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stringlengths 6
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stringlengths 11
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stringlengths 108
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P87369 | MNGTEGPYFNVPMVNTTGIVRSPYEYPQYYLVSPAAYAALGAYMFFLILVGFPINFLTLYVTLEHKKLRTPLNYILLNLAVADLFMVFGGFTTTMYTSMHGYFVLGRLGCNLEGFFATLGGEIGLWSLVVLAIERWVVVCKPISNFRFGENHAIMGLVFTWIMAASCAVPPLVGWSRYIPEGMQCSCGVDYYTRAEGFNNESFVVYMFVCHFLIPLIVVFFCYGRLLCAVKEAAAAQQESETTQRAEREVTRMVVIMVIGFLVCWLPYASVAWYIFTNQGSEFGPLFMTIPAFFAKSSSIYNPAIYICMNKQFRNCMITTLCCGKNPFEEEEGASTTASKTEASSVSSSSVSPA | Function: Photoreceptor required for image-forming vision at low light intensity. While most salt water fish species use retinal as chromophore, most freshwater fish use 3-dehydroretinal, or a mixture of retinal and 3-dehydroretinal . Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylation mediates displacement of the bound G-protein alpha subunit by arrestin and terminates signaling (By similarity).
PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39479
Sequence Length: 354
Subcellular Location: Membrane
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O06493 | MSIEIIISLGIYFIAMLLIGWYAFKKTTDINDYMLGGRGLGPFVTALSAGAADMSGWMLMGVPGAMFATGLSTLWLALGLTIGAYSNYLLLAPRLRAYTEAADDAITIPDFFDKRFQHSSSLLKIVSALIIMIFFTLYTSSGMVSGGRLFESAFGADYKLGLFLTTAVVVLYTLFGGFLAVSLTDFVQGAIMFAALVLVPIVAFTHVGGVAPTFHEIDAVNPHLLDIFKGASVISIISYLAWGLGYYGQPHIIVRFMAIKDIKDLKPARRIGMSWMIITVLGSVLTGLIGVAYAHKFGVAVKDPEMIFIIFSKILFHPLITGFLLSAILAAIMSSISSQLLVTASAVTEDLYRSFFRRKASDKELVMIGRLSVLVIAVIAVLLSLNPNSTILDLVGYAWAGFGSAFGPAILLSLYWKRMNEWGALAAMIVGAATVLIWITTGLAKSTGVYEIIPGFILSMIAGIIVSMITKRPAKASYRLFGVMEKLLKRKK | Function: Catalyzes the uptake of extracellular proline under high-osmolarity growth conditions. Essential for the use of proline present in the environment as an osmoprotectant.
Catalytic Activity: L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53283
Sequence Length: 492
Subcellular Location: Cell membrane
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Q06810 | MSSSSKASASSSLSSTATSSTSATRGSDGCVVCDSTASCPVCASGEYCVMTSLTCDKCPSTYCAKQSDSQLSSLSSSSSSSSSSNSNEKTSLIVGFTVGIVGGAMLIALVALYFINKRYWKPKRQKNKALKLEEASQSYGNEEEYFDDEDDDDEDDEDDGGMRKDESHTLFNTSLVPPTLNVPGNRSSASTTRTRASNILPIAYIPGVTSGLSTDKLQSKLRSSSKRQNAAGDIRSHITLGSSILDGLDDEDDEHNQVLNKDADDNLITAIRAKPKLVQIAEEESDKEIQDLDVIEEQTEADDLSHMAKSEASHGNNDEDDDEEGSFILDLEIPESIRESTQGSRTESPFEDKFEIHDER | Function: Component of the high-osmolarity glycerol (HOG) pathway involved in mating response and osmotolerance. May act as a membrane anchor for the STE50/STE11 complex.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 38901
Sequence Length: 360
Subcellular Location: Cell membrane
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Q9VYZ1 | MSEWLRFLKRDQQLDVYFFAVPRLSLDIMGYWPGKTGDTWPWRSLIHFAILAIGVATELHAGMCFLDRQQITLALETLCPAGTSAVTLLKMFLMLRFRQDLSIMWNRLRGLLFDPNWERPEQRDIRLKHSAMAARINFWPLSAGFFTCTTYNLKPILIAMILYLQNRYEDFVWFTPFNMTMPKVLLNYPFFPLTYIFIAYTGYVTIFMFGGCDGFYFEFCAHLSALFEVLQAEIESMFRPYTDHLELSPVQLYILEQKMRSVIIRHNAIIDLTRFFRDRYTIITLAHFVSAAMVIGFSMVNLLTLGNNGLGAMLYVAYTVAALSQLLVYCYGGTLVAESSTGLCRAMFSCPWQLFKPKQRRLVQLLILRSQRPVSMAVPFFSPSLATFAAILQTSGSIIALVKSFQ | 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. Involved in the behavioral responses to esters, and specifically to ethyl hexanoate, benzaldehyde, and acetophenone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46765
Sequence Length: 406
Subcellular Location: Cell membrane
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Q9VXL0 | MFYSYPYKALSFPIQCVWLKLNGSWPLTESSRPWRSQSLLATAYIVWAWYVIASVGITISYQTAFLLNNLSDIIITTENCCTTFMGVLNFVRLIHLRLNQRKFRQLIENFSYEIWIPNSSKNNVAAECRRRMVTFSIMTSLLACLIIMYCVLPLVEIFFGPAFDAQNKPFPYKMIFPYDAQSSWIRYVMTYIFTSYAGICVVTTLFAEDTILGFFITYTCGQFHLLHQRIAGLFAGSNAELAESIQLERLKRIVEKHNNIISFAKRLEDFFNPILLANLMISSVLICMVGFQIVTGKNMFIGDYVKFIIYISSALSQLYVLCENGDALIKQSTLTAQILYECQWEGSDRIEIQSFTPTTKRIRNQIWFMILCSQQPVRITAFKFSTLSLQSFTAILSTSISYFTLLRSVYFDDEKKLD | 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. Involved in the behavioral responses to octanol, nonanol, and pentyl acetate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48264
Sequence Length: 418
Subcellular Location: Cell membrane
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Q9I816 | MDISKVDSTRALVNHWRIFRIMGIHPPGKRTFWGRHYTAYSMVWNVTFHICIWVSFSVNLLQSNSLETFCESLCVTMPHTLYMLKLINVRRMRGQMISSHWLLRLLDKRLGCDDERQIIMAGIERAEFIFRTIFRGLACTVVLGIIYISASSEPTLMYPTWIPWNWRDSTSAYLATAMLHTTALMANATLVLNLSSYPGTYLILVSVHTKALALRVSKLGYGAPLPAVRMQAILVGYIHDHQIILRLFKSLERSLSMTCFLQFFSTACAQCTICYFLLFGNVGIMRFMNMLFLLVILTTETLLLCYTAELPCKEGESLLTAVYSCNWLSQSVNFRRLLLLMLARCQIPMILVSGVIVPISMKTFTVMIKGAYTMLTLLNEIRKTSLE | 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. Involved in the preference for citrus fruits for oviposition, especially through the response to valencene, the primary ligand of Or19a. Larvae growing on citrus fruits suffer a reduced risk of parasitism since endoparasitoid wasps that parasitize larvae are strongly repelled by the smell of citrus, as well as by valencene.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44228
Sequence Length: 387
Subcellular Location: Cell membrane
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Q9P1Q5 | MRENNQSSTLEFILLGVTGQQEQEDFFYILFLFIYPITLIGNLLIVLAICSDVRLHNPMYFLLANLSLVDIFFSSVTIPKMLANHLLGSKSISFGGCLTQMYFMIALGNTDSYILAAMAYDRAVAISRPLHYTTIMSPRSCIWLIAGSWVIGNANALPHTLLTASLSFCGNQEVANFYCDITPLLKLSCSDIHFHVKMMYLGVGIFSVPLLCIIVSYIRVFSTVFQVPSTKGVLKAFSTCGSHLTVVSLYYGTVMGTYFRPLTNYSLKDAVITVMYTAVTPMLNPFIYSLRNRDMKAALRKLFNKRISS | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34565
Sequence Length: 309
Subcellular Location: Cell membrane
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Q9Y585 | MKKENQSFNLDFILLGVTSQQEQNNVFFVIFLCIYPITLTGNLLIILAICADIRLHNPMYFLLANLSLVDIIFSSVTIPKVLANHLLGSKFISFGGCLMQMYFMIALAKADSYTLAAMAYDRAVAISCPLHYTTIMSPRSCILLIAGSWVIGNTSALPHTLLTASLSFCGNQEVANFYCDIMPLLKLSCSDVHFNVKMMYLGVGVFSLPLLCIIVSYVQVFSTVFQVPSTKSLFKAFCTCGSHLTVVFLYYGTTMGMYFRPLTSYSPKDAVITVMYVAVTPALNPFIYSLRNWDMKAALQKLFSKRISS | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34396
Sequence Length: 309
Subcellular Location: Cell membrane
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Q9W5G6 | MSKLIEVFLGNLWTQRFTFARMGLDLQPDKKGNVLRSPLLYCIMCLTTSFELCTVCAFMVQNRNQIVLCSEALMHGLQMVSSLLKMAIFLAKSHDLVDLIQQIQSPFTEEDLVGTEWRSQNQRGQLMAAIYFMMCAGTSVSFLLMPVALTMLKYHSTGEFAPVSSFRVLLPYDVTQPHVYAMDCCLMVFVLSFFCCSTTGVDTLYGWCALGVSLQYRRLGQQLKRIPSCFNPSRSDFGLSGIFVEHARLLKIVQHFNYSFMEIAFVEVVIICGLYCSVICQYIMPHTNQNFAFLGFFSLVVTTQLCIYLFGAEQVRLEAERFSRLLYEVIPWQNLPPKHRKLFLFPIERAQRETVLGAYFFELGRPLLVWIFRTAGSFTTLMNALYAKYETH | 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. Involved in the behavioral responses to butanal, heptanal, and 2-heptanone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44960
Sequence Length: 392
Subcellular Location: Cell membrane
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Q8NGR6 | MMSFAPNASHSPVFLLLGFSRANISYTLLFFLFLAIYLTTILGNVTLVLLISWDSRLHSPMYYLLRGLSVIDMGLSTVTLPQLLAHLVSHYPTIPAARCLAQFFFFYAFGVTDTLVIAVMALDRYVAICDPLHYALVMNHQRCACLLALSWVVSILHTMLRVGLVLPLCWTGDAGGNVNLPHFFCDHRPLLRASCSDIHSNELAIFFEGGFLMLGPCALIVLSYVRIGAAILRLPSAAGRRRAVSTCGSHLTMVGFLYGTIICVYFQPPFQNSQYQDMVASVMYTAITPLANPFVYSLHNKDVKGALCRLLEWVKVDP | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35293
Sequence Length: 318
Subcellular Location: Cell membrane
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P34982 | MDGGNQSEGSEFLLLGMSESPEQQRILFWMFLSMYLVTVVGNVLIILAISSDSRLHTPVYFFLANLSFTDLFFVTNTIPKMLVNLQSHNKAISYAGCLTQLYFLVSLVALDNLILAVMAYDRYVAICCPLHYTTAMSPKLCILLLSLCWVLSVLYGLIHTLLMTRVTFCGSRKIHYIFCEMYVLLRMACSNIQINHTVLIATGCFIFLIPFGFVIISYVLIIRAILRIPSVSKKYKAFSTCASHLGAVSLFYGTLCMVYLKPLHTYSVKDSVATVMYAVVTPMMNPFIYSLRNKDMHGALGRLLDKHFKRLT | Function: Odorant receptor which may be involved in sperm chemotaxis. Bourgeonal is a strong chemoattractant for sperm in vitro and is shown to be a strong agonist for OR1D2 in vitro. May also function in olfactory reception.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35240
Sequence Length: 312
Subcellular Location: Cell membrane
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Q9TU84 | MDGGNQSEGSEFLLLGMSESPEQQRILFWMFLSMYLVTVLGNVLIILAISSDSRLHTPMYFFLANLSFTDLFFVTNTIPKMLVNLQSQDKAISYAGCLTQLYFLLSLVTLDNLILAVMAYDRYVAICCPLHYVTAMSPRLCILLLSLCWVFSVLYGLIHTLLMTRVTFCGSRKIHYLFCEMYFLLRLACSNIQINHTVLXATGCFIFLIPLGFMIXSYARIVRAILRIPSATGKYKAFSTCASHLAVVSLFYGTLGMVYLQPLQTYSTKDSVATVMYAVVTPMMNPFIYSLRNKDIHGALGRLLQGKAFQKLT | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35269
Sequence Length: 313
Subcellular Location: Cell membrane
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Q8NH43 | MDLKNGSLVTEFILLGFFGRWELQIFFFVTFSLIYGATVMGNILIMVTVTCRSTLHSPLYFLLGNLSFLDMCLSTATTPKMIIDLLTDHKTISVWGCVTQMFFMHFFGGAEMTLLIIMAFDRYVAICKPLHYRTIMSHKLLKGFAILSWIIGFLHSISQIVLTMNLPFCGHNVINNIFCDLPLVIKLACIETYTLELFVIADSGLLSFTCFILLLVSYIVILVSVPKKSSHGLSKALSTLSAHIIVVTLFFGPCIFIYVWPFSSLASNKTLAVFYTVITPLLNPSIYTLRNKKMQEAIRKLRFQYVSSAQNF | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35264
