GAA CCG GGG GAC CCC GAT CTC     7200
Tyr Ser Ser Met Pro Pro Leu Glu Gly Glu Pro Gly Asp Pro Asp Leu
2385                2390                2395                2400
AGT GAC GGG TCT TGG TCT ACC GTG AGC GAG GAA GCT AGT GAG GAT GTC     7248
Ser Asp Gly Ser Trp Ser Thr Val Ser Glu Glu Ala Ser Glu Asp Val
                2405                2410                2415
GTC TGC TGC TCA ATG TCC TAC ACA TGG ACA GGC GCC TTG ATC ACG CCA     7296
Val Cys Cys Ser Met Ser Tyr Thr Trp Thr Gly Ala Leu Ile Thr Pro
            2420                2425                2430
TGC GCT GCG GAG GAA AGC AAG CTG CCC ATC AAC GCG TTG AGC AAC TCT     7344
Cys Ala Ala Glu Glu Ser Lys Leu Pro Ile Asn Ala Leu Ser Asn Ser
        2435                2440                2445
TTG CTG CGC CAC CAT AAC ATG GTT TAT GCC ACA ACA TCT CGC AGC GCA     7392
Leu Leu Arg His His Asn Met Val Tyr Ala Thr Thr Ser Arg Ser Ala
    2450                2455                2460
GGC CTG CGG CAG AAG AAG GTC ACC TTT GAC AGA CTG CAA GTC CTG GAC     7440
Gly Leu Arg Gln Lys Lys Val Thr Phe Asp Arg Leu Gln Val Leu Asp
2465                2470                2475                2480
GAC CAC TAC CGG GAC GTG CTC AAG GAG ATG AAG GCG AAG GCG TCC ACA     7488
Asp His Tyr Arg Asp Val Leu Lys Glu Met Lys Ala Lys Ala Ser Thr
                2485                2490                2495
GTT AAG GCT AAA CTC CTA TCC GTA GAG GAA GCC TGC AAG CTG ACG CCC     7536
Val Lys Ala Lys Leu Leu Ser Val Glu Glu Ala Cys Lys Leu Thr Pro
            2500                2505                2510
CCA CAT TCG GCC AAA TCC AAG TTT GGC TAT GGG GCA AAG GAC GTC CGG     7584
Pro His Ser Ala Lys Ser Lys Phe Gly Tyr Gly Ala Lys Asp Val Arg
        2515                2520                2525
AAC CTA TCC AGC AAG GCC GTT AAC CAC ATC CAC TCC GTG TGG AAG GAC     7632
Asn Leu Ser Ser Lys Ala Val Asn His Ile His Ser Val Trp Lys Asp
    2530                2535                2540
TTG CTG GAA GAC ACT GTG ACA CCA ATT GAC ACC ACC ATC ATG GCA AAA     7680
Leu Leu Glu Asp Thr Val Thr Pro Ile Asp Thr Thr Ile Met Ala Lys
2545                2550                2555                2560
AAT GAG GTT TTC TGT GTC CAA CCA GAG AAA GGA GGC CGT AAG CCA GCC     7728
Asn Glu Val Phe Cys Val Gln Pro Glu Lys Gly Gly Arg Lys Pro Ala
                2565                2570                2575
CGC CTT ATC GTA TTC CCA GAT CTG GGA GTC CGT GTA TGC GAG AAG ATG     7776
Arg Leu Ile Val Phe Pro Asp Leu Gly Val Arg Val Cys Glu Lys Met
            2580                2585                2590
GCC CTC TAT GAT GTG GTC TCC ACC CTT CCT CAG GTC GTG ATG GGC TCC     7824
Ala Leu Tyr Asp Val Val Ser Thr Leu Pro Gln Val Val Met Gly Ser
        2595                2600                2605
TCA TAC GGA TTC CAG TAC TCT CCT GGG CAG CGA GTC GAG TTC CTG GTG     7872
Ser Tyr Gly Phe Gln Tyr Ser Pro Gly Gln Arg Val Glu Phe Leu Val
    2610                2615                2620
AAT ACC TGG AAA TCA AAG AAA AAC CCC ATG GGC TTT TCA TAT GAC ACT     7920
Asn Thr Trp Lys Ser Lys Lys Asn Pro Met Gly Phe Ser Tyr Asp Thr
2625                2630                2635                2640
CGC TGT TTC GAC TCA ACG GTC ACC GAG AAC GAC ATC CGT GTT GAG GAG     7968
Arg Cys Phe Asp Ser Thr Val Thr Glu Asn Asp Ile Arg Val Glu Glu
                2645                2650                2655
TCA ATT TAC CAA TGT TGT GAC TTG GCC CCC GAA GCC AGA CAG GCC ATA     8016
Ser Ile Tyr Gln Cys Cys Asp Leu Ala Pro Glu Ala Arg Gln Ala Ile
            2660                2665                2670
AAA TCG CTC ACA GAG CGG CTT TAT ATC GGG GGT CCT CTG ACT AAT TCA     8064
Lys Ser Leu Thr Glu Arg Leu Tyr Ile Gly Gly Pro Leu Thr Asn Ser
        2675                2680                2685
AAA GGG CAG AAC TGC GGT TAT CGC CGG TGC CGC GCG AGC GGC GTG CTG     8112
Lys Gly Gln Asn Cys Gly Tyr Arg Arg Cys Arg Ala Ser Gly Val Leu
    2690                2695                2700
ACG ACT AGC TGC GGT AAC ACC CTC ACA TGT TAC TTG AAG GCC TCT GCA     8160
Thr Thr Ser Cys Gly Asn Thr Leu Thr Cys Tyr Leu Lys Ala Ser Ala
2705                2710                2715                2720
GCC TGT CGA GCT GCG AAG CTC CAG GAC TGC ACG ATG CTC GTG AAC GGA     8208
Ala Cys Arg Ala Ala Lys Leu Gln Asp Cys Thr Met Leu Val Asn Gly
                2725                2730                2735
GAC GAC CTC GTC GTT ATC TGT GAA AGC GCG GGA ACC CAA GAG GAC GCG     8256
Asp Asp Leu Val Val Ile Cys Glu Ser Ala Gly Thr Gln Glu Asp Ala
            2740                2745                2750
GCG AGC CTA CGA GTC TTC ACG GAG GCT ATG ACT AGG TAC TCC GCC CCC     8304
Ala Ser Leu Arg Val Phe Thr Glu Ala Met Thr Arg Tyr Ser Ala Pro
        2755                2760                2765
CCC GGG GAC CCG CCC CAA CCA GAA TAC GAC TTG GAG CTG ATA ACA TCA     8352
Pro Gly Asp Pro Pro Gln Pro Glu Tyr Asp Leu Glu Leu Ile Thr Ser
    2770                2775                2780
TGT TCC TCC AAT GTG TCG GTC GCC CAC GAT GCA TCA GGC AAA AGG GTG     8400
Cys Ser Ser Asn Val Ser Val Ala His Asp Ala Ser Gly Lys Arg Val
2785                2790                2795                2800
TAC TAC CTC ACC CGT GAT CCC ACC ACC CCC CTA GCA CGG GCT GCG TGG     8448
Tyr Tyr Leu Thr Arg Asp Pro Thr Thr Pro Leu Ala Arg Ala Ala Trp
                2805                2810                2815
GAG ACA GCT AGA CAC ACT CCA GTT AAC TCC TGG CTA GGC AAC ATT ATT     8496
Glu Thr Ala Arg His Thr Pro Val Asn Ser Trp Leu Gly Asn Ile Ile
            2820                2825                2830
ATG TAT GCG CCC ACT TTG TGG GCA AGG ATG ATT CTG ATG ACT CAC TTC     8544
Met Tyr Ala Pro Thr Leu Trp Ala Arg Met Ile Leu Met Thr His Phe
        2835                2840                2845
TTC TCC ATC CTT CTA GCG CAG GAG CAA CTT GAA AAA GCC CTG GAC TGC     8592
Phe Ser Ile Leu Leu Ala Gln Glu Gln Leu Glu Lys Ala Leu Asp Cys
    2850                2855                2860
CAG ATC TAC GGG GCC TGT TAC TCC ATT GAG CCA CTT GAC CTA CCT CAG     8640
Gln Ile Tyr Gly Ala Cys Tyr Ser Ile Glu Pro Leu Asp Leu Pro Gln
2865                2870                2875                2880
ATC ATT GAA CGA CTC CAT GGC CTT AGC GCA TTT TCA CTC CAT AGT TAC     8688
Ile Ile Glu Arg Leu His Gly Leu Ser Ala Phe Ser Leu His Ser Tyr
                2885                2890                2895
TCT CCA GGT GAG ATC AAT AGG GTG GCT TCA TGC CTC AGG AAA CTT GGG     8736
Ser Pro Gly Glu Ile Asn Arg Val Ala Ser Cys Leu Arg Lys Leu Gly
            2900                2905                2910
GTA CCA CCC TTG CGA GTC TGG AGA CAT CGG GCC AGG AGC GTC CGC GCT     8784
Val Pro Pro Leu Arg Val Trp Arg His Arg Ala Arg Ser Val Arg Ala
        2915                2920                2925
AGG CTA CTG TCC CAG GGA GGG AGG GCC GCC ACT TGT GGC AAA TAC CTC     8832
Arg Leu Leu Ser Gln Gly Gly Arg Ala Ala Thr Cys Gly Lys Tyr Leu
    2930                2935                2940
TTC AAC TGG GCA GTA AAA ACC AAA CTT AAA CTC ACT CCA ATC CCG GCT     8880
Phe Asn Trp Ala Val Lys Thr Lys Leu Lys Leu Thr Pro Ile Pro Ala
2945                2950                2955                2960
GCG TCC CGG CTG GAC TTG TCC GGC TGG TTC GTT GCT GGT TAC AGC GGG     8928
Ala Ser Arg Leu Asp Leu Ser Gly Trp Phe Val Ala Gly Tyr Ser Gly
                2965                2970                2975
GGA GAC ATA TAT CAC AGC CTG TCT CGT GCC CGA CCC CGT TGG TTC ATG     8976
Gly Asp Ile Tyr His Ser Leu Ser Arg Ala Arg Pro Arg Trp Phe Met
            2980                2985                2990
CTG TGC CTA CTC CTA CTT TCT GTA GGG GTA GGC ATC TAC CTG CTC CCC     9024
Leu Cys Leu Leu Leu Leu Ser Val Gly Val Gly Ile Tyr Leu Leu Pro
        2995                3000                3005
AAC CGA                                                             9030
Asn Arg
    3010 
           
           
             
               3010 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             14
Met Ser Thr Asn Pro Lys Pro Gln Arg Lys Thr Lys Arg Asn Thr Asn
  1               5                  10                  15
Arg Arg Pro Gln Asp Val Lys Phe Pro Gly Gly Gly Gln Ile Val Gly
             20                  25                  30
Gly Val Tyr Leu Leu Pro Arg Arg Gly Pro Arg Leu Gly Val Arg Ala
         35                  40                  45
Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln Pro
     50                  55                  60
Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala Gln Pro Gly
 65                  70                  75                  80
Tyr Pro Trp Pro Leu Tyr Gly Asn Glu Gly Leu Gly Trp Ala Gly Trp
                 85                  90                  95
Leu Leu Ser Pro Arg Gly Ser Arg Pro Ser Trp Gly Pro Thr Asp Pro
            100                 105                 110
Arg Arg Arg Ser Arg Asn Leu Gly Lys Val Ile Asp Thr Leu Thr Cys
        115                 120                 125
Gly Phe Ala Asp Leu Met Gly Tyr Ile Pro Leu Val Gly Ala Pro Leu
    130                 135                 140
Gly Gly Ala Ala Arg Ala Leu Ala His Gly Val Arg Val Leu Glu Asp
145                 150                 155                 160
Gly Val Asn Tyr Ala Thr Gly Asn Leu Pro Gly Cys Ser Phe Ser Ile
                165                 170                 175
Phe Leu Leu Ala Leu Leu Ser Cys Leu Thr Thr Pro Ala Ser Ala Tyr
            180                 185                 190
Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys Ser
        195                 200                 205
Asn Ala Ser Ile Val Tyr Glu Ala Ala Asp Leu Ile Met His Thr Pro
    210                 215                 220
Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ser Ser Arg Cys Trp Val
225                 230                 235                 240
Ala Leu Thr Pro Thr Leu Ala Ala Arg Asn Val Thr Ile Pro Thr Thr
                245                 250                 255
Thr Ile Arg Arg His Val Asp Leu Leu Val Gly Ala Ala Ala Phe Cys
            260                 265                 270
Ser Ala Met Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val Ser
        275                 280                 285
Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp Cys
    290                 295                 300
Asn Cys Ser Ile Tyr Pro Gly His Val Ser Gly His Arg Met Ala Trp
305                 310                 315                 320
Asp Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ser Gln
                325                 330                 335
Leu Leu Arg Ile Pro Gln Ala Val Val Asp Met Val Ala Gly Ala His
            340                 345                 350
Trp Gly Val Leu Ala Gly Leu Ala Tyr Tyr Ser Met Ala Gly Asn Trp
        355                 360                 365
Ala Lys Val Leu Ile Val Met Leu Leu Phe Ala Gly Val Asp Gly Asp
    370                 375                 380
Thr His Val Thr Gly Gly Ala Gln Ala Lys Thr Thr Asn Arg Leu Val
385                 390                 395                 400
Ser Met Phe Ala Ser Gly Pro Ser Gln Lys Ile Gln Leu Ile Asn Thr
                405                 410                 415
Asn Gly Ser Trp His Ile Asn Arg Thr Ala Leu Asn Cys Asn Asp Ser
            420                 425                 430
Leu Gln Thr Gly Phe Leu Ala Ala Leu Phe Tyr Thr His Ser Phe Asn
        435                 440                 445
Ser Ser Gly Cys Pro Glu Arg Met Ala Gln Cys Arg Thr Ile Asp Lys
    450                 455                 460
Phe Asp Gln Gly Trp Gly Pro Ile Thr Tyr Ala Glu Ser Ser Arg Ser
465                 470                 475                 480
Asp Gln Arg Pro Tyr Cys Trp His Tyr Pro Pro Pro Gln Cys Thr Ile
                485                 490                 495
Val Pro Ala Ser Glu Val Cys Gly Pro Val Tyr Cys Phe Thr Pro Ser
            500                 505                 510
Pro Val Val Val Gly Thr Thr Asp Arg Phe Gly Val Pro Thr Tyr Arg
        515                 520                 525
Trp Gly Glu Asn Glu Thr Asp Val Leu Leu Leu Asn Asn Thr Arg Pro
    530                 535                 540
Pro Gln Gly Asn Trp Phe Gly Cys Thr Trp Met Asn Ser Thr Gly Phe
545                 550                 555                 560
Thr Lys Thr Cys Gly Gly Pro Pro Cys Asn Ile Gly Gly Val Gly Asn
                565                 570                 575
Asn Thr Leu Thr Cys Pro Thr Asp Cys Phe Arg Lys His Pro Glu Ala
            580                 585                 590
Thr Tyr Thr Lys Cys Gly Ser Gly Pro Trp Leu Thr Pro Arg Cys Met
        595                 600                 605
Val Asp Tyr Pro Tyr Arg Leu Trp His Tyr Pro Cys Thr Val Asn Phe
    610                 615                 620
Thr Ile Phe Lys Val Arg Met Tyr Val Gly Gly Val Glu His Arg Leu
625                 630                 635                 640
Asn Ala Ala Cys Asn Trp Thr Arg Gly Glu Arg Cys Asp Leu Glu Asp
                645                 650                 655
Arg Asp Arg Pro Glu Leu Ser Pro Leu Leu Leu Ser Thr Thr Glu Trp
            660                 665                 670
Gln Val Leu Pro Cys Ser Phe Thr Thr Leu Pro Ala Leu Ser Thr Gly
        675                 680                 685
Leu Ile His Leu His Gln Asn Ile Val Asp Val Gln Tyr Leu Tyr Gly
    690                 695                 700
Ile Gly Ser Ala Val Val Ser Phe Ala Ile Lys Trp Glu Tyr Val Leu
705                 710                 715                 720
Leu Leu Phe Leu Leu Leu Ala Asp Ala Arg Val Cys Ala Cys Leu Trp
                725                 730                 735
Met Met Leu Leu Ile Ala Gln Ala Glu Ala Ala Leu Glu Asn Leu Val
            740                 745                 750
Val Leu Asn Ser Ala Ser Val Ala Gly Ala His Gly Ile Leu Ser Phe
        755                 760                 765
Leu Val Phe Phe Cys Ala Ala Trp Tyr Ile Lys Gly Arg Leu Val Pro
    770                 775                 780
Gly Ala Thr Tyr Ala Leu Tyr Gly Val Trp Pro Leu Leu Leu Leu Leu
785                 790                 795                 800
Leu Ala Leu Pro Pro Arg Ala Tyr Ala Met Asp Arg Glu Met Ala Ala
                805                 810                 815
Ser Cys Gly Gly Ala Val Phe Val Gly Leu Val Leu Leu Thr Leu Ser
            820                 825                 830
Pro Tyr Tyr Lys Val Phe Leu Ala Arg Leu Ile Trp Trp Leu Gln Tyr
        835                 840                 845
Phe Thr Thr Arg Ala Glu Ala Asp Leu His Val Trp Ile Pro Pro Leu
    850                 855                 860
Asn Ala Arg Gly Gly Arg Asp Ala Ile Ile Leu Leu Met Cys Ala Val
865                 870                 875                 880
His Pro Glu Leu Ile Phe Asp Ile Thr Lys Leu Leu Ile Ala Ile Leu
                885                 890                 895
Gly Pro Leu Met Val Leu Gln Ala Gly Ile Thr Arg Val Pro Tyr Phe
            900                 905                 910
Val Arg Ala Gln Gly Leu Ile His Ala Cys Met Leu Val Arg Lys Val
        915                 920                 925
Ala Gly Gly His Tyr Val Gln Met Ala Phe Met Lys Leu Gly Ala Leu
    930                 935                 940
Thr Gly Thr Tyr Ile Tyr Asn His Leu Thr Pro Leu Arg Asp Trp Pro
945                 950                 955                 960
Arg Ala Gly Leu Arg Asp Leu Ala Val Ala Val Glu Pro Val Val Phe
                965                 970                 975
Ser Asp Met Glu Thr Lys Ile Ile Thr Trp Gly Ala Asp Thr Ala Ala
            980                 985                 990
Cys Gly Asp Ile Ile Leu Gly Leu Pro Val Ser Ala Arg Arg Gly Lys
        995                 1000                1005
Glu Ile Leu Leu Gly Pro Ala Asp Ser Leu Glu Gly Arg Gly Leu Arg
    1010                1015                1020
Leu Leu Ala Pro Ile Thr Ala Tyr Ser Gln Gln Thr Arg Gly Leu Leu
1025                1030                1035                1040
Gly Cys Ile Ile Thr Ser Leu Thr Gly Arg Asp Lys Asn Gln Val Glu
                1045                1050                1055
Gly Glu Val Gln Val Val Ser Thr Ala Thr Gln Ser Phe Leu Ala Thr
            1060                1065                1070
Cys Val Asn Gly Val Cys Trp Thr Val Tyr His Gly Ala Gly Ser Lys
        1075                1080                1085
Thr Leu Ala Ala Pro Lys Gly Pro Ile Thr Gln Met Tyr Thr Asn Val
    1090                1095                1100
Asp Gln Asp Leu Val Gly Trp Pro Lys Pro Pro Gly Ala Arg Ser Leu
1105                1110                1115                1120
Thr Pro Cys Thr Cys Gly Ser Ser Asp Leu Tyr Leu Val Thr Arg His
                1125                1130                1135
Ala Asp Val Ile Pro Val Arg Arg Arg Gly Asp Ser Arg Gly Ser Leu
            1140                1145                1150
Leu Ser Pro Arg Pro Val Ser Tyr Leu Lys Gly Ser Ser Gly Gly Pro
        1155                1160                1165
Leu Leu Cys Pro Phe Gly His Ala Val Gly Ile Phe Arg Ala Ala Val
    1170                1175                1180
Cys Thr Arg Gly Val Ala Lys Ala Val Asp Phe Val Pro Val Glu Ser
1185                1190                1195                1200
Met Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro
                1205                1210                1215
Pro Ala Val Pro Gln Ser Phe Gln Val Ala His Leu His Ala Pro Thr
            1220                1225                1230
Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala Ala Gln Gly
        1235                1240                1245
Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe
    1250                1255                1260
Gly Ala Tyr Met Ser Lys Ala His Gly Ile Asp Pro Asn Ile Arg Thr
1265                1270                1275                1280
Gly Val Arg Thr Ile Thr Thr Gly Ala Pro Val Thr Tyr Ser Thr Tyr
                1285                1290                1295
Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp Ile
            1300                1305                1310
Ile Ile Cys Asp Glu Cys His Ser Thr Asp Ser Thr Thr Ile Leu Gly
        1315                1320                1325
Ile Gly Thr Val Leu Asp Gln Ala Glu Thr Ala Gly Ala Arg Leu Val
    1330                1335                1340
Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro His Pro
1345                1350                1355                1360
Asn Ile Glu Glu Val Ala Leu Ser Asn Thr Gly Glu Ile Pro Phe Tyr
                1365                1370                1375
Gly Lys Ala Ile Pro Ile Glu Ala Ile Arg Gly Gly Arg His Leu Ile
            1380                1385                1390
Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Ser
        1395                1400                1405
Gly Leu Gly Ile Asn Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser
    1410                1415                1420
Val Ile Pro Thr Ile Gly Asp Val Val Val Val Ala Thr Asp Ala Leu
1425                1430                1435                1440
Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val Ile Asp Cys Asn Thr
                1445                1450                1455
Cys Val Thr Gln Thr Val Asp Phe Ser Leu Asp Pro Thr Phe Thr Ile
            1460                1465                1470
Glu Thr Thr Thr Val Pro Gln Asp Ala Val Ser Arg Ser Gln Arg Arg
        1475                1480                1485
Gly Arg Thr Gly Arg Gly Arg Arg Gly Ile Tyr Arg Phe Val Thr Pro
    1490                1495                1500
Gly Glu Arg Pro Ser Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys
1505                1510                1515                1520
Tyr Asp Ala Gly Cys Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Ser
                1525                1530                1535
Val Arg Leu Arg Ala Tyr Leu Asn Thr Pro Gly Leu Pro Val Cys Gln
            1540                1545                1550
Asp His Leu Glu Phe Trp Glu Ser Val Phe Thr Gly Leu Thr His Ile
        1555                1560                1565
Asp Ala His Phe Leu Ser Gln Thr Lys Gln Ala Gly Asp Asn Phe Pro
    1570                1575                1580
Tyr Leu Val Ala Tyr Gln Ala Thr Val Cys Ala Arg Ala Gln Ala Pro
1585                1590                1595                1600
Pro Pro Ser Trp Asp Gln Met Trp Lys Cys Leu Ile Arg Leu Lys Pro
                1605                1610                1615
Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gln
            1620                1625                1630
Asn Glu Val Thr Leu Thr His Pro Ile Thr Lys Tyr Ile Met Ala Cys
        1635                1640                1645
Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val Gly
    1650                1655                1660
Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Thr Thr Gly Ser Val
1665                1670                1675                1680
Val Ile Val Gly Arg Ile Ile Leu Ser Gly Arg Pro Ala Ile Val Pro
                1685                1690                1695
Asp Arg Glu Leu Leu Tyr Gln Glu Phe Asp Glu Met Glu Glu Cys Ala
            1700                1705                1710
Ser His Leu Pro Tyr Ile Glu Gln Gly Met Gln Leu Ala Glu Gln Phe
        1715                1720                1725
Lys Gln Lys Ala Leu Gly Leu Leu Gln Thr Ala Thr Lys Gln Ala Glu
    1730                1735                1740
Ala Ala Ala Pro Val Val Glu Ser Lys Trp Arg Ala Leu Glu Thr Phe
1745                1750                1755                1760
Trp Ala Lys His Met Trp Asn Phe Ile Ser Gly Ile Gln Tyr Leu Ala
                1765                1770                1775
Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala Ile Ala Ser Leu Met Ala
            1780                1785                1790
Phe Thr Ala Ser Ile Thr Ser Pro Leu Thr Thr Gln Ser Thr Leu Leu
        1795                1800                1805
Phe Asn Ile Leu Gly Gly Trp Val Ala Ala Gln Leu Ala Pro Pro Ser
    1810                1815                1820
Ala Ala Ser Ala Phe Val Gly Ala Gly Ile Ala Gly Ala Ala Val Gly
1825                1830                1835                1840
Ser Ile Gly Leu Gly Lys Val Leu Val Asp Ile Leu Ala Gly Tyr Gly
                1845                1850                1855
Ala Gly Val Ala Gly Ala Leu Val Ala Phe Lys Val Met Ser Gly Glu
            1860                1865                1870
Met Pro Ser Thr Glu Asp Leu Val Asn Leu Leu Pro Ala Ile Leu Ser
        1875                1880                1885
Pro Gly Ala Leu Val Val Gly Val Val Cys Ala Ala Ile Leu Arg Arg
    1890                1895                1900
His Val Gly Pro Gly Glu Gly Ala Val Gln Trp Met Asn Arg Leu Ile
1905                1910                1915                1920
Ala Phe Ala Ser Arg Gly Asn His Val Ser Pro Thr His Tyr Val Pro
                1925                1930                1935
Glu Ser Asp Ala Ala Ala Arg Val Thr Gln Ile Leu Ser Ser Leu Thr
            1940                1945                1950
Ile Thr Gln Leu Leu Lys Arg Leu His Gln Trp Ile Asn Glu Asp Cys
        1955                1960                1965
Ser Thr Pro Cys Ser Gly Ser Trp Leu Arg Asp Val Trp Asp Trp Ile
    1970                1975                1980
Cys Thr Val Leu Thr Asp Phe Lys Thr Trp Leu Gln Ser Lys Leu Leu
1985                1990                1995                2000
Pro Gln Leu Pro Gly Val Pro Phe Phe Ser Cys Gln Arg Gly Tyr Lys
                2005                2010                2015
Gly Val Trp Arg Gly Asp Gly Ile Met Gln Thr Thr Cys Pro Cys Gly
            2020                2025                2030
Ala Gln Ile Thr Gly His Val Lys Asn Gly Ser Met Arg Ile Val Gly
        2035                2040                2045
Pro Lys Thr Cys Ser Asn Thr Trp His Gly Thr Phe Pro Ile Asn Ala
    2050                2055                2060
Tyr Thr Thr Gly Pro Cys Thr Pro Ser Pro Ala Pro Asn Tyr Ser Arg
2065                2070                2075                2080
Ala Leu Trp Arg Val Ala Ala Glu Glu Tyr Val Glu Val Thr Arg Val
                2085                2090                2095
Gly Asp Phe His Tyr Val Thr Gly Met Thr Thr Asp Asn Val Lys Cys
            2100                2105                2110
Pro Cys Gln Val Pro Ala Pro Glu Phe Phe Ser Glu Val Asp Gly Val
        2115                2120                2125
Arg Leu His Arg Tyr Ala Pro Ala Cys Arg Pro Leu Leu Arg Glu Glu
    2130                2135                2140
Val Thr Phe Gln Val Gly Leu Asn Gln Tyr Leu Val Gly Ser Gln Leu
2145                2150                2155                2160
Pro Cys Glu Pro Glu Pro Asp Val Ala Val Leu Thr Ser Met Leu Thr
                2165                2170                2175
Asp Pro Ser His Ile Thr Ala Glu Thr Ala Lys Arg Arg Leu Ala Arg
            2180                2185                2190
Gly Ser Pro Pro Ser Leu Ala Ser Ser Ser Ala Ser Gln Leu Ser Ala
        2195                2200                2205
Pro Ser Leu Lys Ala Thr Cys Thr Thr His His Val Ser Pro Asp Ala
    2210                2215                2220
Asp Leu Ile Glu Ala Asn Leu Leu Trp Arg Gln Glu Met Gly Gly Asn
2225                2230                2235                2240
Ile Thr Arg Val Glu Ser Glu Asn Lys Val Val Val Leu Asp Ser Phe
                2245                2250                2255
Asp Pro Leu Arg Ala Glu Glu Asp Glu Arg Glu Val Ser Val Pro Ala
            2260                2265                2270
Glu Ile Leu Arg Lys Ser Lys Lys Phe Pro Ala Ala Met Pro Ile Trp
        2275                2280                2285
Ala Arg Pro Asp Tyr Asn Pro Pro Leu Leu Glu Ser Trp Lys Asp Pro
    2290                2295                2300
Asp Tyr Val Pro Pro Val Val His Gly Cys Pro Leu Pro Pro Ile Lys
2305                2310                2315                2320
Ala Pro Pro Ile Pro Pro Pro Arg Arg Lys Arg Thr Val Val Leu Thr
                2325                2330                2335
Glu Ser Ser Val Ser Ser Ala Leu Ala Glu Leu Ala Thr Lys Thr Phe
            2340                2345                2350
Gly Ser Ser Glu Ser Ser Ala Val Asp Ser Gly Thr Ala Thr Ala Leu
        2355                2360                2365
Pro Asp Gln Ala Ser Asp Asp Gly Asp Lys Gly Ser Asp Val Glu Ser
    2370                2375                2380
Tyr Ser Ser Met Pro Pro Leu Glu Gly Glu Pro Gly Asp Pro Asp Leu
2385                2390                2395                2400
Ser Asp Gly Ser Trp Ser Thr Val Ser Glu Glu Ala Ser Glu Asp Val
                2405                2410                2415
Val Cys Cys Ser Met Ser Tyr Thr Trp Thr Gly Ala Leu Ile Thr Pro
            2420                2425                2430
Cys Ala Ala Glu Glu Ser Lys Leu Pro Ile Asn Ala Leu Ser Asn Ser
        2435                2440                2445
Leu Leu Arg His His Asn Met Val Tyr Ala Thr Thr Ser Arg Ser Ala
    2450                2455                2460
Gly Leu Arg Gln Lys Lys Val Thr Phe Asp Arg Leu Gln Val Leu Asp
2465                2470                2475                2480
Asp His Tyr Arg Asp Val Leu Lys Glu Met Lys Ala Lys Ala Ser Thr
                2485                2490                2495
Val Lys Ala Lys Leu Leu Ser Val Glu Glu Ala Cys Lys Leu Thr Pro
            2500                2505                2510
Pro His Ser Ala Lys Ser Lys Phe Gly Tyr Gly Ala Lys Asp Val Arg
        2515                2520                2525
Asn Leu Ser Ser Lys Ala Val Asn His Ile His Ser Val Trp Lys Asp
    2530                2535                2540
Leu Leu Glu Asp Thr Val Thr Pro Ile Asp Thr Thr Ile Met Ala Lys
2545                2550                2555                2560
Asn Glu Val Phe Cys Val Gln Pro Glu Lys Gly Gly Arg Lys Pro Ala
                2565                2570                2575
Arg Leu Ile Val Phe Pro Asp Leu Gly Val Arg Val Cys Glu Lys Met
            2580                2585                2590
Ala Leu Tyr Asp Val Val Ser Thr Leu Pro Gln Val Val Met Gly Ser
        2595                2600                2605
Ser Tyr Gly Phe Gln Tyr Ser Pro Gly Gln Arg Val Glu Phe Leu Val
    2610                2615                2620
Asn Thr Trp Lys Ser Lys Lys Asn Pro Met Gly Phe Ser Tyr Asp Thr
2625                2630                2635                2640
Arg Cys Phe Asp Ser Thr Val Thr Glu Asn Asp Ile Arg Val Glu Glu
                2645                2650                2655
Ser Ile Tyr Gln Cys Cys Asp Leu Ala Pro Glu Ala Arg Gln Ala Ile
            2660                2665                2670
Lys Ser Leu Thr Glu Arg Leu Tyr Ile Gly Gly Pro Leu Thr Asn Ser
        2675                2680                2685
Lys Gly Gln Asn Cys Gly Tyr Arg Arg Cys Arg Ala Ser Gly Val Leu
    2690                2695                2700
Thr Thr Ser Cys Gly Asn Thr Leu Thr Cys Tyr Leu Lys Ala Ser Ala
2705                2710                2715                2720
Ala Cys Arg Ala Ala Lys Leu Gln Asp Cys Thr Met Leu Val Asn Gly
                2725                2730                2735
Asp Asp Leu Val Val Ile Cys Glu Ser Ala Gly Thr Gln Glu Asp Ala
            2740                2745                2750
Ala Ser Leu Arg Val Phe Thr Glu Ala Met Thr Arg Tyr Ser Ala Pro
        2755                2760                2765
Pro Gly Asp Pro Pro Gln Pro Glu Tyr Asp Leu Glu Leu Ile Thr Ser
    2770                2775                2780
Cys Ser Ser Asn Val Ser Val Ala His Asp Ala Ser Gly Lys Arg Val
2785                2790                2795                2800
Tyr Tyr Leu Thr Arg Asp Pro Thr Thr Pro Leu Ala Arg Ala Ala Trp
                2805                2810                2815
Glu Thr Ala Arg His Thr Pro Val Asn Ser Trp Leu Gly Asn Ile Ile
            2820                2825                2830
Met Tyr Ala Pro Thr Leu Trp Ala Arg Met Ile Leu Met Thr His Phe
        2835                2840                2845
Phe Ser Ile Leu Leu Ala Gln Glu Gln Leu Glu Lys Ala Leu Asp Cys
    2850                2855                2860
Gln Ile Tyr Gly Ala Cys Tyr Ser Ile Glu Pro Leu Asp Leu Pro Gln
2865                2870                2875                2880
Ile Ile Glu Arg Leu His Gly Leu Ser Ala Phe Ser Leu His Ser Tyr
                2885                2890                2895
Ser Pro Gly Glu Ile Asn Arg Val Ala Ser Cys Leu Arg Lys Leu Gly
            2900                2905                2910
Val Pro Pro Leu Arg Val Trp Arg His Arg Ala Arg Ser Val Arg Ala
        2915                2920                2925
Arg Leu Leu Ser Gln Gly Gly Arg Ala Ala Thr Cys Gly Lys Tyr Leu
    2930                2935                2940
Phe Asn Trp Ala Val Lys Thr Lys Leu Lys Leu Thr Pro Ile Pro Ala
2945                2950                2955                2960
Ala Ser Arg Leu Asp Leu Ser Gly Trp Phe Val Ala Gly Tyr Ser Gly
                2965                2970                2975
Gly Asp Ile Tyr His Ser Leu Ser Arg Ala Arg Pro Arg Trp Phe Met
            2980                2985                2990
Leu Cys Leu Leu Leu Leu Ser Val Gly Val Gly Ile Tyr Leu Leu Pro
        2995                3000                3005
Asn Arg
    3010 
           
