lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4-alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6-glucosidase in glycogen degradation.
Subcellular Localization:
Cytoplasm.
Sequence:
MRISNNNSESGNCGVEYTKLIDSFSEKIRIKDHCVNISTNTSTETKNNNSNINQDIYTITLVGNGSEPPFNAKGLVLPSLGTLRIIIPAGLEVASYNPQIYTNYHHGTDPTSSFQRDKFYIFHKGNIIGYNGNNDLIFEQKIEKYGCFDYYVEWEEVASKNVKCGQIGTFQINPMLKINQQVIPSESICLQTFLTKCMGSIDQWEKHIETASKLGFNMIHYTPVQEIGESGSSYSIYDQQSISSKIFEGGMNRKIINEDEKLLALSSFISDAEKKYGVLGMIDLVWNHTANNSAWLNQHPEAGYNTDNSPHLKSAVQLDQALQDYGKTLYGKEINNIDQLNDVINDVKTKVLPPLKLWEYYVLDIEKEVEIFKNTFFSSGRVKEQIPSSCSTFSPSFLKNIISNPNHEKHEQIKSISKNGIIRAPSYERYSLHINLDYTYKVLDTSVTFSNNSSPEEQIQKYRDILSIVNLEIYKDFDHDTEAILKNIFERIKYERVSDHGPKLGKITKSKPLLTSYFTIVQYRDPNNSSIREIPLANNGWIFNHNPTVDFASSESRAYLRRDVIVWGDCVKMRYGQSPSDNQWLWNHMKTYTQNMARIFHAIRIDNCHSTPIHLAQYLLDAAREIRPDIYITCELFTGSEEIDYFFVKKLGINSLIREAMQCGDSSEFTRVLYRYGGRPIGSIQEPPIGEYLNGCCSRNLGGGIISPNDYASKSLKPSLPPALFMDCTHDNETPHQKRTIADTLSNAAIVAMSACAIGSTRGYDEIFPKTIDLVNETRVYNTNVNLSSGILPIRSLLSKIHLELSCNGFDEIHIHQDGNLIFIQRYSPKLNESIFMVAHCSFSNQQQQQQQDNDKELHVPCKISQFLFGAKITNTHINRNDWNTNTTKLNGIEVDCEIHYHDKVLNQFCQIHEYNNENGALCTTLKLNNFKAGSILFFRGEIPKPNIESIRKIEQLILDENNQLCKSFDNVDLIDMNVLLFRINEEEKQVIGHGAYHVQNPVGELSFCGLQGFVTELNQIAKHNDLGNQLCGNLRKGNWAIDYIVNRLDQRVALKSVKQWLTQCFDQLKQLPRHLIPMYFYQIIMTTYRFATNKSIEKMGNSFVKESDSWFSRALALTSIQFFGVSTPLISNPNVLEGVKDREASLAAGFPHFATGYMRSWGRDTFISLRGILLVTNRYREAINIIVGFGSCLRFGLIPNLLDCGTKPRFNSRDSVWWYLRSIQDTYNCLPTEKEKDQFLNQTKVYRLFPPTNYISPISTIAEIIQEILQAHASGIHFREPNAGREIDDRMRDEGFNISIDLNLTNGFLYGGNRSNCGTWMDKMGESTKANNYGEPATPRDGAPIEITAMLYSTLSWISDLYKLDKFKHGGVEILKSKDNNDNNNNNNSKTDILTYQDWSKLIETNFEKYYYVPSSGDDKKYIINSNYVHRRFIYKDVVGSANVFSDYQLRPNICVAMSFAPKLFNDQHANKCIDIIRNSLVGPIGMKTLDPNDPNYHGNYDNSSDSGYKPTSRGFNYHNGPEWVWCYGFFLESIVQFKQFPSISTKNHLINSLLIKHKLYIQNDKRFSLPELTNREGSFCKDSCDSQAWSIATILASPYQLSITKN
The following text describes a protein:
Function:
As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs.