Sequence Length: 312
Subcellular Location: Cell membrane
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Q8NGD0 | METANYTKVTEFVLTGLSQTREVQLVLFVIFLSFYLFILPGNILIICTIRLDPHLTSPMYFLLANLALLDIWYSSITAPKMLIDFFVERKIISFGGCIAQLFFLHFVGASEMFLLTVMAYDRYAAICRPLHYATIMNRRLCCILVALSWMGGFIHSIIQVALIVRLPFCGPNELDSYFCDITQVVRIACANTFPEELVMICSSGLISVVCFIALLMSYAFLLALLKKHSGSGENTNRAMSTCYSHITIVVLMFGPSIYIYARPFDSFSLDKVVSVFHTVIFPLLNPIIYTLRNKEVKAAMRKVVTKYILCEEK | Function: Olfactory receptor that acts as a receptor of Asprosin hormone, potentially at the surface of hepatocytes and may help to promote hepatocyte glucose release.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35488
Sequence Length: 313
Subcellular Location: Cell membrane
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Q8VFT4 | MEPANDTTVTEFILTGLSQTREVQLVLFVIFLSFYLFILPVNILIICTIRLDSHLSSPMYFLLANLAFLDIWYSSITAPKMLVDFFVERKIISFGGCIAQLFFLHFVGASEMFLLTVMAFDRYAAICRPLHYATIMNRRLCCILVALSWTGGFVHSIIQVALIVRLPFCGPNELDNYFCDITQVVRIACANTFLEEMVMIFSSGLISVVCFIALLMSYAFLLTMLKKHSSSGESTSRAISTCYSHITIVVLMFGPSIYIYARPFDSFSLDKVVSVFHTVIFPLLNPIIYTLRNKEVKAAMRKLVNRYIFCKEK | Function: Olfactory receptor that acts as a receptor of Asprosin hormone at the surface of hepatocytes to promote hepatocyte glucose release . Also binds Asprosin in the arcuate nucleus of the hypothalamus, thereby stimulating appetite by promoting orexigenic AgRP neuronal activity . In testis, Asprosin-binding promotes sperm progressive motility and enhances male fertility . The activity of this receptor is mediated by G proteins which activate adenylyl cyclase, resulting in an elevation of intracellular cAMP .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35601
Sequence Length: 313
Subcellular Location: Cell membrane
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Q8N0Y3 | MKIANNTVVTEFILLGLTQSQDIQLLVFVLILIFYLIILPGNFLIIFTIRSDPGLTAPLYLFLGNLAFLDASYSFIVAPRMLVDFLSEKKVISYRGCITQLFFLHFLGGGEGLLLVVMAFDRYIAICRPLHCSTVMNPRACYAMMLALWLGGFVHSIIQVVLILRLPFCGPNQLDNFFCDVRQVIKLACTDMFVVELLMVFNSGLMTLLCFLGLLASYAVILCHVRRAASEGKNKAMSTCTTRVIIILLMFGPAIFIYMCPFRALPADKMVSLFHTVIFPLMNPMIYTLRNQEVKTSMKRLLSRHVVCQVDFIIRN | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35724
Sequence Length: 316
Subcellular Location: Cell membrane
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Q8NGL7 | MEKSNNSTLFILLGFSQNKNIEVLCFVLFLFCYIAIWMGNLLIMISITCTQLIHQPMYFFLNYLSLSDLCYTSTVTPKLMVDLLAERKTISYNNCMIQLFTTHFFGGIEIFILTGMAYDRYVAICKPLHYTIIMSRQKCNTIIIVCCTGGFIHSASQFLLTIFVPFCGPNEIDHYFCDVYPLLKLACSNIHMIGLLVIANSGLIALVTFVVLLLSYVFILYTIRAYSAERRSKALATCSSHVIVVVLFFAPALFIYIRPVTTFSEDKVFALFYTIIAPMFNPLIYTLRNTEMKNAMRKVWCCQILLKRNQLF | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35795
Sequence Length: 312
Subcellular Location: Cell membrane
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Q8NH05 | MKKEQDSNVTEFVLLGLSSSWELQLFLFLLFLFFYIAIVLGNLLIVVTVQAHAHLLQSPMYYFLGHLSFIDLCLSCVTVPKMLGDFLQQGKSISFSGCLAQIYFLHFLGASEMFLLTVMAYDRYVAICNPLRYLTVMNPQLCLWLVLACWCGGFIHSIMQVILVIQLPFCGPNELDNFYCDVPQVIKLACMDTYVVEVLVIANSGLLSLVCFLVLLFSYAIILITLRTHFCQGQNKVFSTCASHLTVVSLIFVPCVFIYLRPFCSFSVDKIFSLFYTVITPMLNPLIYTLRNTDMKTAMKKLRIKPCGIPLPC | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35491
Sequence Length: 313
Subcellular Location: Cell membrane
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Q8NGB4 | MGAKNNVTEFVLFGLFESREMQHTCFVVFFLFHVLTVLGNLLVIITINARKTLKSPMYFFLSQLSFADICYPSTTIPKMIADTFVEHKIISFNGCMTQLFSAHFFGGTEIFLLTAMAYDRYVAICRPLHYTAIMDCRKCGLLAGASWLAGFLHSILQTLLTVQLPFCGPNEIDNFFCDVHPLLKLACADTYMVGLIVVANSGMISLASFFILIISYVIILLNLRSQSSEDRRKAVSTCGSHVITVLLVLMPPMFMYIRPSTTLAADKLIILFNIVMPPLLNPLIYTLRNNDVKNAMRKLFRVKRSLGEK | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34800
Sequence Length: 309
Subcellular Location: Cell membrane
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Q8NH49 | MVATNNVTEIIFVGFSQNWSEQRVISVMFLLMYTAVVLGNGLIVVTILASKVLTSPMYFFLSYLSFVEICYCSVMAPKLIFDSFIKRKVISLKGCLTQMFSLHFFGGTEAFLLMVMAYDRYVAICKPLHYMAIMNQRMCGLLVRIAWGGGLLHSVGQTFLIFQLPFCGPNIMDHYFCDVHPVLELACADTFFISLLIITNGGSISVVSFFVLMASYLIILHFLRSHNLEGQHKALSTCASHVTVVDLFFIPCSLVYIRPCVTLPADKIVAVFYTVVTPLLNPVIYSFRNAEVKNAMRRFIGGKVI | Function: Odorant receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34222
Sequence Length: 305
Subcellular Location: Cell membrane
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Q16EI9 | MTQSLEFDQTFGFIAKVLQMIGYPSCLAPYPTTFASRLKSSAGFVVCFLMLTYCVFGQIINIGLLMMGHRQTDQVVEEVAIQVSSTGFCIIGLAKMYSLSYNRAILSWLIADFRVKWNAGELTDKDRSIRDGTLRPTVAITTVAALGNIIMVSAFNFQPVVEMIYGRVVTGEWVKLFPYVIWFPFNSTHGAIYYLVYLFEVYSGVIVAVGNVGFNCIFCLLTSHLSMQLKLLCSWIEDMVEVEDEKGVQSKKKLYRIVRYHQDLIRGRNALQSMFSTTLFLNFSASSVLMCMQLYLITTAGITLMVKFTLFMLCILMEIFILCYYGEEILANSSSIAAGAFNSNWYQSKVSQQNPRFGKNLIPIIQQGQRPMVLTAWKFWPITIRTFSAILQTSWSYFTLLKTVMH | Function: Odorant receptor that specifically recognizes the human odorant sulcatone (6-methylhept-5-en-2-onesul), a volatile odorant emitted at uniquely high levels in humans, thereby playing a key role in mosquito's preference in biting human compared to other animals.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46099
Sequence Length: 406
Subcellular Location: Membrane
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Q9V8Y7 | MFKVKDLLLSPTTFEDPIFGTHLRYFQWYGYVASKDQNRPLLSLIRCTILTASIWLSCALMLARVFRGYENLNDGATSYATAVQYFAVSIAMFNAYVQRDKVISLLRVAHSDIQNLMHEADNREMELLVATQAYTRTITLLIWIPSVIAGLMAYSDCIYRSLFLPKSVFNVPAVRRGEEHPILLFQLFPFGELCDNFVVGYLGPWYALGLGITAIPLWHTFITCLMKYVNLKLQILNKRVEEMDITRLNSKLVIGRLTASELTFWQMQLFKEFVKEQLRIRKFVQELQYLICVPVMADFIIFSVLICFLFFALTVGVPSKMDYFFMFIYLFVMAGILWIYHWHATLIVECHDELSLAYFSCGWYNFEMPLQKMLVFMMMHAQRPMKMRALLVDLNLRTFIDIGRGAYSYFNLLRSSHLY | 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. Specific receptor for geosmin, a microbial odorant that constitutes an ecologically relevant stimulus that alerts flies to the presence of harmful microbes and induces avoidance behavior.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48920
Sequence Length: 419
Subcellular Location: Cell membrane
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P81923 | MAEVRVDSLEFFKSHWTAWRYLGVAHFRVENWKNLYVFYSIVSNLLVTLCYPVHLGISLFRNRTITEDILNLTTFATCTACSVKCLLYAYNIKDVLEMERLLRLLDERVVGPEQRSIYGQVRVQLRNVLYVFIGIYMPCALFAELSFLFKEERGLMYPAWFPFDWLHSTRNYYIANAYQIVGISFQLLQNYVSDCFPAVVLCLISSHIKMLYNRFEEVGLDPARDAEKDLEACITDHKHILEWAGGSLVRVLFTFQLFSRLFRRIEAFISLPMLIQFTVTALNVCIGLAALVFFVSEPMARMYFIFYSLAMPLQIFPSCFFGTDNEYWFGRLHYAAFSCNWHTQNRSFKRKMMLFVEQSLKKSTAVAGGMMRIHLDTFFSTLKGAYSLFTIIIRMRK | 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. Involved in the behavioral responses to ethyl acetate, anisole, hexanoic acid, and pyrazines.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46452
Sequence Length: 397
Subcellular Location: Cell membrane
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Q9W1P8 | MAVFKLIKPAPLTEKVQSRQGNIYLYRAMWLIGWIPPKEGVLRYVYLFWTCVPFAFGVFYLPVGFIISYVQEFKNFTPGEFLTSLQVCINVYGASVKSTITYLFLWRLRKTEILLDSLDKRLANDSDRERIHNMVARCNYAFLIYSFIYCGYAGSTFLSYALSGRPPWSVYNPFIDWRDGMGSLWIQAIFEYITMSFAVLQDQLSDTYPLMFTIMFRAHMEVLKDHVRSLRMDPERSEADNYQDLVNCVLDHKTILKCCDMIRPMISRTIFVQFALIGSVLGLTLVNVFFFSNFWKGVASLLFVITILLQTFPFCYTCNMLIDDAQDLSNEIFQSNWVDAEPRYKATLVLFMHHVQQPIIFIAGGIFPISMNSNITVAKFAFSIITIVRQMNLAEQFQ | 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. Forms a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Also plays a role in the response to N,N-Diethyl-meta-toluamide (DEET), the most widely used insect repellent worldwide.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46164
Sequence Length: 398
Subcellular Location: Cell membrane
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Q9W1P7 | MTKFFFKRLQTAPLDQEVSSLDASDYYYRIAFFLGWTPPKGALLRWIYSLWTLTTMWLGIVYLPLGLSLTYVKHFDRFTPTEFLTSLQVDINCIGNVIKSCVTYSQMWRFRRMNELISSLDKRCVTTTQRRIFHKMVARVNLIVILFLSTYLGFCFLTLFTSVFAGKAPWQLYNPLVDWRKGHWQLWIASILEYCVVSIGTMQELMSDTYAIVFISLFRCHLAILRDRIANLRQDPKLSEMEHYEQMVACIQDHRTIIQCSQIIRPILSITIFAQFMLVGIDLGLAAISILFFPNTIWTIMANVSFIVAICTESFPCCMLCEHLIEDSVHVSNALFHSNWITADRSYKSAVLYFLHRAQQPIQFTAGSIFPISVQSNIAVAKFAFTIITIVNQMNLGEKFFSDRSNGDINP | 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).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47474
Sequence Length: 411
Subcellular Location: Cell membrane
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O43913 | MPHLENVVLCRESQVSILQSLFGERHHFSFPSIFIYGHTASGKTYVTQTLLKTLELPHVFVNCVECFTLRLLLEQILNKLNHLSSSEDGCSTEITCETFNDFVRLFKQVTTAENLKDQTVYIVLDKAEYLRDMEANLLPGFLRLQELADRNVTVLFLSEIVWEKFRPNTGCFEPFVLYFPDYSIGNLQKILSHDHPPEYSADFYAAYINILLGVFYTVCRDLKELRHLAVLNFPKYCEPVVKGEASERDTRKLWRNIEPHLKKAMQTVYLREISSSQWEKLQKDDTDPGQLKGLSAHTHVELPYYSKFILIAAYLASYNPARTDKRFFLKHHGKIKKTNFLKKHEKTSNHLLGPKPFPLDRLLAILYSIVDSRVAPTANIFSQITSLVTLQLLTLVGHDDQLDGPKYKCTVSLDFIRAIARTVNFDIIKYLYDFL | Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
PTM: Multi-mono-ubiquitinated by OBI1; ubiquitination is important for efficient DNA replication origin site activation. Ubiquitination levels are low in mitotic and early G1-phAse cells and are induced in late G1-/early S-phase, peaking in S-phase and decrease toward the end of the cell cycle.