           
             
               90 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..90 
                /note “sequence = 474 - 563 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..90 
             
             15
GCG CCC AGG AAG ACT TCC GAG CGG TCG CAA CCT CGT GGA AGG CGA CAA       48
Ala Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln
  1               5                  10                  15
CCT ATC CCC AAG GCT CGC CGG CCC GAG GGC AGG ACC TGG GCT               90
Pro Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala
             20                  25                  30 
           
           
             
               30 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             16
Ala Pro Arg Lys Thr Ser Glu Arg Ser Gln Pro Arg Gly Arg Arg Gln
  1               5                  10                  15
Pro Ile Pro Lys Ala Arg Arg Pro Glu Gly Arg Thr Trp Ala
             20                  25                  30 
           
           
             
               228 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..228 
                /note “sequence = 678 - 905 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..228 
             
             17
TCG CGT AAT TTG GGT AAG GTC ATC GAT ACC CTC ACA TGC GGC TTC GCC       48
Ser Arg Asn Leu Gly Lys Val Ile Asp Thr Leu Thr Cys Gly Phe Ala
  1               5                  10                  15
GAT CTC ATG GGG TAC ATT CCG CTC GTC GGC GCC CCC CTG GGG GGC GCT       96
Asp Leu Met Gly Tyr Ile Pro Leu Val Gly Ala Pro Leu Gly Gly Ala
             20                  25                  30
GCC AGG GCC CTG GCA CAT GGT GTC CGG GTT CTG GAG GAC GGC GTG AAC      144
Ala Arg Ala Leu Ala His Gly Val Arg Val Leu Glu Asp Gly Val Asn
         35                  40                  45
TAT GCA ACA GGG AAT CTG CCC GGT TGC TCT TTT TCT ATC TTC CTC TTG      192
Tyr Ala Thr Gly Asn Leu Pro Gly Cys Ser Phe Ser Ile Phe Leu Leu
     50                  55                  60
GCT CTG CTG TCC TGC CTG ACC ACC CCA GCT TCC GCT                      228
Ala Leu Leu Ser Cys Leu Thr Thr Pro Ala Ser Ala
 65                  70                  75 
           
           
             
               76 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             18
Ser Arg Asn Leu Gly Lys Val Ile Asp Thr Leu Thr Cys Gly Phe Ala
  1               5                  10                  15
Asp Leu Met Gly Tyr Ile Pro Leu Val Gly Ala Pro Leu Gly Gly Ala
             20                  25                  30
Ala Arg Ala Leu Ala His Gly Val Arg Val Leu Glu Asp Gly Val Asn
         35                  40                  45
Tyr Ala Thr Gly Asn Leu Pro Gly Cys Ser Phe Ser Ile Phe Leu Leu
     50                  55                  60
Ala Leu Leu Ser Cys Leu Thr Thr Pro Ala Ser Ala
 65                  70                  75 
           
           
             
               48 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..48 
                /note “sequence = 906 - 953 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..48 
             
             19
TAC GAA GTG CAC AAC GTG TCC GGG ATA TAT CAT GTC ACG AAC GAC TGC       48
Tyr Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys
  1               5                  10                  15 
           
           
             
               16 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             20
Tyr Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys
  1               5                  10                  15 
           
           
             
               594 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..594 
                /note “sequence = 906 - 1499 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..594 
             
             21
TAC GAA GTG CAC AAC GTG TCC GGG ATA TAT CAT GTC ACG AAC GAC TGC       48
Tyr Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys
  1               5                  10                  15
TCC AAC GCA AGC ATT GTG TAT GAG GCA GCG GAC TTG ATC ATG CAT ACT       96
Ser Asn Ala Ser Ile Val Tyr Glu Ala Ala Asp Leu Ile Met His Thr
             20                  25                  30
CCT GGG TGC GTG CCC TGC GTT CGG GAA GGC AAC TCC TCC CGC TGC TGG      144
Pro Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ser Ser Arg Cys Trp
         35                  40                  45
GTA GCG CTC ACT CCC ACG CTC GCA GCC AGG AAC GTC ACC ATC CCC ACC      192
Val Ala Leu Thr Pro Thr Leu Ala Ala Arg Asn Val Thr Ile Pro Thr
     50                  55                  60
ACG ACG ATA CGA CGC CAC GTC GAT CTG CTC GTT GGG GCG GCT GCT TTC      240
Thr Thr Ile Arg Arg His Val Asp Leu Leu Val Gly Ala Ala Ala Phe
 65                  70                  75                  80
TGT TCC GCT ATG TAC GTG GGG GAC CTC TGC GGA TCT GTT TTC CTC GTC      288
Cys Ser Ala Met Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val
                 85                  90                  95
TCT CAG CTG TTC ACC TTC TCG CCT CGC CGG CAT GTG ACA TTA CAG GAC      336
Ser Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp
            100                 105                 110
TGT AAC TGC TCA ATT TAT CCC GGC CAT GTG TCG GGT CAC CGT ATG GCT      384
Cys Asn Cys Ser Ile Tyr Pro Gly His Val Ser Gly His Arg Met Ala
        115                 120                 125
TGG GAC ATG ATG ATG AAC TGG TCG CCC ACA ACA GCC CTA GTG GTG TCG      432
Trp Asp Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ser
    130                 135                 140
CAG TTA CTC CGG ATC CCA CAA GCC GTC GTG GAC ATG GTG GCG GGG GCC      480
Gln Leu Leu Arg Ile Pro Gln Ala Val Val Asp Met Val Ala Gly Ala
145                 150                 155                 160
CAC TGG GGA GTC CTG GCG GGC CTT GCC TAC TAT TCC ATG GCG GGG AAC      528
His Trp Gly Val Leu Ala Gly Leu Ala Tyr Tyr Ser Met Ala Gly Asn
                165                 170                 175
TGG GCT AAG GTT CTG ATT GTG ATG CTA CTT TTT GCT GGC GTT GAC GGG      576
Trp Ala Lys Val Leu Ile Val Met Leu Leu Phe Ala Gly Val Asp Gly
            180                 185                 190
GAT ACC CAC GTG ACA GGG                                              594
Asp Thr His Val Thr Gly
        195 
           
           
             
               198 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             22
Tyr Glu Val His Asn Val Ser Gly Ile Tyr His Val Thr Asn Asp Cys
  1               5                  10                  15
Ser Asn Ala Ser Ile Val Tyr Glu Ala Ala Asp Leu Ile Met His Thr
             20                  25                  30
Pro Gly Cys Val Pro Cys Val Arg Glu Gly Asn Ser Ser Arg Cys Trp
         35                  40                  45
Val Ala Leu Thr Pro Thr Leu Ala Ala Arg Asn Val Thr Ile Pro Thr
     50                  55                  60
Thr Thr Ile Arg Arg His Val Asp Leu Leu Val Gly Ala Ala Ala Phe
 65                  70                  75                  80
Cys Ser Ala Met Tyr Val Gly Asp Leu Cys Gly Ser Val Phe Leu Val
                 85                  90                  95
Ser Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp
            100                 105                 110
Cys Asn Cys Ser Ile Tyr Pro Gly His Val Ser Gly His Arg Met Ala
        115                 120                 125
Trp Asp Met Met Met Asn Trp Ser Pro Thr Thr Ala Leu Val Val Ser
    130                 135                 140
Gln Leu Leu Arg Ile Pro Gln Ala Val Val Asp Met Val Ala Gly Ala
145                 150                 155                 160
His Trp Gly Val Leu Ala Gly Leu Ala Tyr Tyr Ser Met Ala Gly Asn
                165                 170                 175
Trp Ala Lys Val Leu Ile Val Met Leu Leu Phe Ala Gly Val Asp Gly
            180                 185                 190
Asp Thr His Val Thr Gly
        195 
           
           
             
               27 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..27 
                /note “sequence = 1020 - 1046 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..27 
             
             23
GTT CGG GAA GGC AAC TCC TCC CGC TGC                                   27
Val Arg Glu Gly Asn Ser Ser Arg Cys
  1               5 
           
           
             
               9 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             24
Val Arg Glu Gly Asn Ser Ser Arg Cys
  1               5 
           
           
             
               102 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..102 
                /note “sequence = 1020 - 1121 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..102 
             
             25
GTT CGG GAA GGC AAC TCC TCC CGC TGC TGG GTA GCG CTC ACT CCC ACG       48
Val Arg Glu Gly Asn Ser Ser Arg Cys Trp Val Ala Leu Thr Pro Thr
  1               5                  10                  15
CTC GCA GCC AGG AAC GTC ACC ATC CCC ACC ACG ACG ATA CGA CGC CAC       96
Leu Ala Ala Arg Asn Val Thr Ile Pro Thr Thr Thr Ile Arg Arg His
             20                  25                  30
GTC GAT                                                              102
Val Asp 
           
           
             
               34 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             26
Val Arg Glu Gly Asn Ser Ser Arg Cys Trp Val Ala Leu Thr Pro Thr
  1               5                  10                  15
Leu Ala Ala Arg Asn Val Thr Ile Pro Thr Thr Thr Ile Arg Arg His
             20                  25                  30
Val Asp 
           
           
             
               39 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..39 
                /note “sequence = 1194 - 1232 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..39 
             
             27
TCT CAG CTG TTC ACC TTC TCG CCT CGC CGG CAT GTG ACA                   39
Ser Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr
  1               5                  10 
           
           
             
               13 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             28
Ser Gln Leu Phe Thr Phe Ser Pro Arg Arg His Val Thr
  1               5                  10 
           
           
             
               114 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..114 
                /note “sequence = 1209 - 1322 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..114 
             
             29
TTC TCG CCT CGC CGG CAT GTG ACA TTA CAG GAC TGT AAC TGC TCA ATT       48
Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp Cys Asn Cys Ser Ile
  1               5                  10                  15
TAT CCC GGC CAT GTG TCG GGT CAC CGT ATG GCT TGG GAC ATG ATG ATG       96
Tyr Pro Gly His Val Ser Gly His Arg Met Ala Trp Asp Met Met Met
             20                  25                  30
AAC TGG TCG CCC ACA ACA                                              114
Asn Trp Ser Pro Thr Thr
         35 
           
           
             
               38 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             30
Phe Ser Pro Arg Arg His Val Thr Leu Gln Asp Cys Asn Cys Ser Ile
  1               5                  10                  15
Tyr Pro Gly His Val Ser Gly His Arg Met Ala Trp Asp Met Met Met
             20                  25                  30
Asn Trp Ser Pro Thr Thr
         35 
           
           
             
               7917 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               CDS 
                1..7862 
             
             
               misc_feature 
                1..7916 
                /note= “sequence = 1500 - 9416 of
              SEQ ID NO 1” 
             