Sequence:
MPRDRDEPAAVRVYTVCDESRYLIVRNVPSLGCGDDLASLFGTYGPVEECTPMDAEDSEPYTDVFFVKFSQVNNASSSLPAAQVLPSFLAVKVQNQRPPFEMQNWCSCCRFAKRKLDESVFLGNRLQVTYAPQFESPQDTKEKLEVRRKEVLGRIKSSAGRPEGSSPAQGSSSGNHHQMNSNKREYMKTIHASPIEDPRFSHVSSDKDYFPSESMNATVKLVRGKLDKIQSGGDNSSTSAASRKPGVDKRRRI
The following text describes a protein:
Function:
Involved in double-stranded break repair. Plays a central role in genetic recombination and DNA repair by promoting the annealing of complementary single-stranded DNA and by stimulation of the RAD51 recombinase.
Sequence:
NVFLCLVQCQYTADEYQAIQAALRQRLGPEYISSRQAGGGQKVCYIEGHRVISLANEMFGYNGWAHSVTQQNVDFVDLNNGKFYVGVCAFVKVQLKDGAYHEDVGYGVSEGLKSKALSLEKARKEAVTDGLKRALKCFGNALGNCILDKDYLRSVNKLPRQIPPDLDLSKAKRQDFEPVVEKARYDSCLQKASKGQNHLSAITPGSSDQWNSSRSMVEQDQQNRLVLWSDFSSHFAMGMHSESLKFNSVCVTVXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXNVLFWGSEH
The following text describes a protein:
Function:
Transcription regulator involved in gene regulation during late embryogenesis. Its expression to the epidermis is sufficient to control foliar organ identity by regulating positively the synthesis abscisic acid (ABA) and negatively gibberellin production. Negatively regulates TTG1 in the embryo. Positively regulates the abundance of the ABI3 protein in the seed. Cooperates with KIN10 to regulate developmental phase transitions and lateral organ development and act both as positive regulators of abscisic acid (ABA) signaling during germination.
Subcellular Localization:
Nucleus.
Sequence:
MMVDENVETKASTLVASVDHGFGSGSGHDHHGLSASVPLLGVNWKKRRMPRQRRSSSSFNLLSFPPPMPPISHVPTPLPARKIDPRKLRFLFQKELKNSDVSSLRRMILPKKAAEAHLPALECKEGIPIRMEDLDGFHVWTFKYRYWPNNNSRMYVLENTGDFVNAHGLQLGDFIMVYQDLYSNNYVIQARKASEEEEVDVINLEEDDVYTNLTRIENTVVNDLLLQDFNHHNNNNNNNSNSNSNKCSYYYPVIDDVTTNTESFVYDTTALTSNDTPLDFLGGHTTTTNNYYSKFGTFDGLGSVENISLDDFY
The following text describes a protein:
Function:
Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability (By similarity).
Miscellaneous:
MISCELLANEOUS: The atypical heteromeric and topological design of the odorant receptors appears to be an insect-specific solution for odor recognition, making the OR/Orco complex an attractive target for the development of highly selective insect repellents to disrupt olfactory-mediated host-seeking behaviors of insect disease vectors. Odor-evoked OR currents are independent of known G-protein-coupled second messenger pathways.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MVTEDFYKYQVWYFQILGVWQLPTWAADHQRRFQSMRFGFILVILFIMLLLFSFEMLNNISQVREILKVFFMFATEISCMAKLLHLKLKSRKLAGLVDAMLSPEFGVKSEQEMQMLELDRVAVVRMRNSYGIMSLGAASLILIVPCFDNFGELPLAMLEVCSIEGWICYWSQYLFHSICLLPTCVLNITYDSVAYSLLCFLKVQLQMLVLRLEKLGPVIEPQDNEKIAMELRECAAYYNRIVRFKDLVELFIKGPGSVQLMCSVLVLVSNLYDMSTMSIANGDAIFMLKTCIYQLVMLWQIFIICYASNEVTVQSSRLCHSIYSSQWTGWNRANRRIVLLMMQRFNSPMLLSTFNPTFAFSLEAFGSIVNCSYSYFALLKRVNS
The following text describes a protein:
Function:
Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate.
Subcellular Localization:
Cytoplasm.