Sequence Mass (Da): 50283
Sequence Length: 435
Subcellular Location: Nucleus
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Q9WUV0 | MSHLESMVLCREAQVSTLQSLFGERHHFSFPSIFIYGHTASGKTYVTQTLLKTLELPHAFVNCVECFTSRLLLEQILNKLSHLNSSDAGCSTEMTCETFNDFVQLFKQVTSAEHLKDQTVYIVLDKAEYLRDMEANLLPGLLRLQELTDRNVTVIFLSEIIWEKFRPNTGCFEPFVLYFPDYSIGNLQKILSHDHPPEYSADFYAAYINILLGVFYTVCRDLKELRHLAVLNFPKYCEPVVKGEAGERDTRKLWRNIEPHLKKAMQTVYLREISSSQWEKLQKDNTDPGQLKGLSAYTHMELPYYSKFILIAAYLASYNPARTDKRFFLKHHGKIKKTNFLKKHEKTSNHLLGPKPFPLDRLLAILYSIVDSRVAPTANIFSQITSLVTLQLLTIVGHEDQLNGPKYKCTVSLDFIRAIARMVNFDIIKYLYDFL | Function: Component of the origin recognition complex (ORC) that binds origins of replication. DNA-binding is ATP-dependent. The specific DNA sequences that define origins of replication have not been identified yet. ORC is required to assemble the pre-replication complex necessary to initiate DNA replication.
PTM: Multi-mono-ubiquitinated by OBI1; ubiquitination is important for efficient DNA replication origin site activation. Ubiquitination levels are low in mitotic and early G1-phAse cells and are induced in late G1-/early S-phase, peaking in S-phase and decrease toward the end of the cell cycle.
Sequence Mass (Da): 50217
Sequence Length: 435
Subcellular Location: Nucleus
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O96237 | MYKIKNNESDINSDDCNETAQECIYGFSSPKKSRKESPIFVQNNDDTCSSNNIYEKKTCSNTSASSVKKYDKKEQSLCSDINNYNKVNIEGLKINERNYDRINNSEEETNINDDNNDDNNGDYDDDNNSDDDDDNDDNNNNDDNNNDDDEDVDDFEDIKENDEYKDPTYSDIYKEAKKCNIRCENIMNSSVNKKNLEEINESDPLNSSDNSMTSSSEESCSEESDKESDKESDKDGNLYDEELNEIIEEGYFKELIPAIPHDILQAYISCLKICGFERQVQLHRLINLLGDLRDPISVIQILGLPGMGKTKVVKNFIKLTNVPFAYVNCLMAVYQSGRSAKNVIYHTILKDLSINLLNEFNEYKKINNITNYSYDPTKLVPNHVSNTDNFFSILHKLLSFKPEDILNNKRTTENIRSPSNSNNNKKKKKEQNDSTGKNSKEECNNNEDDDDDNNKNNFNNNNSNNVRFNSNTNYYKDKLYDRSVVFILDNIRYLVRTHPDLFYALTRIHEYIKGPYNDVTKANKTTRGLCIILINRSPLPDEIFDGLPQPPTVWFDSYTSEMCKNILYRLYNSMCFESLLTYNDKDLKIYYVKHNKNEFLIKRNDVILENDVIYDIWCRYVDYIINVSYKDYKSDFHELLFICSHMWPLFIKPILDGVLEPIVENMNALQRNIDTHIRVATYNHSSHFTFELIDSVFLNENNLKNKIDLSFYSKILLVGAYLASRNLPLTDKRFFNATVKGGAFTLPKKRKGKNKNESILTLLSKSIPKNFTFIRWLCLTDCLLVCFFDEQLILNSLICQQINTLIQLGFISFSSPNNLSCLVRNSLMNGVQWSGYCGSALLNTTTNFSSLTNNIFCETNNSMTYESLDPYTKLVIQVPEETIRNISKEMKIPLDELII | Function: Component of the origin recognition complex (ORC) that binds origins of replication.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 103992
Sequence Length: 899
Subcellular Location: Nucleus
EC: 3.6.4.-
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Q9Y619 | MKSNPAIQAAIDLTAGAAGGTACVLTGQPFDTMKVKMQTFPDLYRGLTDCCLKTYSQVGFRGFYKGTSPALIANIAENSVLFMCYGFCQQVVRKVAGLDKQAKLSDLQNAAAGSFASAFAALVLCPTELVKCRLQTMYEMETSGKIAKSQNTVWSVIKSILRKDGPLGFYHGLSSTLLREVPGYFFFFGGYELSRSFFASGRSKDELGPVPLMLSGGVGGICLWLAVYPVDCIKSRIQVLSMSGKQAGFIRTFINVVKNEGITALYSGLKPTMIRAFPANGALFLAYEYSRKLMMNQLEAY | Function: Mitochondrial ornithine-citrulline antiporter (Probable). Catalyzes the exchange between cytosolic ornithine and mitochondrial citrulline plus an H(+), the proton compensates the positive charge of ornithine thus leading to an electroneutral transport. Plays a crucial role in the urea cycle, by connecting the cytosolic and the intramitochondrial reactions of the urea cycle (Probable). Lysine and arginine are also transported by the antiport mechanism (Probable). In addition, catalyzes an electroneutral exchange of ornithine or lysine for H(+), a reaction driven by the pH gradient across the inner membrane (By similarity).
Catalytic Activity: H(+)(in) + L-citrulline(in) + L-ornithine(out) = H(+)(out) + L-citrulline(out) + L-ornithine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32736
Sequence Length: 301
Subcellular Location: Mitochondrion inner membrane
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A0A0G2K309 | MKSNPAIQAAIDLTAGAAGGTACVLTGQPFDTMKVKMQTFPDLYRGLTDCCLRTYSQVGFRGFYKGTSPALIANIAENSVLFMCYGFCQQVVRKVVGLDRQAKLSDLQNAAAGSFASAFAALVLCPTELVKCRLQTMYEMETSGKIAASQNTVWSVVKEIFRKDGPLGFYHGLSSTLLREVPGYFFFFGGYELSRSFFASGRSKDELGPIPLMLSGGFGGICLWLAVYPVDCIKSRIQVLSMTGKQTGLIRTFLSIVKNEGITALYSGLKPTMIRAFPANGALFLAYEYSRKLMMSQLEAC | Function: Mitochondrial ornithine-citrulline antiporter. Catalyzes the exchange between cytosolic ornithine and mitochondrial citrulline plus an H(+), the proton compensates the positive charge of ornithine thus leading to an electroneutral transport. Plays a crucial role in the urea cycle, by connecting the cytosolic and the intramitochondrial reactions of the urea cycle . Lysine and arginine are also transported by the antiport mechanism (By similarity). In addition, catalyzes an electroneutral exchange of ornithine or lysine for H(+), a reaction driven by the pH gradient across the inner membrane .
Catalytic Activity: H(+)(in) + L-citrulline(in) + L-ornithine(out) = H(+)(out) + L-citrulline(out) + L-ornithine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32797
Sequence Length: 301
Subcellular Location: Mitochondrion inner membrane
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Q9BXI2 | MKSGPGIQAAIDLTAGAAGGTACVLTGQPFDTIKVKMQTFPDLYKGLTDCFLKTYAQVGLRGFYKGTGPALMAYVAENSVLFMCYGFCQQFVRKVAGMDKQAKLSDLQTAAAGSFASAFAALALCPTELVKCRLQTMYEMEMSGKIAKSHNTIWSVVKGILKKDGPLGFYHGLSSTLLQEVPGYFFFFGGYELSRSFFASGRSKDELGPVHLMLSGGVAGICLWLVVFPVDCIKSRIQVLSMYGKQAGFIGTLLSVVRNEGIVALYSGLKATMIRAIPANGALFVAYEYSRKMMMKQLEAY | Function: Mitochondrial transporter of the positively charged amino acids ornithine, lysine and arginine, and the neutral amino acid citrulline . In addition, transports the basic amino acids histidine, homoarginine, and asymmetric dimethylarginine (aDMA), but not symmetric DMA, and the D-forms of lysine, arginine, ornithine and histidine . Functions by both counter-exchange and uniport mechanisms .
Catalytic Activity: L-lysine(in) + L-ornithine(out) = L-lysine(out) + L-ornithine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32580
Sequence Length: 301
Subcellular Location: Mitochondrion membrane
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A1TND9 | MSDTAPVSVPPVLPKSDLNFVWLDCEMTGLDPEKDRLLEIAVVVTGPELEPRVEGPVFAIHQSDALLDGMDAWNKGTHGRSGLIEKVRASTVTEAEAEQAILEFLARYVRKGVAPMCGNSIGQDRRFLVRYMPKLEAFFHYRNVDVSTLKELSRRWKPEVYASFKKAQKHTALADVHESIEELAHYRKHLLVP | Function: 3'-to-5' exoribonuclease specific for small oligoribonucleotides.
Sequence Mass (Da): 21780
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.1.15.-
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A6VN13 | MAQDKENLIWIDLEMTGLDPEQERIIEIATIVTDKNLNILAEGPVLAVHQPNQLLDKMSDWCIKTHTANGLVERVKASKLTERAAELQTIDFLKLWVPKGASPICGNSVAQDKRFLFKYMPDLADYFHYRHLDVSTLKELARRWKPEISDGFQKANTHLALDDIRESIKELAYYREHFIKLD | Function: 3'-to-5' exoribonuclease specific for small oligoribonucleotides.