             31
GGG GCG CAA GCC AAA ACC ACC AAC AGG CTC GTG TCC ATG TTC GCA AGT       48
Gly Ala Gln Ala Lys Thr Thr Asn Arg Leu Val Ser Met Phe Ala Ser
  1               5                  10                  15
GGG CCG TCT CAG AAA ATC CAG CTT ATA AAC ACC AAT GGG AGT TGG CAC       96
Gly Pro Ser Gln Lys Ile Gln Leu Ile Asn Thr Asn Gly Ser Trp His
             20                  25                  30
ATC AAC AGG ACT GCC CTG AAC TGC AAT GAC TCT CTC CAG ACT GGG TTT      144
Ile Asn Arg Thr Ala Leu Asn Cys Asn Asp Ser Leu Gln Thr Gly Phe
         35                  40                  45
CTT GCC GCG CTG TTC TAC ACA CAT AGT TTC AAC TCG TCC GGG TGC CCA      192
Leu Ala Ala Leu Phe Tyr Thr His Ser Phe Asn Ser Ser Gly Cys Pro
     50                  55                  60
GAG CGC ATG GCC CAG TGC CGC ACC ATT GAC AAG TTC GAC CAG GGA TGG      240
Glu Arg Met Ala Gln Cys Arg Thr Ile Asp Lys Phe Asp Gln Gly Trp
 65                  70                  75                  80
GGT CCC ATT ACT TAT GCT GAG TCT AGC AGA TCA GAC CAG AGG CCA TAT      288
Gly Pro Ile Thr Tyr Ala Glu Ser Ser Arg Ser Asp Gln Arg Pro Tyr
                 85                  90                  95
TGC TGG CAC TAC CCA CCT CCA CAA TGT ACC ATC GTA CCT GCG TCG GAG      336
Cys Trp His Tyr Pro Pro Pro Gln Cys Thr Ile Val Pro Ala Ser Glu
            100                 105                 110
GTG TGC GGC CCA GTG TAC TGC TTC ACC CCA AGC CCT GTC GTC GTG GGG      384
Val Cys Gly Pro Val Tyr Cys Phe Thr Pro Ser Pro Val Val Val Gly
        115                 120                 125
ACG ACC GAT CGT TTC GGT GTC CCT ACG TAT AGA TGG GGG GAG AAC GAG      432
Thr Thr Asp Arg Phe Gly Val Pro Thr Tyr Arg Trp Gly Glu Asn Glu
    130                 135                 140
ACT GAC GTG CTG CTG CTC AAC AAC ACG CGG CCG CCG CAA GGC AAC TGG      480
Thr Asp Val Leu Leu Leu Asn Asn Thr Arg Pro Pro Gln Gly Asn Trp
145                 150                 155                 160
TTC GGC TGC ACA TGG ATG AAT AGC ACC GGG TTC ACC AAG ACA TGT GGG      528
Phe Gly Cys Thr Trp Met Asn Ser Thr Gly Phe Thr Lys Thr Cys Gly
                165                 170                 175
GGG CCC CCG TGT AAC ATC GGG GGG GTC GGC AAC AAC ACC CTG ACC TGC      576
Gly Pro Pro Cys Asn Ile Gly Gly Val Gly Asn Asn Thr Leu Thr Cys
            180                 185                 190
CCC ACG GAC TGC TTC CGG AAG CAC CCC GAG GCT ACC TAC ACA AAA TGT      624
Pro Thr Asp Cys Phe Arg Lys His Pro Glu Ala Thr Tyr Thr Lys Cys
        195                 200                 205
GGT TCG GGG CCT TGG CTG ACA CCT AGG TGC ATG GTT GAC TAT CCA TAC      672
Gly Ser Gly Pro Trp Leu Thr Pro Arg Cys Met Val Asp Tyr Pro Tyr
    210                 215                 220
AGG CTC TGG CAT TAC CCC TGC ACT GTT AAC TTT ACC ATC TTC AAG GTT      720
Arg Leu Trp His Tyr Pro Cys Thr Val Asn Phe Thr Ile Phe Lys Val
225                 230                 235                 240
AGG ATG TAT GTG GGG GGG GTG GAG CAC AGG CTC AAT GCT GCA TGC AAT      768
Arg Met Tyr Val Gly Gly Val Glu His Arg Leu Asn Ala Ala Cys Asn
                245                 250                 255
TGG ACC CGA GGA GAG CGT TGT GAC TTG GAG GAC AGG GAT AGG CCG GAG      816
Trp Thr Arg Gly Glu Arg Cys Asp Leu Glu Asp Arg Asp Arg Pro Glu
            260                 265                 270
CTC AGC CCG CTG CTG CTG TCT ACA ACA GAG TGG CAG GTA CTG CCC TGT      864
Leu Ser Pro Leu Leu Leu Ser Thr Thr Glu Trp Gln Val Leu Pro Cys
        275                 280                 285
TCC TTC ACC ACC CTA CCA GCT CTG TCC ACT GGC TTG ATT CAC CTC CAT      912
Ser Phe Thr Thr Leu Pro Ala Leu Ser Thr Gly Leu Ile His Leu His
    290                 295                 300
CAG AAC ATC GTG GAC GTG CAA TAC CTA TAC GGT ATA GGG TCA GCG GTT      960
Gln Asn Ile Val Asp Val Gln Tyr Leu Tyr Gly Ile Gly Ser Ala Val
305                 310                 315                 320
GTC TCC TTT GCA ATC AAA TGG GAG TAT GTC CTG TTG CTT TTC CTT CTC     1008
Val Ser Phe Ala Ile Lys Trp Glu Tyr Val Leu Leu Leu Phe Leu Leu
                325                 330                 335
CTA GCG GAC GCA CGT GTC TGT GCC TGC TTG TGG ATG ATG CTG CTG ATA     1056
Leu Ala Asp Ala Arg Val Cys Ala Cys Leu Trp Met Met Leu Leu Ile
            340                 345                 350
GCC CAG GCC GAG GCC GCC TTG GAG AAC CTG GTG GTC CTC AAT TCG GCG     1104
Ala Gln Ala Glu Ala Ala Leu Glu Asn Leu Val Val Leu Asn Ser Ala
        355                 360                 365
TCT GTG GCC GGC GCA CAT GGC ATC CTC TCC TTC CTT GTG TTC TTC TGT     1152
Ser Val Ala Gly Ala His Gly Ile Leu Ser Phe Leu Val Phe Phe Cys
    370                 375                 380
GCC GCC TGG TAC ATC AAA GGC AGG CTG GTC CCT GGG GCG ACA TAT GCT     1200
Ala Ala Trp Tyr Ile Lys Gly Arg Leu Val Pro Gly Ala Thr Tyr Ala
385                 390                 395                 400
CTT TAT GGC GTG TGG CCG CTG CTC CTG CTC TTG CTG GCA TTA CCA CCG     1248
Leu Tyr Gly Val Trp Pro Leu Leu Leu Leu Leu Leu Ala Leu Pro Pro
                405                 410                 415
CGA GCT TAC GCC ATG GAC CGG GAG ATG GCT GCA TCG TGC GGA GGC GCG     1296
Arg Ala Tyr Ala Met Asp Arg Glu Met Ala Ala Ser Cys Gly Gly Ala
            420                 425                 430
GTT TTT GTG GGT CTG GTA CTC CTG ACT TTG TCA CCA TAC TAC AAG GTG     1344
Val Phe Val Gly Leu Val Leu Leu Thr Leu Ser Pro Tyr Tyr Lys Val
        435                 440                 445
TTC CTC GCT AGG CTC ATA TGG TGG TTA CAA TAT TTT ACC ACC AGA GCC     1392
Phe Leu Ala Arg Leu Ile Trp Trp Leu Gln Tyr Phe Thr Thr Arg Ala
    450                 455                 460
GAG GCG GAC TTA CAT GTG TGG ATC CCC CCC CTC AAC GCT CGG GGA GGC     1440
Glu Ala Asp Leu His Val Trp Ile Pro Pro Leu Asn Ala Arg Gly Gly
465                 470                 475                 480
CGC GAT GCC ATC ATC CTC CTC ATG TGC GCA GTC CAT CCA GAG CTA ATC     1488
Arg Asp Ala Ile Ile Leu Leu Met Cys Ala Val His Pro Glu Leu Ile
                485                 490                 495
TTT GAC ATC ACC AAA CTT CTA ATT GCC ATA CTC GGT CCG CTC ATG GTG     1536
Phe Asp Ile Thr Lys Leu Leu Ile Ala Ile Leu Gly Pro Leu Met Val
            500                 505                 510
CTC CAA GCT GGC ATA ACC AGA GTG CCG TAC TTC GTG CGC GCT CAA GGG     1584
Leu Gln Ala Gly Ile Thr Arg Val Pro Tyr Phe Val Arg Ala Gln Gly
        515                 520                 525
CTC ATT CAT GCA TGC ATG TTA GTG CGG AAG GTC GCT GGG GGT CAT TAT     1632
Leu Ile His Ala Cys Met Leu Val Arg Lys Val Ala Gly Gly His Tyr
    530                 535                 540
GTC CAA ATG GCC TTC ATG AAG CTG GGC GCG CTG ACA GGC ACG TAC ATT     1680
Val Gln Met Ala Phe Met Lys Leu Gly Ala Leu Thr Gly Thr Tyr Ile
545                 550                 555                 560
TAC AAC CAT CTT ACC CCG CTA CGG GAT TGG CCA CGC GCG GGC CTA CGA     1728
Tyr Asn His Leu Thr Pro Leu Arg Asp Trp Pro Arg Ala Gly Leu Arg
                565                 570                 575
GAC CTT GCG GTG GCA GTG GAG CCC GTC GTC TTC TCC GAC ATG GAG ACC     1776
Asp Leu Ala Val Ala Val Glu Pro Val Val Phe Ser Asp Met Glu Thr
            580                 585                 590
AAG ATC ATC ACC TGG GGA GCA GAC ACC GCG GCG TGT GGG GAC ATC ATC     1824
Lys Ile Ile Thr Trp Gly Ala Asp Thr Ala Ala Cys Gly Asp Ile Ile
        595                 600                 605
TTG GGT CTG CCC GTC TCC GCC CGA AGG GGA AAG GAG ATA CTC CTG GGC     1872
Leu Gly Leu Pro Val Ser Ala Arg Arg Gly Lys Glu Ile Leu Leu Gly
    610                 615                 620
CCG GCC GAT AGT CTT GAA GGG CGG GGG TTG CGA CTC CTC GCG CCC ATC     1920
Pro Ala Asp Ser Leu Glu Gly Arg Gly Leu Arg Leu Leu Ala Pro Ile
625                 630                 635                 640
ACG GCC TAC TCC CAA CAG ACG CGG GGC CTA CTT GGT TGC ATC ATC ACT     1968
Thr Ala Tyr Ser Gln Gln Thr Arg Gly Leu Leu Gly Cys Ile Ile Thr
                645                 650                 655
AGC CTT ACA GGC CGG GAC AAG AAC CAG GTC GAG GGA GAG GTT CAG GTG     2016
Ser Leu Thr Gly Arg Asp Lys Asn Gln Val Glu Gly Glu Val Gln Val
            660                 665                 670
GTT TCC ACC GCA ACA CAA TCC TTC CTG GCG ACC TGC GTC AAC GGC GTG     2064
Val Ser Thr Ala Thr Gln Ser Phe Leu Ala Thr Cys Val Asn Gly Val
        675                 680                 685
TGT TGG ACC GTT TAC CAT GGT GCT GGC TCA AAG ACC TTA GCC GCG CCA     2112
Cys Trp Thr Val Tyr His Gly Ala Gly Ser Lys Thr Leu Ala Ala Pro
    690                 695                 700
AAG GGG CCA ATC ACC CAG ATG TAC ACT AAT GTG GAC CAG GAC CTC GTC     2160
Lys Gly Pro Ile Thr Gln Met Tyr Thr Asn Val Asp Gln Asp Leu Val
705                 710                 715                 720
GGC TGG CCC AAG CCC CCC GGG GCG CGT TCC TTG ACA CCA TGC ACC TGT     2208
Gly Trp Pro Lys Pro Pro Gly Ala Arg Ser Leu Thr Pro Cys Thr Cys
                725                 730                 735
GGC AGC TCA GAC CTT TAC TTG GTC ACG AGA CAT GCT GAC GTC ATT CCG     2256
Gly Ser Ser Asp Leu Tyr Leu Val Thr Arg His Ala Asp Val Ile Pro
            740                 745                 750
GTG CGC CGG CGG GGC GAC AGT AGG GGG AGC CTG CTC TCC CCC AGG CCT     2304
Val Arg Arg Arg Gly Asp Ser Arg Gly Ser Leu Leu Ser Pro Arg Pro
        755                 760                 765
GTC TCC TAC TTG AAG GGC TCT TCG GGT GGT CCA CTG CTC TGC CCC TTC     2352
Val Ser Tyr Leu Lys Gly Ser Ser Gly Gly Pro Leu Leu Cys Pro Phe
    770                 775                 780
GGG CAC GCT GTG GGC ATC TTC CGG GCT GCC GTA TGC ACC CGG GGG GTT     2400
Gly His Ala Val Gly Ile Phe Arg Ala Ala Val Cys Thr Arg Gly Val
785                 790                 795                 800
GCG AAG GCG GTG GAC TTT GTG CCC GTA GAG TCC ATG GAA ACT ACT ATG     2448
Ala Lys Ala Val Asp Phe Val Pro Val Glu Ser Met Glu Thr Thr Met
                805                 810                 815
CGG TCT CCG GTC TTC ACG GAC AAC TCA TCC CCC CCG GCC GTA CCG CAG     2496
Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro Pro Ala Val Pro Gln
            820                 825                 830
TCA TTT CAA GTG GCC CAC CTA CAC GCT CCC ACT GGC AGC GGC AAG AGT     2544
Ser Phe Gln Val Ala His Leu His Ala Pro Thr Gly Ser Gly Lys Ser
        835                 840                 845
ACT AAA GTG CCG GCT GCA TAT GCA GCC CAA GGG TAC AAG GTG CTC GTC     2592
Thr Lys Val Pro Ala Ala Tyr Ala Ala Gln Gly Tyr Lys Val Leu Val
    850                 855                 860
CTC AAT CCG TCC GTT GCC GCT ACC TTA GGG TTT GGG GCG TAT ATG TCT     2640
Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe Gly Ala Tyr Met Ser
865                 870                 875                 880
AAG GCA CAC GGT ATT GAC CCC AAC ATC AGA ACT GGG GTA AGG ACC ATT     2688
Lys Ala His Gly Ile Asp Pro Asn Ile Arg Thr Gly Val Arg Thr Ile
                885                 890                 895
ACC ACA GGC GCC CCC GTC ACA TAC TCT ACC TAT GGC AAG TTT CTT GCC     2736
Thr Thr Gly Ala Pro Val Thr Tyr Ser Thr Tyr Gly Lys Phe Leu Ala
            900                 905                 910
GAT GGT GGT TGC TCT GGG GGC GCT TAT GAC ATC ATA ATA TGT GAT GAG     2784
Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp Ile Ile Ile Cys Asp Glu
        915                 920                 925
TGC CAT TCA ACT GAC TCG ACT ACA ATC TTG GGC ATC GGC ACA GTC CTG     2832
Cys His Ser Thr Asp Ser Thr Thr Ile Leu Gly Ile Gly Thr Val Leu
    930                 935                 940
GAC CAA GCG GAG ACG GCT GGA GCG CGG CTT GTC GTG CTC GCC ACC GCT     2880
Asp Gln Ala Glu Thr Ala Gly Ala Arg Leu Val Val Leu Ala Thr Ala
945                 950                 955                 960
ACG CCT CCG GGA TCG GTC ACC GTG CCA CAC CCA AAC ATC GAG GAG GTG     2928
Thr Pro Pro Gly Ser Val Thr Val Pro His Pro Asn Ile Glu Glu Val
                965                 970                 975
GCC CTG TCT AAT ACT GGA GAG ATC CCC TTC TAT GGC AAA GCC ATC CCC     2976
Ala Leu Ser Asn Thr Gly Glu Ile Pro Phe Tyr Gly Lys Ala Ile Pro
            980                 985                 990
ATT GAA GCC ATC AGG GGG GGA AGG CAT CTC ATT TTC TGT CAT TCC AAG     3024
Ile Glu Ala Ile Arg Gly Gly Arg His Leu Ile Phe Cys His Ser Lys
        995                 1000                1005
AAG AAG TGC GAC GAG CTC GCC GCA AAG CTG TCA GGC CTC GGA ATC AAC     3072
Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Ser Gly Leu Gly Ile Asn
    1010                1015                1020
GCT GTG GCG TAT TAC CGG GGG CTC GAT GTG TCC GTC ATA CCA ACT ATC     3120
Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser Val Ile Pro Thr Ile
1025                1030                1035                1040
GGA GAC GTC GTT GTC GTG GCA ACA GAC GCT CTG ATG ACG GGC TAT ACG     3168
Gly Asp Val Val Val Val Ala Thr Asp Ala Leu Met Thr Gly Tyr Thr
                1045                1050                1055
GGC GAC TTT GAC TCA GTG ATC GAC TGT AAC ACA TGT GTC ACC CAG ACA     3216
Gly Asp Phe Asp Ser Val Ile Asp Cys Asn Thr Cys Val Thr Gln Thr
            1060                1065                1070
GTC GAC TTC AGC TTG GAT CCC ACC TTC ACC ATT GAG ACG ACG ACC GTG     3264
Val Asp Phe Ser Leu Asp Pro Thr Phe Thr Ile Glu Thr Thr Thr Val
        1075                1080                1085
CCT CAA GAC GCA GTG TCG CGC TCG CAG CGG CGG GGT AGG ACT GGC AGG     3312
Pro Gln Asp Ala Val Ser Arg Ser Gln Arg Arg Gly Arg Thr Gly Arg
    1090                1095                1100
GGT AGG AGA GGC ATC TAC AGG TTT GTG ACT CCG GGA GAA CGG CCC TCG     3360
Gly Arg Arg Gly Ile Tyr Arg Phe Val Thr Pro Gly Glu Arg Pro Ser
1105                1110                1115                1120
GGC ATG TTC GAT TCC TCG GTC CTG TGT GAG TGC TAT GAC GCG GGC TGT     3408
Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys Tyr Asp Ala Gly Cys
                1125                1130                1135
GCT TGG TAC GAG CTC ACC CCG GCC GAG ACC TCG GTT AGG TTG CGG GCC     3456
Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Ser Val Arg Leu Arg Ala
            1140                1145                1150
TAC CTG AAC ACA CCA GGG TTG CCC GTT TGC CAG GAC CAC CTG GAG TTC     3504
Tyr Leu Asn Thr Pro Gly Leu Pro Val Cys Gln Asp His Leu Glu Phe
        1155                1160                1165
TGG GAG AGT GTC TTC ACA GGC CTC ACC CAT ATA GAT GCA CAC TTC TTG     3552
Trp Glu Ser Val Phe Thr Gly Leu Thr His Ile Asp Ala His Phe Leu
    1170                1175                1180
TCC CAG ACC AAG CAG GCA GGA GAC AAC TTC CCC TAC CTG GTA GCA TAC     3600
Ser Gln Thr Lys Gln Ala Gly Asp Asn Phe Pro Tyr Leu Val Ala Tyr
1185                1190                1195                1200
CAA GCC ACG GTG TGC GCC AGG GCT CAG GCC CCA CCT CCA TCA TGG GAT     3648
Gln Ala Thr Val Cys Ala Arg Ala Gln Ala Pro Pro Pro Ser Trp Asp
                1205                1210                1215
CAA ATG TGG AAG TGT CTC ATA CGG CTG AAA CCT ACG CTG CAC GGG CCA     3696
Gln Met Trp Lys Cys Leu Ile Arg Leu Lys Pro Thr Leu His Gly Pro
            1220                1225                1230
ACA CCC TTG CTG TAC AGG CTG GGA GCC GTC CAG AAT GAG GTC ACC CTC     3744
Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gln Asn Glu Val Thr Leu
        1235                1240                1245
ACC CAC CCC ATA ACC AAA TAC ATC ATG GCA TGC ATG TCG GCT GAC CTG     3792
Thr His Pro Ile Thr Lys Tyr Ile Met Ala Cys Met Ser Ala Asp Leu
    1250                1255                1260
GAG GTC GTC ACT AGC ACC TGG GTG CTG GTG GGC GGA GTC CTT GCA GCT     3840
Glu Val Val Thr Ser Thr Trp Val Leu Val Gly Gly Val Leu Ala Ala
1265                1270                1275                1280
CTG GCC GCG TAT TGC CTG ACA ACA GGC AGT GTG GTC ATT GTG GGT AGG     3888
Leu Ala Ala Tyr Cys Leu Thr Thr Gly Ser Val Val Ile Val Gly Arg
                1285                1290                1295
ATT ATC TTG TCC GGG AGG CCG GCC ATT GTT CCC GAC AGG GAG CTT CTC     3936
Ile Ile Leu Ser Gly Arg Pro Ala Ile Val Pro Asp Arg Glu Leu Leu
            1300                1305                1310
TAC CAG GAG TTC GAT GAA ATG GAA GAG TGC GCC TCG CAC CTC CCT TAC     3984
Tyr Gln Glu Phe Asp Glu Met Glu Glu Cys Ala Ser His Leu Pro Tyr
        1315                1320                1325
ATC GAG CAG GGA ATG CAG CTC GCC GAG CAA TTC AAG CAG AAA GCG CTC     4032
Ile Glu Gln Gly Met Gln Leu Ala Glu Gln Phe Lys Gln Lys Ala Leu
    1330                1335                1340
GGG TTA CTG CAA ACA GCC ACC AAA CAA GCG GAG GCT GCT GCT CCC GTG     4080
Gly Leu Leu Gln Thr Ala Thr Lys Gln Ala Glu Ala Ala Ala Pro Val
1345                1350                1355                1360
GTG GAG TCC AAG TGG CGA GCC CTT GAG ACA TTC TGG GCG AAG CAC ATG     4128
Val Glu Ser Lys Trp Arg Ala Leu Glu Thr Phe Trp Ala Lys His Met
                1365                1370                1375
TGG AAT TTC ATC AGC GGG ATA CAG TAC TTA GCA GGC TTA TCC ACT CTG     4176
Trp Asn Phe Ile Ser Gly Ile Gln Tyr Leu Ala Gly Leu Ser Thr Leu
            1380                1385                1390
CCT GGG AAC CCC GCA ATA GCA TCA TTG ATG GCA TTC ACA GCC TCT ATC     4224
Pro Gly Asn Pro Ala Ile Ala Ser Leu Met Ala Phe Thr Ala Ser Ile
        1395                1400                1405
ACC AGC CCG CTC ACC ACC CAA AGT ACC CTC CTG TTT AAC ATC TTG GGG     4272
Thr Ser Pro Leu Thr Thr Gln Ser Thr Leu Leu Phe Asn Ile Leu Gly
    1410                1415                1420
GGG TGG GTG GCT GCC CAA CTC GCC CCC CCC AGC GCC GCT TCG GCT TTC     4320
Gly Trp Val Ala Ala Gln Leu Ala Pro Pro Ser Ala Ala Ser Ala Phe
1425                1430                1435                1440
GTG GGC GCC GGC ATC GCC GGT GCG GCT GTT GGC AGC ATA GGC CTT GGG     4368
Val Gly Ala Gly Ile Ala Gly Ala Ala Val Gly Ser Ile Gly Leu Gly
                1445                1450                1455
AAG GTG CTT GTG GAC ATT CTG GCG GGT TAT GGA GCA GGA GTG GCC GGC     4416
Lys Val Leu Val Asp Ile Leu Ala Gly Tyr Gly Ala Gly Val Ala Gly
            1460                1465                1470
GCG CTC GTG GCC TTT AAG GTC ATG AGC GGC GAG ATG CCC TCC ACC GAG     4464
Ala Leu Val Ala Phe Lys Val Met Ser Gly Glu Met Pro Ser Thr Glu
        1475                1480                1485
GAC CTG GTC AAT CTA CTT CCT GCC ATC CTC TCT CCT GGC GCC CTG GTC     4512
Asp Leu Val Asn Leu Leu Pro Ala Ile Leu Ser Pro Gly Ala Leu Val
    1490                1495                1500
GTC GGG GTC GTG TGT GCA GCA ATA CTG CGT CGA CAC GTG GGT CCG GGA     4560
Val Gly Val Val Cys Ala Ala Ile Leu Arg Arg His Val Gly Pro Gly
1505                1510                1515                1520
GAG GGG GCT GTG CAG TGG ATG AAC CGG CTG ATA GCG TTC GCC TCG CGG     4608
Glu Gly Ala Val Gln Trp Met Asn Arg Leu Ile Ala Phe Ala Ser Arg
                1525                1530                1535
GGT AAT CAT GTT TCC CCC ACG CAC TAT GTG CCT GAG AGC GAC GCC GCA     4656
Gly Asn His Val Ser Pro Thr His Tyr Val Pro Glu Ser Asp Ala Ala
            1540                1545                1550
GCG CGT GTT ACT CAG ATC CTC TCC AGC CTT ACC ATC ACT CAG CTG CTG     4704
Ala Arg Val Thr Gln Ile Leu Ser Ser Leu Thr Ile Thr Gln Leu Leu
        1555                1560                1565
AAA AGG CTC CAC CAG TGG ATT AAT GAA GAC TGC TCC ACA CCG TGT TCC     4752
Lys Arg Leu His Gln Trp Ile Asn Glu Asp Cys Ser Thr Pro Cys Ser
    1570                1575                1580
GGC TCG TGG CTA AGG GAT GTT TGG GAC TGG ATA TGC ACG GTG TTG ACT     4800
Gly Ser Trp Leu Arg Asp Val Trp Asp Trp Ile Cys Thr Val Leu Thr
1585                1590                1595                1600
GAC TTC AAG ACC TGG CTC CAG TCC AAG CTC CTG CCG CAG CTA CCT GGA     4848
Asp Phe Lys Thr Trp Leu Gln Ser Lys Leu Leu Pro Gln Leu Pro Gly
                1605                1610                1615
GTC CCT TTT TTC TCG TGC CAA CGC GGG TAC AAG GGA GTC TGG CGG GGA     4896
Val Pro Phe Phe Ser Cys Gln Arg Gly Tyr Lys Gly Val Trp Arg Gly
            1620                1625                1630
GAC GGC ATC ATG CAA ACC ACC TGC CCA TGT GGA GCA CAG ATC ACC GGA     4944
Asp Gly Ile Met Gln Thr Thr Cys Pro Cys Gly Ala Gln Ile Thr Gly
        1635                1640                1645
CAT GTC AAA AAC GGT TCC ATG AGG ATC GTC GGG CCT AAG ACC TGC AGC     4992
His Val Lys Asn Gly Ser Met Arg Ile Val Gly Pro Lys Thr Cys Ser
    1650                1655                1660
AAC ACG TGG CAT GGA ACA TTC CCC ATC AAC GCA TAC ACC ACG GGC CCC     5040
Asn Thr Trp His Gly Thr Phe Pro Ile Asn Ala Tyr Thr Thr Gly Pro
1665                1670                1675                1680
TGC ACA CCC TCT CCA GCG CCA AAC TAT TCT AGG GCG CTG TGG CGG GTG     5088
Cys Thr Pro Ser Pro Ala Pro Asn Tyr Ser Arg Ala Leu Trp Arg Val
                1685                1690                1695
GCC GCT GAG GAG TAC GTG GAG GTC ACG CGG GTG GGG GAT TTC CAC TAC     5136
Ala Ala Glu Glu Tyr Val Glu Val Thr Arg Val Gly Asp Phe His Tyr
            1700                1705                1710
GTG ACG GGC ATG ACC ACT GAC AAC GTA AAG TGC CCA TGC CAG GTT CCG     5184
Val Thr Gly Met Thr Thr Asp Asn Val Lys Cys Pro Cys Gln Val Pro
        1715                1720                1725
GCT CCT GAA TTC TTC TCG GAG GTG GAC GGA GTG CGG TTG CAC AGG TAC     5232
Ala Pro Glu Phe Phe Ser Glu Val Asp Gly Val Arg Leu His Arg Tyr
    1730                1735                1740
GCT CCG GCG TGC AGG CCT CTC CTA CGG GAG GAG GTT ACA TTC CAG GTC     5280
Ala Pro Ala Cys Arg Pro Leu Leu Arg Glu Glu Val Thr Phe Gln Val
1745                1750                1755                1760
GGG CTC AAC CAA TAC CTG GTT GGG TCA CAG CTA CCA TGC GAG CCC GAA     5328
Gly Leu Asn Gln Tyr Leu Val Gly Ser Gln Leu Pro Cys Glu Pro Glu
                1765                1770                1775
CCG GAT GTA GCA GTG CTC ACT TCC ATG CTC ACC GAC CCC TCC CAC ATC     5376
Pro Asp Val Ala Val Leu Thr Ser Met Leu Thr Asp Pro Ser His Ile
            1780                1785                1790
ACA GCA GAA ACG GCT AAG CGT AGG TTG GCC AGG GGG TCT CCC CCC TCC     5424
Thr Ala Glu Thr Ala Lys Arg Arg Leu Ala Arg Gly Ser Pro Pro Ser
        1795                1800                1805
TTG GCC AGC TCT TCA GCT AGC CAG TTG TCT GCG CCT TCC TTG AAG GCG     5472
Leu Ala Ser Ser Ser Ala Ser Gln Leu Ser Ala Pro Ser Leu Lys Ala
    1810                1815                1820
ACA TGC ACT ACC CAC CAT GTC TCT CCG GAC GCT GAC CTC ATC GAG GCC     5520
Thr Cys Thr Thr His His Val Ser Pro Asp Ala Asp Leu Ile Glu Ala
1825                1830                1835                1840
AAC CTC CTG TGG CGG CAG GAG ATG GGC GGG AAC ATC ACC CGC GTG GAG     5568
Asn Leu Leu Trp Arg Gln Glu Met Gly Gly Asn Ile Thr Arg Val Glu
                1845                1850                1855
TCG GAG AAC AAG GTG GTA GTC CTG GAC TCT TTC GAC CCG CTT CGA GCG     5616
Ser Glu Asn Lys Val Val Val Leu Asp Ser Phe Asp Pro Leu Arg Ala
            1860                1865                1870
GAG GAG GAT GAG AGG GAA GTA TCC GTT CCG GCG GAG ATC CTG CGG AAA     5664
Glu Glu Asp Glu Arg Glu Val Ser Val Pro Ala Glu Ile Leu Arg Lys
        1875                1880                1885
TCC AAG AAG TTC CCC GCA GCG ATG CCC ATC TGG GCG CGC CCG GAT TAC     5712
Ser Lys Lys Phe Pro Ala Ala Met Pro Ile Trp Ala Arg Pro Asp Tyr
    1890                1895                1900
AAC CCT CCA CTG TTA GAG TCC TGG AAG GAC CCG GAC TAC GTC CCT CCG     5760
Asn Pro Pro Leu Leu Glu Ser Trp Lys Asp Pro Asp Tyr Val Pro Pro
1905                1910                1915                1920
GTG GTG CAC GGG TGC CCG TTG CCA CCT ATC AAG GCC CCT CCA ATA CCA     5808
Val Val His Gly Cys Pro Leu Pro Pro Ile Lys Ala Pro Pro Ile Pro
                1925                1930                1935
CCT CCA CGG AGA AAG AGG ACG GTT GTC CTA ACA GAG TCC TCC GTG TCT     5856
Pro Pro Arg Arg Lys Arg Thr Val Val Leu Thr Glu Ser Ser Val Ser
            1940                1945                1950
TCT GCC TTA GCG GAG CTC GCT ACT AAG ACC TTC GGC AGC TCC GAA TCA     5904
Ser Ala Leu Ala Glu Leu Ala Thr Lys Thr Phe Gly Ser Ser Glu Ser
        1955                1960                1965
TCG GCC GTC GAC AGC GGC ACG GCG ACC GCC CTT CCT GAC CAG GCC TCC     5952
Ser Ala Val Asp Ser Gly Thr Ala Thr Ala Leu Pro Asp Gln Ala Ser
    1970                1975                1980
GAC GAC GGT GAC AAA GGA TCC GAC GTT GAG TCG TAC TCC TCC ATG CCC     6000
Asp Asp Gly Asp Lys Gly Ser Asp Val Glu Ser Tyr Ser Ser Met Pro
1985                1990                1995                2000
CCC CTT GAG GGG GAA CCG GGG GAC CCC GAT CTC AGT GAC GGG TCT TGG     6048
Pro Leu Glu Gly Glu Pro Gly Asp Pro Asp Leu Ser Asp Gly Ser Trp
                2005                2010                2015
TCT ACC GTG AGC GAG GAA GCT AGT GAG GAT GTC GTC TGC TGC TCA ATG     6096
Ser Thr Val Ser Glu Glu Ala Ser Glu Asp Val Val Cys Cys Ser Met
            2020                2025                2030
TCC TAC ACA TGG ACA GGC GCC TTG ATC ACG CCA TGC GCT GCG GAG GAA     6144
Ser Tyr Thr Trp Thr Gly Ala Leu Ile Thr Pro Cys Ala Ala Glu Glu
        2035                2040                2045
AGC AAG CTG CCC ATC AAC GCG TTG AGC AAC TCT TTG CTG CGC CAC CAT     6192
Ser Lys Leu Pro Ile Asn Ala Leu Ser Asn Ser Leu Leu Arg His His
    2050                2055                2060
AAC ATG GTT TAT GCC ACA ACA TCT CGC AGC GCA GGC CTG CGG CAG AAG     6240
Asn Met Val Tyr Ala Thr Thr Ser Arg Ser Ala Gly Leu Arg Gln Lys
2065                2070                2075                2080
AAG GTC ACC TTT GAC AGA CTG CAA GTC CTG GAC GAC CAC TAC CGG GAC     6288
Lys Val Thr Phe Asp Arg Leu Gln Val Leu Asp Asp His Tyr Arg Asp
                2085                2090                2095
GTG CTC AAG GAG ATG AAG GCG AAG GCG TCC ACA GTT AAG GCT AAA CTC     6336
Val Leu Lys Glu Met Lys Ala Lys Ala Ser Thr Val Lys Ala Lys Leu
            2100                2105                2110
CTA TCC GTA GAG GAA GCC TGC AAG CTG ACG CCC CCA CAT TCG GCC AAA     6384
Leu Ser Val Glu Glu Ala Cys Lys Leu Thr Pro Pro His Ser Ala Lys
        2115                2120                2125
TCC AAG TTT GGC TAT GGG GCA AAG GAC GTC CGG AAC CTA TCC AGC AAG     6432
Ser Lys Phe Gly Tyr Gly Ala Lys Asp Val Arg Asn Leu Ser Ser Lys
    2130                2135                2140
GCC GTT AAC CAC ATC CAC TCC GTG TGG AAG GAC TTG CTG GAA GAC ACT     6480
Ala Val Asn His Ile His Ser Val Trp Lys Asp Leu Leu Glu Asp Thr
2145                2150                2155                2160
GTG ACA CCA ATT GAC ACC ACC ATC ATG GCA AAA AAT GAG GTT TTC TGT     6528
Val Thr Pro Ile Asp Thr Thr Ile Met Ala Lys Asn Glu Val Phe Cys
                2165                2170                2175
GTC CAA CCA GAG AAA GGA GGC CGT AAG CCA GCC CGC CTT ATC GTA TTC     6576
Val Gln Pro Glu Lys Gly Gly Arg Lys Pro Ala Arg Leu Ile Val Phe
            2180                2185                2190
CCA GAT CTG GGA GTC CGT GTA TGC GAG AAG ATG GCC CTC TAT GAT GTG     6624
Pro Asp Leu Gly Val Arg Val Cys Glu Lys Met Ala Leu Tyr Asp Val
        2195                2200                2205
GTC TCC ACC CTT CCT CAG GTC GTG ATG GGC TCC TCA TAC GGA TTC CAG     6672
Val Ser Thr Leu Pro Gln Val Val Met Gly Ser Ser Tyr Gly Phe Gln
    2210                2215                2220
TAC TCT CCT GGG CAG CGA GTC GAG TTC CTG GTG AAT ACC TGG AAA TCA     6720
Tyr Ser Pro Gly Gln Arg Val Glu Phe Leu Val Asn Thr Trp Lys Ser
2225                2230                2235                2240
AAG AAA AAC CCC ATG GGC TTT TCA TAT GAC ACT CGC TGT TTC GAC TCA     6768
Lys Lys Asn Pro Met Gly Phe Ser Tyr Asp Thr Arg Cys Phe Asp Ser
                2245                2250                2255
ACG GTC ACC GAG AAC GAC ATC CGT GTT GAG GAG TCA ATT TAC CAA TGT     6816
Thr Val Thr Glu Asn Asp Ile Arg Val Glu Glu Ser Ile Tyr Gln Cys
            2260                2265                2270
TGT GAC TTG GCC CCC GAA GCC AGA CAG GCC ATA AAA TCG CTC ACA GAG     6864
Cys Asp Leu Ala Pro Glu Ala Arg Gln Ala Ile Lys Ser Leu Thr Glu
        2275                2280                2285
CGG CTT TAT ATC GGG GGT CCT CTG ACT AAT TCA AAA GGG CAG AAC TGC     6912
Arg Leu Tyr Ile Gly Gly Pro Leu Thr Asn Ser Lys Gly Gln Asn Cys
    2290                2295                2300
GGT TAT CGC CGG TGC CGC GCG AGC GGC GTG CTG ACG ACT AGC TGC GGT     6960
Gly Tyr Arg Arg Cys Arg Ala Ser Gly Val Leu Thr Thr Ser Cys Gly
2305                2310                2315                2320
AAC ACC CTC ACA TGT TAC TTG AAG GCC TCT GCA GCC TGT CGA GCT GCG     7008
Asn Thr Leu Thr Cys Tyr Leu Lys Ala Ser Ala Ala Cys Arg Ala Ala
                2325                2330                2335
AAG CTC CAG GAC TGC ACG ATG CTC GTG AAC GGA GAC GAC CTC GTC GTT     7056
Lys Leu Gln Asp Cys Thr Met Leu Val Asn Gly Asp Asp Leu Val Val
            2340                2345                2350
ATC TGT GAA AGC GCG GGA ACC CAA GAG GAC GCG GCG AGC CTA CGA GTC     7104
Ile Cys Glu Ser Ala Gly Thr Gln Glu Asp Ala Ala Ser Leu Arg Val
        2355                2360                2365
TTC ACG GAG GCT ATG ACT AGG TAC TCC GCC CCC CCC GGG GAC CCG CCC     7152
Phe Thr Glu Ala Met Thr Arg Tyr Ser Ala Pro Pro Gly Asp Pro Pro
    2370                2375                2380
CAA CCA GAA TAC GAC TTG GAG CTG ATA ACA TCA TGT TCC TCC AAT GTG     7200
Gln Pro Glu Tyr Asp Leu Glu Leu Ile Thr Ser Cys Ser Ser Asn Val
2385                2390                2395                2400
TCG GTC GCC CAC GAT GCA TCA GGC AAA AGG GTG TAC TAC CTC ACC CGT     7248
Ser Val Ala His Asp Ala Ser Gly Lys Arg Val Tyr Tyr Leu Thr Arg
                2405                2410                2415
GAT CCC ACC ACC CCC CTA GCA CGG GCT GCG TGG GAG ACA GCT AGA CAC     7296
Asp Pro Thr Thr Pro Leu Ala Arg Ala Ala Trp Glu Thr Ala Arg His
            2420                2425                2430
ACT CCA GTT AAC TCC TGG CTA GGC AAC ATT ATT ATG TAT GCG CCC ACT     7344
Thr Pro Val Asn Ser Trp Leu Gly Asn Ile Ile Met Tyr Ala Pro Thr
        2435                2440                2445
TTG TGG GCA AGG ATG ATT CTG ATG ACT CAC TTC TTC TCC ATC CTT CTA     7392
Leu Trp Ala Arg Met Ile Leu Met Thr His Phe Phe Ser Ile Leu Leu
    2450                2455                2460
GCG CAG GAG CAA CTT GAA AAA GCC CTG GAC TGC CAG ATC TAC GGG GCC     7440
Ala Gln Glu Gln Leu Glu Lys Ala Leu Asp Cys Gln Ile Tyr Gly Ala
2465                2470                2475                2480
TGT TAC TCC ATT GAG CCA CTT GAC CTA CCT CAG ATC ATT GAA CGA CTC     7488
Cys Tyr Ser Ile Glu Pro Leu Asp Leu Pro Gln Ile Ile Glu Arg Leu
                2485                2490                2495
CAT GGC CTT AGC GCA TTT TCA CTC CAT AGT TAC TCT CCA GGT GAG ATC     7536
His Gly Leu Ser Ala Phe Ser Leu His Ser Tyr Ser Pro Gly Glu Ile
            2500                2505                2510
AAT AGG GTG GCT TCA TGC CTC AGG AAA CTT GGG GTA CCA CCC TTG CGA     7584
Asn Arg Val Ala Ser Cys Leu Arg Lys Leu Gly Val Pro Pro Leu Arg
        2515                2520                2525
GTC TGG AGA CAT CGG GCC AGG AGC GTC CGC GCT AGG CTA CTG TCC CAG     7632
Val Trp Arg His Arg Ala Arg Ser Val Arg Ala Arg Leu Leu Ser Gln
    2530                2535                2540
GGA GGG AGG GCC GCC ACT TGT GGC AAA TAC CTC TTC AAC TGG GCA GTA     7680
Gly Gly Arg Ala Ala Thr Cys Gly Lys Tyr Leu Phe Asn Trp Ala Val
2545                2550                2555                2560
AAA ACC AAA CTT AAA CTC ACT CCA ATC CCG GCT GCG TCC CGG CTG GAC     7728
Lys Thr Lys Leu Lys Leu Thr Pro Ile Pro Ala Ala Ser Arg Leu Asp
                2565                2570                2575
TTG TCC GGC TGG TTC GTT GCT GGT TAC AGC GGG GGA GAC ATA TAT CAC     7776
Leu Ser Gly Trp Phe Val Ala Gly Tyr Ser Gly Gly Asp Ile Tyr His
            2580                2585                2590
AGC CTG TCT CGT GCC CGA CCC CGT TGG TTC ATG CTG TGC CTA CTC CTA     7824
Ser Leu Ser Arg Ala Arg Pro Arg Trp Phe Met Leu Cys Leu Leu Leu
        2595                2600                2605
CTT TCT GTA GGG GTA GGC ATC TAC CTG CTC CCC AAC CG ATGAACGGGG       7872
Leu Ser Val Gly Val Gly Ile Tyr Leu Leu Pro Asn
    2610                2615                262
AGATAAACAC TCCAGGCCAA TAGGCCATCC CCCTTTTTTT TTTTT                   7917 
           
           
             