Sequence:
MIKILADDRIPFVSELFGDFGELILKPGAHIQNRDLLAVNALLTRSITSVDSALLEGTAVEFVGSATAGFDHIDSTWLKKQSIHWAYAPGANATAVAEYVLHCVAYLHKKNLLPRKSATAAIIGVGHVGCVVSDRLRKIGFTVFHNDPPRAQLEKDFISVPLASLANVDLVCLHTPLVKTGNFPTYHLIDNRFLKMLKPGSVLLNAGRGAVIDNNALLQCDHVITCLDVWENEPTVNLQLLEKTTIATPHIAGYSKQAKLRATLMIYDAFLKYFHLSDTRRFSELQQLQETMTLNIQDGRNAEDILLTLFDPGRESQRMRETLAENPDQFEYLRRHFPLRNEFSAIQLTPTPSALLRKELDDWGFK
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MSQLILFFFVNQVIFAFIVLTILIYAFNKYILPRLLYIYTTHKKVIKNKVKVLNNDINKTCEFLEITLVEKIIIRINTVKIITIFLIRPLIKKLLDILQEILQQLGYSIGAVPENIIYYISILVGFIMLLGIFEFELLNWIKSLKPNLGIMECLINYIKTNKIQATIKSIGPGVLTNIKCVDKEGRILGPDGSLLGEENKGNIYEYYIQDEVIVRSDGFKRGFYDKDWGIASEEMPKGSNYTNKCKVHNTKVEIVNNKINYLRDWAAHLKNNYTFEFIVCPNYRINNEQINIAINHINEHMKVYDQLNELITRYNNYYNHIKIKKPYLPLVLPPLNVEADRDLIRSLENLEQHLKIQKDNSNLSS
The following text describes a protein:
Function:
Essential for plant growth, promotes cell division in root meristems. Catalyzes the biosynthesis of ceramide sphingolipids with C(16) to C(28) fatty acids, structural membrane lipids involved in membrane trafficking (e.g. early endosomes) and cell polarity (e.g. polar auxin transport related proteins); mostly active with t18:0 and saturated very long saturated fatty acids (C24:0 and C26:0), such as long-chain base (LCB) phytosphingosine (t18:0), lignoceroyl- and hexacosanoyl-CoAs. Mediates resistance to sphinganine-analog mycotoxins (SAMs, e.g. fumonisin B(1)) by restoring the sphingolipid biosynthesis (By similarity). Could salvage the transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi apparatus in ceramides-depleted cells after SAM exposure (By similarity). May prevent precocious cell death by delaying PR1 accumulation during aging. Contributes to hypoxic conditions tolerance (e.g. submergences), especially in the dark, by promoting the formation of very-long-chain (VLC) ceramide species (22:1, 24:1 and 26:1) and of VLC unsaturated ceramides, which are modulating CTR1-mediated ethylene signaling leading to endoplasmic reticulum (ER)-to-nucleus translocation of EIN2 and EIN3.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGLFESVKSIDWEQESFPTYQDLGFLPLFAVFFPTIRFLLDRFVFEKLASLVIYGRMSTNKSDNIKDRKKNSPKVRKFKESAWKCIYYLSAELLALSVTYNEPWFSNTLYFWIGPGDQIWPDQPMKMKLKFLYMFAAGFYTYSIFALVFWETRRSDFGVSMGHHITTLVLIVLSYICRLTRAGSVILALHDASDVFLEIGKMSKYCGAESLASISFVLFALSWVVLRLIYYPFWILWSTSYQIIMTVDKEKHPNGPILYYMFNTLLYFLLVLHIFWWVLIYRMLVKQVQDRGKLSEDVRSDSESDDEHED
The following text describes a protein:
Function:
Activates the small RNA gene sgrS under glucose-phosphate stress conditions as well as yfdZ. Represses its own transcription under both stress and non-stress conditions. Might act as a sensor of the intracellular accumulation of phosphoglucose by binding these molecules in its C-terminal solute-binding domain.