Sequence Mass (Da): 21048
Sequence Length: 182
Subcellular Location: Cytoplasm
EC: 3.1.15.-
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Q0A8I6 | MGFSEHNLVWLDLEMTGLDPDTDRIIEIATLVTDSQLNILAEGPVLAVRQSEQALAAMDEWNTRTHGESGLIERVRASHLDEAAAEAETLAFLRRWVPERASPMCGNSICQDRRFLYRYMPRLEAWFHYRNLDVSTLKLLANRWHPEVLQGFSKKATHQALEDIRESVAELRHYRAHFLRLPAAGAEGGGAAD | Function: 3'-to-5' exoribonuclease specific for small oligoribonucleotides.
Sequence Mass (Da): 21878
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.1.15.-
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Q6ZC03 | MDQARISFFPDGLRVMIIDDDAKAVRRATATLSQLQYAVVATHSTASAGLRALSGDNVVEIQAILCDVHKVVSSGFDFRRVVESELRIPVIYLLSKMEEEDMVAGEDAEFLNHLLLTATYIVRKPLNPTVMARLWRVVAWRMYCLEERIQANVAANAGAGGEDDDDDDDVVIVEEPQVHFKVVRRTSGGSRKRQLTINVVDDGNRGSGSGGGGGGGADANPTRILQHITSNLQEFRTKHQKKDMAIERPLISSDSMFLKAILPTLKISPCNPLTLTGGIGSSSVAAEAFAGGSSSAAPLQIPVFQQQSTGNGNTVISFSNNASPMAMRAPTDNTMISFNNVSAAPVANAVISFSNISRSAAMQAPAARGQHLSGDVQQLDFPQQKLYFGPFSYQGPPPPSMHNHINLLPPTSSPVTCSMDKGKVPIIELPYGMPVDDFLVSQTTYGGAGPSIGATDAAAAAYPYTDAPSNNVATGCLMVPPMGPAFSITEPTVVAQGEGTGTGVDAGTSEKNAIVEAPNNPAPLMVLDQVAADAAMDVQEDIMFSLESLLGPDYDLLPMEDVSAPDTAAAGDAAGGSLDGEEGGMDIGWDLDLDDILVENVNDFAFLDNLAGSE | Function: Functions as a response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. May directly activate some type-A response regulators in response to cytokinins.
PTM: Two-component system major event consists of a His-to-Asp phosphorelay between a sensor histidine kinase (HK) and a response regulator (RR). In plants, the His-to-Asp phosphorelay involves an additional intermediate named Histidine-containing phosphotransfer protein (HPt). This multistep phosphorelay consists of a His-Asp-His-Asp sequential transfer of a phosphate group between first an His and an Asp of the HK protein, followed by the transfer to a conserved His of the HPt protein and finally the transfer to an Asp in the receiver domain of the RR protein.
Sequence Mass (Da): 64789
Sequence Length: 614
Subcellular Location: Nucleus
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C7Q942 | MHRLALTAQDNLAVAPMLADLAGRYPDIEDPELIRSAPVLAAKGLPPHLLAFLDDFRLREPSALCVISGLDVDQDRLGPTPEHWRDSQIGSRSLNLEIFFLLCGAALGDVFGWATQQDGRIMHDVLPIKGHEHYELGSNSLQHLSWHTEDSFHPCRGDYVALMCLKNPYEAETMVCDAGDLDWPNLDVDALFEPVFTQMPDNSHLPQNTAESTGDPTKDRLRARSFELIKSWNENPVRRAVLYGDRQNPYMALDPYHMKMDDWSERSLEAFQALCEEIEAKMQDVVLHPGDIAFIDNFRAVHGRRSFRARYDGSDRWLKRLNITRNLRGSRAWRPAPDDRVIY | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Alpha-ketoglutarate-dependent dioxygenase that in vitro catalyzes the regio- and stereoselective hydroxylation of L-ornithine and L-arginine, leading to (3S)-3-hydroxy-L-ornithine and (3S)-3-hydroxy-L-arginine, respectively. Cannot use L-lysine, D-ornithine, or D-arginine as substrate.
Catalytic Activity: 2-oxoglutarate + L-ornithine + O2 = (3S)-3-hydroxy-L-ornithine + CO2 + succinate
Sequence Mass (Da): 39116
Sequence Length: 343
EC: 1.14.11.-
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Q8ZPK1 | MHTLTLKRVLGFTIVILLLLALFIWGIGLETLKARQVDLLYLGQRHLMLVFTSMFFALLVGIPSGILLSRPAAKGFAEYVMQIFNVGNTLPPLAVLALAMVIIGIGDTPAIVALFLASLLPIVRNTYAGLCSVPASLIEAANGIGMTKWQRLRQVELPNAWPVMLSGIRIATAINVGTAPLAFLIGASSYGELIFPGIYLNDFPTLILGATATALFALILDTLLAWFGRRLSPHTV | Function: Part of the OsmU ABC transporter complex, which is involved in the uptake of osmoprotectants such as choline-O-sulfate and glycine betaine. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25411
Sequence Length: 236
Subcellular Location: Cell inner membrane
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P0CD70 | GFLSALKKYLPIVLKHV | Function: Synthetic peptide exhibits hemolytic activities (less than melittin) and inhibits bacterial (M.luteus and E.coli) and fungal (F.oxysporum) growth at micromolar concentrations . In the context of inflammation and cancer tests, is weakly cytotoxic to normal cells, induces calcium signaling but does not impact cAMP production . In addition, prevents LPS-induced nitric oxid (NO) synthesis but does not affect the IP3 signaling and pro-inflammatory activation of endothelial cells . Does not show significant antiproliferative activity on the breast cancer cell line MDA-MB-231 .
PTM: C-terminal amidation is important for activity, since the non-amidated peptide shows weaker hemolytic, antibacterial and antifungal activities.
Sequence Mass (Da): 1926
Sequence Length: 17
Subcellular Location: Secreted
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P0CL66 | MKKYLLGIGLILALIACKQNVSSLDEKNSVSVDLPGEMKVLVSKEKNKDGKYDLIATVDKLELKGTSDKNNGSGVLEGVKADKSKVKLTISDDLGQTTLEVFKEDGKTLVSKKVTSKDKSSTEEKFNEKGEVSEKIITRADGTRLEYTGIKSDGSGKAKEVLKGYVLEGTLTAEKTTLVVKEGTVTLSKNISKSGEVSVELNDTDSSAATKKTAAWNSGTSTLTITVNSKKTKDLVFTKENTITVQQYDSNGTKLEGSAVEITKLDEIKNALK | Function: Induces host (human and mouse) cytokine release by monocyte cell lines via TLR2 and CD14; nonlipidated protein does not stimulate host cells .
Location Topology: Lipid-anchor
Sequence Mass (Da): 29367
Sequence Length: 273
Subcellular Location: Cell outer membrane
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G2TRU0 | MSLNELIVAALKLFFYNKEQKSDCIFFCQVQIVIQISSSMFSLVIRRIHIRKLWYITVFTINASMFSGFFNNPSLLTPNENLLFQVGLHYSFAV | 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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10947
Sequence Length: 94
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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Q92316 | MTYEQLYKEFHSSKSFQPFIHLDTQPKFAICGLIVTLAVLSSALFAVGSKSSYIKKLFFYTILSVIGSLFAGLTTVFASNSFGVYV | 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.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 9517
Sequence Length: 86
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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Q03723 | MKWCSTYIIIWLAIIFHKFQKSTATASHNIDDILQLKDDTGVITVTADNYPLLSRGVPGYFNILYITMRGTNSNGMSCQLCHDFEKTYHAVADVIRSQAPQSLNLFFTVDVNEVPQLVKDLKLQNVPHLVVYPPAESNKQSQFEWKTSPFYQYSLVPENAENTLQFGDFLAKILNISITVPQAFNVQEFVYYFVACMVVFIFIKKVILPKVTNKWKLFSMILSLGILLPSITGYKFVEMNAIPFIARDAKNRIMYFSGGSGWQFGIEIFSVSLMYIVMSALSVLLIYVPKISCVSEKMRGLLSSFLACVLFYFFSYFISCYLIKNPGYPIVF | 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 . Can participate in redox reactions and is able to catalyze dithiol-disulfide exchange reactions with other proteins, albeit with relatively low efficiency. May form transient disulfide bonds with nascent polypeptides in the endoplasmic reticulum and thereby promote efficient glycosylation .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37891
Sequence Length: 332
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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O17204 | MEIVKTIIPHNRSYIEPPIPSATEWLANMSVMHVSCLTIACVFVAITFLSSFFHLFFVLKYVSNERIRNDMYALIFMFPITTFASLVGMFIPRAAIFLYAVSLVYFMFTLFIMVTLLFNIFGGRQEMSAYLLQRNIRVNFTVPPLCFFKFLPTVESTDQNLRRIEWLVFQTPIIRTLLELVSVVVSMEQEGRRESVWFVFSQLMALLSMCIAFYGCYVMVPLGREKHAPYRFDFLFRTCDIAQCIYTIQKFVFEFAAAVGLITSDRYLPAAAKALWWASFMCTWEMMLLSALCSYCLRPAKCKFFDLYPGNDMPALSARDGSNSRVPSFSRRLSIEYEPRIAGVMLEPPSRSSLSITPRDKIEDPTTVSYFADNFDSLSQIQGQ | Function: Probable transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44205
Sequence Length: 384
Subcellular Location: Cell membrane
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Q18071 | MLEISPWETLVKLLTDSLLNCTGTHEDVPHAKTFLRSLTTTYIASLAVATAVTVGTVCLAVLHLIYIHFYITHSSRRLHIVLLACTAPLVSLLALVAMYMPRVWFLSHLLSFLYFSFALWVIICLLLHIFDGHHALVTKMMQRLQYVEIATPPFCCLFPCLPKVRLEGKKIRWCELMVMQAPIVRLFATLVSLVIYFEYQDQGLVPLKVLDFITLPSLLAGIYGTHILVTTVSRMDELISYRYVVVFRLLDFFFMVFGLQQPVFDFLARYGAFGCGTVLPAIETSFYWKNFFTVIEAFCVTLISTVLLQPSKSSFFDKHPSCRSMSSARSTITDVDTDESTT | Function: Probable transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38831
Sequence Length: 342
Subcellular Location: Cell membrane
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Q9XU63 | MAKEHGAMRSVLNLIGSVMLPQDTSNCSDRHDTPSAPEFLSHLQPFQTVLLSIASFSTTIVLCLSLIHWFYVYKYVSIEKRRNKLYWLIAVFPVACSCSFIAMCVPRTAVILTCIGVLYYLMCLFVIVSLARHLFGGRESFSTCLQYDDRPIDFRSPPFCCIIPKLPTARSTEKNIRRLEWCVLQAPIVRSIIIFLDVVAVAEMREDATPYIRYSDMASLCSLLLAIFGVHTLARVTSNKLSAYCFMSMFRLVDISLLFFSAQQPMIFQNVLLRFNLISCGPLLNAQENAYFVCNFIITCEMLLLSVLATWLLAPRHNAMFDAYRPSMALSETTASLNETEQSMILDH | Function: Probable transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39464
Sequence Length: 348
Subcellular Location: Cell membrane
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Q66I08 | METSNFTLFDPRCRAEAPFAIDAIKQLDIFGKVLYTVLTLMATASMLVFIEECIYIYKKVPAHKKSTIIWVTGVAPVMAIMSCLGMWVPRATMFTDMTSATYFAIVVFKFLILMIEEVGGDNAFLRRCEKQTFKISTGPCCCCCPCLPNVPITRRSLFILKLGSYQFALMKLVLTIFSIVLWTNGSFSLTNVSASGAAIWINSFIGVLTIIALWPVAIMFMHVREALRTLKIVPKYAMYQLVLILSQLQTAIINILALNGTIACSPPYSSQARGYMMSQQLLIVEMFIITLVTRVLYRRQYEPIPEPDDVEEKKTVLSSKKAIDVA | Function: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for the translocation of bile acids (such as taurocholate), steroids (such as estrone sulfate), and eicosanoids (such as prostaglandin E2).