               2620 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             32
Gly Ala Gln Ala Lys Thr Thr Asn Arg Leu Val Ser Met Phe Ala Ser
  1               5                  10                  15
Gly Pro Ser Gln Lys Ile Gln Leu Ile Asn Thr Asn Gly Ser Trp His
             20                  25                  30
Ile Asn Arg Thr Ala Leu Asn Cys Asn Asp Ser Leu Gln Thr Gly Phe
         35                  40                  45
Leu Ala Ala Leu Phe Tyr Thr His Ser Phe Asn Ser Ser Gly Cys Pro
     50                  55                  60
Glu Arg Met Ala Gln Cys Arg Thr Ile Asp Lys Phe Asp Gln Gly Trp
 65                  70                  75                  80
Gly Pro Ile Thr Tyr Ala Glu Ser Ser Arg Ser Asp Gln Arg Pro Tyr
                 85                  90                  95
Cys Trp His Tyr Pro Pro Pro Gln Cys Thr Ile Val Pro Ala Ser Glu
            100                 105                 110
Val Cys Gly Pro Val Tyr Cys Phe Thr Pro Ser Pro Val Val Val Gly
        115                 120                 125
Thr Thr Asp Arg Phe Gly Val Pro Thr Tyr Arg Trp Gly Glu Asn Glu
    130                 135                 140
Thr Asp Val Leu Leu Leu Asn Asn Thr Arg Pro Pro Gln Gly Asn Trp
145                 150                 155                 160
Phe Gly Cys Thr Trp Met Asn Ser Thr Gly Phe Thr Lys Thr Cys Gly
                165                 170                 175
Gly Pro Pro Cys Asn Ile Gly Gly Val Gly Asn Asn Thr Leu Thr Cys
            180                 185                 190
Pro Thr Asp Cys Phe Arg Lys His Pro Glu Ala Thr Tyr Thr Lys Cys
        195                 200                 205
Gly Ser Gly Pro Trp Leu Thr Pro Arg Cys Met Val Asp Tyr Pro Tyr
    210                 215                 220
Arg Leu Trp His Tyr Pro Cys Thr Val Asn Phe Thr Ile Phe Lys Val
225                 230                 235                 240
Arg Met Tyr Val Gly Gly Val Glu His Arg Leu Asn Ala Ala Cys Asn
                245                 250                 255
Trp Thr Arg Gly Glu Arg Cys Asp Leu Glu Asp Arg Asp Arg Pro Glu
            260                 265                 270
Leu Ser Pro Leu Leu Leu Ser Thr Thr Glu Trp Gln Val Leu Pro Cys
        275                 280                 285
Ser Phe Thr Thr Leu Pro Ala Leu Ser Thr Gly Leu Ile His Leu His
    290                 295                 300
Gln Asn Ile Val Asp Val Gln Tyr Leu Tyr Gly Ile Gly Ser Ala Val
305                 310                 315                 320
Val Ser Phe Ala Ile Lys Trp Glu Tyr Val Leu Leu Leu Phe Leu Leu
                325                 330                 335
Leu Ala Asp Ala Arg Val Cys Ala Cys Leu Trp Met Met Leu Leu Ile
            340                 345                 350
Ala Gln Ala Glu Ala Ala Leu Glu Asn Leu Val Val Leu Asn Ser Ala
        355                 360                 365
Ser Val Ala Gly Ala His Gly Ile Leu Ser Phe Leu Val Phe Phe Cys
    370                 375                 380
Ala Ala Trp Tyr Ile Lys Gly Arg Leu Val Pro Gly Ala Thr Tyr Ala
385                 390                 395                 400
Leu Tyr Gly Val Trp Pro Leu Leu Leu Leu Leu Leu Ala Leu Pro Pro
                405                 410                 415
Arg Ala Tyr Ala Met Asp Arg Glu Met Ala Ala Ser Cys Gly Gly Ala
            420                 425                 430
Val Phe Val Gly Leu Val Leu Leu Thr Leu Ser Pro Tyr Tyr Lys Val
        435                 440                 445
Phe Leu Ala Arg Leu Ile Trp Trp Leu Gln Tyr Phe Thr Thr Arg Ala
    450                 455                 460
Glu Ala Asp Leu His Val Trp Ile Pro Pro Leu Asn Ala Arg Gly Gly
465                 470                 475                 480
Arg Asp Ala Ile Ile Leu Leu Met Cys Ala Val His Pro Glu Leu Ile
                485                 490                 495
Phe Asp Ile Thr Lys Leu Leu Ile Ala Ile Leu Gly Pro Leu Met Val
            500                 505                 510
Leu Gln Ala Gly Ile Thr Arg Val Pro Tyr Phe Val Arg Ala Gln Gly
        515                 520                 525
Leu Ile His Ala Cys Met Leu Val Arg Lys Val Ala Gly Gly His Tyr
    530                 535                 540
Val Gln Met Ala Phe Met Lys Leu Gly Ala Leu Thr Gly Thr Tyr Ile
545                 550                 555                 560
Tyr Asn His Leu Thr Pro Leu Arg Asp Trp Pro Arg Ala Gly Leu Arg
                565                 570                 575
Asp Leu Ala Val Ala Val Glu Pro Val Val Phe Ser Asp Met Glu Thr
            580                 585                 590
Lys Ile Ile Thr Trp Gly Ala Asp Thr Ala Ala Cys Gly Asp Ile Ile
        595                 600                 605
Leu Gly Leu Pro Val Ser Ala Arg Arg Gly Lys Glu Ile Leu Leu Gly
    610                 615                 620
Pro Ala Asp Ser Leu Glu Gly Arg Gly Leu Arg Leu Leu Ala Pro Ile
625                 630                 635                 640
Thr Ala Tyr Ser Gln Gln Thr Arg Gly Leu Leu Gly Cys Ile Ile Thr
                645                 650                 655
Ser Leu Thr Gly Arg Asp Lys Asn Gln Val Glu Gly Glu Val Gln Val
            660                 665                 670
Val Ser Thr Ala Thr Gln Ser Phe Leu Ala Thr Cys Val Asn Gly Val
        675                 680                 685
Cys Trp Thr Val Tyr His Gly Ala Gly Ser Lys Thr Leu Ala Ala Pro
    690                 695                 700
Lys Gly Pro Ile Thr Gln Met Tyr Thr Asn Val Asp Gln Asp Leu Val
705                 710                 715                 720
Gly Trp Pro Lys Pro Pro Gly Ala Arg Ser Leu Thr Pro Cys Thr Cys
                725                 730                 735
Gly Ser Ser Asp Leu Tyr Leu Val Thr Arg His Ala Asp Val Ile Pro
            740                 745                 750
Val Arg Arg Arg Gly Asp Ser Arg Gly Ser Leu Leu Ser Pro Arg Pro
        755                 760                 765
Val Ser Tyr Leu Lys Gly Ser Ser Gly Gly Pro Leu Leu Cys Pro Phe
    770                 775                 780
Gly His Ala Val Gly Ile Phe Arg Ala Ala Val Cys Thr Arg Gly Val
785                 790                 795                 800
Ala Lys Ala Val Asp Phe Val Pro Val Glu Ser Met Glu Thr Thr Met
                805                 810                 815
Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro Pro Ala Val Pro Gln
            820                 825                 830
Ser Phe Gln Val Ala His Leu His Ala Pro Thr Gly Ser Gly Lys Ser
        835                 840                 845
Thr Lys Val Pro Ala Ala Tyr Ala Ala Gln Gly Tyr Lys Val Leu Val
    850                 855                 860
Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe Gly Ala Tyr Met Ser
865                 870                 875                 880
Lys Ala His Gly Ile Asp Pro Asn Ile Arg Thr Gly Val Arg Thr Ile
                885                 890                 895
Thr Thr Gly Ala Pro Val Thr Tyr Ser Thr Tyr Gly Lys Phe Leu Ala
            900                 905                 910
Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp Ile Ile Ile Cys Asp Glu
        915                 920                 925
Cys His Ser Thr Asp Ser Thr Thr Ile Leu Gly Ile Gly Thr Val Leu
    930                 935                 940
Asp Gln Ala Glu Thr Ala Gly Ala Arg Leu Val Val Leu Ala Thr Ala
945                 950                 955                 960
Thr Pro Pro Gly Ser Val Thr Val Pro His Pro Asn Ile Glu Glu Val
                965                 970                 975
Ala Leu Ser Asn Thr Gly Glu Ile Pro Phe Tyr Gly Lys Ala Ile Pro
            980                 985                 990
Ile Glu Ala Ile Arg Gly Gly Arg His Leu Ile Phe Cys His Ser Lys
        995                 1000                1005
Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Ser Gly Leu Gly Ile Asn
    1010                1015                1020
Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser Val Ile Pro Thr Ile
1025                1030                1035                1040
Gly Asp Val Val Val Val Ala Thr Asp Ala Leu Met Thr Gly Tyr Thr
                1045                1050                1055
Gly Asp Phe Asp Ser Val Ile Asp Cys Asn Thr Cys Val Thr Gln Thr
            1060                1065                1070
Val Asp Phe Ser Leu Asp Pro Thr Phe Thr Ile Glu Thr Thr Thr Val
        1075                1080                1085
Pro Gln Asp Ala Val Ser Arg Ser Gln Arg Arg Gly Arg Thr Gly Arg
    1090                1095                1100
Gly Arg Arg Gly Ile Tyr Arg Phe Val Thr Pro Gly Glu Arg Pro Ser
1105                1110                1115                1120
Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys Tyr Asp Ala Gly Cys
                1125                1130                1135
Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Ser Val Arg Leu Arg Ala
            1140                1145                1150
Tyr Leu Asn Thr Pro Gly Leu Pro Val Cys Gln Asp His Leu Glu Phe
        1155                1160                1165
Trp Glu Ser Val Phe Thr Gly Leu Thr His Ile Asp Ala His Phe Leu
    1170                1175                1180
Ser Gln Thr Lys Gln Ala Gly Asp Asn Phe Pro Tyr Leu Val Ala Tyr
1185                1190                1195                1200
Gln Ala Thr Val Cys Ala Arg Ala Gln Ala Pro Pro Pro Ser Trp Asp
                1205                1210                1215
Gln Met Trp Lys Cys Leu Ile Arg Leu Lys Pro Thr Leu His Gly Pro
            1220                1225                1230
Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gln Asn Glu Val Thr Leu
        1235                1240                1245
Thr His Pro Ile Thr Lys Tyr Ile Met Ala Cys Met Ser Ala Asp Leu
    1250                1255                1260
Glu Val Val Thr Ser Thr Trp Val Leu Val Gly Gly Val Leu Ala Ala
1265                1270                1275                1280
Leu Ala Ala Tyr Cys Leu Thr Thr Gly Ser Val Val Ile Val Gly Arg
                1285                1290                1295
Ile Ile Leu Ser Gly Arg Pro Ala Ile Val Pro Asp Arg Glu Leu Leu
            1300                1305                1310
Tyr Gln Glu Phe Asp Glu Met Glu Glu Cys Ala Ser His Leu Pro Tyr
        1315                1320                1325
Ile Glu Gln Gly Met Gln Leu Ala Glu Gln Phe Lys Gln Lys Ala Leu
    1330                1335                1340
Gly Leu Leu Gln Thr Ala Thr Lys Gln Ala Glu Ala Ala Ala Pro Val
1345                1350                1355                1360
Val Glu Ser Lys Trp Arg Ala Leu Glu Thr Phe Trp Ala Lys His Met
                1365                1370                1375
Trp Asn Phe Ile Ser Gly Ile Gln Tyr Leu Ala Gly Leu Ser Thr Leu
            1380                1385                1390
Pro Gly Asn Pro Ala Ile Ala Ser Leu Met Ala Phe Thr Ala Ser Ile
        1395                1400                1405
Thr Ser Pro Leu Thr Thr Gln Ser Thr Leu Leu Phe Asn Ile Leu Gly
    1410                1415                1420
Gly Trp Val Ala Ala Gln Leu Ala Pro Pro Ser Ala Ala Ser Ala Phe
1425                1430                1435                1440
Val Gly Ala Gly Ile Ala Gly Ala Ala Val Gly Ser Ile Gly Leu Gly
                1445                1450                1455
Lys Val Leu Val Asp Ile Leu Ala Gly Tyr Gly Ala Gly Val Ala Gly
            1460                1465                1470
Ala Leu Val Ala Phe Lys Val Met Ser Gly Glu Met Pro Ser Thr Glu
        1475                1480                1485
Asp Leu Val Asn Leu Leu Pro Ala Ile Leu Ser Pro Gly Ala Leu Val
    1490                1495                1500
Val Gly Val Val Cys Ala Ala Ile Leu Arg Arg His Val Gly Pro Gly
1505                1510                1515                1520
Glu Gly Ala Val Gln Trp Met Asn Arg Leu Ile Ala Phe Ala Ser Arg
                1525                1530                1535
Gly Asn His Val Ser Pro Thr His Tyr Val Pro Glu Ser Asp Ala Ala
            1540                1545                1550
Ala Arg Val Thr Gln Ile Leu Ser Ser Leu Thr Ile Thr Gln Leu Leu
        1555                1560                1565
Lys Arg Leu His Gln Trp Ile Asn Glu Asp Cys Ser Thr Pro Cys Ser
    1570                1575                1580
Gly Ser Trp Leu Arg Asp Val Trp Asp Trp Ile Cys Thr Val Leu Thr
1585                1590                1595                1600
Asp Phe Lys Thr Trp Leu Gln Ser Lys Leu Leu Pro Gln Leu Pro Gly
                1605                1610                1615
Val Pro Phe Phe Ser Cys Gln Arg Gly Tyr Lys Gly Val Trp Arg Gly
            1620                1625                1630
Asp Gly Ile Met Gln Thr Thr Cys Pro Cys Gly Ala Gln Ile Thr Gly
        1635                1640                1645
His Val Lys Asn Gly Ser Met Arg Ile Val Gly Pro Lys Thr Cys Ser
    1650                1655                1660
Asn Thr Trp His Gly Thr Phe Pro Ile Asn Ala Tyr Thr Thr Gly Pro
1665                1670                1675                1680
Cys Thr Pro Ser Pro Ala Pro Asn Tyr Ser Arg Ala Leu Trp Arg Val
                1685                1690                1695
Ala Ala Glu Glu Tyr Val Glu Val Thr Arg Val Gly Asp Phe His Tyr
            1700                1705                1710
Val Thr Gly Met Thr Thr Asp Asn Val Lys Cys Pro Cys Gln Val Pro
        1715                1720                1725
Ala Pro Glu Phe Phe Ser Glu Val Asp Gly Val Arg Leu His Arg Tyr
    1730                1735                1740
Ala Pro Ala Cys Arg Pro Leu Leu Arg Glu Glu Val Thr Phe Gln Val
1745                1750                1755                1760
Gly Leu Asn Gln Tyr Leu Val Gly Ser Gln Leu Pro Cys Glu Pro Glu
                1765                1770                1775
Pro Asp Val Ala Val Leu Thr Ser Met Leu Thr Asp Pro Ser His Ile
            1780                1785                1790
Thr Ala Glu Thr Ala Lys Arg Arg Leu Ala Arg Gly Ser Pro Pro Ser
        1795                1800                1805
Leu Ala Ser Ser Ser Ala Ser Gln Leu Ser Ala Pro Ser Leu Lys Ala
    1810                1815                1820
Thr Cys Thr Thr His His Val Ser Pro Asp Ala Asp Leu Ile Glu Ala
1825                1830                1835                1840
Asn Leu Leu Trp Arg Gln Glu Met Gly Gly Asn Ile Thr Arg Val Glu
                1845                1850                1855
Ser Glu Asn Lys Val Val Val Leu Asp Ser Phe Asp Pro Leu Arg Ala
            1860                1865                1870
Glu Glu Asp Glu Arg Glu Val Ser Val Pro Ala Glu Ile Leu Arg Lys
        1875                1880                1885
Ser Lys Lys Phe Pro Ala Ala Met Pro Ile Trp Ala Arg Pro Asp Tyr
    1890                1895                1900
Asn Pro Pro Leu Leu Glu Ser Trp Lys Asp Pro Asp Tyr Val Pro Pro
1905                1910                1915                1920
Val Val His Gly Cys Pro Leu Pro Pro Ile Lys Ala Pro Pro Ile Pro
                1925                1930                1935
Pro Pro Arg Arg Lys Arg Thr Val Val Leu Thr Glu Ser Ser Val Ser
            1940                1945                1950
Ser Ala Leu Ala Glu Leu Ala Thr Lys Thr Phe Gly Ser Ser Glu Ser
        1955                1960                1965
Ser Ala Val Asp Ser Gly Thr Ala Thr Ala Leu Pro Asp Gln Ala Ser
    1970                1975                1980
Asp Asp Gly Asp Lys Gly Ser Asp Val Glu Ser Tyr Ser Ser Met Pro
1985                1990                1995                2000
Pro Leu Glu Gly Glu Pro Gly Asp Pro Asp Leu Ser Asp Gly Ser Trp
                2005                2010                2015
Ser Thr Val Ser Glu Glu Ala Ser Glu Asp Val Val Cys Cys Ser Met
            2020                2025                2030
Ser Tyr Thr Trp Thr Gly Ala Leu Ile Thr Pro Cys Ala Ala Glu Glu
        2035                2040                2045
Ser Lys Leu Pro Ile Asn Ala Leu Ser Asn Ser Leu Leu Arg His His
    2050                2055                2060
Asn Met Val Tyr Ala Thr Thr Ser Arg Ser Ala Gly Leu Arg Gln Lys
2065                2070                2075                2080
Lys Val Thr Phe Asp Arg Leu Gln Val Leu Asp Asp His Tyr Arg Asp
                2085                2090                2095
Val Leu Lys Glu Met Lys Ala Lys Ala Ser Thr Val Lys Ala Lys Leu
            2100                2105                2110
Leu Ser Val Glu Glu Ala Cys Lys Leu Thr Pro Pro His Ser Ala Lys
        2115                2120                2125
Ser Lys Phe Gly Tyr Gly Ala Lys Asp Val Arg Asn Leu Ser Ser Lys
    2130                2135                2140
Ala Val Asn His Ile His Ser Val Trp Lys Asp Leu Leu Glu Asp Thr
2145                2150                2155                2160
Val Thr Pro Ile Asp Thr Thr Ile Met Ala Lys Asn Glu Val Phe Cys
                2165                2170                2175
Val Gln Pro Glu Lys Gly Gly Arg Lys Pro Ala Arg Leu Ile Val Phe
            2180                2185                2190
Pro Asp Leu Gly Val Arg Val Cys Glu Lys Met Ala Leu Tyr Asp Val
        2195                2200                2205
Val Ser Thr Leu Pro Gln Val Val Met Gly Ser Ser Tyr Gly Phe Gln
    2210                2215                2220
Tyr Ser Pro Gly Gln Arg Val Glu Phe Leu Val Asn Thr Trp Lys Ser
2225                2230                2235                2240
Lys Lys Asn Pro Met Gly Phe Ser Tyr Asp Thr Arg Cys Phe Asp Ser
                2245                2250                2255
Thr Val Thr Glu Asn Asp Ile Arg Val Glu Glu Ser Ile Tyr Gln Cys
            2260                2265                2270
Cys Asp Leu Ala Pro Glu Ala Arg Gln Ala Ile Lys Ser Leu Thr Glu
        2275                2280                2285
Arg Leu Tyr Ile Gly Gly Pro Leu Thr Asn Ser Lys Gly Gln Asn Cys
    2290                2295                2300
Gly Tyr Arg Arg Cys Arg Ala Ser Gly Val Leu Thr Thr Ser Cys Gly
2305                2310                2315                2320
Asn Thr Leu Thr Cys Tyr Leu Lys Ala Ser Ala Ala Cys Arg Ala Ala
                2325                2330                2335
Lys Leu Gln Asp Cys Thr Met Leu Val Asn Gly Asp Asp Leu Val Val
            2340                2345                2350
Ile Cys Glu Ser Ala Gly Thr Gln Glu Asp Ala Ala Ser Leu Arg Val
        2355                2360                2365
Phe Thr Glu Ala Met Thr Arg Tyr Ser Ala Pro Pro Gly Asp Pro Pro
    2370                2375                2380
Gln Pro Glu Tyr Asp Leu Glu Leu Ile Thr Ser Cys Ser Ser Asn Val
2385                2390                2395                2400
Ser Val Ala His Asp Ala Ser Gly Lys Arg Val Tyr Tyr Leu Thr Arg
                2405                2410                2415
Asp Pro Thr Thr Pro Leu Ala Arg Ala Ala Trp Glu Thr Ala Arg His
            2420                2425                2430
Thr Pro Val Asn Ser Trp Leu Gly Asn Ile Ile Met Tyr Ala Pro Thr
        2435                2440                2445
Leu Trp Ala Arg Met Ile Leu Met Thr His Phe Phe Ser Ile Leu Leu
    2450                2455                2460
Ala Gln Glu Gln Leu Glu Lys Ala Leu Asp Cys Gln Ile Tyr Gly Ala
2465                2470                2475                2480
Cys Tyr Ser Ile Glu Pro Leu Asp Leu Pro Gln Ile Ile Glu Arg Leu
                2485                2490                2495
His Gly Leu Ser Ala Phe Ser Leu His Ser Tyr Ser Pro Gly Glu Ile
            2500                2505                2510
Asn Arg Val Ala Ser Cys Leu Arg Lys Leu Gly Val Pro Pro Leu Arg
        2515                2520                2525
Val Trp Arg His Arg Ala Arg Ser Val Arg Ala Arg Leu Leu Ser Gln
    2530                2535                2540
Gly Gly Arg Ala Ala Thr Cys Gly Lys Tyr Leu Phe Asn Trp Ala Val
2545                2550                2555                2560
Lys Thr Lys Leu Lys Leu Thr Pro Ile Pro Ala Ala Ser Arg Leu Asp
                2565                2570                2575
Leu Ser Gly Trp Phe Val Ala Gly Tyr Ser Gly Gly Asp Ile Tyr His
            2580                2585                2590
Ser Leu Ser Arg Ala Arg Pro Arg Trp Phe Met Leu Cys Leu Leu Leu
        2595                2600                2605
Leu Ser Val Gly Val Gly Ile Tyr Leu Leu Pro Asn
    2610                2615                2620 
           
           
             
               1020 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..1020 
                /note “sequence = 1500 - 2519 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..1020 
             
             33
GGG GCG CAA GCC AAA ACC ACC AAC AGG CTC GTG TCC ATG TTC GCA AGT       48
Gly Ala Gln Ala Lys Thr Thr Asn Arg Leu Val Ser Met Phe Ala Ser
  1               5                  10                  15
GGG CCG TCT CAG AAA ATC CAG CTT ATA AAC ACC AAT GGG AGT TGG CAC       96
Gly Pro Ser Gln Lys Ile Gln Leu Ile Asn Thr Asn Gly Ser Trp His
             20                  25                  30
ATC AAC AGG ACT GCC CTG AAC TGC AAT GAC TCT CTC CAG ACT GGG TTT      144
Ile Asn Arg Thr Ala Leu Asn Cys Asn Asp Ser Leu Gln Thr Gly Phe
         35                  40                  45
CTT GCC GCG CTG TTC TAC ACA CAT AGT TTC AAC TCG TCC GGG TGC CCA      192
Leu Ala Ala Leu Phe Tyr Thr His Ser Phe Asn Ser Ser Gly Cys Pro
     50                  55                  60
GAG CGC ATG GCC CAG TGC CGC ACC ATT GAC AAG TTC GAC CAG GGA TGG      240
Glu Arg Met Ala Gln Cys Arg Thr Ile Asp Lys Phe Asp Gln Gly Trp
 65                  70                  75                  80
GGT CCC ATT ACT TAT GCT GAG TCT AGC AGA TCA GAC CAG AGG CCA TAT      288
Gly Pro Ile Thr Tyr Ala Glu Ser Ser Arg Ser Asp Gln Arg Pro Tyr
                 85                  90                  95
TGC TGG CAC TAC CCA CCT CCA CAA TGT ACC ATC GTA CCT GCG TCG GAG      336
Cys Trp His Tyr Pro Pro Pro Gln Cys Thr Ile Val Pro Ala Ser Glu
            100                 105                 110
GTG TGC GGC CCA GTG TAC TGC TTC ACC CCA AGC CCT GTC GTC GTG GGG      384
Val Cys Gly Pro Val Tyr Cys Phe Thr Pro Ser Pro Val Val Val Gly
        115                 120                 125
ACG ACC GAT CGT TTC GGT GTC CCT ACG TAT AGA TGG GGG GAG AAC GAG      432
Thr Thr Asp Arg Phe Gly Val Pro Thr Tyr Arg Trp Gly Glu Asn Glu
    130                 135                 140
ACT GAC GTG CTG CTG CTC AAC AAC ACG CGG CCG CCG CAA GGC AAC TGG      480
Thr Asp Val Leu Leu Leu Asn Asn Thr Arg Pro Pro Gln Gly Asn Trp
145                 150                 155                 160
TTC GGC TGC ACA TGG ATG AAT AGC ACC GGG TTC ACC AAG ACA TGT GGG      528
Phe Gly Cys Thr Trp Met Asn Ser Thr Gly Phe Thr Lys Thr Cys Gly
                165                 170                 175
GGG CCC CCG TGT AAC ATC GGG GGG GTC GGC AAC AAC ACC CTG ACC TGC      576
Gly Pro Pro Cys Asn Ile Gly Gly Val Gly Asn Asn Thr Leu Thr Cys
            180                 185                 190
CCC ACG GAC TGC TTC CGG AAG CAC CCC GAG GCT ACC TAC ACA AAA TGT      624
Pro Thr Asp Cys Phe Arg Lys His Pro Glu Ala Thr Tyr Thr Lys Cys
        195                 200                 205
GGT TCG GGG CCT TGG CTG ACA CCT AGG TGC ATG GTT GAC TAT CCA TAC      672
Gly Ser Gly Pro Trp Leu Thr Pro Arg Cys Met Val Asp Tyr Pro Tyr
    210                 215                 220
AGG CTC TGG CAT TAC CCC TGC ACT GTT AAC TTT ACC ATC TTC AAG GTT      720
Arg Leu Trp His Tyr Pro Cys Thr Val Asn Phe Thr Ile Phe Lys Val
225                 230                 235                 240
AGG ATG TAT GTG GGG GGG GTG GAG CAC AGG CTC AAT GCT GCA TGC AAT      768
Arg Met Tyr Val Gly Gly Val Glu His Arg Leu Asn Ala Ala Cys Asn
                245                 250                 255
TGG ACC CGA GGA GAG CGT TGT GAC TTG GAG GAC AGG GAT AGG CCG GAG      816
Trp Thr Arg Gly Glu Arg Cys Asp Leu Glu Asp Arg Asp Arg Pro Glu
            260                 265                 270
CTC AGC CCG CTG CTG CTG TCT ACA ACA GAG TGG CAG GTA CTG CCC TGT      864
Leu Ser Pro Leu Leu Leu Ser Thr Thr Glu Trp Gln Val Leu Pro Cys
        275                 280                 285
TCC TTC ACC ACC CTA CCA GCT CTG TCC ACT GGC TTG ATT CAC CTC CAT      912
Ser Phe Thr Thr Leu Pro Ala Leu Ser Thr Gly Leu Ile His Leu His
    290                 295                 300
CAG AAC ATC GTG GAC GTG CAA TAC CTA TAC GGT ATA GGG TCA GCG GTT      960
Gln Asn Ile Val Asp Val Gln Tyr Leu Tyr Gly Ile Gly Ser Ala Val
305                 310                 315                 320
GTC TCC TTT GCA ATC AAA TGG GAG TAT GTC CTG TTG CTT TTC CTT CTC     1008
Val Ser Phe Ala Ile Lys Trp Glu Tyr Val Leu Leu Leu Phe Leu Leu
                325                 330                 335
CTA GCG GAC GCA                                                     1020
Leu Ala Asp Ala
            340 
           
           
             
               340 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             34
Gly Ala Gln Ala Lys Thr Thr Asn Arg Leu Val Ser Met Phe Ala Ser
  1               5                  10                  15
Gly Pro Ser Gln Lys Ile Gln Leu Ile Asn Thr Asn Gly Ser Trp His
             20                  25                  30
Ile Asn Arg Thr Ala Leu Asn Cys Asn Asp Ser Leu Gln Thr Gly Phe
         35                  40                  45
Leu Ala Ala Leu Phe Tyr Thr His Ser Phe Asn Ser Ser Gly Cys Pro
     50                  55                  60
Glu Arg Met Ala Gln Cys Arg Thr Ile Asp Lys Phe Asp Gln Gly Trp
 65                  70                  75                  80
Gly Pro Ile Thr Tyr Ala Glu Ser Ser Arg Ser Asp Gln Arg Pro Tyr
                 85                  90                  95
Cys Trp His Tyr Pro Pro Pro Gln Cys Thr Ile Val Pro Ala Ser Glu
            100                 105                 110
Val Cys Gly Pro Val Tyr Cys Phe Thr Pro Ser Pro Val Val Val Gly
        115                 120                 125
Thr Thr Asp Arg Phe Gly Val Pro Thr Tyr Arg Trp Gly Glu Asn Glu
    130                 135                 140
Thr Asp Val Leu Leu Leu Asn Asn Thr Arg Pro Pro Gln Gly Asn Trp
145                 150                 155                 160
Phe Gly Cys Thr Trp Met Asn Ser Thr Gly Phe Thr Lys Thr Cys Gly
                165                 170                 175
Gly Pro Pro Cys Asn Ile Gly Gly Val Gly Asn Asn Thr Leu Thr Cys
            180                 185                 190
Pro Thr Asp Cys Phe Arg Lys His Pro Glu Ala Thr Tyr Thr Lys Cys
        195                 200                 205
Gly Ser Gly Pro Trp Leu Thr Pro Arg Cys Met Val Asp Tyr Pro Tyr
    210                 215                 220
Arg Leu Trp His Tyr Pro Cys Thr Val Asn Phe Thr Ile Phe Lys Val
225                 230                 235                 240
Arg Met Tyr Val Gly Gly Val Glu His Arg Leu Asn Ala Ala Cys Asn
                245                 250                 255
Trp Thr Arg Gly Glu Arg Cys Asp Leu Glu Asp Arg Asp Arg Pro Glu
            260                 265                 270
Leu Ser Pro Leu Leu Leu Ser Thr Thr Glu Trp Gln Val Leu Pro Cys
        275                 280                 285
Ser Phe Thr Thr Leu Pro Ala Leu Ser Thr Gly Leu Ile His Leu His
    290                 295                 300
Gln Asn Ile Val Asp Val Gln Tyr Leu Tyr Gly Ile Gly Ser Ala Val
305                 310                 315                 320
Val Ser Phe Ala Ile Lys Trp Glu Tyr Val Leu Leu Leu Phe Leu Leu
                325                 330                 335
Leu Ala Asp Ala
            340 
           
           
             
               7863 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               CDS 
                1..7863 
             
             
               misc_feature 
                1..7863 
                /note= “sequence = 1500 - 9362 of
              SEQ ID NO 1” 
             