Sequence:
MPSGRLQQQFIRLWQCCDGKTQDTTLNELADLLNCSRRHMRTLLNTMQARGWLTWEAEVGRGKRSRLTFLYTGLALQQQRAEDLLEQDRIDQLVQLVGDKSAVRQMLISHLGRSFRQGRHILRVLYYRPMHNLLPGTALRRSETHIARQIFSSLTRVNEENGELEADIAHHWQQISPLLWRFYLRPGIHFHHGRELEMEDVISSLTRINTLPLYSHITKIDSPTAWTLDIHLSQPDRWLPWLLGQVPAMILPRKWETLANFASHPIGTGPYAVRRNTPNQLKILAFDDYFGYRALIDEVNVWVLPDISEEPACGLMLEGPIQGGEKAIESRLEEGCYYLLFDARTPRGAHPQVREWVSHVLSPTNLLYHADEPLQQLWFPAYGLLPRWHHARPGPGEKPAGLETLTLTFYREHIEHRVIARIMSALLAEHQVHLHIQEIDYDQWHAGEIESDIWLNSANFTLPLDFSLFAHLCEVPLLQNCIPRDWQGDAAQWRAGEMNLANWCQQLLANKAIVPLIHHWLIIQGQRSMRGLRMNTLGWFDFKSAWFAPPDP
The following text describes a protein:
Function:
Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.
Subcellular Localization:
Cytoplasm. Rough endoplasmic reticulum.
Sequence:
MSQVQVQVQNPSAALSGSQILNKNQSLLSQPLMSIPSTASSLPSENAGRPIQNSALPSASLTSTSAAAESITPTVELNALCMKLGKKPMYKPVDPYSRMQSTYNYNMRGGAYPPRYFYPFPVPPLLYQVELSVGGQQFNGKGKTRQAAKHDAAAKALRILQSEPPSERLEVNGRESEEENLNKSEISQVFEIALKRNLPVNFEVARESGPPHMKSFVTRVSVGEFVGEGEGKSKKISKKNAAIAVLEELKKLPPLPTVERVKPRIKKKTKSIVRLQGGPECGQGMNPISRLAQIQQAKKEKEPEYLLLAERGLPRRREFVMQVKVGNHTAEGSGTNKKVAKRNAAENMLEILGFKVPQAQPSKPALKSEEKTPIKKPGDGRKVTFFEPGSGDENGTSNKEDEFRMPYLSHQQLPAGILPMVPEVAQAVGVSQGHHTKDFARVAPNPAKATVTAMIARELLYGGTSPTAETILKSNISSGHAPHGPLTRPSEQLDYLCTVQGFQVEYKDFPKNNKNEFVSLINCSSQPPLISHGIGKDVESCHDMAALNILKLLSELDQQNTEMPRTGNGPMSVCGRC
The following text describes a protein:
Function:
Lectin which binds carbohydrates in vitro. Interacts through its lectin domain with glycan structures containing one or more Lewis X, Lewis Y or lactosamine motifs. May play a role in abiotic stress responses (Probable). May play a role in abscisic acid-induced stomatal closure. May play a role in disease resistance against Pseudomonas syringae through its involvement in stomatal movement.
Miscellaneous:
MISCELLANEOUS: Plants silencing EULS3 exhibit an aberrant abscisic acid-induced stomatal closure.
Subcellular Localization:
Nucleus. Cytoplasm.
Domain:
The ricin B-type lectin domain binds glycan structures.