Catalytic Activity: taurocholate(out) = taurocholate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36589
Sequence Length: 326
Subcellular Location: Cell membrane
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Q9VVV2 | MNASENYFTMDPTENISQVLDQNRNNTNSLRTHPTVEEYYENMTAFLSLAIFIASLLTILNISIFATTVSRLRRHLDKPLLGPSIMMVGLYPIISVAALVTILVPYSWFICHTVMHVMFMVGGPVFRTLLFRYVGSEQNYVKETAGEAVQLNTPPCCCCCLCLPMVIPTKAKLCISRYMVWQMPFWQGSIMLVMNILYYRDIQLYRQVMFFFIPFIVCSIVLGAWSLQITVRMITKVRGDYQLRKKMFCLQLVVMLCKLQYLVLYDQLDGIKMGGEYPINHTVYKQTIINILILVEMVLVSMMVQSAYRTPVQVQIDEVNKEKEVTRI | Function: Probable transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37866
Sequence Length: 328
Subcellular Location: Cell membrane
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Q86UW1 | MEPGRTQIKLDPRYTADLLEVLKTNYGIPSACFSQPPTAAQLLRALGPVELALTSILTLLALGSIAIFLEDAVYLYKNTLCPIKRRTLLWKSSAPTVVSVLCCFGLWIPRSLVLVEMTITSFYAVCFYLLMLVMVEGFGGKEAVLRTLRDTPMMVHTGPCCCCCPCCPRLLLTRKKLQLLMLGPFQYAFLKITLTLVGLFLVPDGIYDPADISEGSTALWINTFLGVSTLLALWTLGIISRQARLHLGEQNMGAKFALFQVLLILTALQPSIFSVLANGGQIACSPPYSSKTRSQVMNCHLLILETFLMTVLTRMYYRRKDHKVGYETFSSPDLDLNLKA | Function: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood . Efficiently transports the major species of bile acids (taurocholate) . Taurine conjugates are transported more efficiently across the basolateral membrane than glycine-conjugated bile acids (By similarity). Can also transport steroids such as estrone 3-sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a role in the enterohepatic circulation of sterols . Able to transport eicosanoids such as prostaglandin E2 (By similarity).
Catalytic Activity: taurocholate(out) = taurocholate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37735
Sequence Length: 340
Subcellular Location: Cell membrane
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Q90YM5 | MDVAHPEEVTRFSPDILMEKFNVSEACFLPPPISIQLILQLTWLDIGVFAALTAMTVLTIAIYLEIVCYLMDKVKCPIKRKTLMWNSAAPTVIAITSCLGLWVPRAIMFVDMAAAMYFGVGFYLMLLIIVQGYGGEEAMLQHLATHTIRISTGPCCCCCPCLPHIHLTRQKYKIFVLGAFQVAFLRPALFLLGVVLWTNGLYDPDDWSSTSIFLWLNLFLGVSTILGLWPVNVLFRHSKVLMADQKLTCKFALFQAILILSSLQNSIIGTLAGAGHIGCAPPYSARTRGQQMNNQLLIIEMFFVGILTRISYRKRDDRPGHRHVGEVQQIVRECDQPAIADQQADHSSISHI | Function: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for the translocation of bile acids (such as taurocholate), steroids (such as estrone sulfate), and eicosanoids (such as prostaglandin E2).
Catalytic Activity: taurocholate(out) = taurocholate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39345
Sequence Length: 352
Subcellular Location: Cell membrane
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Q8R000 | MEPGRTHIKLDPRYTAELLELLETNYSISPACFSHPPTAAQLLRALGPVDIALTIILTFLTTGSVAIFLEDAVYLYKNTLCPIKKRTLIWSSSAPTVVSVFCCFGLWIPRALTLVEMAITSFYAVCFYLLMMVMVEGFGGKKAVLRTLKDTPMRVHTGPCCCCCPCCPPLILTRKKLQLLLLGPFQYAFFKITLSIVGLFLIPDGIYDPGEISEKSAALWINNLLAVSTLLALWSLAILFRQAKMHLGEQNMGSKFALFQVLVILTALQPAIFSILANSGQIACSPPYSSKIRSQVMNCHMLILETFLMTVLTRMYYRRKDDKVGYEACSLPDLDSALKA | Function: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood . Efficiently transports the major species of bile acids (taurocholate) . Taurine conjugates are transported more efficiently across the basolateral membrane than glycine-conjugated bile acids . Can also transport steroids such as estrone 3-sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a role in the enterohepatic circulation of sterols (By similarity). Able to transport eicosanoids such as prostaglandin E2 (By similarity).
PTM: N-glycosylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: taurocholate(out) = taurocholate(in)
Sequence Mass (Da): 37759
Sequence Length: 340
Subcellular Location: Cell membrane
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A9ULC7 | MDPEQNDTKPPFNPICATRQAPYSHEILENLDITGILLFAILTFMTLVSLLVFLEEAYYMYRKIPNPKNSIIIWINAGAMMIATTSCFGMWIPRSTMFTDFTASVFLAVLIHKFQLMLVNECGGRREFLSTFGDTKLKISTGPFCCCCLCLPHKDINRKTLFILKLGTFQFAFLRPVLMFLAVVLWTNGTYMIGNSSAEKATIWINIGVGITTITALWAVGIMFNLVKDNLKEKNIIGKFAVYQFTVILSQLQTSIINILGTTGVISCVPPLPGPSRASYMNQQLLIMEMFLVTVICRVLYRRRYDDKNLLENQETNDNLRNSMMHLNGKALEDGPQSV | Function: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for the translocation of bile acids (such as taurocholate), steroids (such as estrone sulfate), and eicosanoids (such as prostaglandin E2).
Catalytic Activity: taurocholate(out) = taurocholate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38291
Sequence Length: 339
Subcellular Location: Cell membrane
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A0JNM1 | MNYSEKLTGAPPMTEVPLELLEEMLWFFRVEDATPWNCSMFVLAALVAIISFILLGRNIQANRNQKKLPPEKQTPEVLYLAEGGNKDDKNLTSLTETLLSEKPTLAQGEMEAKCSDVPRVHLPDPQEPES | Function: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. The Ost-alpha/Ost-beta complex efficiently transports the major species of bile acids (taurocholate). Taurine conjugates are transported more efficiently across the basolateral membrane than glycine-conjugated bile acids (By similarity). Can also transport steroids such as estrone 3-sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a role in the enterohepatic circulation of sterols (By similarity). Able to transport eicosanoids such as prostaglandin E2 (By similarity). Modulates SLC51A glycosylation, membrane trafficking and stability activities (By similarity).
Catalytic Activity: taurocholate(out) = taurocholate(in)
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 14599
Sequence Length: 130
Domain: The transmembrane domain (TM) is the major site of interaction with SLC51A. The extracellular-membrane interface is absolutely required for transport activity. The intracellular-membrane interface is necessary for establishing the correct membrane orientation that is essential for the heterodimer Ost-alpha/Ost-beta complex formation and transport activity at the cell membrane surface (By similarity).
Subcellular Location: Cell membrane
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Q86UW2 | MEHSEGAPGDPAGTVVPQELLEEMLWFFRVEDASPWNHSILALAAVVVIISMVLLGRSIQASRKEKMQPPEKETPEVLHLDEAKDHNSLNNLRETLLSEKPNLAQVELELKERDVLSVFLPDVPETES | Function: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood . Modulates SLC51A glycosylation, membrane trafficking and stability activities . The Ost-alpha/Ost-beta complex efficiently transports the major species of bile acids (taurocholate) . Taurine conjugates are transported more efficiently across the basolateral membrane than glycine-conjugated bile acids (By similarity). Can also transport steroids such as estrone 3-sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a role in the enterohepatic circulation of sterols . Able to transport eicosanoids such as prostaglandin E2 (By similarity).
Catalytic Activity: taurocholate(out) = taurocholate(in)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14346
Sequence Length: 128
Domain: The transmembrane domain (TM) is the major site of interaction with SLC51A. The extracellular-membrane interface is absolutely required for transport activity. The intracellular-membrane interface is necessary for establishing the correct membrane orientation that is essential for the heterodimer Ost-alpha/Ost-beta complex formation and transport activity at the cell membrane surface (By similarity).
Subcellular Location: Cell membrane
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Q90YM4 | MSGLLKYLFGCFILCLLLQGKTHMTSATISKPHETIDIEKQNMTGERNSTLAQQLSFPMEDPTNWNYAILALAFVVLFLAFLILAQNSRANRTRKMKALNGAGGRNETEADSTQKAMMQYVVEVDNLAETDQMLQSKPTYISLNQVAQTSSPKVLPKEGQILVEWKDGNIGFLYTDSKEDDV | Function: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. Efficiently transports the major species of bile acids. May modulate slc51a glycosylation, membrane trafficking and stability activities (By similarity). Able to transport taurocholate, estrone sulfate, digoxin, and prostaglandin E(2), but not p-aminohippurate or S-dinitrophenyl glutathione.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 20343
Sequence Length: 182
Domain: The transmembrane domain (TM) is the major site of interaction with slc51a. The extracellular-membrane interface is absolutely required for transport activity. The intracellular-membrane interface is necessary for establishing the correct membrane orientation that is essential for the heterodimer Ost-alpha/Ost-beta complex formation and transport activity at the cell membrane surface (By similarity).
Subcellular Location: Cell membrane
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Q80WK2 | MDHSAEKAAANAEVPQELLEEMLWYFRAEDAAPWNYSILVLAVLVVMTSMFLLRRSILANRNRKKQPQDKETPEDLHLDDSIMKENNSQVFLRETLISEKPDLAPGEPELKEKDSSLVFLPDPQETES | Function: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood . The Ost-alpha/Ost-beta complex efficiently transports the major species of bile acids (taurocholate) . Taurine conjugates are transported more efficiently across the basolateral membrane than glycine-conjugated bile acids . Can also transport steroids such as estrone 3-sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a role in the enterohepatic circulation of sterols (By similarity). Able to transport eicosanoids such as prostaglandin E2 (By similarity). Modulates SLC51A glycosylation, membrane trafficking and stability activities .
Catalytic Activity: taurocholate(out) = taurocholate(in)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14684
Sequence Length: 128
Domain: The transmembrane domain (TM) is the major site of interaction with SLC51A. The extracellular-membrane interface is absolutely required for transport activity. The intracellular-membrane interface is necessary for establishing the correct membrane orientation that is essential for the heterodimer Ost-alpha/Ost-beta complex formation and transport activity at the cell membrane surface.