             35
GGG GCG CAA GCC AAA ACC ACC AAC AGG CTC GTG TCC ATG TTC GCA AGT       48
Gly Ala Gln Ala Lys Thr Thr Asn Arg Leu Val Ser Met Phe Ala Ser
  1               5                  10                  15
GGG CCG TCT CAG AAA ATC CAG CTT ATA AAC ACC AAT GGG AGT TGG CAC       96
Gly Pro Ser Gln Lys Ile Gln Leu Ile Asn Thr Asn Gly Ser Trp His
             20                  25                  30
ATC AAC AGG ACT GCC CTG AAC TGC AAT GAC TCT CTC CAG ACT GGG TTT      144
Ile Asn Arg Thr Ala Leu Asn Cys Asn Asp Ser Leu Gln Thr Gly Phe
         35                  40                  45
CTT GCC GCG CTG TTC TAC ACA CAT AGT TTC AAC TCG TCC GGG TGC CCA      192
Leu Ala Ala Leu Phe Tyr Thr His Ser Phe Asn Ser Ser Gly Cys Pro
     50                  55                  60
GAG CGC ATG GCC CAG TGC CGC ACC ATT GAC AAG TTC GAC CAG GGA TGG      240
Glu Arg Met Ala Gln Cys Arg Thr Ile Asp Lys Phe Asp Gln Gly Trp
 65                  70                  75                  80
GGT CCC ATT ACT TAT GCT GAG TCT AGC AGA TCA GAC CAG AGG CCA TAT      288
Gly Pro Ile Thr Tyr Ala Glu Ser Ser Arg Ser Asp Gln Arg Pro Tyr
                 85                  90                  95
TGC TGG CAC TAC CCA CCT CCA CAA TGT ACC ATC GTA CCT GCG TCG GAG      336
Cys Trp His Tyr Pro Pro Pro Gln Cys Thr Ile Val Pro Ala Ser Glu
            100                 105                 110
GTG TGC GGC CCA GTG TAC TGC TTC ACC CCA AGC CCT GTC GTC GTG GGG      384
Val Cys Gly Pro Val Tyr Cys Phe Thr Pro Ser Pro Val Val Val Gly
        115                 120                 125
ACG ACC GAT CGT TTC GGT GTC CCT ACG TAT AGA TGG GGG GAG AAC GAG      432
Thr Thr Asp Arg Phe Gly Val Pro Thr Tyr Arg Trp Gly Glu Asn Glu
    130                 135                 140
ACT GAC GTG CTG CTG CTC AAC AAC ACG CGG CCG CCG CAA GGC AAC TGG      480
Thr Asp Val Leu Leu Leu Asn Asn Thr Arg Pro Pro Gln Gly Asn Trp
145                 150                 155                 160
TTC GGC TGC ACA TGG ATG AAT AGC ACC GGG TTC ACC AAG ACA TGT GGG      528
Phe Gly Cys Thr Trp Met Asn Ser Thr Gly Phe Thr Lys Thr Cys Gly
                165                 170                 175
GGG CCC CCG TGT AAC ATC GGG GGG GTC GGC AAC AAC ACC CTG ACC TGC      576
Gly Pro Pro Cys Asn Ile Gly Gly Val Gly Asn Asn Thr Leu Thr Cys
            180                 185                 190
CCC ACG GAC TGC TTC CGG AAG CAC CCC GAG GCT ACC TAC ACA AAA TGT      624
Pro Thr Asp Cys Phe Arg Lys His Pro Glu Ala Thr Tyr Thr Lys Cys
        195                 200                 205
GGT TCG GGG CCT TGG CTG ACA CCT AGG TGC ATG GTT GAC TAT CCA TAC      672
Gly Ser Gly Pro Trp Leu Thr Pro Arg Cys Met Val Asp Tyr Pro Tyr
    210                 215                 220
AGG CTC TGG CAT TAC CCC TGC ACT GTT AAC TTT ACC ATC TTC AAG GTT      720
Arg Leu Trp His Tyr Pro Cys Thr Val Asn Phe Thr Ile Phe Lys Val
225                 230                 235                 240
AGG ATG TAT GTG GGG GGG GTG GAG CAC AGG CTC AAT GCT GCA TGC AAT      768
Arg Met Tyr Val Gly Gly Val Glu His Arg Leu Asn Ala Ala Cys Asn
                245                 250                 255
TGG ACC CGA GGA GAG CGT TGT GAC TTG GAG GAC AGG GAT AGG CCG GAG      816
Trp Thr Arg Gly Glu Arg Cys Asp Leu Glu Asp Arg Asp Arg Pro Glu
            260                 265                 270
CTC AGC CCG CTG CTG CTG TCT ACA ACA GAG TGG CAG GTA CTG CCC TGT      864
Leu Ser Pro Leu Leu Leu Ser Thr Thr Glu Trp Gln Val Leu Pro Cys
        275                 280                 285
TCC TTC ACC ACC CTA CCA GCT CTG TCC ACT GGC TTG ATT CAC CTC CAT      912
Ser Phe Thr Thr Leu Pro Ala Leu Ser Thr Gly Leu Ile His Leu His
    290                 295                 300
CAG AAC ATC GTG GAC GTG CAA TAC CTA TAC GGT ATA GGG TCA GCG GTT      960
Gln Asn Ile Val Asp Val Gln Tyr Leu Tyr Gly Ile Gly Ser Ala Val
305                 310                 315                 320
GTC TCC TTT GCA ATC AAA TGG GAG TAT GTC CTG TTG CTT TTC CTT CTC     1008
Val Ser Phe Ala Ile Lys Trp Glu Tyr Val Leu Leu Leu Phe Leu Leu
                325                 330                 335
CTA GCG GAC GCA CGT GTC TGT GCC TGC TTG TGG ATG ATG CTG CTG ATA     1056
Leu Ala Asp Ala Arg Val Cys Ala Cys Leu Trp Met Met Leu Leu Ile
            340                 345                 350
GCC CAG GCC GAG GCC GCC TTG GAG AAC CTG GTG GTC CTC AAT TCG GCG     1104
Ala Gln Ala Glu Ala Ala Leu Glu Asn Leu Val Val Leu Asn Ser Ala
        355                 360                 365
TCT GTG GCC GGC GCA CAT GGC ATC CTC TCC TTC CTT GTG TTC TTC TGT     1152
Ser Val Ala Gly Ala His Gly Ile Leu Ser Phe Leu Val Phe Phe Cys
    370                 375                 380
GCC GCC TGG TAC ATC AAA GGC AGG CTG GTC CCT GGG GCG ACA TAT GCT     1200
Ala Ala Trp Tyr Ile Lys Gly Arg Leu Val Pro Gly Ala Thr Tyr Ala
385                 390                 395                 400
CTT TAT GGC GTG TGG CCG CTG CTC CTG CTC TTG CTG GCA TTA CCA CCG     1248
Leu Tyr Gly Val Trp Pro Leu Leu Leu Leu Leu Leu Ala Leu Pro Pro
                405                 410                 415
CGA GCT TAC GCC ATG GAC CGG GAG ATG GCT GCA TCG TGC GGA GGC GCG     1296
Arg Ala Tyr Ala Met Asp Arg Glu Met Ala Ala Ser Cys Gly Gly Ala
            420                 425                 430
GTT TTT GTG GGT CTG GTA CTC CTG ACT TTG TCA CCA TAC TAC AAG GTG     1344
Val Phe Val Gly Leu Val Leu Leu Thr Leu Ser Pro Tyr Tyr Lys Val
        435                 440                 445
TTC CTC GCT AGG CTC ATA TGG TGG TTA CAA TAT TTT ACC ACC AGA GCC     1392
Phe Leu Ala Arg Leu Ile Trp Trp Leu Gln Tyr Phe Thr Thr Arg Ala
    450                 455                 460
GAG GCG GAC TTA CAT GTG TGG ATC CCC CCC CTC AAC GCT CGG GGA GGC     1440
Glu Ala Asp Leu His Val Trp Ile Pro Pro Leu Asn Ala Arg Gly Gly
465                 470                 475                 480
CGC GAT GCC ATC ATC CTC CTC ATG TGC GCA GTC CAT CCA GAG CTA ATC     1488
Arg Asp Ala Ile Ile Leu Leu Met Cys Ala Val His Pro Glu Leu Ile
                485                 490                 495
TTT GAC ATC ACC AAA CTT CTA ATT GCC ATA CTC GGT CCG CTC ATG GTG     1536
Phe Asp Ile Thr Lys Leu Leu Ile Ala Ile Leu Gly Pro Leu Met Val
            500                 505                 510
CTC CAA GCT GGC ATA ACC AGA GTG CCG TAC TTC GTG CGC GCT CAA GGG     1584
Leu Gln Ala Gly Ile Thr Arg Val Pro Tyr Phe Val Arg Ala Gln Gly
        515                 520                 525
CTC ATT CAT GCA TGC ATG TTA GTG CGG AAG GTC GCT GGG GGT CAT TAT     1632
Leu Ile His Ala Cys Met Leu Val Arg Lys Val Ala Gly Gly His Tyr
    530                 535                 540
GTC CAA ATG GCC TTC ATG AAG CTG GGC GCG CTG ACA GGC ACG TAC ATT     1680
Val Gln Met Ala Phe Met Lys Leu Gly Ala Leu Thr Gly Thr Tyr Ile
545                 550                 555                 560
TAC AAC CAT CTT ACC CCG CTA CGG GAT TGG CCA CGC GCG GGC CTA CGA     1728
Tyr Asn His Leu Thr Pro Leu Arg Asp Trp Pro Arg Ala Gly Leu Arg
                565                 570                 575
GAC CTT GCG GTG GCA GTG GAG CCC GTC GTC TTC TCC GAC ATG GAG ACC     1776
Asp Leu Ala Val Ala Val Glu Pro Val Val Phe Ser Asp Met Glu Thr
            580                 585                 590
AAG ATC ATC ACC TGG GGA GCA GAC ACC GCG GCG TGT GGG GAC ATC ATC     1824
Lys Ile Ile Thr Trp Gly Ala Asp Thr Ala Ala Cys Gly Asp Ile Ile
        595                 600                 605
TTG GGT CTG CCC GTC TCC GCC CGA AGG GGA AAG GAG ATA CTC CTG GGC     1872
Leu Gly Leu Pro Val Ser Ala Arg Arg Gly Lys Glu Ile Leu Leu Gly
    610                 615                 620
CCG GCC GAT AGT CTT GAA GGG CGG GGG TTG CGA CTC CTC GCG CCC ATC     1920
Pro Ala Asp Ser Leu Glu Gly Arg Gly Leu Arg Leu Leu Ala Pro Ile
625                 630                 635                 640
ACG GCC TAC TCC CAA CAG ACG CGG GGC CTA CTT GGT TGC ATC ATC ACT     1968
Thr Ala Tyr Ser Gln Gln Thr Arg Gly Leu Leu Gly Cys Ile Ile Thr
                645                 650                 655
AGC CTT ACA GGC CGG GAC AAG AAC CAG GTC GAG GGA GAG GTT CAG GTG     2016
Ser Leu Thr Gly Arg Asp Lys Asn Gln Val Glu Gly Glu Val Gln Val
            660                 665                 670
GTT TCC ACC GCA ACA CAA TCC TTC CTG GCG ACC TGC GTC AAC GGC GTG     2064
Val Ser Thr Ala Thr Gln Ser Phe Leu Ala Thr Cys Val Asn Gly Val
        675                 680                 685
TGT TGG ACC GTT TAC CAT GGT GCT GGC TCA AAG ACC TTA GCC GCG CCA     2112
Cys Trp Thr Val Tyr His Gly Ala Gly Ser Lys Thr Leu Ala Ala Pro
    690                 695                 700
AAG GGG CCA ATC ACC CAG ATG TAC ACT AAT GTG GAC CAG GAC CTC GTC     2160
Lys Gly Pro Ile Thr Gln Met Tyr Thr Asn Val Asp Gln Asp Leu Val
705                 710                 715                 720
GGC TGG CCC AAG CCC CCC GGG GCG CGT TCC TTG ACA CCA TGC ACC TGT     2208
Gly Trp Pro Lys Pro Pro Gly Ala Arg Ser Leu Thr Pro Cys Thr Cys
                725                 730                 735
GGC AGC TCA GAC CTT TAC TTG GTC ACG AGA CAT GCT GAC GTC ATT CCG     2256
Gly Ser Ser Asp Leu Tyr Leu Val Thr Arg His Ala Asp Val Ile Pro
            740                 745                 750
GTG CGC CGG CGG GGC GAC AGT AGG GGG AGC CTG CTC TCC CCC AGG CCT     2304
Val Arg Arg Arg Gly Asp Ser Arg Gly Ser Leu Leu Ser Pro Arg Pro
        755                 760                 765
GTC TCC TAC TTG AAG GGC TCT TCG GGT GGT CCA CTG CTC TGC CCC TTC     2352
Val Ser Tyr Leu Lys Gly Ser Ser Gly Gly Pro Leu Leu Cys Pro Phe
    770                 775                 780
GGG CAC GCT GTG GGC ATC TTC CGG GCT GCC GTA TGC ACC CGG GGG GTT     2400
Gly His Ala Val Gly Ile Phe Arg Ala Ala Val Cys Thr Arg Gly Val
785                 790                 795                 800
GCG AAG GCG GTG GAC TTT GTG CCC GTA GAG TCC ATG GAA ACT ACT ATG     2448
Ala Lys Ala Val Asp Phe Val Pro Val Glu Ser Met Glu Thr Thr Met
                805                 810                 815
CGG TCT CCG GTC TTC ACG GAC AAC TCA TCC CCC CCG GCC GTA CCG CAG     2496
Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro Pro Ala Val Pro Gln
            820                 825                 830
TCA TTT CAA GTG GCC CAC CTA CAC GCT CCC ACT GGC AGC GGC AAG AGT     2544
Ser Phe Gln Val Ala His Leu His Ala Pro Thr Gly Ser Gly Lys Ser
        835                 840                 845
ACT AAA GTG CCG GCT GCA TAT GCA GCC CAA GGG TAC AAG GTG CTC GTC     2592
Thr Lys Val Pro Ala Ala Tyr Ala Ala Gln Gly Tyr Lys Val Leu Val
    850                 855                 860
CTC AAT CCG TCC GTT GCC GCT ACC TTA GGG TTT GGG GCG TAT ATG TCT     2640
Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe Gly Ala Tyr Met Ser
865                 870                 875                 880
AAG GCA CAC GGT ATT GAC CCC AAC ATC AGA ACT GGG GTA AGG ACC ATT     2688
Lys Ala His Gly Ile Asp Pro Asn Ile Arg Thr Gly Val Arg Thr Ile
                885                 890                 895
ACC ACA GGC GCC CCC GTC ACA TAC TCT ACC TAT GGC AAG TTT CTT GCC     2736
Thr Thr Gly Ala Pro Val Thr Tyr Ser Thr Tyr Gly Lys Phe Leu Ala
            900                 905                 910
GAT GGT GGT TGC TCT GGG GGC GCT TAT GAC ATC ATA ATA TGT GAT GAG     2784
Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp Ile Ile Ile Cys Asp Glu
        915                 920                 925
TGC CAT TCA ACT GAC TCG ACT ACA ATC TTG GGC ATC GGC ACA GTC CTG     2832
Cys His Ser Thr Asp Ser Thr Thr Ile Leu Gly Ile Gly Thr Val Leu
    930                 935                 940
GAC CAA GCG GAG ACG GCT GGA GCG CGG CTT GTC GTG CTC GCC ACC GCT     2880
Asp Gln Ala Glu Thr Ala Gly Ala Arg Leu Val Val Leu Ala Thr Ala
945                 950                 955                 960
ACG CCT CCG GGA TCG GTC ACC GTG CCA CAC CCA AAC ATC GAG GAG GTG     2928
Thr Pro Pro Gly Ser Val Thr Val Pro His Pro Asn Ile Glu Glu Val
                965                 970                 975
GCC CTG TCT AAT ACT GGA GAG ATC CCC TTC TAT GGC AAA GCC ATC CCC     2976
Ala Leu Ser Asn Thr Gly Glu Ile Pro Phe Tyr Gly Lys Ala Ile Pro
            980                 985                 990
ATT GAA GCC ATC AGG GGG GGA AGG CAT CTC ATT TTC TGT CAT TCC AAG     3024
Ile Glu Ala Ile Arg Gly Gly Arg His Leu Ile Phe Cys His Ser Lys
        995                 1000                1005
AAG AAG TGC GAC GAG CTC GCC GCA AAG CTG TCA GGC CTC GGA ATC AAC     3072
Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Ser Gly Leu Gly Ile Asn
    1010                1015                1020
GCT GTG GCG TAT TAC CGG GGG CTC GAT GTG TCC GTC ATA CCA ACT ATC     3120
Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser Val Ile Pro Thr Ile
1025                1030                1035                1040
GGA GAC GTC GTT GTC GTG GCA ACA GAC GCT CTG ATG ACG GGC TAT ACG     3168
Gly Asp Val Val Val Val Ala Thr Asp Ala Leu Met Thr Gly Tyr Thr
                1045                1050                1055
GGC GAC TTT GAC TCA GTG ATC GAC TGT AAC ACA TGT GTC ACC CAG ACA     3216
Gly Asp Phe Asp Ser Val Ile Asp Cys Asn Thr Cys Val Thr Gln Thr
            1060                1065                1070
GTC GAC TTC AGC TTG GAT CCC ACC TTC ACC ATT GAG ACG ACG ACC GTG     3264
Val Asp Phe Ser Leu Asp Pro Thr Phe Thr Ile Glu Thr Thr Thr Val
        1075                1080                1085
CCT CAA GAC GCA GTG TCG CGC TCG CAG CGG CGG GGT AGG ACT GGC AGG     3312
Pro Gln Asp Ala Val Ser Arg Ser Gln Arg Arg Gly Arg Thr Gly Arg
    1090                1095                1100
GGT AGG AGA GGC ATC TAC AGG TTT GTG ACT CCG GGA GAA CGG CCC TCG     3360
Gly Arg Arg Gly Ile Tyr Arg Phe Val Thr Pro Gly Glu Arg Pro Ser
1105                1110                1115                1120
GGC ATG TTC GAT TCC TCG GTC CTG TGT GAG TGC TAT GAC GCG GGC TGT     3408
Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys Tyr Asp Ala Gly Cys
                1125                1130                1135
GCT TGG TAC GAG CTC ACC CCG GCC GAG ACC TCG GTT AGG TTG CGG GCC     3456
Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Ser Val Arg Leu Arg Ala
            1140                1145                1150
TAC CTG AAC ACA CCA GGG TTG CCC GTT TGC CAG GAC CAC CTG GAG TTC     3504
Tyr Leu Asn Thr Pro Gly Leu Pro Val Cys Gln Asp His Leu Glu Phe
        1155                1160                1165
TGG GAG AGT GTC TTC ACA GGC CTC ACC CAT ATA GAT GCA CAC TTC TTG     3552
Trp Glu Ser Val Phe Thr Gly Leu Thr His Ile Asp Ala His Phe Leu
    1170                1175                1180
TCC CAG ACC AAG CAG GCA GGA GAC AAC TTC CCC TAC CTG GTA GCA TAC     3600
Ser Gln Thr Lys Gln Ala Gly Asp Asn Phe Pro Tyr Leu Val Ala Tyr
1185                1190                1195                1200
CAA GCC ACG GTG TGC GCC AGG GCT CAG GCC CCA CCT CCA TCA TGG GAT     3648
Gln Ala Thr Val Cys Ala Arg Ala Gln Ala Pro Pro Pro Ser Trp Asp
                1205                1210                1215
CAA ATG TGG AAG TGT CTC ATA CGG CTG AAA CCT ACG CTG CAC GGG CCA     3696
Gln Met Trp Lys Cys Leu Ile Arg Leu Lys Pro Thr Leu His Gly Pro
            1220                1225                1230
ACA CCC TTG CTG TAC AGG CTG GGA GCC GTC CAG AAT GAG GTC ACC CTC     3744
Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gln Asn Glu Val Thr Leu
        1235                1240                1245
ACC CAC CCC ATA ACC AAA TAC ATC ATG GCA TGC ATG TCG GCT GAC CTG     3792
Thr His Pro Ile Thr Lys Tyr Ile Met Ala Cys Met Ser Ala Asp Leu
    1250                1255                1260
GAG GTC GTC ACT AGC ACC TGG GTG CTG GTG GGC GGA GTC CTT GCA GCT     3840
Glu Val Val Thr Ser Thr Trp Val Leu Val Gly Gly Val Leu Ala Ala
1265                1270                1275                1280
CTG GCC GCG TAT TGC CTG ACA ACA GGC AGT GTG GTC ATT GTG GGT AGG     3888
Leu Ala Ala Tyr Cys Leu Thr Thr Gly Ser Val Val Ile Val Gly Arg
                1285                1290                1295
ATT ATC TTG TCC GGG AGG CCG GCC ATT GTT CCC GAC AGG GAG CTT CTC     3936
Ile Ile Leu Ser Gly Arg Pro Ala Ile Val Pro Asp Arg Glu Leu Leu
            1300                1305                1310
TAC CAG GAG TTC GAT GAA ATG GAA GAG TGC GCC TCG CAC CTC CCT TAC     3984
Tyr Gln Glu Phe Asp Glu Met Glu Glu Cys Ala Ser His Leu Pro Tyr
        1315                1320                1325
ATC GAG CAG GGA ATG CAG CTC GCC GAG CAA TTC AAG CAG AAA GCG CTC     4032
Ile Glu Gln Gly Met Gln Leu Ala Glu Gln Phe Lys Gln Lys Ala Leu
    1330                1335                1340
GGG TTA CTG CAA ACA GCC ACC AAA CAA GCG GAG GCT GCT GCT CCC GTG     4080
Gly Leu Leu Gln Thr Ala Thr Lys Gln Ala Glu Ala Ala Ala Pro Val
1345                1350                1355                1360
GTG GAG TCC AAG TGG CGA GCC CTT GAG ACA TTC TGG GCG AAG CAC ATG     4128
Val Glu Ser Lys Trp Arg Ala Leu Glu Thr Phe Trp Ala Lys His Met
                1365                1370                1375
TGG AAT TTC ATC AGC GGG ATA CAG TAC TTA GCA GGC TTA TCC ACT CTG     4176
Trp Asn Phe Ile Ser Gly Ile Gln Tyr Leu Ala Gly Leu Ser Thr Leu
            1380                1385                1390
CCT GGG AAC CCC GCA ATA GCA TCA TTG ATG GCA TTC ACA GCC TCT ATC     4224
Pro Gly Asn Pro Ala Ile Ala Ser Leu Met Ala Phe Thr Ala Ser Ile
        1395                1400                1405
ACC AGC CCG CTC ACC ACC CAA AGT ACC CTC CTG TTT AAC ATC TTG GGG     4272
Thr Ser Pro Leu Thr Thr Gln Ser Thr Leu Leu Phe Asn Ile Leu Gly
    1410                1415                1420
GGG TGG GTG GCT GCC CAA CTC GCC CCC CCC AGC GCC GCT TCG GCT TTC     4320
Gly Trp Val Ala Ala Gln Leu Ala Pro Pro Ser Ala Ala Ser Ala Phe
1425                1430                1435                1440
GTG GGC GCC GGC ATC GCC GGT GCG GCT GTT GGC AGC ATA GGC CTT GGG     4368
Val Gly Ala Gly Ile Ala Gly Ala Ala Val Gly Ser Ile Gly Leu Gly
                1445                1450                1455
AAG GTG CTT GTG GAC ATT CTG GCG GGT TAT GGA GCA GGA GTG GCC GGC     4416
Lys Val Leu Val Asp Ile Leu Ala Gly Tyr Gly Ala Gly Val Ala Gly
            1460                1465                1470
GCG CTC GTG GCC TTT AAG GTC ATG AGC GGC GAG ATG CCC TCC ACC GAG     4464
Ala Leu Val Ala Phe Lys Val Met Ser Gly Glu Met Pro Ser Thr Glu
        1475                1480                1485
GAC CTG GTC AAT CTA CTT CCT GCC ATC CTC TCT CCT GGC GCC CTG GTC     4512
Asp Leu Val Asn Leu Leu Pro Ala Ile Leu Ser Pro Gly Ala Leu Val
    1490                1495                1500
GTC GGG GTC GTG TGT GCA GCA ATA CTG CGT CGA CAC GTG GGT CCG GGA     4560
Val Gly Val Val Cys Ala Ala Ile Leu Arg Arg His Val Gly Pro Gly
1505                1510                1515                1520
GAG GGG GCT GTG CAG TGG ATG AAC CGG CTG ATA GCG TTC GCC TCG CGG     4608
Glu Gly Ala Val Gln Trp Met Asn Arg Leu Ile Ala Phe Ala Ser Arg
                1525                1530                1535
GGT AAT CAT GTT TCC CCC ACG CAC TAT GTG CCT GAG AGC GAC GCC GCA     4656
Gly Asn His Val Ser Pro Thr His Tyr Val Pro Glu Ser Asp Ala Ala
            1540                1545                1550
GCG CGT GTT ACT CAG ATC CTC TCC AGC CTT ACC ATC ACT CAG CTG CTG     4704
Ala Arg Val Thr Gln Ile Leu Ser Ser Leu Thr Ile Thr Gln Leu Leu
        1555                1560                1565
AAA AGG CTC CAC CAG TGG ATT AAT GAA GAC TGC TCC ACA CCG TGT TCC     4752
Lys Arg Leu His Gln Trp Ile Asn Glu Asp Cys Ser Thr Pro Cys Ser
    1570                1575                1580
GGC TCG TGG CTA AGG GAT GTT TGG GAC TGG ATA TGC ACG GTG TTG ACT     4800
Gly Ser Trp Leu Arg Asp Val Trp Asp Trp Ile Cys Thr Val Leu Thr
1585                1590                1595                1600
GAC TTC AAG ACC TGG CTC CAG TCC AAG CTC CTG CCG CAG CTA CCT GGA     4848
Asp Phe Lys Thr Trp Leu Gln Ser Lys Leu Leu Pro Gln Leu Pro Gly
                1605                1610                1615
GTC CCT TTT TTC TCG TGC CAA CGC GGG TAC AAG GGA GTC TGG CGG GGA     4896
Val Pro Phe Phe Ser Cys Gln Arg Gly Tyr Lys Gly Val Trp Arg Gly
            1620                1625                1630
GAC GGC ATC ATG CAA ACC ACC TGC CCA TGT GGA GCA CAG ATC ACC GGA     4944
Asp Gly Ile Met Gln Thr Thr Cys Pro Cys Gly Ala Gln Ile Thr Gly
        1635                1640                1645
CAT GTC AAA AAC GGT TCC ATG AGG ATC GTC GGG CCT AAG ACC TGC AGC     4992
His Val Lys Asn Gly Ser Met Arg Ile Val Gly Pro Lys Thr Cys Ser
    1650                1655                1660
AAC ACG TGG CAT GGA ACA TTC CCC ATC AAC GCA TAC ACC ACG GGC CCC     5040
Asn Thr Trp His Gly Thr Phe Pro Ile Asn Ala Tyr Thr Thr Gly Pro
1665                1670                1675                1680
TGC ACA CCC TCT CCA GCG CCA AAC TAT TCT AGG GCG CTG TGG CGG GTG     5088
Cys Thr Pro Ser Pro Ala Pro Asn Tyr Ser Arg Ala Leu Trp Arg Val
                1685                1690                1695
GCC GCT GAG GAG TAC GTG GAG GTC ACG CGG GTG GGG GAT TTC CAC TAC     5136
Ala Ala Glu Glu Tyr Val Glu Val Thr Arg Val Gly Asp Phe His Tyr
            1700                1705                1710
GTG ACG GGC ATG ACC ACT GAC AAC GTA AAG TGC CCA TGC CAG GTT CCG     5184
Val Thr Gly Met Thr Thr Asp Asn Val Lys Cys Pro Cys Gln Val Pro
        1715                1720                1725
GCT CCT GAA TTC TTC TCG GAG GTG GAC GGA GTG CGG TTG CAC AGG TAC     5232
Ala Pro Glu Phe Phe Ser Glu Val Asp Gly Val Arg Leu His Arg Tyr
    1730                1735                1740
GCT CCG GCG TGC AGG CCT CTC CTA CGG GAG GAG GTT ACA TTC CAG GTC     5280
Ala Pro Ala Cys Arg Pro Leu Leu Arg Glu Glu Val Thr Phe Gln Val
1745                1750                1755                1760
GGG CTC AAC CAA TAC CTG GTT GGG TCA CAG CTA CCA TGC GAG CCC GAA     5328
Gly Leu Asn Gln Tyr Leu Val Gly Ser Gln Leu Pro Cys Glu Pro Glu
                1765                1770                1775
CCG GAT GTA GCA GTG CTC ACT TCC ATG CTC ACC GAC CCC TCC CAC ATC     5376
Pro Asp Val Ala Val Leu Thr Ser Met Leu Thr Asp Pro Ser His Ile
            1780                1785                1790
ACA GCA GAA ACG GCT AAG CGT AGG TTG GCC AGG GGG TCT CCC CCC TCC     5424
Thr Ala Glu Thr Ala Lys Arg Arg Leu Ala Arg Gly Ser Pro Pro Ser
        1795                1800                1805
TTG GCC AGC TCT TCA GCT AGC CAG TTG TCT GCG CCT TCC TTG AAG GCG     5472
Leu Ala Ser Ser Ser Ala Ser Gln Leu Ser Ala Pro Ser Leu Lys Ala
    1810                1815                1820
ACA TGC ACT ACC CAC CAT GTC TCT CCG GAC GCT GAC CTC ATC GAG GCC     5520
Thr Cys Thr Thr His His Val Ser Pro Asp Ala Asp Leu Ile Glu Ala
1825                1830                1835                1840
AAC CTC CTG TGG CGG CAG GAG ATG GGC GGG AAC ATC ACC CGC GTG GAG     5568
Asn Leu Leu Trp Arg Gln Glu Met Gly Gly Asn Ile Thr Arg Val Glu
                1845                1850                1855
TCG GAG AAC AAG GTG GTA GTC CTG GAC TCT TTC GAC CCG CTT CGA GCG     5616
Ser Glu Asn Lys Val Val Val Leu Asp Ser Phe Asp Pro Leu Arg Ala
            1860                1865                1870
GAG GAG GAT GAG AGG GAA GTA TCC GTT CCG GCG GAG ATC CTG CGG AAA     5664
Glu Glu Asp Glu Arg Glu Val Ser Val Pro Ala Glu Ile Leu Arg Lys
        1875                1880                1885
TCC AAG AAG TTC CCC GCA GCG ATG CCC ATC TGG GCG CGC CCG GAT TAC     5712
Ser Lys Lys Phe Pro Ala Ala Met Pro Ile Trp Ala Arg Pro Asp Tyr
    1890                1895                1900
AAC CCT CCA CTG TTA GAG TCC TGG AAG GAC CCG GAC TAC GTC CCT CCG     5760
Asn Pro Pro Leu Leu Glu Ser Trp Lys Asp Pro Asp Tyr Val Pro Pro
1905                1910                1915                1920
GTG GTG CAC GGG TGC CCG TTG CCA CCT ATC AAG GCC CCT CCA ATA CCA     5808
Val Val His Gly Cys Pro Leu Pro Pro Ile Lys Ala Pro Pro Ile Pro
                1925                1930                1935
CCT CCA CGG AGA AAG AGG ACG GTT GTC CTA ACA GAG TCC TCC GTG TCT     5856
Pro Pro Arg Arg Lys Arg Thr Val Val Leu Thr Glu Ser Ser Val Ser
            1940                1945                1950
TCT GCC TTA GCG GAG CTC GCT ACT AAG ACC TTC GGC AGC TCC GAA TCA     5904
Ser Ala Leu Ala Glu Leu Ala Thr Lys Thr Phe Gly Ser Ser Glu Ser
        1955                1960                1965
TCG GCC GTC GAC AGC GGC ACG GCG ACC GCC CTT CCT GAC CAG GCC TCC     5952
Ser Ala Val Asp Ser Gly Thr Ala Thr Ala Leu Pro Asp Gln Ala Ser
    1970                1975                1980
GAC GAC GGT GAC AAA GGA TCC GAC GTT GAG TCG TAC TCC TCC ATG CCC     6000
Asp Asp Gly Asp Lys Gly Ser Asp Val Glu Ser Tyr Ser Ser Met Pro
1985                1990                1995                2000
CCC CTT GAG GGG GAA CCG GGG GAC CCC GAT CTC AGT GAC GGG TCT TGG     6048
Pro Leu Glu Gly Glu Pro Gly Asp Pro Asp Leu Ser Asp Gly Ser Trp
                2005                2010                2015
TCT ACC GTG AGC GAG GAA GCT AGT GAG GAT GTC GTC TGC TGC TCA ATG     6096
Ser Thr Val Ser Glu Glu Ala Ser Glu Asp Val Val Cys Cys Ser Met
            2020                2025                2030
TCC TAC ACA TGG ACA GGC GCC TTG ATC ACG CCA TGC GCT GCG GAG GAA     6144
Ser Tyr Thr Trp Thr Gly Ala Leu Ile Thr Pro Cys Ala Ala Glu Glu
        2035                2040                2045
AGC AAG CTG CCC ATC AAC GCG TTG AGC AAC TCT TTG CTG CGC CAC CAT     6192
Ser Lys Leu Pro Ile Asn Ala Leu Ser Asn Ser Leu Leu Arg His His
    2050                2055                2060
AAC ATG GTT TAT GCC ACA ACA TCT CGC AGC GCA GGC CTG CGG CAG AAG     6240
Asn Met Val Tyr Ala Thr Thr Ser Arg Ser Ala Gly Leu Arg Gln Lys
2065                2070                2075                2080
AAG GTC ACC TTT GAC AGA CTG CAA GTC CTG GAC GAC CAC TAC CGG GAC     6288
Lys Val Thr Phe Asp Arg Leu Gln Val Leu Asp Asp His Tyr Arg Asp
                2085                2090                2095
GTG CTC AAG GAG ATG AAG GCG AAG GCG TCC ACA GTT AAG GCT AAA CTC     6336
Val Leu Lys Glu Met Lys Ala Lys Ala Ser Thr Val Lys Ala Lys Leu
            2100                2105                2110
CTA TCC GTA GAG GAA GCC TGC AAG CTG ACG CCC CCA CAT TCG GCC AAA     6384
Leu Ser Val Glu Glu Ala Cys Lys Leu Thr Pro Pro His Ser Ala Lys
        2115                2120                2125
TCC AAG TTT GGC TAT GGG GCA AAG GAC GTC CGG AAC CTA TCC AGC AAG     6432
Ser Lys Phe Gly Tyr Gly Ala Lys Asp Val Arg Asn Leu Ser Ser Lys
    2130                2135                2140
GCC GTT AAC CAC ATC CAC TCC GTG TGG AAG GAC TTG CTG GAA GAC ACT     6480
Ala Val Asn His Ile His Ser Val Trp Lys Asp Leu Leu Glu Asp Thr
2145                2150                2155                2160
GTG ACA CCA ATT GAC ACC ACC ATC ATG GCA AAA AAT GAG GTT TTC TGT     6528
Val Thr Pro Ile Asp Thr Thr Ile Met Ala Lys Asn Glu Val Phe Cys
                2165                2170                2175
GTC CAA CCA GAG AAA GGA GGC CGT AAG CCA GCC CGC CTT ATC GTA TTC     6576
Val Gln Pro Glu Lys Gly Gly Arg Lys Pro Ala Arg Leu Ile Val Phe
            2180                2185                2190
CCA GAT CTG GGA GTC CGT GTA TGC GAG AAG ATG GCC CTC TAT GAT GTG     6624
Pro Asp Leu Gly Val Arg Val Cys Glu Lys Met Ala Leu Tyr Asp Val
        2195                2200                2205
GTC TCC ACC CTT CCT CAG GTC GTG ATG GGC TCC TCA TAC GGA TTC CAG     6672
Val Ser Thr Leu Pro Gln Val Val Met Gly Ser Ser Tyr Gly Phe Gln
    2210                2215                2220
TAC TCT CCT GGG CAG CGA GTC GAG TTC CTG GTG AAT ACC TGG AAA TCA     6720
Tyr Ser Pro Gly Gln Arg Val Glu Phe Leu Val Asn Thr Trp Lys Ser
2225                2230                2235                2240
AAG AAA AAC CCC ATG GGC TTT TCA TAT GAC ACT CGC TGT TTC GAC TCA     6768
Lys Lys Asn Pro Met Gly Phe Ser Tyr Asp Thr Arg Cys Phe Asp Ser
                2245                2250                2255
ACG GTC ACC GAG AAC GAC ATC CGT GTT GAG GAG TCA ATT TAC CAA TGT     6816
Thr Val Thr Glu Asn Asp Ile Arg Val Glu Glu Ser Ile Tyr Gln Cys
            2260                2265                2270
TGT GAC TTG GCC CCC GAA GCC AGA CAG GCC ATA AAA TCG CTC ACA GAG     6864
Cys Asp Leu Ala Pro Glu Ala Arg Gln Ala Ile Lys Ser Leu Thr Glu
        2275                2280                2285
CGG CTT TAT ATC GGG GGT CCT CTG ACT AAT TCA AAA GGG CAG AAC TGC     6912
Arg Leu Tyr Ile Gly Gly Pro Leu Thr Asn Ser Lys Gly Gln Asn Cys
    2290                2295                2300
GGT TAT CGC CGG TGC CGC GCG AGC GGC GTG CTG ACG ACT AGC TGC GGT     6960
Gly Tyr Arg Arg Cys Arg Ala Ser Gly Val Leu Thr Thr Ser Cys Gly
2305                2310                2315                2320
AAC ACC CTC ACA TGT TAC TTG AAG GCC TCT GCA GCC TGT CGA GCT GCG     7008
Asn Thr Leu Thr Cys Tyr Leu Lys Ala Ser Ala Ala Cys Arg Ala Ala
                2325                2330                2335
AAG CTC CAG GAC TGC ACG ATG CTC GTG AAC GGA GAC GAC CTC GTC GTT     7056
Lys Leu Gln Asp Cys Thr Met Leu Val Asn Gly Asp Asp Leu Val Val
            2340                2345                2350
ATC TGT GAA AGC GCG GGA ACC CAA GAG GAC GCG GCG AGC CTA CGA GTC     7104
Ile Cys Glu Ser Ala Gly Thr Gln Glu Asp Ala Ala Ser Leu Arg Val
        2355                2360                2365
TTC ACG GAG GCT ATG ACT AGG TAC TCC GCC CCC CCC GGG GAC CCG CCC     7152
Phe Thr Glu Ala Met Thr Arg Tyr Ser Ala Pro Pro Gly Asp Pro Pro
    2370                2375                2380
CAA CCA GAA TAC GAC TTG GAG CTG ATA ACA TCA TGT TCC TCC AAT GTG     7200
Gln Pro Glu Tyr Asp Leu Glu Leu Ile Thr Ser Cys Ser Ser Asn Val
2385                2390                2395                2400
TCG GTC GCC CAC GAT GCA TCA GGC AAA AGG GTG TAC TAC CTC ACC CGT     7248
Ser Val Ala His Asp Ala Ser Gly Lys Arg Val Tyr Tyr Leu Thr Arg
                2405                2410                2415
GAT CCC ACC ACC CCC CTA GCA CGG GCT GCG TGG GAG ACA GCT AGA CAC     7296
Asp Pro Thr Thr Pro Leu Ala Arg Ala Ala Trp Glu Thr Ala Arg His
            2420                2425                2430
ACT CCA GTT AAC TCC TGG CTA GGC AAC ATT ATT ATG TAT GCG CCC ACT     7344
Thr Pro Val Asn Ser Trp Leu Gly Asn Ile Ile Met Tyr Ala Pro Thr
        2435                2440                2445
TTG TGG GCA AGG ATG ATT CTG ATG ACT CAC TTC TTC TCC ATC CTT CTA     7392
Leu Trp Ala Arg Met Ile Leu Met Thr His Phe Phe Ser Ile Leu Leu
    2450                2455                2460
GCG CAG GAG CAA CTT GAA AAA GCC CTG GAC TGC CAG ATC TAC GGG GCC     7440
Ala Gln Glu Gln Leu Glu Lys Ala Leu Asp Cys Gln Ile Tyr Gly Ala
2465                2470                2475                2480
TGT TAC TCC ATT GAG CCA CTT GAC CTA CCT CAG ATC ATT GAA CGA CTC     7488
Cys Tyr Ser Ile Glu Pro Leu Asp Leu Pro Gln Ile Ile Glu Arg Leu
                2485                2490                2495
CAT GGC CTT AGC GCA TTT TCA CTC CAT AGT TAC TCT CCA GGT GAG ATC     7536
His Gly Leu Ser Ala Phe Ser Leu His Ser Tyr Ser Pro Gly Glu Ile
            2500                2505                2510
AAT AGG GTG GCT TCA TGC CTC AGG AAA CTT GGG GTA CCA CCC TTG CGA     7584
Asn Arg Val Ala Ser Cys Leu Arg Lys Leu Gly Val Pro Pro Leu Arg
        2515                2520                2525
GTC TGG AGA CAT CGG GCC AGG AGC GTC CGC GCT AGG CTA CTG TCC CAG     7632
Val Trp Arg His Arg Ala Arg Ser Val Arg Ala Arg Leu Leu Ser Gln
    2530                2535                2540
GGA GGG AGG GCC GCC ACT TGT GGC AAA TAC CTC TTC AAC TGG GCA GTA     7680
Gly Gly Arg Ala Ala Thr Cys Gly Lys Tyr Leu Phe Asn Trp Ala Val
2545                2550                2555                2560
AAA ACC AAA CTT AAA CTC ACT CCA ATC CCG GCT GCG TCC CGG CTG GAC     7728
Lys Thr Lys Leu Lys Leu Thr Pro Ile Pro Ala Ala Ser Arg Leu Asp
                2565                2570                2575
TTG TCC GGC TGG TTC GTT GCT GGT TAC AGC GGG GGA GAC ATA TAT CAC     7776
Leu Ser Gly Trp Phe Val Ala Gly Tyr Ser Gly Gly Asp Ile Tyr His
            2580                2585                2590
AGC CTG TCT CGT GCC CGA CCC CGT TGG TTC ATG CTG TGC CTA CTC CTA     7824
Ser Leu Ser Arg Ala Arg Pro Arg Trp Phe Met Leu Cys Leu Leu Leu
        2595                2600                2605
CTT TCT GTA GGG GTA GGC ATC TAC CTG CTC CCC AAC CGA                 7863
Leu Ser Val Gly Val Gly Ile Tyr Leu Leu Pro Asn Arg
    2610                2615                2620 
           