Sequence:
MEHHHQHHRHHQRDDGEDDRQSFGVPPPHVDAPPQPHGLYQSQPHFDPYAPTPQAPAPYRSETQFEPHAPPPYRSEPYFETPAPPPSFGHVSHVGHQSPNESYPPEHHRYGGYQQPSNSLLESHGDHSGVTHVAHHSSNQPQSSSGVYHKPDENRLPDNLAGLAGRATVKVYSKAEPNYNLTIRDGKVILAPADPSDEAQHWYKDEKYSTKVKDADGHPCFALVNKATGEAMKHSVGATHPVHLIRYVPDKLDESVLWTESKDFGDGYRTIRMVNNTRLNVDAYHGDSKSGGVRDGTTIVLWDWNKGDNQLWKIFPF
The following text describes a protein:
Function:
G-protein-coupled receptor for histamine, a biogenic amine that functions as an immune modulator and a neurotransmitter. Through the H1 receptor, histamine mediates the contraction of smooth muscles and increases capillary permeability due to contraction of terminal venules. Also mediates neurotransmission in the central nervous system and thereby regulates circadian rhythms, emotional and locomotor activities as well as cognitive functions.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
IDNSFNGTWKKQSDAEERRLNNSSVTFHNHINDALLGLVLGTVSLLTVIMNILVLYAVKKERTLHTVGNLYIVSLSVADLIVGATVMPLSIVYLLEKEWRLGNMVCQFWLVMDYVASTASIFSLFILCVDRYRSVRQPLRYLKYRTRARASVMISGAWLLSMTWVIPILGWRTFSDVDPQPETENKCDTDFRFVTWFKVLTAVLNFYVPSVLMLWFYAQIYMAVRKHYRQREIIKESKPSSYNRNCFANNCKISGKRRKTDAALFTIPKHQKQLQEDMFLTDKEKHPLASLGTQGDTNEQHLAMGPETPLKVACLPLGILQSENEDVNAMFVSVSDCNLIVPNSVAGVCEITDISDVQRFATVLCKDEFSHPEPPSWSHSSSPKVDTASVNNLKQSWQKFCSQSKQYVQSLRISKERKAAKQLGFIIAGFMVCWIPYFVTFMVMAFCKTCVHHDLHMFTIWLGYINSTLNPFIYPLCNENFKKIFKNIL
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MEQEDLTTMSFKDTAFLQLLGLNEHNALDYFSMSQFYDKSCLNEQLKMQVRHNELQAQQLDGRQMKGLEYTLWYFTPQPSLYVIRKQTRLSPTRVDLVAVYYIVEGTIYQSPTLCQVLANRVRTSLYFTKDALHVARESYRYNPILGHTWSNEPDLFEQLQTSLEKKQQLRSNATISDTACSSDMDMDVSKPCADELTSTANVVSLDEQHRAEIFSMTVDQLIASTETWSANAPPVSTSMDNKPETISRIHTRHTNDSPLATMEIKKEHSSPGIAKVASQQSKTSSGKRMSIQ
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MAPPPRLAAPLLLLLLVGACGSAARADLVISRADRKVDLTSHIVRVLTSLKVENAGSEPVSKVLLAFPNIQSKNLAAIRAFGTEGKVKGLSSILPIEVVEPSGVPPELTFFSALLNKPLEKGKILHLDVLTVFTHFLQPFPEEITQADSQLVVFQDSSHYLSPYPVKVQTLSIRLPGGRVESYTKYGNTKLVESELKYGPYEDVPPFSYNPIIVHFENNNPFAVAKELIREIEISHWGNVQITEHYNIVHGGARLKGEFSRLDYQSRPYARGVSSFRHLIARLPPRAHSIYYRDEIGNISTSHLWSDSKKTQLEIEPRFPLFGGWQTTFTIGYGLPLEDFVFSSDGRRFLNITFGSPMEEILIEKLIVKVVLPEGSKDFDVSAPFPANQWQEVKYSHLDIAGRPVLILEKADVIPEHNLHFQVYYKFNNISLLIEPMMLITGFFLLFVACIAYMHTDMSISKNSPSYLAKLQWDEVQATVQQIQGIFEQCLAVHDKLEISLHDLSRTGDTKSCKATRKAADAQFKELAKELKPLLLSVQSSPQSYLIWPKLEDLVAKEREMQEKLMARHATVVDSFEKKQRGQDIENRIASQQQKIAALRQEVESLLEYLSEI
The following text describes a protein:
Function:
O-linked mannose beta-1,4-N-acetylglucosaminyltransferase that transfers UDP-N-acetyl-D-glucosamine to the 4-position of the mannose to generate N-acetyl-D-glucosamine-beta-1,4-O-D-mannosylprotein. Involved in the biosynthesis of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MAGVVTRPPVGNRDFASFALCTGAYLYASTKRMVNDMKQSAIFPVIFHVCVFLALQITYNVVVQQWNVDLSKLTVATTSCKSKKVSKLSSFESLRLGSSVWCSGTSKSDRICKFKNLCYHPVHKEYMFFHGLNSVIDGVPKDRFNPALLDLSSVDDHNVQYFNYVDFPAHSLDAYENVTIFDGNNYIFHRFHPDNIMHAIHDDLLPLFHTMKQYSNSGSSQIDLNSRLVFMEGYELGPYSELYQLFSRLQLVIKDNLTVNNTLKCFQNAVVGLSKFTTWYQYGFDQIQGPLPEIQITAKQIYEFTRFVRERLGINESVSHTQSPQVVLCTRHHNRLILNDQEISNAIITKMNKRVAKVSFETHSLERMIRIIGRSSGLIGMHGSILVMAMFLPQGSFLMELFPYGVVPWNYRPYKTLAGLPGMNLVYQDWINTNEENTVTHPDRLPAFGGIAHLSKDEQEDIINTKEVPLHYCCNDPYWLYRIYQDTKIDIDSFSASLNTAIEGSHKLFTQGFQAANELLLPGKVLNVSCVVPEGGHTVPALAISWKPPINVQYFENFTVQYEVWIQKEVARDYLAYILAPTEYVFTEGLVRHTKYRIWVRCLVNDLVGPFGVMGSCTTE
The following text describes a protein:
Function:
Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate.
Subcellular Localization:
Cytoplasm.
Sequence:
MNGDQKLDAYARERQDFIQHFSQIVKVLTEEDIGHPEIGDAVARLKEVLEYNVVGGKYNRGITVLVVFRELVEPRKQDADSLQRALTVGWCIELLQAFFLVADDIEDSSLTRRGQTCWYRKPGIGLDAINDAFLLEACIYRLLKFYCREQPYYLNLIELFLQTSYNTEIGQTLDLIAGPQGNVDLSRFTEKRYKSIVKYKTAFYSFYLPVAAAMYMAGIDGEKEHANAKKILMEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQDNKCSWLVVQCLQRASPEQRQILQENYGQKDAEKVARVKALYEEMNLQAVFLQYEEDSYSHLMGLIEQYAAPLPPAIFLELAHKIYKRRK
The following text describes a protein:
Function:
Probably binds to the DNA sequence 5'-TGAC-3'.
Subcellular Localization:
Nucleus.
Sequence:
ADRELKEMLLKKYSGCLSRLRSEFLKKRKKGKLPKDARSALMDWWNTHYRWPYPTEEDKVRLAAATGLDPKQINNWFINQRKRHWKPS
The following text describes a protein:
Function:
Mediates the reversible addition of palmitate to target proteins, thereby regulating their membrane association and biological function.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The DHHC domain is required for palmitoyltransferase activity.
Sequence:
MITFSNPWIGVIIPCIIIFTLSTFSAIYILPHHVSNNELTLFICASAMVWISYIIAIIVPPGSPPKNYTPPENGMKMYCLKCKAYKPERTHHSKALGVCVLKMDHHCPWTNNTVGHRNMPHFMRFLVWVDMTVGYLFIRLCIRIMKLWRDKHLPSYLFDKTEVILSIVFLPASFFVLFTVGILTIRVFVNMCNGITQIESWECDRIESLVRRKIVTEERAEFPYDIELFTNIFNAVGSPLTFWLPWGQPRGDGITFEKNESGYTEEGEPLCWPPDHVDYDPENVPLQNLKDGLRRRGEEPDCLLGGIGAGKMQAENDFYKRDHWRNVEGEKLADFGVEHTDI
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MIGSMGLRIPRATSSLLGRAVNAVATNQSAVAGASIAAQRRWQHYLMPLRDNFEQEGIRNFLSPGSVNMAYTEYQTFILEKLNALVVGTDFEQKDTKSIVLATARDPELAHVFNHASMAHNNHFFFDHLSPVPVKMGDKLFYHINENFGSVDTLRDEMIGTAVSMFGPGFVWLVRTQLPGQPVALRVMATYLAGSPYPGAHWRRQEMDAQTSIGSSPQGLSNGQRFFERSAAGFKGNKLEPTAPGGTDLIPILCLNTWEYAWLREYGTGVGGMGGKLAYAQSWWNMIDWAKVEEEARLETRILTGGDSSV
The following text describes a protein:
Function:
Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular Localization:
Cytoplasm.