Subcellular Location: Cell membrane
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O59866 | MKSALCIALALTWSLLVQAARQTVLAVADHDIGGYSTFLQSLTDRDFDVKTSYIKDESAKLFEYGERLYDNLILLSSQSKSLGPVFSPKSLLEFVQSGGNLFVVAGSQLPEGIRELGRQLDMFLAERQSVVVDHFNHAEGSDDIILLDGISENPYIISDETRAAGPILYKGIGHYLGPNPQTQPILRGNPTSYIYNTKTEAEVSKNPWAAGTQLFLVSVLQSSTGERVGLSGSIDMLKDEYLSPQSPSFSKSNFLFARDLTNWVFQRKGVLQATNMTYGKVAEPLESRNASCYRIKDEMIFSIDISLLEDGQQTPYVADDVQLELIMLDPYYRVNLVPVPSDSQTSQHYEAVLVAPDHYGDFTFKIEYKRPGLTPIEEKSTFTLRQFFHNEFPRFLPHAYPYYASCFSVLGAFLLFCGIWLLQKPAKPVVPSAKKQN | 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.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48899
Sequence Length: 437
Domain: The cytoplasmic C-terminal domain contains a functional dilysine-retrieval motif, which is involved in the retrograde Golgi-to-ER transport of the protein.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum
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P33767 | MRTDWNFFFCILLQAIFVVGTQTSRTLVLYDQSTEPLEEYSVYLKDLEQRNYKLEYLDINSTSTTVDLYDKEQRLFDNIIVFPTKGGKNLARQIPVKQLIKFFENEGNILCMSSPGAVPNTIRLFLNELGIYPSPKGHVIRDYFSPSSEELVVSSNHLLNKYVYNARKSEDFVFGESSAALLENREQIVPILNAPRTSFTESKGKCNSWTSGSQGFLVVGFQNLNNARLVWIGSSDFLKNKNQDSNQEFAKELLKWTFNEKSVIKSVHAVHSHADGTSYDEEPYKIKDKVIYSVGFSEWNGEEWLPHIADDIQFELRQVDPYYRLTLSPSGNDSETQYYTTGEFILPDRHGVFTFLTDYRKIGLSFTTDKDVKAIRHLANDEYPRSWEISNSWVYISAICGVIVAWIFFVVSFVTTSSVGKKLETFKKTN | 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.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 49392
Sequence Length: 430
Domain: The cytoplasmic C-terminal domain contains a functional dilysine-retrieval motif, which is involved in the retrograde Golgi-to-ER transport of the protein.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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Q89VE8 | MSKSPKHFLDINELPLSELKSMLDASSAMKAKQKAHQPVRPLEGKTLAMIFERPSTRTRVSFDVAMRQLGGEPIMLTGAEMQLGRGETIADTARVLSRYVDAIMIRILNHDALLELAANATVPVINGLTRRSHPCQVMADLLTYQEHRGPIEGRTVAWTGDDNNVLASWAHAAERFKFQLNVATPPELAPKKAMRDWIKASGAPIMLGTDPEAAVRGADCVVTDTWVSMGDKEGEHRHNVLKPYQVNAKLMSLAKPDALFMHCLPAHRGEEVTDEVIDGPQSVVFDEAENRLHAQKGILAWCFDAVK | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 33903
Sequence Length: 307
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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Q2YPH2 | MANDNGIKHFIDLSTVPATELRAILEDAKARKARLKAGEVERPYAGKVLAMIFEKLSTRTRVSFDVGMRQLGGETIMLTGSEMQLGRSETIADTAKVLSRYVDAIMIRTTAHERMLELAEYATVPVINALTDDTHPCQIMADVLTYEEHRGPIKGKTFAWMGDGNNVLHSLVEAAARFDFNVNIATPKGSEPKSQYIDWARANGAGIMSTTDPEKAASGADCIVTDTWVSMGQEDHARGHNVFIPYQVNANLMAKADPKALFMHCLPAHRGEEVTDEVIDGPQSVVFDEAENRLHAQKAILAWCLQDRGLGA | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 34239
Sequence Length: 312
Pathway: Amino-acid degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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Q7VAW6 | MNMNSLSVSRVLADLAGKDFISCSDFTSDQVKALLQLSSQLKNGDRRIDLGNRVLGLIFSKASTRTRVSFQVAMARLGGQTIDLSNQATQLARGEPLKDTARVLSRYCDALALRTFGNDELIEYAKWSSIPVINALTDLEHPCQALADFLTIKEAFGSLDGITLAYIGDGNNVLNSLMICGTLLGVNIQIASPKGFEPLPSIVERAKTLAHPTLKICVSNNPIDAVSGAHVIYTDVWASMGQESEQAQRKEIFEGYTVNKDLVDKAEKESIILHCLPAHRGEEITDDVLESSASRIFDQAENRLHVQQALLAALLGGL | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 34571
Sequence Length: 318
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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Q8ZW40 | MKHLLTLMEFAPHEVEYLLRVSREFKTRFLAGEIYTPLFPGRVLILYFEKHSTRTRLSLTSAAAQLGIQAVYTTPNELQIARGETVADTMRVISRYAAAVAARVYKHETLEEMARHSAIPVINALSDKHHPLQALADALTLWERAGRLHNVKIAFVGDVSNNVATSLAIIGAKLGWEVRLVGPKQLWNQRLVDELAEDAAKTGARIYFTDSINEVAGVDGVYTDVWVSMGFEKEAEERRRLLKPYQVNQRVMEIAGKKAVFLHCLPAHRGEEVTDDVIDGPQSAVWDQAENRMHTAKAVLAYLLK | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 34241
Sequence Length: 305
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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A1RVH4 | MRHLLTLMEYKPHEVENILRMSRDFKTRYLAGEVYTPIFPGRLVVLYFEKPSTRTRLSLTAAAAQLGMQAVYTTPSELQIGRGETIADTMRVLSRYAVAVAARVYRHETLEEMAQNSSISVINALSDKHHPLQALADALTLWEYVGKLHGIKVAFVGDVSNNVATSLAIIGAKLGWEVRLVGPKQLWNMKLVEELSEDLAKTGGRIYFTDSINDVAGVDGVYTDVWVSMGFEKEAEERRRMLKPYQVNQRVMEIAGRKAIFLHCLPAHRGEEVTDDVIDGPQSVVWDQAENRMHTAKAVFAYLLR | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 34365
Sequence Length: 305
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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A0R4M9 | MSPESGHETISGTSDFVVVANRLPVDLERLPDGTTRWKRSPGGLVTALEPLLRKRRGSWIGWAGVADSDEEPIVQDGLQLHPVRLSADDVAKYYEGFSNATLWPLYHDLIVKPEYHREWWDRYVEVNRRFAEATARAAAEGATVWIQDYQLQLVPKMLRMLRPDVTIGFFLHIPFPPVELFMQMPWRTEIVEGLLGADLVGFHLPGGAQNFLVLSRRLVGANTSRASIGVRSRFGEVQVGFRTVKVGAFPISIDSAELDGKARNRAIRQRARQIRAELGNPRKIMLGVDRLDYTKGIDVRLRALSELLEEKRIKRDDTVLVQLATPSRERVESYIAMREDIERQVGHINGEYGEVGHPIVHYLHRPIPRDELIAFFVAADVMLVTPLRDGMNLVAKEYVACRSDLGGALVLSEFTGAAAELRQAYLVNPHDLEGVKDKIEAAVNQNPEEGKRRMRALRRQVLAHDVDRWARSFLDALAATGETGDSGVTGESTPAPESDSGSF | Function: Involved in the production of glycogen and alpha-glucan via the TreS-Pep2 branch involved in the biosynthesis of maltose-1-phosphate (M1P), and probably in the osmoprotection via the biosynthesis of trehalose . Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to glucose-6-phosphate (Glc-6-P) to form trehalose-6-phosphate (Ref.4). ADP-Glc, CDP-Glc, GDP-Glc and TDP-Glc are also glucosyl donors, however, when the pyrimidine sugar nucleotides (CDP-Glc, TDP-Glc and UDP-Glc) are used as substrates, there is an absolute requirement for a high molecular weight polyanion for activity (Ref.4).
Catalytic Activity: ADP-alpha-D-glucose + D-glucose 6-phosphate = ADP + alpha,alpha-trehalose 6-phosphate + H(+)
Sequence Mass (Da): 56280
Sequence Length: 503
Pathway: Glycan biosynthesis; trehalose biosynthesis.
EC: 2.4.1.15
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Q96RQ9 | MAPLALHLLVLVPILLSLVASQDWKAERSQDPFEKCMQDPDYEQLLKVVTWGLNRTLKPQRVIVVGAGVAGLVAAKVLSDAGHKVTILEADNRIGGRIFTYRDQNTGWIGELGAMRMPSSHRILHKLCQGLGLNLTKFTQYDKNTWTEVHEVKLRNYVVEKVPEKLGYALRPQEKGHSPEDIYQMALNQALKDLKALGCRKAMKKFERHTLLEYLLGEGNLSRPAVQLLGDVMSEDGFFYLSFAEALRAHSCLSDRLQYSRIVGGWDLLPRALLSSLSGLVLLNAPVVAMTQGPHDVHVQIETSPPARNLKVLKADVVLLTASGPAVKRITFSPPLPRHMQEALRRLHYVPATKVFLSFRRPFWREEHIEGGHSNTDRPSRMIFYPPPREGALLLASYTWSDAAAAFAGLSREEALRLALDDVAALHGPVVRQLWDGTGVVKRWAEDQHSQGGFVVQPPALWQTEKDDWTVPYGRIYFAGEHTAYPHGWVETAVKSALRAAIKINSRKGPASDTASPEGHASDMEGQGHVHGVASSPSHDLAKEEGSHPPVQGQLSLQNTTHTRTSH | Function: Secreted L-amino-acid oxidase that acts as a key immunoregulator . Has preference for L-aromatic amino acids: converts phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp) to phenylpyruvic acid (PP), hydroxyphenylpyruvic acid (HPP), and indole-3-pyruvic acid (I3P), respectively . Also has weak L-arginine oxidase activity . Acts as a negative regulator of anti-tumor immunity by mediating Trp degradation via an indole pyruvate pathway that activates the transcription factor AHR . IL4I1-mediated Trp catabolism generates I3P, giving rise to indole metabolites (indole-3-acetic acid (IAA) and indole-3-aldehyde (I3A)) and kynurenic acid, which act as ligands for AHR, a ligand-activated transcription factor that plays important roles in immunity and cancer . AHR activation by indoles following IL4I1-mediated Trp degradation enhances tumor progression by promoting cancer cell motility and suppressing adaptive immunity . Also has an immunoregulatory function in some immune cells, probably by mediating Trp degradation and promoting downstream AHR activation: inhibits T-cell activation and proliferation, promotes the differentiation of naive CD4(+) T-cells into FOXP3(+) regulatory T-cells (Treg) and regulates the development and function of B-cells . Also regulates M2 macrophage polarization by inhibiting T-cell activation (By similarity). Also has antibacterial properties by inhibiting growth of Gram negative and Gram positive bacteria through the production of NH4(+) and H2O2 .
PTM: N-glycosylated.
Catalytic Activity: an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+)
Sequence Mass (Da): 62881
Sequence Length: 567
Pathway: Amino-acid degradation; L-tryptophan degradation via pyruvate pathway.
Subcellular Location: Secreted
EC: 1.4.3.2
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P0C2D4 | DDRRSPLEECFQQNDYEEFLEIAKNGLKKTXNPKHVXV | Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme . Is very active against L-Phe and L-Tyr, moderately active against L-Trp, L-Met, L-Leu, L-norleucine (L-2-aminohexanoate), L-Arg and L-norvaline (L-2-aminopentanoate), and slightly active against L-His, L-cystine, and L-Ile . L-Gln, L-Lys, L-Asn, L-ornithine, L-Ala and L-Val are oxidized very slowly . Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis of vascular endothelial cells or tumor cell lines, antibacterial and antiparasitic activities (By similarity). This protein inhibits both agonist- and shear stress-induced platelet aggregation (SIPA) . Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions.
PTM: N-glycosylated.
Catalytic Activity: an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+)
Sequence Mass (Da): 4514
Sequence Length: 38
Subcellular Location: Secreted
EC: 1.4.3.2
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P0DI91 | DDRRSPLEECFQQNDYEEFLEIARNSQLYQESLREDSSYHLSFIESLKSDALFSYEKKFWEADGIHGGKVINDLSLIHDLPKREIQALCYPSIKK | Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme . Is highly active on L-Met, L-Leu, L-Phe, L-Trp, and L-Arg, and no weakly or no active on L-His, L-Tyr, L-Ile, L-Gln, and L-Lys . Exhibits diverse biological activities, such as antibacterial activity against both Gram-positive (B.subtilis) and Gram-negative (E.coli) bacteria, and inhibition of ADP- or collagen-induced platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. This protein may also induce hemorrhage, hemolysis, edema, apoptosis, and have antiparasitic activities.
PTM: N-glycosylated.
Catalytic Activity: an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+)
Sequence Mass (Da): 11216
Sequence Length: 95
Subcellular Location: Secreted
EC: 1.4.3.2
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P81383 | MNDFLLLLLVLFLGVPRSENHVINLEECFQEPEYENWLATASHGLTKTLNPKKIVIVGAGISGLTAAKLFREAGHEVVILEASDRVGGRIKTHREDGWYVDVGPMRVPQTHRIVREYIKKFNISLNPFRQTDENAWYLIKHVRQKMSANNPENFGYQLNPNERGKSASQLFDETLDKVTDDCTLQKEKYDSFSTKEYLIKEGKLSTGAVEMIGDFLNEEAGFHNSFLISVMDHFLFLNNSFDEITGGFDQLPERFFKDMDSIVHLNSTVEKIVHINNKVTVFYEGLSTNMRLVADYVLITATARATRLIKFVPPLSIPKTRALRSLIYASATKIILVCTDKFWEKDGIHGGRSITDLPSRVIYYPNHDFTNGIGVLLASYTWYSDSEFYTTLSDEKCVDVVMDDLVEIHNVSKDYLKSVCGKHVVQKWALDQYSMGAFSTYTPYQITHYSQMLAQNEGRIYFAGEYTAHPHGWIETSMKSAIREAINIHNA | Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme . Is very active against L-Lys, L-Phe, L-Leu, L-Tyr, L-Trp, L-Arg, and L-Met, moderately active against L-His, L-cystine, and L-Ile, and slightly active against L-Gln, L-Asn, L-Ala, and L-Val . L-Glu, L-Ser, L-Pro and Gly are oxidized very slowly . Its activity on platelet aggregation is controversial. It has potent inhibitory activity on platelet aggregation induced by ADP and the thromboxane analog U46619, but not by thrombin, mucetin, ristocetin and stejnulxin , but it has also been shown to induce platelet aggregation through the formation of hydrogen peroxide . It binds to bacteria and shows antibacterial activities by generating hydrogen peroxide. Binding and antibacterial activities are higher against Gram-positive than against Gram-negative bacteria. May also have an ability to induce hemorrhage, hemolysis, edema, apoptosis.