           
             
               2621 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             36
Gly Ala Gln Ala Lys Thr Thr Asn Arg Leu Val Ser Met Phe Ala Ser
  1               5                  10                  15
Gly Pro Ser Gln Lys Ile Gln Leu Ile Asn Thr Asn Gly Ser Trp His
             20                  25                  30
Ile Asn Arg Thr Ala Leu Asn Cys Asn Asp Ser Leu Gln Thr Gly Phe
         35                  40                  45
Leu Ala Ala Leu Phe Tyr Thr His Ser Phe Asn Ser Ser Gly Cys Pro
     50                  55                  60
Glu Arg Met Ala Gln Cys Arg Thr Ile Asp Lys Phe Asp Gln Gly Trp
 65                  70                  75                  80
Gly Pro Ile Thr Tyr Ala Glu Ser Ser Arg Ser Asp Gln Arg Pro Tyr
                 85                  90                  95
Cys Trp His Tyr Pro Pro Pro Gln Cys Thr Ile Val Pro Ala Ser Glu
            100                 105                 110
Val Cys Gly Pro Val Tyr Cys Phe Thr Pro Ser Pro Val Val Val Gly
        115                 120                 125
Thr Thr Asp Arg Phe Gly Val Pro Thr Tyr Arg Trp Gly Glu Asn Glu
    130                 135                 140
Thr Asp Val Leu Leu Leu Asn Asn Thr Arg Pro Pro Gln Gly Asn Trp
145                 150                 155                 160
Phe Gly Cys Thr Trp Met Asn Ser Thr Gly Phe Thr Lys Thr Cys Gly
                165                 170                 175
Gly Pro Pro Cys Asn Ile Gly Gly Val Gly Asn Asn Thr Leu Thr Cys
            180                 185                 190
Pro Thr Asp Cys Phe Arg Lys His Pro Glu Ala Thr Tyr Thr Lys Cys
        195                 200                 205
Gly Ser Gly Pro Trp Leu Thr Pro Arg Cys Met Val Asp Tyr Pro Tyr
    210                 215                 220
Arg Leu Trp His Tyr Pro Cys Thr Val Asn Phe Thr Ile Phe Lys Val
225                 230                 235                 240
Arg Met Tyr Val Gly Gly Val Glu His Arg Leu Asn Ala Ala Cys Asn
                245                 250                 255
Trp Thr Arg Gly Glu Arg Cys Asp Leu Glu Asp Arg Asp Arg Pro Glu
            260                 265                 270
Leu Ser Pro Leu Leu Leu Ser Thr Thr Glu Trp Gln Val Leu Pro Cys
        275                 280                 285
Ser Phe Thr Thr Leu Pro Ala Leu Ser Thr Gly Leu Ile His Leu His
    290                 295                 300
Gln Asn Ile Val Asp Val Gln Tyr Leu Tyr Gly Ile Gly Ser Ala Val
305                 310                 315                 320
Val Ser Phe Ala Ile Lys Trp Glu Tyr Val Leu Leu Leu Phe Leu Leu
                325                 330                 335
Leu Ala Asp Ala Arg Val Cys Ala Cys Leu Trp Met Met Leu Leu Ile
            340                 345                 350
Ala Gln Ala Glu Ala Ala Leu Glu Asn Leu Val Val Leu Asn Ser Ala
        355                 360                 365
Ser Val Ala Gly Ala His Gly Ile Leu Ser Phe Leu Val Phe Phe Cys
    370                 375                 380
Ala Ala Trp Tyr Ile Lys Gly Arg Leu Val Pro Gly Ala Thr Tyr Ala
385                 390                 395                 400
Leu Tyr Gly Val Trp Pro Leu Leu Leu Leu Leu Leu Ala Leu Pro Pro
                405                 410                 415
Arg Ala Tyr Ala Met Asp Arg Glu Met Ala Ala Ser Cys Gly Gly Ala
            420                 425                 430
Val Phe Val Gly Leu Val Leu Leu Thr Leu Ser Pro Tyr Tyr Lys Val
        435                 440                 445
Phe Leu Ala Arg Leu Ile Trp Trp Leu Gln Tyr Phe Thr Thr Arg Ala
    450                 455                 460
Glu Ala Asp Leu His Val Trp Ile Pro Pro Leu Asn Ala Arg Gly Gly
465                 470                 475                 480
Arg Asp Ala Ile Ile Leu Leu Met Cys Ala Val His Pro Glu Leu Ile
                485                 490                 495
Phe Asp Ile Thr Lys Leu Leu Ile Ala Ile Leu Gly Pro Leu Met Val
            500                 505                 510
Leu Gln Ala Gly Ile Thr Arg Val Pro Tyr Phe Val Arg Ala Gln Gly
        515                 520                 525
Leu Ile His Ala Cys Met Leu Val Arg Lys Val Ala Gly Gly His Tyr
    530                 535                 540
Val Gln Met Ala Phe Met Lys Leu Gly Ala Leu Thr Gly Thr Tyr Ile
545                 550                 555                 560
Tyr Asn His Leu Thr Pro Leu Arg Asp Trp Pro Arg Ala Gly Leu Arg
                565                 570                 575
Asp Leu Ala Val Ala Val Glu Pro Val Val Phe Ser Asp Met Glu Thr
            580                 585                 590
Lys Ile Ile Thr Trp Gly Ala Asp Thr Ala Ala Cys Gly Asp Ile Ile
        595                 600                 605
Leu Gly Leu Pro Val Ser Ala Arg Arg Gly Lys Glu Ile Leu Leu Gly
    610                 615                 620
Pro Ala Asp Ser Leu Glu Gly Arg Gly Leu Arg Leu Leu Ala Pro Ile
625                 630                 635                 640
Thr Ala Tyr Ser Gln Gln Thr Arg Gly Leu Leu Gly Cys Ile Ile Thr
                645                 650                 655
Ser Leu Thr Gly Arg Asp Lys Asn Gln Val Glu Gly Glu Val Gln Val
            660                 665                 670
Val Ser Thr Ala Thr Gln Ser Phe Leu Ala Thr Cys Val Asn Gly Val
        675                 680                 685
Cys Trp Thr Val Tyr His Gly Ala Gly Ser Lys Thr Leu Ala Ala Pro
    690                 695                 700
Lys Gly Pro Ile Thr Gln Met Tyr Thr Asn Val Asp Gln Asp Leu Val
705                 710                 715                 720
Gly Trp Pro Lys Pro Pro Gly Ala Arg Ser Leu Thr Pro Cys Thr Cys
                725                 730                 735
Gly Ser Ser Asp Leu Tyr Leu Val Thr Arg His Ala Asp Val Ile Pro
            740                 745                 750
Val Arg Arg Arg Gly Asp Ser Arg Gly Ser Leu Leu Ser Pro Arg Pro
        755                 760                 765
Val Ser Tyr Leu Lys Gly Ser Ser Gly Gly Pro Leu Leu Cys Pro Phe
    770                 775                 780
Gly His Ala Val Gly Ile Phe Arg Ala Ala Val Cys Thr Arg Gly Val
785                 790                 795                 800
Ala Lys Ala Val Asp Phe Val Pro Val Glu Ser Met Glu Thr Thr Met
                805                 810                 815
Arg Ser Pro Val Phe Thr Asp Asn Ser Ser Pro Pro Ala Val Pro Gln
            820                 825                 830
Ser Phe Gln Val Ala His Leu His Ala Pro Thr Gly Ser Gly Lys Ser
        835                 840                 845
Thr Lys Val Pro Ala Ala Tyr Ala Ala Gln Gly Tyr Lys Val Leu Val
    850                 855                 860
Leu Asn Pro Ser Val Ala Ala Thr Leu Gly Phe Gly Ala Tyr Met Ser
865                 870                 875                 880
Lys Ala His Gly Ile Asp Pro Asn Ile Arg Thr Gly Val Arg Thr Ile
                885                 890                 895
Thr Thr Gly Ala Pro Val Thr Tyr Ser Thr Tyr Gly Lys Phe Leu Ala
            900                 905                 910
Asp Gly Gly Cys Ser Gly Gly Ala Tyr Asp Ile Ile Ile Cys Asp Glu
        915                 920                 925
Cys His Ser Thr Asp Ser Thr Thr Ile Leu Gly Ile Gly Thr Val Leu
    930                 935                 940
Asp Gln Ala Glu Thr Ala Gly Ala Arg Leu Val Val Leu Ala Thr Ala
945                 950                 955                 960
Thr Pro Pro Gly Ser Val Thr Val Pro His Pro Asn Ile Glu Glu Val
                965                 970                 975
Ala Leu Ser Asn Thr Gly Glu Ile Pro Phe Tyr Gly Lys Ala Ile Pro
            980                 985                 990
Ile Glu Ala Ile Arg Gly Gly Arg His Leu Ile Phe Cys His Ser Lys
        995                 1000                1005
Lys Lys Cys Asp Glu Leu Ala Ala Lys Leu Ser Gly Leu Gly Ile Asn
    1010                1015                1020
Ala Val Ala Tyr Tyr Arg Gly Leu Asp Val Ser Val Ile Pro Thr Ile
1025                1030                1035                1040
Gly Asp Val Val Val Val Ala Thr Asp Ala Leu Met Thr Gly Tyr Thr
                1045                1050                1055
Gly Asp Phe Asp Ser Val Ile Asp Cys Asn Thr Cys Val Thr Gln Thr
            1060                1065                1070
Val Asp Phe Ser Leu Asp Pro Thr Phe Thr Ile Glu Thr Thr Thr Val
        1075                1080                1085
Pro Gln Asp Ala Val Ser Arg Ser Gln Arg Arg Gly Arg Thr Gly Arg
    1090                1095                1100
Gly Arg Arg Gly Ile Tyr Arg Phe Val Thr Pro Gly Glu Arg Pro Ser
1105                1110                1115                1120
Gly Met Phe Asp Ser Ser Val Leu Cys Glu Cys Tyr Asp Ala Gly Cys
                1125                1130                1135
Ala Trp Tyr Glu Leu Thr Pro Ala Glu Thr Ser Val Arg Leu Arg Ala
            1140                1145                1150
Tyr Leu Asn Thr Pro Gly Leu Pro Val Cys Gln Asp His Leu Glu Phe
        1155                1160                1165
Trp Glu Ser Val Phe Thr Gly Leu Thr His Ile Asp Ala His Phe Leu
    1170                1175                1180
Ser Gln Thr Lys Gln Ala Gly Asp Asn Phe Pro Tyr Leu Val Ala Tyr
1185                1190                1195                1200
Gln Ala Thr Val Cys Ala Arg Ala Gln Ala Pro Pro Pro Ser Trp Asp
                1205                1210                1215
Gln Met Trp Lys Cys Leu Ile Arg Leu Lys Pro Thr Leu His Gly Pro
            1220                1225                1230
Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val Gln Asn Glu Val Thr Leu
        1235                1240                1245
Thr His Pro Ile Thr Lys Tyr Ile Met Ala Cys Met Ser Ala Asp Leu
    1250                1255                1260
Glu Val Val Thr Ser Thr Trp Val Leu Val Gly Gly Val Leu Ala Ala
1265                1270                1275                1280
Leu Ala Ala Tyr Cys Leu Thr Thr Gly Ser Val Val Ile Val Gly Arg
                1285                1290                1295
Ile Ile Leu Ser Gly Arg Pro Ala Ile Val Pro Asp Arg Glu Leu Leu
            1300                1305                1310
Tyr Gln Glu Phe Asp Glu Met Glu Glu Cys Ala Ser His Leu Pro Tyr
        1315                1320                1325
Ile Glu Gln Gly Met Gln Leu Ala Glu Gln Phe Lys Gln Lys Ala Leu
    1330                1335                1340
Gly Leu Leu Gln Thr Ala Thr Lys Gln Ala Glu Ala Ala Ala Pro Val
1345                1350                1355                1360
Val Glu Ser Lys Trp Arg Ala Leu Glu Thr Phe Trp Ala Lys His Met
                1365                1370                1375
Trp Asn Phe Ile Ser Gly Ile Gln Tyr Leu Ala Gly Leu Ser Thr Leu
            1380                1385                1390
Pro Gly Asn Pro Ala Ile Ala Ser Leu Met Ala Phe Thr Ala Ser Ile
        1395                1400                1405
Thr Ser Pro Leu Thr Thr Gln Ser Thr Leu Leu Phe Asn Ile Leu Gly
    1410                1415                1420
Gly Trp Val Ala Ala Gln Leu Ala Pro Pro Ser Ala Ala Ser Ala Phe
1425                1430                1435                1440
Val Gly Ala Gly Ile Ala Gly Ala Ala Val Gly Ser Ile Gly Leu Gly
                1445                1450                1455
Lys Val Leu Val Asp Ile Leu Ala Gly Tyr Gly Ala Gly Val Ala Gly
            1460                1465                1470
Ala Leu Val Ala Phe Lys Val Met Ser Gly Glu Met Pro Ser Thr Glu
        1475                1480                1485
Asp Leu Val Asn Leu Leu Pro Ala Ile Leu Ser Pro Gly Ala Leu Val
    1490                1495                1500
Val Gly Val Val Cys Ala Ala Ile Leu Arg Arg His Val Gly Pro Gly
1505                1510                1515                1520
Glu Gly Ala Val Gln Trp Met Asn Arg Leu Ile Ala Phe Ala Ser Arg
                1525                1530                1535
Gly Asn His Val Ser Pro Thr His Tyr Val Pro Glu Ser Asp Ala Ala
            1540                1545                1550
Ala Arg Val Thr Gln Ile Leu Ser Ser Leu Thr Ile Thr Gln Leu Leu
        1555                1560                1565
Lys Arg Leu His Gln Trp Ile Asn Glu Asp Cys Ser Thr Pro Cys Ser
    1570                1575                1580
Gly Ser Trp Leu Arg Asp Val Trp Asp Trp Ile Cys Thr Val Leu Thr
1585                1590                1595                1600
Asp Phe Lys Thr Trp Leu Gln Ser Lys Leu Leu Pro Gln Leu Pro Gly
                1605                1610                1615
Val Pro Phe Phe Ser Cys Gln Arg Gly Tyr Lys Gly Val Trp Arg Gly
            1620                1625                1630
Asp Gly Ile Met Gln Thr Thr Cys Pro Cys Gly Ala Gln Ile Thr Gly
        1635                1640                1645
His Val Lys Asn Gly Ser Met Arg Ile Val Gly Pro Lys Thr Cys Ser
    1650                1655                1660
Asn Thr Trp His Gly Thr Phe Pro Ile Asn Ala Tyr Thr Thr Gly Pro
1665                1670                1675                1680
Cys Thr Pro Ser Pro Ala Pro Asn Tyr Ser Arg Ala Leu Trp Arg Val
                1685                1690                1695
Ala Ala Glu Glu Tyr Val Glu Val Thr Arg Val Gly Asp Phe His Tyr
            1700                1705                1710
Val Thr Gly Met Thr Thr Asp Asn Val Lys Cys Pro Cys Gln Val Pro
        1715                1720                1725
Ala Pro Glu Phe Phe Ser Glu Val Asp Gly Val Arg Leu His Arg Tyr
    1730                1735                1740
Ala Pro Ala Cys Arg Pro Leu Leu Arg Glu Glu Val Thr Phe Gln Val
1745                1750                1755                1760
Gly Leu Asn Gln Tyr Leu Val Gly Ser Gln Leu Pro Cys Glu Pro Glu
                1765                1770                1775
Pro Asp Val Ala Val Leu Thr Ser Met Leu Thr Asp Pro Ser His Ile
            1780                1785                1790
Thr Ala Glu Thr Ala Lys Arg Arg Leu Ala Arg Gly Ser Pro Pro Ser
        1795                1800                1805
Leu Ala Ser Ser Ser Ala Ser Gln Leu Ser Ala Pro Ser Leu Lys Ala
    1810                1815                1820
Thr Cys Thr Thr His His Val Ser Pro Asp Ala Asp Leu Ile Glu Ala
1825                1830                1835                1840
Asn Leu Leu Trp Arg Gln Glu Met Gly Gly Asn Ile Thr Arg Val Glu
                1845                1850                1855
Ser Glu Asn Lys Val Val Val Leu Asp Ser Phe Asp Pro Leu Arg Ala
            1860                1865                1870
Glu Glu Asp Glu Arg Glu Val Ser Val Pro Ala Glu Ile Leu Arg Lys
        1875                1880                1885
Ser Lys Lys Phe Pro Ala Ala Met Pro Ile Trp Ala Arg Pro Asp Tyr
    1890                1895                1900
Asn Pro Pro Leu Leu Glu Ser Trp Lys Asp Pro Asp Tyr Val Pro Pro
1905                1910                1915                1920
Val Val His Gly Cys Pro Leu Pro Pro Ile Lys Ala Pro Pro Ile Pro
                1925                1930                1935
Pro Pro Arg Arg Lys Arg Thr Val Val Leu Thr Glu Ser Ser Val Ser
            1940                1945                1950
Ser Ala Leu Ala Glu Leu Ala Thr Lys Thr Phe Gly Ser Ser Glu Ser
        1955                1960                1965
Ser Ala Val Asp Ser Gly Thr Ala Thr Ala Leu Pro Asp Gln Ala Ser
    1970                1975                1980
Asp Asp Gly Asp Lys Gly Ser Asp Val Glu Ser Tyr Ser Ser Met Pro
1985                1990                1995                2000
Pro Leu Glu Gly Glu Pro Gly Asp Pro Asp Leu Ser Asp Gly Ser Trp
                2005                2010                2015
Ser Thr Val Ser Glu Glu Ala Ser Glu Asp Val Val Cys Cys Ser Met
            2020                2025                2030
Ser Tyr Thr Trp Thr Gly Ala Leu Ile Thr Pro Cys Ala Ala Glu Glu
        2035                2040                2045
Ser Lys Leu Pro Ile Asn Ala Leu Ser Asn Ser Leu Leu Arg His His
    2050                2055                2060
Asn Met Val Tyr Ala Thr Thr Ser Arg Ser Ala Gly Leu Arg Gln Lys
2065                2070                2075                2080
Lys Val Thr Phe Asp Arg Leu Gln Val Leu Asp Asp His Tyr Arg Asp
                2085                2090                2095
Val Leu Lys Glu Met Lys Ala Lys Ala Ser Thr Val Lys Ala Lys Leu
            2100                2105                2110
Leu Ser Val Glu Glu Ala Cys Lys Leu Thr Pro Pro His Ser Ala Lys
        2115                2120                2125
Ser Lys Phe Gly Tyr Gly Ala Lys Asp Val Arg Asn Leu Ser Ser Lys
    2130                2135                2140
Ala Val Asn His Ile His Ser Val Trp Lys Asp Leu Leu Glu Asp Thr
2145                2150                2155                2160
Val Thr Pro Ile Asp Thr Thr Ile Met Ala Lys Asn Glu Val Phe Cys
                2165                2170                2175
Val Gln Pro Glu Lys Gly Gly Arg Lys Pro Ala Arg Leu Ile Val Phe
            2180                2185                2190
Pro Asp Leu Gly Val Arg Val Cys Glu Lys Met Ala Leu Tyr Asp Val
        2195                2200                2205
Val Ser Thr Leu Pro Gln Val Val Met Gly Ser Ser Tyr Gly Phe Gln
    2210                2215                2220
Tyr Ser Pro Gly Gln Arg Val Glu Phe Leu Val Asn Thr Trp Lys Ser
2225                2230                2235                2240
Lys Lys Asn Pro Met Gly Phe Ser Tyr Asp Thr Arg Cys Phe Asp Ser
                2245                2250                2255
Thr Val Thr Glu Asn Asp Ile Arg Val Glu Glu Ser Ile Tyr Gln Cys
            2260                2265                2270
Cys Asp Leu Ala Pro Glu Ala Arg Gln Ala Ile Lys Ser Leu Thr Glu
        2275                2280                2285
Arg Leu Tyr Ile Gly Gly Pro Leu Thr Asn Ser Lys Gly Gln Asn Cys
    2290                2295                2300
Gly Tyr Arg Arg Cys Arg Ala Ser Gly Val Leu Thr Thr Ser Cys Gly
2305                2310                2315                2320
Asn Thr Leu Thr Cys Tyr Leu Lys Ala Ser Ala Ala Cys Arg Ala Ala
                2325                2330                2335
Lys Leu Gln Asp Cys Thr Met Leu Val Asn Gly Asp Asp Leu Val Val
            2340                2345                2350
Ile Cys Glu Ser Ala Gly Thr Gln Glu Asp Ala Ala Ser Leu Arg Val
        2355                2360                2365
Phe Thr Glu Ala Met Thr Arg Tyr Ser Ala Pro Pro Gly Asp Pro Pro
    2370                2375                2380
Gln Pro Glu Tyr Asp Leu Glu Leu Ile Thr Ser Cys Ser Ser Asn Val
2385                2390                2395                2400
Ser Val Ala His Asp Ala Ser Gly Lys Arg Val Tyr Tyr Leu Thr Arg
                2405                2410                2415
Asp Pro Thr Thr Pro Leu Ala Arg Ala Ala Trp Glu Thr Ala Arg His
            2420                2425                2430
Thr Pro Val Asn Ser Trp Leu Gly Asn Ile Ile Met Tyr Ala Pro Thr
        2435                2440                2445
Leu Trp Ala Arg Met Ile Leu Met Thr His Phe Phe Ser Ile Leu Leu
    2450                2455                2460
Ala Gln Glu Gln Leu Glu Lys Ala Leu Asp Cys Gln Ile Tyr Gly Ala
2465                2470                2475                2480
Cys Tyr Ser Ile Glu Pro Leu Asp Leu Pro Gln Ile Ile Glu Arg Leu
                2485                2490                2495
His Gly Leu Ser Ala Phe Ser Leu His Ser Tyr Ser Pro Gly Glu Ile
            2500                2505                2510
Asn Arg Val Ala Ser Cys Leu Arg Lys Leu Gly Val Pro Pro Leu Arg
        2515                2520                2525
Val Trp Arg His Arg Ala Arg Ser Val Arg Ala Arg Leu Leu Ser Gln
    2530                2535                2540
Gly Gly Arg Ala Ala Thr Cys Gly Lys Tyr Leu Phe Asn Trp Ala Val
2545                2550                2555                2560
Lys Thr Lys Leu Lys Leu Thr Pro Ile Pro Ala Ala Ser Arg Leu Asp
                2565                2570                2575
Leu Ser Gly Trp Phe Val Ala Gly Tyr Ser Gly Gly Asp Ile Tyr His
            2580                2585                2590
Ser Leu Ser Arg Ala Arg Pro Arg Trp Phe Met Leu Cys Leu Leu Leu
        2595                2600                2605
Leu Ser Val Gly Val Gly Ile Tyr Leu Leu Pro Asn Arg
    2610                2615                2620 
           