Sequence:
MAAQKSFRIKQKMAKAKKQNRPLPQWIRLRTNNTIRYNAKRRNWRRTKMNI
The following text describes a protein:
Function:
Trypsin-like serine protease that plays an essential role in regulating the immune response by controlling all complement pathways. Inhibits these pathways by cleaving three peptide bonds in the alpha-chain of C3b and two bonds in the alpha-chain of C4b thereby inactivating these proteins. Essential cofactors for these reactions include factor H and C4BP in the fluid phase and membrane cofactor protein/CD46 and CR1 on cell surfaces. The presence of these cofactors on healthy cells allows degradation of deposited C3b by CFI in order to prevent undesired complement activation, while in apoptotic cells or microbes, the absence of such cofactors leads to C3b-mediated complement activation and subsequent opsonization.
Subcellular Localization:
Secreted, extracellular space. Secreted.
Sequence:
MKLLHVFLLFLCFHLRFCKVTYTSQEDLVEKKCLAKKYTHLSCDKVFCQPWQRCIEGTCVCKLPYQCPKNGTAVCATNRRSFPTYCQQKSLECLHPGTKFLNNGTCTAEGKFSVSLKHGNTDSEGIVEVKLVDQDKTMFICKSSWSMREANVACLDLGFQQGADTQRRFKLSDLSINSTECLHVHCRGLETSLAECTFTKRRTMGYQDFADVVCYTQKADSPMDDFFQCVNGKYISQMKACDGINDCGDQSDELCCKACQGKGFHCKSGVCIPSQYQCNGEVDCITGEDEVGCAGFASVTQEETEILTADMDAERRRIKSLLPKLSCGVKNRMHIRRKRIVGGKRAQLGDLPWQVAIKDASGITCGGIYIGGCWILTAAHCLRASKTHRYQIWTTVVDWIHPDLKRIVIEYVDRIIFHENYNAGTYQNDIALIEMKKDGNKKDCELPRSIPACVPWSPYLFQPNDTCIVSGWGREKDNERVFSLQWGEVKLISNCSKFYGNRFYEKEMECAGTYDGSIDACKGDSGGPLVCMDANNVTYVWGVVSWGENCGKPEFPGVYTKVANYFDWISYHVGRPFISQYNV
The following text describes a protein:
Function:
Required for the assembly and stability of the mitochondrial ubiquinol-cytochrome c reductase complex (complex III (CIII) or cytochrome b-c1 complex), a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain (ETC) which drives oxidative phosphorylation.
Miscellaneous:
MISCELLANEOUS: Expressed from one of two small open reading frames (smORFs) encoded by a bicistronic transcript. The ORF for sloth1 has a non-canonical Kozak sequence while the ORF for sloth2 has a classical optimal Kozak sequence. Both ORFs are expressed because ribosomes occasionally fail to initiate translation of sloth1 and continue scanning to initiate translation of sloth2, a process known as 'leaky scanning'; MISCELLANEOUS: The 'sloth' peptides were named for the slow movement phenotype of mutant flies.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein. Mitochondrion.
Sequence:
MSPYSGSVRRLLDSWPGKKRFGVYRFLPLFFLLGAGLEFSMINWTVGETNFYRTFKRRQAKNYVEEQQHLQARAANNTN
The following text describes a protein:
Function:
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MALICIGSVCFSLFHIGVIILLIINYFSSHIKKIFPSFFKNPNKEEIDKHIGNILEAKRKNKQLEQSIYIELKNTGSLNQVFSSTQNSSIVIKFGAVWCKPCNKIKEYFKNQLNYYYVTLVDIDVDIHPKLNDQHNIKALPTFEFYFNLNNEWVLVHTVEGANQNDIEKAFQKYCLEKAK