PTM: N-glycosylated.
Catalytic Activity: an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+)
Sequence Mass (Da): 55977
Sequence Length: 491
Subcellular Location: Secreted
EC: 1.4.3.2
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P0C2D6 | ADNKNPLEECFRETNYEEFLEIAR | Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (By similarity). Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis, and antiparasitic activities (By similarity). This protein has antibacterial activity (against E.coli, S.aureus, and B.dysenteriae), cytotoxic activity, as well as an ability to induce platelet aggregation . Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation (By similarity). These different effects are probably due to different experimental conditions (By similarity).
PTM: N-glycosylated.
Catalytic Activity: an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+)
Sequence Mass (Da): 2931
Sequence Length: 24
Subcellular Location: Secreted
EC: 1.4.3.2
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Q8VPD4 | MAFTRRSFMKGLGATGGAGLAYGAMSTLGLAPSTAAPARTFQPLAAGDLIGKVKGSHSVVVLGGGPAGLCSAFELQKAGYKVTVLEARTRPGGRVWTARGGSEETDLSGETQKCTFSEGHFYNVGATRIPQSHITLDYCRELGVEIQGFGNQNANTFVNYQSDTSLSGQSVTYRAAKADTFGYMSELLKKATDQGALDQVLSREDKDALSEFLSDFGDLSDDGRYLGSSRRGYDSEPGAGLNFGTEKKPFAMQEVIRSGIGRNFSFDFGYDQAMMMFTPVGGMDRIYYAFQDRIGTDNIVFGAEVTSMKNVSEGVTVEYTAGGSKKSITADYAICTIPPHLVGRLQNNLPGDVLTALKAAKPSSSGKLGIEYSRRWWETEDRIYGGASNTDKDISQIMFPYDHYNSDRGVVVAYYSSGKRQEAFESLTHRQRLAKAIAEGSEIHGEKYTRDISSSFSGSWRRTKYSESAWANWAGSGGSHGGAATPEYEKLLEPVDKIYFAGDHLSNAIAWQHGALTSARDVVTHIHERVAQEA | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes an oxidative deamination of basic, hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (Ref.1). Is active on most L-amino acid (39 on 43 tested) with the exception of L-Thr, L-Pro, and L-Gly (Ref.1).
PTM: Predicted to be exported by the Tat system.
Catalytic Activity: an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+)
Sequence Mass (Da): 57805
Sequence Length: 534
Subcellular Location: Cytoplasm
EC: 1.4.3.2
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P86810 | MDLHRAPWKSSAAAAVLLLALFSGAAASSVEKNLAACLRDNDYDQLLQTVQDGLPHINTSNHVVIVGAGVAGLTAAKLLQDAGHRVTIVEANSRIGGRVETYRNKEEGWYADLGAMRIPSDHSIFRWFAKTLGVKLNPFIMDDHNTFYFVNGLLKRTYTVEANPDILNYKVRSSEKGKSANTLFQDALQKVKDEVEAHGCRAALMKYDKYSAKEYLKEVAGLSSEALRMIGDLLNEQSLMYTALSEMIYDQADVNDNVQYDEVTGGTDLFPRAFLSVLDVPILLNSKVQRIRRSRDGVTVSFKESQRSSLTDLHADMVLVTTTAKAALYMDFEPSLSIRKMEALRAVHYDSSTKIILTFSSRFWEEDGIRGGKSITDRPSRYIYYPSHTFPANSSVGVLLASYTWSDDSLLLQAASDEELKEMALRDLVKIHGERVRALCTGVVVKKWSLDPYSFGAFALFTPYQHLEYAKELFRSEGRVHFAGEHTAFPHAWMESAMKSAIRAATNINKQTLLNEGMNECPAPDEL | Function: Inhibits the growth of both Gram-negative and Gram-positive bacteria. Displays strong antibacterial activity towards V.cholerae and E.tarda. Causes deformation of the surface of S.aureus and the formation of pores on the surface of E.coli. Strong antiparasitic activity is seen towards C.irritans, T.brucei and I.multifiliis. Cilia of treated theronts are lost and the macronucleus swells, inducing cell membrane rupture and efflux of the cytoplasm.
Catalytic Activity: an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+)
Sequence Mass (Da): 58811
Sequence Length: 527
Subcellular Location: Secreted
EC: 1.4.3.2
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Q6GTS8 | MAQRCVCVLALVAMLLLVFPTVSRSMGPRSGEHQRASRIPSQFSKEERVAMKEALKGAIQIPTVTFSSEKSNTTALAEFGKYIHKVFPTVVSTSFIQHEVVEEYSHLFTIQGSDPSLQPYLLMAHFDVVPAPEEGWEVPPFSGLERDGIIYGRGTLDDKNSVMALLQALELLLIRKYIPRRSFFISLGHDEESSGTGAQRISALLQSRGVQLAFIVDEGGFILDDFIPNFKKPIALIAVSEKGSMNLMLQVNMTSGHSSAPPKETSIGILAAAVSRLEQTPMPIIFGSGTVVTVLQQLANEFPFPVNIILSNPWLFEPLISRFMERNPLTNAIIRTTTALTIFKAGVKFNVIPPVAQATVNFRIHPGQTVQEVLELTKNIVADNRVQFHVLSAFDPLPVSPSDDKALGYQLLRQTVQSVFPEVNITAPVTSIGNTDSRFFTNLTTGIYRFYPIYIQPEDFKRIHGVNEKISVQAYETQVKFIFELIQNADTDQEPVSHLHKL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Secreted enzyme that regulates the endogenous N-fatty acyl amino acid (NAAs) tissue and circulating levels by functioning as a bidirectional NAA synthase/hydrolase . It condenses free fatty acids and free amino acids to generate NAAs and bidirectionally catalyzes the reverse hydrolysis reaction . Some of these NAAs stimulate oxidative metabolism via mitochondrial uncoupling, increasing energy expenditure in a UPC1-independent manner. Thereby, this secreted protein may indirectly regulate whole body energy expenditure. PM20D1 circulates in tight association with both low- and high-density (LDL and HDL,respectively) lipoprotein particles (By similarity).
Catalytic Activity: an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid
Sequence Mass (Da): 55741
Sequence Length: 502
Pathway: Amino-acid metabolism.
Subcellular Location: Secreted
EC: 3.5.1.114
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Q8C165 | MAELLASLPAWAAVLLLFFATVSGSTGPRSRENRGASRIPSQFSEEERVAIKEALKGAIQIPTVSFSHEESNTTALAEFGEYIRKAFPTVFHSSLVQHEVVAKYSHLFTIQGSDPSLQPYMLMAHIDVVPAPEEGWEVPPFSGLERNGFIYGRGALDNKNSVMAILHALELLLIRNYSPKRSFFIALGHDEEVSGEKGAQKISALLQARGVQLAFLVDEGSFILEGFIPNLEKPVAMISVTEKGALDLMLQVNMTPGHSSAPPKETSIGILSAAVSRLEQTPMPNMFGGGPLKKTMKLLANEFSFPINIVLRNLWLFHPIVSRIMERNPITNALVRTTTALTMFNAGIKVNVIPPLAQATINCRIHPSQTVHEVLELVKNTVADDRVQLHVLRSFEPLPISPSDDQAMGYQLLQETIRSVFPEVDIVVPGICIANTDTRHYANITNGMYRFNPLPLNPQDFSGVHGINEKVSVQNYQNQVKFIFEFIQNADTYKEPVPHLHEL | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Secreted enzyme that regulates the endogenous N-fatty acyl amino acid (NAAs) tissue and circulating levels by functioning as a bidirectional NAA synthase/hydrolase. It condenses free fatty acids and free amino acids to generate NAAs and bidirectionally catalyzes the reverse hydrolysis reaction (Probable). Some of these NAAs stimulate oxidative metabolism via mitochondrial uncoupling, increasing energy expenditure in a UPC1-independent manner. Thereby, this secreted protein may indirectly regulate whole body energy expenditure . PM20D1 circulates in tight association with both low- and high-density (LDL and HDL,respectively) lipoprotein particles .
Catalytic Activity: an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid
Sequence Mass (Da): 55663
Sequence Length: 503
Pathway: Amino-acid metabolism.
Subcellular Location: Secreted
EC: 3.5.1.114
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B6QHD2 | MKVSSLLPSVLLLVGATRASPHPAQPPQQQPLNNIIEESNTQTNPPNKHDLEHVIDTSPLLSLHRDLVKFESISGNEADVGDFLIQYLQARDFKVEKQIVVPKGPKGQGERFNIYAYPNSTPEPRVLLSSHMDTVPPYIPYSLDLPSSNGSTTDSLNWRDNILIAGRGSVDAKASVASQILAVLEYLQLHPEAPLGLLFVVGEEVDGIGMQYFSQSELNTSPPTVHTVIFGEPTELALVSGHKGSLFFKISAKGKAAHSGYPWLGQSAVSALLPALVKLDTLADIPVEDGGIPGSEKLGKSTINIGRIDAGIASNVVPASAEASVNIRLAYHDVEKVKEIVTKAVDEATNGDENVTIEWGNKGKGHAPIDFDTDVDGFKVMTVNYATDAWYLKFHEGSGGSPEGRVHTYLYGPGSIFVAHGADEAITVRDLEDAVSGYKKLIEAAFERNKV | Cofactor: Binds 2 Zn(2+) ions per subunit.
Sequence Mass (Da): 48575
Sequence Length: 451
Subcellular Location: Secreted
EC: 3.4.17.-
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Q08BT9 | MAVSRWKAVGSTLLAAFLVGLVVLIAVLLIRTYTLPTAVRKWNRNESLITELAEKERKQLVEALKGAIRIPTVSFSEEEQNTTALREFGEYIQKVFPQVFSSSLIQHEVLGGYSHLFKVQGSDHNLLPYMLLAHIDVVPAPPESWEVPPFSGEERDGYIYGRGTLDDKNCVIGILQSLEFLLKRGHKPRRSFYIGLGHDEEISGHKGAQKIVEKLQSQGVKLAFVLDEGLAVLDGVIQGISQPVALVGTTEKGSVTLDLTVNRLPGHSSMPPSETSIGILAAAVSRLEQNMMPNMFGNGPEQDMFEHLSTKFDFPLNIIMANLWLFSPILSRILELSPSTNAIVRTTTALTIFKAGIKSNVIPPTATATVNFRLHPAQTVQEVLDIVQNTIKDERVELSVLNSFDPLPVSPNDMSLGYHILQRTIHDVFSGPPVAPGVCVGNTDSRHFVNLTNSIYRFSPVVLKKEDVDRIHGLNERISKEAIELLVQFYIQLIQNSDTDNIPPPHLDTHEL | Function: Secreted enzyme that regulates the endogenous N-fatty acyl amino acid (NAAs) tissue and circulating levels by functioning as a bidirectional NAA synthase/hydrolase. It condenses free fatty acids and free amino acids to generate NAAs and bidirectionally catalyzes the reverse hydrolysis reaction. Some of these NAAs stimulate oxidative metabolism via mitochondrial uncoupling, increasing energy expenditure in a UPC1-independent manner. Thereby, this secreted protein may indirectly regulate whole body energy expenditure. PM20D1 circulates in tight association with both low- and high-density (LDL and HDL,respectively) lipoprotein particles.