           
             
               831 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..831 
                /note “sequence = 2520 - 3350 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..831 
             
             37
CGT GTC TGT GCC TGC TTG TGG ATG ATG CTG CTG ATA GCC CAG GCC GAG       48
Arg Val Cys Ala Cys Leu Trp Met Met Leu Leu Ile Ala Gln Ala Glu
  1               5                  10                  15
GCC GCC TTG GAG AAC CTG GTG GTC CTC AAT TCG GCG TCT GTG GCC GGC       96
Ala Ala Leu Glu Asn Leu Val Val Leu Asn Ser Ala Ser Val Ala Gly
             20                  25                  30
GCA CAT GGC ATC CTC TCC TTC CTT GTG TTC TTC TGT GCC GCC TGG TAC      144
Ala His Gly Ile Leu Ser Phe Leu Val Phe Phe Cys Ala Ala Trp Tyr
         35                  40                  45
ATC AAA GGC AGG CTG GTC CCT GGG GCG ACA TAT GCT CTT TAT GGC GTG      192
Ile Lys Gly Arg Leu Val Pro Gly Ala Thr Tyr Ala Leu Tyr Gly Val
     50                  55                  60
TGG CCG CTG CTC CTG CTC TTG CTG GCA TTA CCA CCG CGA GCT TAC GCC      240
Trp Pro Leu Leu Leu Leu Leu Leu Ala Leu Pro Pro Arg Ala Tyr Ala
 65                  70                  75                  80
ATG GAC CGG GAG ATG GCT GCA TCG TGC GGA GGC GCG GTT TTT GTG GGT      288
Met Asp Arg Glu Met Ala Ala Ser Cys Gly Gly Ala Val Phe Val Gly
                 85                  90                  95
CTG GTA CTC CTG ACT TTG TCA CCA TAC TAC AAG GTG TTC CTC GCT AGG      336
Leu Val Leu Leu Thr Leu Ser Pro Tyr Tyr Lys Val Phe Leu Ala Arg
            100                 105                 110
CTC ATA TGG TGG TTA CAA TAT TTT ACC ACC AGA GCC GAG GCG GAC TTA      384
Leu Ile Trp Trp Leu Gln Tyr Phe Thr Thr Arg Ala Glu Ala Asp Leu
        115                 120                 125
CAT GTG TGG ATC CCC CCC CTC AAC GCT CGG GGA GGC CGC GAT GCC ATC      432
His Val Trp Ile Pro Pro Leu Asn Ala Arg Gly Gly Arg Asp Ala Ile
    130                 135                 140
ATC CTC CTC ATG TGC GCA GTC CAT CCA GAG CTA ATC TTT GAC ATC ACC      480
Ile Leu Leu Met Cys Ala Val His Pro Glu Leu Ile Phe Asp Ile Thr
145                 150                 155                 160
AAA CTT CTA ATT GCC ATA CTC GGT CCG CTC ATG GTG CTC CAA GCT GGC      528
Lys Leu Leu Ile Ala Ile Leu Gly Pro Leu Met Val Leu Gln Ala Gly
                165                 170                 175
ATA ACC AGA GTG CCG TAC TTC GTG CGC GCT CAA GGG CTC ATT CAT GCA      576
Ile Thr Arg Val Pro Tyr Phe Val Arg Ala Gln Gly Leu Ile His Ala
            180                 185                 190
TGC ATG TTA GTG CGG AAG GTC GCT GGG GGT CAT TAT GTC CAA ATG GCC      624
Cys Met Leu Val Arg Lys Val Ala Gly Gly His Tyr Val Gln Met Ala
        195                 200                 205
TTC ATG AAG CTG GGC GCG CTG ACA GGC ACG TAC ATT TAC AAC CAT CTT      672
Phe Met Lys Leu Gly Ala Leu Thr Gly Thr Tyr Ile Tyr Asn His Leu
    210                 215                 220
ACC CCG CTA CGG GAT TGG CCA CGC GCG GGC CTA CGA GAC CTT GCG GTG      720
Thr Pro Leu Arg Asp Trp Pro Arg Ala Gly Leu Arg Asp Leu Ala Val
225                 230                 235                 240
GCA GTG GAG CCC GTC GTC TTC TCC GAC ATG GAG ACC AAG ATC ATC ACC      768
Ala Val Glu Pro Val Val Phe Ser Asp Met Glu Thr Lys Ile Ile Thr
                245                 250                 255
TGG GGA GCA GAC ACC GCG GCG TGT GGG GAC ATC ATC TTG GGT CTG CCC      816
Trp Gly Ala Asp Thr Ala Ala Cys Gly Asp Ile Ile Leu Gly Leu Pro
            260                 265                 270
GTC TCC GCC CGA AGG                                                  831
Val Ser Ala Arg Arg
        275 
           
           
             
               277 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             38
Arg Val Cys Ala Cys Leu Trp Met Met Leu Leu Ile Ala Gln Ala Glu
  1               5                  10                  15
Ala Ala Leu Glu Asn Leu Val Val Leu Asn Ser Ala Ser Val Ala Gly
             20                  25                  30
Ala His Gly Ile Leu Ser Phe Leu Val Phe Phe Cys Ala Ala Trp Tyr
         35                  40                  45
Ile Lys Gly Arg Leu Val Pro Gly Ala Thr Tyr Ala Leu Tyr Gly Val
     50                  55                  60
Trp Pro Leu Leu Leu Leu Leu Leu Ala Leu Pro Pro Arg Ala Tyr Ala
 65                  70                  75                  80
Met Asp Arg Glu Met Ala Ala Ser Cys Gly Gly Ala Val Phe Val Gly
                 85                  90                  95
Leu Val Leu Leu Thr Leu Ser Pro Tyr Tyr Lys Val Phe Leu Ala Arg
            100                 105                 110
Leu Ile Trp Trp Leu Gln Tyr Phe Thr Thr Arg Ala Glu Ala Asp Leu
        115                 120                 125
His Val Trp Ile Pro Pro Leu Asn Ala Arg Gly Gly Arg Asp Ala Ile
    130                 135                 140
Ile Leu Leu Met Cys Ala Val His Pro Glu Leu Ile Phe Asp Ile Thr
145                 150                 155                 160
Lys Leu Leu Ile Ala Ile Leu Gly Pro Leu Met Val Leu Gln Ala Gly
                165                 170                 175
Ile Thr Arg Val Pro Tyr Phe Val Arg Ala Gln Gly Leu Ile His Ala
            180                 185                 190
Cys Met Leu Val Arg Lys Val Ala Gly Gly His Tyr Val Gln Met Ala
        195                 200                 205
Phe Met Lys Leu Gly Ala Leu Thr Gly Thr Tyr Ile Tyr Asn His Leu
    210                 215                 220
Thr Pro Leu Arg Asp Trp Pro Arg Ala Gly Leu Arg Asp Leu Ala Val
225                 230                 235                 240
Ala Val Glu Pro Val Val Phe Ser Asp Met Glu Thr Lys Ile Ile Thr
                245                 250                 255
Trp Gly Ala Asp Thr Ala Ala Cys Gly Asp Ile Ile Leu Gly Leu Pro
            260                 265                 270
Val Ser Ala Arg Arg
        275 
           
           
             
               1827 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..1827 
                /note “sequence = 3351 - 5177 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..1827 
             
             39
GGA AAG GAG ATA CTC CTG GGC CCG GCC GAT AGT CTT GAA GGG CGG GGG       48
Gly Lys Glu Ile Leu Leu Gly Pro Ala Asp Ser Leu Glu Gly Arg Gly
  1               5                  10                  15
TTG CGA CTC CTC GCG CCC ATC ACG GCC TAC TCC CAA CAG ACG CGG GGC       96
Leu Arg Leu Leu Ala Pro Ile Thr Ala Tyr Ser Gln Gln Thr Arg Gly
             20                  25                  30
CTA CTT GGT TGC ATC ATC ACT AGC CTT ACA GGC CGG GAC AAG AAC CAG      144
Leu Leu Gly Cys Ile Ile Thr Ser Leu Thr Gly Arg Asp Lys Asn Gln
         35                  40                  45
GTC GAG GGA GAG GTT CAG GTG GTT TCC ACC GCA ACA CAA TCC TTC CTG      192
Val Glu Gly Glu Val Gln Val Val Ser Thr Ala Thr Gln Ser Phe Leu
     50                  55                  60
GCG ACC TGC GTC AAC GGC GTG TGT TGG ACC GTT TAC CAT GGT GCT GGC      240
Ala Thr Cys Val Asn Gly Val Cys Trp Thr Val Tyr His Gly Ala Gly
 65                  70                  75                  80
TCA AAG ACC TTA GCC GCG CCA AAG GGG CCA ATC ACC CAG ATG TAC ACT      288
Ser Lys Thr Leu Ala Ala Pro Lys Gly Pro Ile Thr Gln Met Tyr Thr
                 85                  90                  95
AAT GTG GAC CAG GAC CTC GTC GGC TGG CCC AAG CCC CCC GGG GCG CGT      336
Asn Val Asp Gln Asp Leu Val Gly Trp Pro Lys Pro Pro Gly Ala Arg
            100                 105                 110
TCC TTG ACA CCA TGC ACC TGT GGC AGC TCA GAC CTT TAC TTG GTC ACG      384
Ser Leu Thr Pro Cys Thr Cys Gly Ser Ser Asp Leu Tyr Leu Val Thr
        115                 120                 125
AGA CAT GCT GAC GTC ATT CCG GTG CGC CGG CGG GGC GAC AGT AGG GGG      432
Arg His Ala Asp Val Ile Pro Val Arg Arg Arg Gly Asp Ser Arg Gly
    130                 135                 140
AGC CTG CTC TCC CCC AGG CCT GTC TCC TAC TTG AAG GGC TCT TCG GGT      480
Ser Leu Leu Ser Pro Arg Pro Val Ser Tyr Leu Lys Gly Ser Ser Gly
145                 150                 155                 160
GGT CCA CTG CTC TGC CCC TTC GGG CAC GCT GTG GGC ATC TTC CGG GCT      528
Gly Pro Leu Leu Cys Pro Phe Gly His Ala Val Gly Ile Phe Arg Ala
                165                 170                 175
GCC GTA TGC ACC CGG GGG GTT GCG AAG GCG GTG GAC TTT GTG CCC GTA      576
Ala Val Cys Thr Arg Gly Val Ala Lys Ala Val Asp Phe Val Pro Val
            180                 185                 190
GAG TCC ATG GAA ACT ACT ATG CGG TCT CCG GTC TTC ACG GAC AAC TCA      624
Glu Ser Met Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn Ser
        195                 200                 205
TCC CCC CCG GCC GTA CCG CAG TCA TTT CAA GTG GCC CAC CTA CAC GCT      672
Ser Pro Pro Ala Val Pro Gln Ser Phe Gln Val Ala His Leu His Ala
    210                 215                 220
CCC ACT GGC AGC GGC AAG AGT ACT AAA GTG CCG GCT GCA TAT GCA GCC      720
Pro Thr Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala Ala
225                 230                 235                 240
CAA GGG TAC AAG GTG CTC GTC CTC AAT CCG TCC GTT GCC GCT ACC TTA      768
Gln Gly Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr Leu
                245                 250                 255
GGG TTT GGG GCG TAT ATG TCT AAG GCA CAC GGT ATT GAC CCC AAC ATC      816
Gly Phe Gly Ala Tyr Met Ser Lys Ala His Gly Ile Asp Pro Asn Ile
            260                 265                 270
AGA ACT GGG GTA AGG ACC ATT ACC ACA GGC GCC CCC GTC ACA TAC TCT      864
Arg Thr Gly Val Arg Thr Ile Thr Thr Gly Ala Pro Val Thr Tyr Ser
        275                 280                 285
ACC TAT GGC AAG TTT CTT GCC GAT GGT GGT TGC TCT GGG GGC GCT TAT      912
Thr Tyr Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala Tyr
    290                 295                 300
GAC ATC ATA ATA TGT GAT GAG TGC CAT TCA ACT GAC TCG ACT ACA ATC      960
Asp Ile Ile Ile Cys Asp Glu Cys His Ser Thr Asp Ser Thr Thr Ile
305                 310                 315                 320
TTG GGC ATC GGC ACA GTC CTG GAC CAA GCG GAG ACG GCT GGA GCG CGG     1008
Leu Gly Ile Gly Thr Val Leu Asp Gln Ala Glu Thr Ala Gly Ala Arg
                325                 330                 335
CTT GTC GTG CTC GCC ACC GCT ACG CCT CCG GGA TCG GTC ACC GTG CCA     1056
Leu Val Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro
            340                 345                 350
CAC CCA AAC ATC GAG GAG GTG GCC CTG TCT AAT ACT GGA GAG ATC CCC     1104
His Pro Asn Ile Glu Glu Val Ala Leu Ser Asn Thr Gly Glu Ile Pro
        355                 360                 365
TTC TAT GGC AAA GCC ATC CCC ATT GAA GCC ATC AGG GGG GGA AGG CAT     1152
Phe Tyr Gly Lys Ala Ile Pro Ile Glu Ala Ile Arg Gly Gly Arg His
    370                 375                 380
CTC ATT TTC TGT CAT TCC AAG AAG AAG TGC GAC GAG CTC GCC GCA AAG     1200
Leu Ile Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala Lys
385                 390                 395                 400
CTG TCA GGC CTC GGA ATC AAC GCT GTG GCG TAT TAC CGG GGG CTC GAT     1248
Leu Ser Gly Leu Gly Ile Asn Ala Val Ala Tyr Tyr Arg Gly Leu Asp
                405                 410                 415
GTG TCC GTC ATA CCA ACT ATC GGA GAC GTC GTT GTC GTG GCA ACA GAC     1296
Val Ser Val Ile Pro Thr Ile Gly Asp Val Val Val Val Ala Thr Asp
            420                 425                 430
GCT CTG ATG ACG GGC TAT ACG GGC GAC TTT GAC TCA GTG ATC GAC TGT     1344
Ala Leu Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val Ile Asp Cys
        435                 440                 445
AAC ACA TGT GTC ACC CAG ACA GTC GAC TTC AGC TTG GAT CCC ACC TTC     1392
Asn Thr Cys Val Thr Gln Thr Val Asp Phe Ser Leu Asp Pro Thr Phe
    450                 455                 460
ACC ATT GAG ACG ACG ACC GTG CCT CAA GAC GCA GTG TCG CGC TCG CAG     1440
Thr Ile Glu Thr Thr Thr Val Pro Gln Asp Ala Val Ser Arg Ser Gln
465                 470                 475                 480
CGG CGG GGT AGG ACT GGC AGG GGT AGG AGA GGC ATC TAC AGG TTT GTG     1488
Arg Arg Gly Arg Thr Gly Arg Gly Arg Arg Gly Ile Tyr Arg Phe Val
                485                 490                 495
ACT CCG GGA GAA CGG CCC TCG GGC ATG TTC GAT TCC TCG GTC CTG TGT     1536
Thr Pro Gly Glu Arg Pro Ser Gly Met Phe Asp Ser Ser Val Leu Cys
            500                 505                 510
GAG TGC TAT GAC GCG GGC TGT GCT TGG TAC GAG CTC ACC CCG GCC GAG     1584
Glu Cys Tyr Asp Ala Gly Cys Ala Trp Tyr Glu Leu Thr Pro Ala Glu
        515                 520                 525
ACC TCG GTT AGG TTG CGG GCC TAC CTG AAC ACA CCA GGG TTG CCC GTT     1632
Thr Ser Val Arg Leu Arg Ala Tyr Leu Asn Thr Pro Gly Leu Pro Val
    530                 535                 540
TGC CAG GAC CAC CTG GAG TTC TGG GAG AGT GTC TTC ACA GGC CTC ACC     1680
Cys Gln Asp His Leu Glu Phe Trp Glu Ser Val Phe Thr Gly Leu Thr
545                 550                 555                 560
CAT ATA GAT GCA CAC TTC TTG TCC CAG ACC AAG CAG GCA GGA GAC AAC     1728
His Ile Asp Ala His Phe Leu Ser Gln Thr Lys Gln Ala Gly Asp Asn
                565                 570                 575
TTC CCC TAC CTG GTA GCA TAC CAA GCC ACG GTG TGC GCC AGG GCT CAG     1776
Phe Pro Tyr Leu Val Ala Tyr Gln Ala Thr Val Cys Ala Arg Ala Gln
            580                 585                 590
GCC CCA CCT CCA TCA TGG GAT CAA ATG TGG AAG TGT CTC ATA CGG CTG     1824
Ala Pro Pro Pro Ser Trp Asp Gln Met Trp Lys Cys Leu Ile Arg Leu
        595                 600                 605
AAA                                                                 1827
Lys 
           
           
             
               609 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             40
Gly Lys Glu Ile Leu Leu Gly Pro Ala Asp Ser Leu Glu Gly Arg Gly
  1               5                  10                  15
Leu Arg Leu Leu Ala Pro Ile Thr Ala Tyr Ser Gln Gln Thr Arg Gly
             20                  25                  30
Leu Leu Gly Cys Ile Ile Thr Ser Leu Thr Gly Arg Asp Lys Asn Gln
         35                  40                  45
Val Glu Gly Glu Val Gln Val Val Ser Thr Ala Thr Gln Ser Phe Leu
     50                  55                  60
Ala Thr Cys Val Asn Gly Val Cys Trp Thr Val Tyr His Gly Ala Gly
 65                  70                  75                  80
Ser Lys Thr Leu Ala Ala Pro Lys Gly Pro Ile Thr Gln Met Tyr Thr
                 85                  90                  95
Asn Val Asp Gln Asp Leu Val Gly Trp Pro Lys Pro Pro Gly Ala Arg
            100                 105                 110
Ser Leu Thr Pro Cys Thr Cys Gly Ser Ser Asp Leu Tyr Leu Val Thr
        115                 120                 125
Arg His Ala Asp Val Ile Pro Val Arg Arg Arg Gly Asp Ser Arg Gly
    130                 135                 140
Ser Leu Leu Ser Pro Arg Pro Val Ser Tyr Leu Lys Gly Ser Ser Gly
145                 150                 155                 160
Gly Pro Leu Leu Cys Pro Phe Gly His Ala Val Gly Ile Phe Arg Ala
                165                 170                 175
Ala Val Cys Thr Arg Gly Val Ala Lys Ala Val Asp Phe Val Pro Val
            180                 185                 190
Glu Ser Met Glu Thr Thr Met Arg Ser Pro Val Phe Thr Asp Asn Ser
        195                 200                 205
Ser Pro Pro Ala Val Pro Gln Ser Phe Gln Val Ala His Leu His Ala
    210                 215                 220
Pro Thr Gly Ser Gly Lys Ser Thr Lys Val Pro Ala Ala Tyr Ala Ala
225                 230                 235                 240
Gln Gly Tyr Lys Val Leu Val Leu Asn Pro Ser Val Ala Ala Thr Leu
                245                 250                 255
Gly Phe Gly Ala Tyr Met Ser Lys Ala His Gly Ile Asp Pro Asn Ile
            260                 265                 270
Arg Thr Gly Val Arg Thr Ile Thr Thr Gly Ala Pro Val Thr Tyr Ser
        275                 280                 285
Thr Tyr Gly Lys Phe Leu Ala Asp Gly Gly Cys Ser Gly Gly Ala Tyr
    290                 295                 300
Asp Ile Ile Ile Cys Asp Glu Cys His Ser Thr Asp Ser Thr Thr Ile
305                 310                 315                 320
Leu Gly Ile Gly Thr Val Leu Asp Gln Ala Glu Thr Ala Gly Ala Arg
                325                 330                 335
Leu Val Val Leu Ala Thr Ala Thr Pro Pro Gly Ser Val Thr Val Pro
            340                 345                 350
His Pro Asn Ile Glu Glu Val Ala Leu Ser Asn Thr Gly Glu Ile Pro
        355                 360                 365
Phe Tyr Gly Lys Ala Ile Pro Ile Glu Ala Ile Arg Gly Gly Arg His
    370                 375                 380
Leu Ile Phe Cys His Ser Lys Lys Lys Cys Asp Glu Leu Ala Ala Lys
385                 390                 395                 400
Leu Ser Gly Leu Gly Ile Asn Ala Val Ala Tyr Tyr Arg Gly Leu Asp
                405                 410                 415
Val Ser Val Ile Pro Thr Ile Gly Asp Val Val Val Val Ala Thr Asp
            420                 425                 430
Ala Leu Met Thr Gly Tyr Thr Gly Asp Phe Asp Ser Val Ile Asp Cys
        435                 440                 445
Asn Thr Cys Val Thr Gln Thr Val Asp Phe Ser Leu Asp Pro Thr Phe
    450                 455                 460
Thr Ile Glu Thr Thr Thr Val Pro Gln Asp Ala Val Ser Arg Ser Gln
465                 470                 475                 480
Arg Arg Gly Arg Thr Gly Arg Gly Arg Arg Gly Ile Tyr Arg Phe Val
                485                 490                 495
Thr Pro Gly Glu Arg Pro Ser Gly Met Phe Asp Ser Ser Val Leu Cys
            500                 505                 510
Glu Cys Tyr Asp Ala Gly Cys Ala Trp Tyr Glu Leu Thr Pro Ala Glu
        515                 520                 525
Thr Ser Val Arg Leu Arg Ala Tyr Leu Asn Thr Pro Gly Leu Pro Val
    530                 535                 540
Cys Gln Asp His Leu Glu Phe Trp Glu Ser Val Phe Thr Gly Leu Thr
545                 550                 555                 560
His Ile Asp Ala His Phe Leu Ser Gln Thr Lys Gln Ala Gly Asp Asn
                565                 570                 575
Phe Pro Tyr Leu Val Ala Tyr Gln Ala Thr Val Cys Ala Arg Ala Gln
            580                 585                 590
Ala Pro Pro Pro Ser Trp Asp Gln Met Trp Lys Cys Leu Ile Arg Leu
        595                 600                 605
Lys 
           
           
             
               90 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..90 
                /note “sequence = 4485 - 4574 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..90 
             
             41
ATC AGG GGG GGA AGG CAT CTC ATT TTC TGT CAT TCC AAG AAG AAG TGC       48
Ile Arg Gly Gly Arg His Leu Ile Phe Cys His Ser Lys Lys Lys Cys
  1               5                  10                  15
GAC GAG CTC GCC GCA AAG CTG TCA GGC CTC GGA ATC AAC GCT               90
Asp Glu Leu Ala Ala Lys Leu Ser Gly Leu Gly Ile Asn Ala
             20                  25                  30 
           
           
             
               30 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             42
Ile Arg Gly Gly Arg His Leu Ile Phe Cys His Ser Lys Lys Lys Cys
  1               5                  10                  15
Asp Glu Leu Ala Ala Lys Leu Ser Gly Leu Gly Ile Asn Ala
             20                  25                  30 
           
           
             
               741 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..741 
                /note “sequence = 5178 - 5918 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..741 
             
             43
CCT ACG CTG CAC GGG CCA ACA CCC TTG CTG TAC AGG CTG GGA GCC GTC       48
Pro Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val
  1               5                  10                  15
CAG AAT GAG GTC ACC CTC ACC CAC CCC ATA ACC AAA TAC ATC ATG GCA       96
Gln Asn Glu Val Thr Leu Thr His Pro Ile Thr Lys Tyr Ile Met Ala
             20                  25                  30
TGC ATG TCG GCT GAC CTG GAG GTC GTC ACT AGC ACC TGG GTG CTG GTG      144
Cys Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val
         35                  40                  45
GGC GGA GTC CTT GCA GCT CTG GCC GCG TAT TGC CTG ACA ACA GGC AGT      192
Gly Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Thr Thr Gly Ser
     50                  55                  60
GTG GTC ATT GTG GGT AGG ATT ATC TTG TCC GGG AGG CCG GCC ATT GTT      240
Val Val Ile Val Gly Arg Ile Ile Leu Ser Gly Arg Pro Ala Ile Val
 65                  70                  75                  80
CCC GAC AGG GAG CTT CTC TAC CAG GAG TTC GAT GAA ATG GAA GAG TGC      288
Pro Asp Arg Glu Leu Leu Tyr Gln Glu Phe Asp Glu Met Glu Glu Cys
                 85                  90                  95
GCC TCG CAC CTC CCT TAC ATC GAG CAG GGA ATG CAG CTC GCC GAG CAA      336
Ala Ser His Leu Pro Tyr Ile Glu Gln Gly Met Gln Leu Ala Glu Gln
            100                 105                 110
TTC AAG CAG AAA GCG CTC GGG TTA CTG CAA ACA GCC ACC AAA CAA GCG      384
Phe Lys Gln Lys Ala Leu Gly Leu Leu Gln Thr Ala Thr Lys Gln Ala
        115                 120                 125
GAG GCT GCT GCT CCC GTG GTG GAG TCC AAG TGG CGA GCC CTT GAG ACA      432
Glu Ala Ala Ala Pro Val Val Glu Ser Lys Trp Arg Ala Leu Glu Thr
    130                 135                 140
TTC TGG GCG AAG CAC ATG TGG AAT TTC ATC AGC GGG ATA CAG TAC TTA      480
Phe Trp Ala Lys His Met Trp Asn Phe Ile Ser Gly Ile Gln Tyr Leu
145                 150                 155                 160
GCA GGC TTA TCC ACT CTG CCT GGG AAC CCC GCA ATA GCA TCA TTG ATG      528
Ala Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala Ile Ala Ser Leu Met
                165                 170                 175
GCA TTC ACA GCC TCT ATC ACC AGC CCG CTC ACC ACC CAA AGT ACC CTC      576
Ala Phe Thr Ala Ser Ile Thr Ser Pro Leu Thr Thr Gln Ser Thr Leu
            180                 185                 190
CTG TTT AAC ATC TTG GGG GGG TGG GTG GCT GCC CAA CTC GCC CCC CCC      624
Leu Phe Asn Ile Leu Gly Gly Trp Val Ala Ala Gln Leu Ala Pro Pro
        195                 200                 205
AGC GCC GCT TCG GCT TTC GTG GGC GCC GGC ATC GCC GGT GCG GCT GTT      672
Ser Ala Ala Ser Ala Phe Val Gly Ala Gly Ile Ala Gly Ala Ala Val
    210                 215                 220
GGC AGC ATA GGC CTT GGG AAG GTG CTT GTG GAC ATT CTG GCG GGT TAT      720
Gly Ser Ile Gly Leu Gly Lys Val Leu Val Asp Ile Leu Ala Gly Tyr
225                 230                 235                 240
GGA GCA GGA GTG GCC GGC GCG                                          741
Gly Ala Gly Val Ala Gly Ala
                245 
           
           
             
               247 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             44
Pro Thr Leu His Gly Pro Thr Pro Leu Leu Tyr Arg Leu Gly Ala Val
  1               5                  10                  15
Gln Asn Glu Val Thr Leu Thr His Pro Ile Thr Lys Tyr Ile Met Ala
             20                  25                  30
Cys Met Ser Ala Asp Leu Glu Val Val Thr Ser Thr Trp Val Leu Val
         35                  40                  45
Gly Gly Val Leu Ala Ala Leu Ala Ala Tyr Cys Leu Thr Thr Gly Ser
     50                  55                  60
Val Val Ile Val Gly Arg Ile Ile Leu Ser Gly Arg Pro Ala Ile Val
 65                  70                  75                  80
Pro Asp Arg Glu Leu Leu Tyr Gln Glu Phe Asp Glu Met Glu Glu Cys
                 85                  90                  95
Ala Ser His Leu Pro Tyr Ile Glu Gln Gly Met Gln Leu Ala Glu Gln
            100                 105                 110
Phe Lys Gln Lys Ala Leu Gly Leu Leu Gln Thr Ala Thr Lys Gln Ala
        115                 120                 125
Glu Ala Ala Ala Pro Val Val Glu Ser Lys Trp Arg Ala Leu Glu Thr
    130                 135                 140
Phe Trp Ala Lys His Met Trp Asn Phe Ile Ser Gly Ile Gln Tyr Leu
145                 150                 155                 160
Ala Gly Leu Ser Thr Leu Pro Gly Asn Pro Ala Ile Ala Ser Leu Met
                165                 170                 175
Ala Phe Thr Ala Ser Ile Thr Ser Pro Leu Thr Thr Gln Ser Thr Leu
            180                 185                 190
Leu Phe Asn Ile Leu Gly Gly Trp Val Ala Ala Gln Leu Ala Pro Pro
        195                 200                 205
Ser Ala Ala Ser Ala Phe Val Gly Ala Gly Ile Ala Gly Ala Ala Val
    210                 215                 220
Gly Ser Ile Gly Leu Gly Lys Val Leu Val Asp Ile Leu Ala Gly Tyr
225                 230                 235                 240
Gly Ala Gly Val Ala Gly Ala
                245 
           
           
             
               90 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..90 
                /note “sequence = 5544 - 5633 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..90 
             
             45
ACA GCC ACC AAA CAA GCG GAG GCT GCT GCT CCC GTG GTG GAG TCC AAG       48
Thr Ala Thr Lys Gln Ala Glu Ala Ala Ala Pro Val Val Glu Ser Lys
  1               5                  10                  15
TGG CGA GCC CTT GAG ACA TTC TGG GCG AAG CAC ATG TGG AAT               90
Trp Arg Ala Leu Glu Thr Phe Trp Ala Lys His Met Trp Asn
             20                  25                  30 
           
           
             
               30 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             46
Thr Ala Thr Lys Gln Ala Glu Ala Ala Ala Pro Val Val Glu Ser Lys
  1               5                  10                  15
Trp Arg Ala Leu Glu Thr Phe Trp Ala Lys His Met Trp Asn
             20                  25                  30 
           
           
             
               453 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..453 
                /note “sequence = 5919 - 6371 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..453 
             
             47
CTC GTG GCC TTT AAG GTC ATG AGC GGC GAG ATG CCC TCC ACC GAG GAC       48
Leu Val Ala Phe Lys Val Met Ser Gly Glu Met Pro Ser Thr Glu Asp
  1               5                  10                  15
CTG GTC AAT CTA CTT CCT GCC ATC CTC TCT CCT GGC GCC CTG GTC GTC       96
Leu Val Asn Leu Leu Pro Ala Ile Leu Ser Pro Gly Ala Leu Val Val
             20                  25                  30
GGG GTC GTG TGT GCA GCA ATA CTG CGT CGA CAC GTG GGT CCG GGA GAG      144
Gly Val Val Cys Ala Ala Ile Leu Arg Arg His Val Gly Pro Gly Glu
         35                  40                  45
GGG GCT GTG CAG TGG ATG AAC CGG CTG ATA GCG TTC GCC TCG CGG GGT      192
Gly Ala Val Gln Trp Met Asn Arg Leu Ile Ala Phe Ala Ser Arg Gly
     50                  55                  60
AAT CAT GTT TCC CCC ACG CAC TAT GTG CCT GAG AGC GAC GCC GCA GCG      240
Asn His Val Ser Pro Thr His Tyr Val Pro Glu Ser Asp Ala Ala Ala
 65                  70                  75                  80
CGT GTT ACT CAG ATC CTC TCC AGC CTT ACC ATC ACT CAG CTG CTG AAA      288
Arg Val Thr Gln Ile Leu Ser Ser Leu Thr Ile Thr Gln Leu Leu Lys
                 85                  90                  95
AGG CTC CAC CAG TGG ATT AAT GAA GAC TGC TCC ACA CCG TGT TCC GGC      336
Arg Leu His Gln Trp Ile Asn Glu Asp Cys Ser Thr Pro Cys Ser Gly
            100                 105                 110
TCG TGG CTA AGG GAT GTT TGG GAC TGG ATA TGC ACG GTG TTG ACT GAC      384
Ser Trp Leu Arg Asp Val Trp Asp Trp Ile Cys Thr Val Leu Thr Asp
        115                 120                 125
TTC AAG ACC TGG CTC CAG TCC AAG CTC CTG CCG CAG CTA CCT GGA GTC      432
Phe Lys Thr Trp Leu Gln Ser Lys Leu Leu Pro Gln Leu Pro Gly Val
    130                 135                 140
CCT TTT TTC TCG TGC CAA CGC                                          453
Pro Phe Phe Ser Cys Gln Arg
145                 150 
           
           
             
               151 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             48
Leu Val Ala Phe Lys Val Met Ser Gly Glu Met Pro Ser Thr Glu Asp
  1               5                  10                  15
Leu Val Asn Leu Leu Pro Ala Ile Leu Ser Pro Gly Ala Leu Val Val
             20                  25                  30
Gly Val Val Cys Ala Ala Ile Leu Arg Arg His Val Gly Pro Gly Glu
         35                  40                  45
Gly Ala Val Gln Trp Met Asn Arg Leu Ile Ala Phe Ala Ser Arg Gly
     50                  55                  60
Asn His Val Ser Pro Thr His Tyr Val Pro Glu Ser Asp Ala Ala Ala
 65                  70                  75                  80
Arg Val Thr Gln Ile Leu Ser Ser Leu Thr Ile Thr Gln Leu Leu Lys
                 85                  90                  95
Arg Leu His Gln Trp Ile Asn Glu Asp Cys Ser Thr Pro Cys Ser Gly
            100                 105                 110
Ser Trp Leu Arg Asp Val Trp Asp Trp Ile Cys Thr Val Leu Thr Asp
        115                 120                 125
Phe Lys Thr Trp Leu Gln Ser Lys Leu Leu Pro Gln Leu Pro Gly Val
    130                 135                 140
Pro Phe Phe Ser Cys Gln Arg
145                 150 
           
           
             
               2991 base pairs 
               nucleic acid 
               single 
               linear 
             
             
               cDNA from genomic RNA 
             
             
               unknown 
             
             
               misc_feature 
                1..2991 
                /note “sequence = 6372 - 9362 of
              SEQ ID NO 1” 
             
             
               CDS 
                1..2991 
             
             49
GGG TAC AAG GGA GTC TGG CGG GGA GAC GGC ATC ATG CAA ACC ACC TGC       48
Gly Tyr Lys Gly Val Trp Arg Gly Asp Gly Ile Met Gln Thr Thr Cys
  1               5                  10                  15
CCA TGT GGA GCA CAG ATC ACC GGA CAT GTC AAA AAC GGT TCC ATG AGG       96
Pro Cys Gly Ala Gln Ile Thr Gly His Val Lys Asn Gly Ser Met Arg
             20                  25                  30
ATC GTC GGG CCT AAG ACC TGC AGC AAC ACG TGG CAT GGA ACA TTC CCC      144
Ile Val Gly Pro Lys Thr Cys Ser Asn Thr Trp His Gly Thr Phe Pro
         35                  40                  45
ATC AAC GCA TAC ACC ACG GGC CCC TGC ACA CCC TCT CCA GCG CCA AAC      192
Ile Asn Ala Tyr Thr Thr Gly Pro Cys Thr Pro Ser Pro Ala Pro Asn
     50                  55                  60
TAT TCT AGG GCG CTG TGG CGG GTG GCC GCT GAG GAG TAC GTG GAG GTC      240
Tyr Ser Arg Ala Leu Trp Arg Val Ala Ala Glu Glu Tyr Val Glu Val
 65                  70                  75                  80
ACG CGG GTG GGG GAT TTC CAC TAC GTG ACG GGC ATG ACC ACT GAC AAC      288
Thr Arg Val Gly Asp Phe His Tyr Val Thr Gly Met Thr Thr Asp Asn
                 85                  90                  95
GTA AAG TGC CCA TGC CAG GTT CCG GCT CCT GAA TTC TTC TCG GAG GTG      336
Val Lys Cys Pro Cys Gln Val Pro Ala Pro Glu Phe Phe Ser Glu Val
            100                 105                 110
GAC GGA GTG CGG TTG CAC AGG TAC GCT CCG GCG TGC AGG CCT CTC CTA      384
Asp Gly Val Arg Leu His Arg Tyr Ala Pro Ala Cys Arg Pro Leu Leu
        115                 120                 125
CGG GAG GAG GTT ACA TTC CAG GTC GGG CTC AAC CAA TAC CTG GTT GGG      432
Arg Glu Glu Val Thr Phe Gln Val Gly Leu Asn Gln Tyr Leu Val Gly
    130                 135                 140
TCA CAG CTA CCA TGC GAG CCC GAA CCG GAT GTA GCA GTG CTC ACT TCC      480
Ser Gln Leu Pro Cys Glu Pro Glu Pro Asp Val Ala Val Leu Thr Ser
145                 150                 155                 160
ATG CTC ACC GAC CCC TCC CAC ATC ACA GCA GAA ACG GCT AAG CGT AGG      528
Met Leu Thr Asp Pro Ser His Ile Thr Ala Glu Thr Ala Lys Arg Arg
                165                 170                 175
TTG GCC AGG GGG TCT CCC CCC TCC TTG GCC AGC TCT TCA GCT AGC CAG      576
Leu Ala Arg Gly Ser Pro Pro Ser Leu Ala Ser Ser Ser Ala Ser Gln
            180                 185                 190
TTG TCT GCG CCT TCC TTG AAG GCG ACA TGC ACT ACC CAC CAT GTC TCT      624
Leu Ser Ala Pro Ser Leu Lys Ala Thr Cys Thr Thr His His Val Ser
        195                 200                 205
CCG GAC GCT GAC CTC ATC GAG GCC AAC CTC CTG TGG CGG CAG GAG ATG      672
Pro Asp Ala Asp Leu Ile Glu Ala Asn Leu Leu Trp Arg Gln Glu Met
    210                 215                 220
GGC GGG AAC ATC ACC CGC GTG GAG TCG GAG AAC AAG GTG GTA GTC CTG      720
Gly Gly Asn Ile Thr Arg Val Glu Ser Glu Asn Lys Val Val Val Leu
225                 230                 235                 240
GAC TCT TTC GAC CCG CTT CGA GCG GAG GAG GAT GAG AGG GAA GTA TCC      768
Asp Ser Phe Asp Pro Leu Arg Ala Glu Glu Asp Glu Arg Glu Val Ser
                245                 250                 255
GTT CCG GCG GAG ATC CTG CGG AAA TCC AAG AAG TTC CCC GCA GCG ATG      816
Val Pro Ala Glu Ile Leu Arg Lys Ser Lys Lys Phe Pro Ala Ala Met
            260                 265                 270
CCC ATC TGG GCG CGC CCG GAT TAC AAC CCT CCA CTG TTA GAG TCC TGG      864
Pro Ile Trp Ala Arg Pro Asp Tyr Asn Pro Pro Leu Leu Glu Ser Trp
        275                 280                 285
AAG GAC CCG GAC TAC GTC CCT CCG GTG GTG CAC GGG TGC CCG TTG CCA      912
Lys Asp Pro Asp Tyr Val Pro Pro Val Val His Gly Cys Pro Leu Pro
    290                 295                 300
CCT ATC AAG GCC CCT CCA ATA CCA CCT CCA CGG AGA AAG AGG ACG GTT      960
Pro Ile Lys Ala Pro Pro Ile Pro Pro Pro Arg Arg Lys Arg Thr Val
305                 310                 315                 320
GTC CTA ACA GAG TCC TCC GTG TCT TCT GCC TTA GCG GAG CTC GCT ACT     1008
Val Leu Thr Glu Ser Ser Val Ser Ser Ala Leu Ala Glu Leu Ala Thr
                325                 330                 335
AAG ACC TTC GGC AGC TCC GAA TCA TCG GCC GTC GAC AGC GGC ACG GCG     1056
Lys Thr Phe Gly Ser Ser Glu Ser Ser Ala Val Asp Ser Gly Thr Ala
            340                 345                 350
ACC GCC CTT CCT GAC CAG GCC TCC GAC GAC GGT GAC AAA GGA TCC GAC     1104
Thr Ala Leu Pro Asp Gln Ala Ser Asp Asp Gly Asp Lys Gly Ser Asp
        355                 360                 365
GTT GAG TCG TAC TCC TCC ATG CCC CCC CTT GAG GGG GAA CCG GGG GAC     1152
Val Glu Ser Tyr Ser Ser Met Pro Pro Leu Glu Gly Glu Pro Gly Asp
    370                 375                 380
CCC GAT CTC AGT GAC GGG TCT TGG TCT ACC GTG AGC GAG GAA GCT AGT     1200
Pro Asp Leu Ser Asp Gly Ser Trp Ser Thr Val Ser Glu Glu Ala Ser
385                 390                 395                 400
GAG GAT GTC GTC TGC TGC TCA ATG TCC TAC ACA TGG ACA GGC GCC TTG     1248
Glu Asp Val Val Cys Cys Ser Met Ser Tyr Thr Trp Thr Gly Ala Leu
                405                 410                 415
ATC ACG CCA TGC GCT GCG GAG GAA AGC AAG CTG CCC ATC AAC GCG TTG     1296
Ile Thr Pro Cys Ala Ala Glu Glu Ser Lys Leu Pro Ile Asn Ala Leu
            420                 425                 430
AGC AAC TCT TTG CTG CGC CAC CAT AAC ATG GTT TAT GCC ACA ACA TCT     1344
Ser Asn Ser Leu Leu Arg His His Asn Met Val Tyr Ala Thr Thr Ser
        435                 440                 445
CGC AGC GCA GGC CTG CGG CAG AAG AAG GTC ACC TTT GAC AGA CTG CAA     1392
Arg Ser Ala Gly Leu Arg Gln Lys Lys Val Thr Phe Asp Arg Leu Gln
    450                 455                 460
GTC CTG GAC GAC CAC TAC CGG GAC GTG CTC AAG GAG ATG AAG GCG AAG     1440
Val Leu Asp Asp His Tyr Arg Asp Val Leu Lys Glu Met Lys Ala Lys
465                 470                 475                 480
GCG TCC ACA GTT AAG GCT AAA CTC CTA TCC GTA GAG GAA GCC TGC AAG     1488
Ala Ser Thr Val Lys Ala Lys Leu Leu Ser Val Glu Glu Ala Cys Lys
                485                 490                 495
CTG ACG CCC CCA CAT TCG GCC AAA TCC AAG TTT GGC TAT GGG GCA AAG     1536
Leu Thr Pro Pro His Ser Ala Lys Ser Lys Phe Gly Tyr Gly Ala Lys
            500                 505                 510
GAC GTC CGG AAC CTA TCC AGC AAG GCC GTT AAC CAC ATC CAC TCC GTG     1584
Asp Val Arg Asn Leu Ser Ser Lys Ala Val Asn His Ile His Ser Val
        515                 520                 525
TGG AAG GAC TTG CTG GAA GAC ACT GTG ACA CCA ATT GAC ACC ACC ATC     1632
Trp Lys Asp Leu Leu Glu Asp Thr Val Thr Pro Ile Asp Thr Thr Ile
    530                 535                 540
ATG GCA AAA AAT GAG GTT TTC TGT GTC CAA CCA GAG AAA GGA GGC CGT     1680
Met Ala Lys Asn Glu Val Phe Cys Val Gln Pro Glu Lys Gly Gly Arg
545                 550                 555                 560
AAG CCA GCC CGC CTT ATC GTA TTC CCA GAT CTG GGA GTC CGT GTA TGC     1728
Lys Pro Ala Arg Leu Ile Val Phe Pro Asp Leu Gly Val Arg Val Cys
                565                 570                 575
GAG AAG ATG GCC CTC TAT GAT GTG GTC TCC ACC CTT CCT CAG GTC GTG     1776
Glu Lys Met Ala Leu Tyr Asp Val Val Ser Thr Leu Pro Gln Val Val
            580                 585                 590
ATG GGC TCC TCA TAC GGA TTC CAG TAC TCT CCT GGG CAG CGA GTC GAG     1824
Met Gly Ser Ser Tyr Gly Phe Gln Tyr Ser Pro Gly Gln Arg Val Glu
        595                 600                 605
TTC CTG GTG AAT ACC TGG AAA TCA AAG AAA AAC CCC ATG GGC TTT TCA     1872
Phe Leu Val Asn Thr Trp Lys Ser Lys Lys Asn Pro Met Gly Phe Ser
    610                 615                 620
TAT GAC ACT CGC TGT TTC GAC TCA ACG GTC ACC GAG AAC GAC ATC CGT     1920
Tyr Asp Thr Arg Cys Phe Asp Ser Thr Val Thr Glu Asn Asp Ile Arg
625                 630                 635                 640
GTT GAG GAG TCA ATT TAC CAA TGT TGT GAC TTG GCC CCC GAA GCC AGA     1968
Val Glu Glu Ser Ile Tyr Gln Cys Cys Asp Leu Ala Pro Glu Ala Arg
                645                 650                 655
CAG GCC ATA AAA TCG CTC ACA GAG CGG CTT TAT ATC GGG GGT CCT CTG     2016
Gln Ala Ile Lys Ser Leu Thr Glu Arg Leu Tyr Ile Gly Gly Pro Leu
            660                 665                 670
ACT AAT TCA AAA GGG CAG AAC TGC GGT TAT CGC CGG TGC CGC GCG AGC     2064
Thr Asn Ser Lys Gly Gln Asn Cys Gly Tyr Arg Arg Cys Arg Ala Ser
        675                 680                 685
GGC GTG CTG ACG ACT AGC TGC GGT AAC ACC CTC ACA TGT TAC TTG AAG     2112
Gly Val Leu Thr Thr Ser Cys Gly Asn Thr Leu Thr Cys Tyr Leu Lys
    690                 695                 700
GCC TCT GCA GCC TGT CGA GCT GCG AAG CTC CAG GAC TGC ACG ATG CTC     2160
Ala Ser Ala Ala Cys Arg Ala Ala Lys Leu Gln Asp Cys Thr Met Leu
705                 710                 715                 720
GTG AAC GGA GAC GAC CTC GTC GTT ATC TGT GAA AGC GCG GGA ACC CAA     2208
Val Asn Gly Asp Asp Leu Val Val Ile Cys Glu Ser Ala Gly Thr Gln
                725                 730                 735
GAG GAC GCG GCG AGC CTA CGA GTC TTC ACG GAG GCT ATG ACT AGG TAC     2256
Glu Asp Ala Ala Ser Leu Arg Val Phe Thr Glu Ala Met Thr Arg Tyr
            740                 745                 750
TCC GCC CCC CCC GGG GAC CCG CCC CAA CCA GAA TAC GAC TTG GAG CTG     2304
Ser Ala Pro Pro Gly Asp Pro Pro Gln Pro Glu Tyr Asp Leu Glu Leu
        755                 760                 765
ATA ACA TCA TGT TCC TCC AAT GTG TCG GTC GCC CAC GAT GCA TCA GGC     2352
Ile Thr Ser Cys Ser Ser Asn Val Ser Val Ala His Asp Ala Ser Gly
    770                 775                 780
AAA AGG GTG TAC TAC CTC ACC CGT GAT CCC ACC ACC CCC CTA GCA CGG     2400
Lys Arg Val Tyr Tyr Leu Thr Arg Asp Pro Thr Thr Pro Leu Ala Arg
785                 790                 795                 800
GCT GCG TGG GAG ACA GCT AGA CAC ACT CCA GTT AAC TCC TGG CTA GGC     2448
Ala Ala Trp Glu Thr Ala Arg His Thr Pro Val Asn Ser Trp Leu Gly
                805                 810                 815
AAC ATT ATT ATG TAT GCG CCC ACT TTG TGG GCA AGG ATG ATT CTG ATG     2496
Asn Ile Ile Met Tyr Ala Pro Thr Leu Trp Ala Arg Met Ile Leu Met
            820                 825                 830
ACT CAC TTC TTC TCC ATC CTT CTA GCG CAG GAG CAA CTT GAA AAA GCC     2544
Thr His Phe Phe Ser Ile Leu Leu Ala Gln Glu Gln Leu Glu Lys Ala
        835                 840                 845
CTG GAC TGC CAG ATC TAC GGG GCC TGT TAC TCC ATT GAG CCA CTT GAC     2592
Leu Asp Cys Gln Ile Tyr Gly Ala Cys Tyr Ser Ile Glu Pro Leu Asp
    850                 855                 860
CTA CCT CAG ATC ATT GAA CGA CTC CAT GGC CTT AGC GCA TTT TCA CTC     2640
Leu Pro Gln Ile Ile Glu Arg Leu His Gly Leu Ser Ala Phe Ser Leu
865                 870                 875                 880
CAT AGT TAC TCT CCA GGT GAG ATC AAT AGG GTG GCT TCA TGC CTC AGG     2688
His Ser Tyr Ser Pro Gly Glu Ile Asn Arg Val Ala Ser Cys Leu Arg
                885                 890                 895
AAA CTT GGG GTA CCA CCC TTG CGA GTC TGG AGA CAT CGG GCC AGG AGC     2736
Lys Leu Gly Val Pro Pro Leu Arg Val Trp Arg His Arg Ala Arg Ser
            900                 905                 910
GTC CGC GCT AGG CTA CTG TCC CAG GGA GGG AGG GCC GCC ACT TGT GGC     2784
Val Arg Ala Arg Leu Leu Ser Gln Gly Gly Arg Ala Ala Thr Cys Gly
        915                 920                 925
AAA TAC CTC TTC AAC TGG GCA GTA AAA ACC AAA CTT AAA CTC ACT CCA     2832
Lys Tyr Leu Phe Asn Trp Ala Val Lys Thr Lys Leu Lys Leu Thr Pro
    930                 935                 940
ATC CCG GCT GCG TCC CGG CTG GAC TTG TCC GGC TGG TTC GTT GCT GGT     2880
Ile Pro Ala Ala Ser Arg Leu Asp Leu Ser Gly Trp Phe Val Ala Gly
945                 950                 955                 960
TAC AGC GGG GGA GAC ATA TAT CAC AGC CTG TCT CGT GCC CGA CCC CGT     2928
Tyr Ser Gly Gly Asp Ile Tyr His Ser Leu Ser Arg Ala Arg Pro Arg
                965                 970                 975
TGG TTC ATG CTG TGC CTA CTC CTA CTT TCT GTA GGG GTA GGC ATC TAC     2976
Trp Phe Met Leu Cys Leu Leu Leu Leu Ser Val Gly Val Gly Ile Tyr
            980                 985                 990
CTG CTC CCC AAC CGA                                                 2991
Leu Leu Pro Asn Arg
        995 
           
           
             
               997 amino acids 
               amino acid 
               linear 
             
             
               protein 
             
             
               unknown 
             
             50
Gly Tyr Lys Gly Val Trp Arg Gly Asp Gly Ile Met Gln Thr Thr Cys
  1               5                  10                  15
Pro Cys Gly Ala Gln Ile Thr Gly His Val Lys Asn Gly Ser Met Arg
             20                  25                  30
Ile Val Gly Pro Lys Thr Cys Ser Asn Thr Trp His Gly Thr Phe Pro
         35                  40                  45
Ile Asn Ala Tyr Thr Thr Gly Pro Cys Thr Pro Ser Pro Ala Pro Asn
     50                  55                  60
Tyr Ser Arg Ala Leu Trp Arg Val Ala Ala Glu Glu Tyr Val Glu Val
 65                  70                  75                  80
Thr Arg Val Gly Asp Phe His Tyr Val Thr Gly Met Thr Thr Asp Asn
                 85                  90                  95
Val Lys Cys Pro Cys Gln Val Pro Ala Pro Glu Phe Phe Ser Glu Val
            100                 105                 110
Asp Gly Val Arg Leu His Arg Tyr Ala Pro Ala Cys Arg Pro Leu Leu
        115                 120                 125
Arg Glu Glu Val Thr Phe Gln Val Gly Leu Asn Gln Tyr Leu Val Gly
    130                 135                 140
Ser Gln Leu Pro Cys Glu Pro Glu Pro Asp Val Ala Val Leu Thr Ser
145                 150                 155                 160
Met Leu Thr Asp Pro Ser His Ile Thr Ala Glu Thr Ala Lys Arg Arg
                165                 170                 175
Leu Ala Arg Gly Ser Pro Pro Ser Leu Ala Ser Ser Ser Ala Ser Gln
            180                 185                 190
Leu Ser Ala Pro Ser Leu Lys Ala Thr Cys Thr Thr His His Val Ser
        195                 200                 205
Pro Asp Ala Asp Leu Ile Glu Ala Asn Leu Leu Trp Arg Gln Glu Met
    210                 215                 220
Gly Gly Asn Ile Thr Arg Val Glu Ser Glu Asn Lys Val Val Val Leu
225                 230                 235                 240
Asp Ser Phe Asp Pro Leu Arg Ala Glu Glu Asp Glu Arg Glu Val Ser
                245                 250                 255
Val Pro Ala Glu Ile Leu Arg Lys Ser Lys Lys Phe Pro Ala Ala Met
            260                 265                 270
Pro Ile Trp Ala Arg Pro Asp Tyr Asn Pro Pro Leu Leu Glu Ser Trp
        275                 280                 285
Lys Asp Pro Asp Tyr Val Pro Pro Val Val His Gly Cys Pro Leu Pro
    290                 295                 300
Pro Ile Lys Ala Pro Pro Ile Pro Pro Pro Arg Arg Lys Arg Thr Val
305                 310                 315                 320
Val Leu Thr Glu Ser Ser Val Ser Ser Ala Leu Ala Glu Leu Ala Thr
                325                 330                 335
Lys Thr Phe Gly Ser Ser Glu Ser Ser Ala Val Asp Ser Gly Thr Ala
            340                 345                 350
Thr Ala Leu Pro Asp Gln Ala Ser Asp Asp Gly Asp Lys Gly Ser Asp
        355                 360                 365
Val Glu Ser Tyr Ser Ser Met Pro Pro Leu Glu Gly Glu Pro Gly Asp
    370                 375                 380
Pro Asp Leu Ser Asp Gly Ser Trp Ser Thr Val Ser Glu Glu Ala Ser
385                 390                 395                 400
Glu Asp Val Val Cys Cys Ser Met Ser Tyr Thr Trp Thr Gly Ala Leu
                405                 410                 415
Ile Thr Pro Cys Ala Ala Glu Glu Ser Lys Leu Pro Ile Asn Ala Leu
            420                 425                 430
Ser Asn Ser Leu Leu Arg His His Asn Met Val Tyr Ala Thr Thr Ser
        435                 440                 445
Arg Ser Ala Gly Leu Arg Gln Lys Lys Val Thr Phe Asp Arg Leu Gln
    450                 455                 460
Val Leu Asp Asp His Tyr Arg Asp Val Leu Lys Glu Met Lys Ala Lys
465                 470                 475                 480
Ala Ser Thr Val Lys Ala Lys Leu Leu Ser Val Glu Glu Ala Cys Lys
                485                 490                 495
Leu Thr Pro Pro His Ser Ala Lys Ser Lys Phe Gly Tyr Gly Ala Lys
            500                 505                 510
Asp Val Arg Asn Leu Ser Ser Lys Ala Val Asn His Ile His Ser Val
        515                 520                 525
Trp Lys Asp Leu Leu Glu Asp Thr Val Thr Pro Ile Asp Thr Thr Ile
    530                 535                 540
Met Ala Lys Asn Glu Val Phe Cys Val Gln Pro Glu Lys Gly Gly Arg
545                 550                 555                 560
Lys Pro Ala Arg Leu Ile Val Phe Pro Asp Leu Gly Val Arg Val Cys
                565                 570                 575
Glu Lys Met Ala Leu Tyr Asp Val Val Ser Thr Leu Pro Gln Val Val
            580                 585                 590
Met Gly Ser Ser Tyr Gly Phe Gln Tyr Ser Pro Gly Gln Arg Val Glu
        595                 600                 605
Phe Leu Val Asn Thr Trp Lys Ser Lys Lys Asn Pro Met Gly Phe Ser
    610                 615                 620
Tyr Asp Thr Arg Cys Phe Asp Ser Thr Val Thr Glu Asn Asp Ile Arg
625                 630                 635                 640
Val Glu Glu Ser Ile Tyr Gln Cys Cys Asp Leu Ala Pro Glu Ala Arg
                645                 650                 655
Gln Ala Ile Lys Ser Leu Thr Glu Arg Leu Tyr Ile Gly Gly Pro Leu
            660                 665                 670
Thr Asn Ser Lys Gly Gln Asn Cys Gly Tyr Arg Arg Cys Arg Ala Ser
        675                 680                 685
Gly Val Leu Thr Thr Ser Cys Gly Asn Thr Leu Thr Cys Tyr Leu Lys
    690                 695                 700
Ala Ser Ala Ala Cys Arg Ala Ala Lys Leu Gln Asp Cys Thr Met Leu
705                 710                 715                 720
Val Asn Gly Asp Asp Leu Val Val Ile Cys Glu Ser Ala Gly Thr Gln
                725                 730                 735
Glu Asp Ala Ala Ser Leu Arg Val Phe Thr Glu Ala Met Thr Arg Tyr
            740                 745                 750
Ser Ala Pro Pro Gly Asp Pro Pro Gln Pro Glu Tyr Asp Leu Glu Leu
        755                 760                 765
Ile Thr Ser Cys Ser Ser Asn Val Ser Val Ala His Asp Ala Ser Gly
    770                 775                 780
Lys Arg Val Tyr Tyr Leu Thr Arg Asp Pro Thr Thr Pro Leu Ala Arg
785                 790                 795                 800
Ala Ala Trp Glu Thr Ala Arg His Thr Pro Val Asn Ser Trp Leu Gly
                805                 810                 815
Asn Ile Ile Met Tyr Ala Pro Thr Leu Trp Ala Arg Met Ile Leu Met
            820                 825                 830
Thr His Phe Phe Ser Ile Leu Leu Ala Gln Glu Gln Leu Glu Lys Ala
        835                 840                 845
Leu Asp Cys Gln Ile Tyr Gly Ala Cys Tyr Ser Ile Glu Pro Leu Asp
    850                 855                 860
Leu Pro Gln Ile Ile Glu Arg Leu His Gly Leu Ser Ala Phe Ser Leu
865                 870                 875                 880
His Ser Tyr Ser Pro Gly Glu Ile Asn Arg Val Ala Ser Cys Leu Arg
                885                 890                 895
Lys Leu Gly Val Pro Pro Leu Arg Val Trp Arg His Arg Ala Arg Ser
            900                 905                 910
Val Arg Ala Arg Leu Leu Ser Gln Gly Gly Arg Ala Ala Thr Cys Gly
        915                 920                 925
Lys Tyr Leu Phe Asn Trp Ala Val Lys Thr Lys Leu Lys Leu Thr Pro
    930                 935                 940
Ile Pro Ala Ala Ser Arg Leu Asp Leu Ser Gly Trp Phe Val Ala Gly
945                 950                 955                 960
Tyr Ser Gly Gly Asp Ile Tyr His Ser Leu Ser Arg Ala Arg Pro Arg
                965                 970                 975
Trp Phe Met Leu Cys Leu Leu Leu Leu Ser Val Gly Val Gly Ile Tyr
            980                 985                 990
Leu Leu Pro Asn Arg
        995