Catalytic Activity: an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-amino acid
Sequence Mass (Da): 56710
Sequence Length: 512
Pathway: Amino-acid metabolism.
Subcellular Location: Secreted
EC: 3.5.1.114
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Q8IYS1 | MRPGGERPVEGGACNGRSELELLKLRSAECIDEAAERLGALSRAIWSQPELAYEEHHAHRVLTHFFEREPPAASWAVQPHYQLPTAFRAEWEPPEARAPSATPRPLHLGFLCEYDALPGIGHACGHNLIAEVGAAAALGVRGALEGLPRPPPPVKVVVLGTPAEEDGGGKIDLIEAGAFTNLDVVFMAHPSQENAAYLPDMAEHDVTVKYYGKASHSASYPWEGLNALDAAVLAYNNLSVFRQQMKPTWRVHGIIKNGGVKPNIIPSYSELIYYFRAPSMKELQVLTKKAEDCFRAAALASGCTVEIKGGAHDYYNVLPNKSLWKAYMENGRKLGIEFISEDTMLNGPSGSTDFGNVSFVVPGIHPYFHIGSNALNHTEQYTEAAGSQEAQFYTLRTAKALAMTALDVIFKPELLEGIREDFKLKLQEEQFVNAVE | Function: Catalyzes the peptide bond hydrolysis in dipeptides having basic amino acids lysine, ornithine or arginine at C-terminus. Postulated to function in a metabolite repair mechanism by eliminating alternate dipeptide by-products formed during carnosine synthesis.
Catalytic Activity: beta-alanyl-L-lysine + H2O = beta-alanine + L-lysine
Sequence Mass (Da): 47776
Sequence Length: 436
EC: 3.4.13.4
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A3KG59 | MGPVVERPAEPGTSSAAELELLKRRAAERIDEAAERLGALSRAIWSAPELAYEEHRAHGELTRFFECEPPAASWAVQPHFGLPTAFRAEWAPPESAAGPRALQVAFLCEYDALPALGHACGHNLIAEVGVAAALGLRAALESIAAPPPVKVIVLGTPAEEDGGGKIDLIEAGAFENLDVVFMAHPSQENAAYLPDVAEHDVTVKYYGKASHAAAYPWEGVNALDAAVLAYTNLSVLRQQMKPTWRVHGIIKNGGVKPNIIPSYSELVYYFRAPSMKELQVLTKKAEDCFRAAALATGCTVDIESEAHDYYNVIPNKTLCSAYTENGKKLGMEFISEDAVLNGPSGSTDFGNVSFVVPGIHPYFYIGTDALNHTEQYTEAAGSQAAQLYTLRTAKALAMTALDVIFKPALLEGVRKEFKCKLQEEQLLNTAA | Function: Catalyzes the peptide bond hydrolysis in dipeptides having basic amino acids lysine, ornithine or arginine at C-terminus. Postulated to function in a metabolite repair mechanism by eliminating alternate dipeptide by-products formed during carnosine synthesis.
Catalytic Activity: beta-alanyl-L-lysine + H2O = beta-alanine + L-lysine
Sequence Mass (Da): 46482
Sequence Length: 431
EC: 3.4.13.4
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Q6L5H6 | MAAAAAAAAICGEDETAARVGCTGEWAGGIERVDLGERKEAVAAAGAGKRSVYLMDCAPVWGCASTRGRSAEMEDASAAVPRFADVPVRLLASRRDLDALGLDADALRLPAHLFGVFDGHGGAEVANYCRERIHVVLSEELKRLGKNLGEMGEVDMKEHWDDVFTKCFQRVDDEVSGRVTRVVNGGGEVRSEPVTAENVGSTAVVALVCSSHVVVANCGDSRIVLCRGKEPVALSIDHKPDRKDERARIEAQGGKVIQWNGYRVSGILAMSRSIGDRYLKPFVIPKPEVMVVPRAKDDDCLILASDGLWDVVSNEEACKVARRQILLWHKNNGAASPLSDEGEGSTDPAAQAAADYLMRLALKKGSEDNITVIVVDLKPRKKLKNIS | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase involved in abscisic acid (ABA) signaling. Together with PYL3 and SAPK10, may form an ABA signaling module involved in stress response.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 41554
Sequence Length: 387
EC: 3.1.3.16
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Q93YS2 | MTSSIKSSLLNLGLLIIFFVFFFLVINCRGESSTCLAVYKQGGAPAVFQSPKCPRWILQNWGSPTHSGAGRCHTAAIQGRRNYQEDRLLCALDLRIPFPGKTGTPKDVLVGIAAVFDGHNGAEASDMASKLLLDYFALHINFLLDATFSAMTRKLIGRFPTKGDHSVILHGVSRDEIMHLYNLDFQMQFRDSLPLHFDDSLPLDIMKEALLRAIHDIDVTFTKEASNRKLNSGSTATIALIADGQLMVASIGDSKALLCSEKFETLEEARATLVKLYRERRRNRGSSPSRFSDFKLEHGNGLLRFIAKELTKDHHPNREDEKIRVEAAGGYVTEWAGVPRVNGQLTVSRAIGDLTYRSYGVISAPEVMDWQPLVANDSFLVVSSDGIFEKLEVQEVCDLLWEVNNQTSSGAGVPSYCSISLADCLVNTAFEKGSMDNMAAVVVPLKSNLVTQLQRKEQSMNDNKDKIASALPCSNCTLPLPNDINLGPLQLKQAQPLGTMFNRLLRLKTEVFAAFICQRTLLGHLKGK | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 58354
Sequence Length: 528
Subcellular Location: Membrane
EC: 3.1.3.16
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Q65XK7 | MRETGATDEGHACEVVVAGGDGKAAAARRRRRLELRRLGLAAEDDAAAKRIRSVKDGSSSDDSSTEVVPRSWPACVSHGSVSVIGRRREMEDAVAIERTFMASTGDGAGAIRGGGEGEEDFFAVYDGHGGSRVAEACRKRMHVVLAEEVSLRRLRGQSASGGDVRWKEAMLASFARMDGEVVGSVAAAAPRVDGTEPSGFRTVGSTAVVAVVGRRRIVVANCGDSRAVLSRGGVALPLSTDHKPDRPDELERVEAAGGRVINWNGYRVLGVLATSRSIGDYYLKPFVSAEPEVRVVERTDKDEFLILASDGLWDVVSNEVACKIARNCLNGRAASMFPESVSGSSAADAAALLAELAVSRGSRDNISVVVVELRRLKSRAA | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase that acts as positive regulator of seed germination. Involved in the positive regulation of alpha-amylase gene expression. Acts as negative regulator of abscisic acid-mediated responses. May function directly by dephosphorylating ABI5 and suppressing its activity.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 40349
Sequence Length: 381
Subcellular Location: Nucleus
EC: 3.1.3.16
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Q8GY60 | MGGCVSTSSKSTCSSWSNGEKPVRRPYLGIGCCVSKRAKRTFSDHIVSLQNLTSIPNRITSSSKSRSSCIFTQQGRKGINQDAMIVWEDFMSEDVTFCGVFDGHGPYGHLVARKVRDTLPVKLQFFFQTLQSKQNCSKGTRFRRNSSKSAVQEAVKEGSDEDKLKGLWGEAFLKSFKAMDKELRSHPNLDCFCSGSTGVTILKQGSNLFMGNIGDSRAILGSKDSNDSMVATQLTVDLKPDLPREAERIKRCKGRVFAMEDEPEVPRVWLPYDDAPGLAMARAFGDFCLKEYGVISVPEFTHRVLTDRDQFIVLASDGVWDVLSNEEVVDIVASATSRASAARTLVNSAAREWKLKYPTSKMDDCAVVCLFLDGKMDSESDYDEQGFSSATNAVESDDGQRSEPCLQRNFTVRSSSDQENETYGNVNTETDAEDEKTVGDQNWLGLQGVTRVNSLVQLPRFSEEKSKT | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 51851
Sequence Length: 468
EC: 3.1.3.16
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Q6L5C4 | MVYDGAVKDQESSANPASASAALSEASAAASEVTAAAAAGAGAGAAEEGAAVSGRPPRPPHDKRLGVRHPLKHRRFRAGGKVMVEPGDPPSAQEVADEEASEVEQEAAPVEREPPQEEGGDVEVSSAPAEMEVVEGDAMEVSPEPAVAVGESELEGRPGEEEEVSSPVVSQGERKQETAAAAPVPAVEEKKHKDQENKHKEREREKERERVDEVGYMSGGWKSEDGFLSCGYSSFRGKRASMEDFYDIKSSKIDDKQISLFGIFDGHGGSRAAEYLKEHLFENLMKHPEFMTNTKLAISETYKKTDSEFLDSESHTHRDDGSTASTAVLVGNHLYVANVGDSRAVISKAGKAIALSEDHKPNRSDERKRIESAGGVVMWAGTWRVGGVLAMSRAFGNRLLKQFVVADPEIQEQEIDDELEFLILASDGLWDVVPNEDAVSLVKIEEEPEAAARKLTETAFSRGSGDNITCIVVKFQHDKMDGDSSPTSDKS | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 52919
Sequence Length: 491
EC: 3.1.3.16
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Q6L4R7 | MEDLALPAAPPAPTLSFTLLAAAAAVAEAMEEALGAALPPLTAPVPAPGDDSACGSPCSVASDCSSVASADFEGFAELGTSLLAGPAVLFDDLTAASVAVAEAAEPRAVGATARSVFAMDCVPLWGLESICGRRPEMEDDYAVVPRFFDLPLWMVAGDAAVDGLDRASFRLPAHFFAVYDGHGGVQVANYCRKRIHAVLTEELRRAEDDACGSDLSGLESKKLWEKAFVDCFSRVDAEVGGNAASGAPPVAPDTVGSTAVVAVVCSSHVIVANCGDSRAVLCRGKQPLPLSLDHKPNREDEYARIEALGGKVIQWNGYRVLGVLAMSRSIGDKYLKPYIIPVPEVTVVARAKDDDCLILASDGLWDVMSNEEVCDAARKRILLWHKKNAATASTSSAQISGDSSDPAAQAAADYLSKLALQKGSKDNITVVVIDLKAHRKFKSKA | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase that acts as negative regulator of abscisic acid (ABA) signaling. Involved in the regulation of root architecture development and drought resistance. Can dephosphorylate SAPK8 and SAPK10 in vitro. Together with PYL10, SAPK8 and SAPK10, may form an ABA signaling module involved in stress response.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 46684
Sequence Length: 445
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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Q9T010 | MKTDTTLPIIAEDGDCGDSKRVRVADSGYTVGGQDRPVKLPKIENNGDVGTSEGTHVLVDALMAEVAIKDKDGKTNAGHGVVSVMGRQRAMTTAVSTVVDEIPSYDIFGIFDGLRLAKFFEDRLRRLVKEEVKACHGRGVAADWNKVMKSCFSEAVGTVGTTTSAVVTIVGKEEVIVLCRGGARVVLYSHDGVALPLCHIHHHKDGVEQILKIHKRKKIDDFIVLACDGLWDVVSDDDTYQLVKRCLYGKLPPDGCISESSSTKAAVILAELAIARGSKENINVIVIDLKSSTVS | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 31787
Sequence Length: 295
EC: 3.1.3.16
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Q5SMK6 | MCVEESEGAERLDFGEPAAAAADAGKSKSKSPDELPSPRMERVCENTTAADFKQNKSGNFVPNIRSGDWSDIGGRQYMEDTHVCITDLAKNFGYQSVDNEAISFYGVFDGHGGKDAAHFVRDNLPRIIVEDADFPLELEKVVRRSFVHADNQFAKTTLSSGTTALTAMIFGRTLLIANAGDCRAVLSRCGTAIEMSVDHRPCSLSEKLRVESLGGYVDDGYLNGLLGVTRALGDWHLEGMKEAGNPGGPLSAEPELKMITLTKDDEFLIIGSDGIWDVFSNQNVVDFARRRLQEHNDVKSCCREIVEEAIKRGATDNLTAVLVSFHLEAPPQVRVSRPGRVARSISAEGLNSLRTLLRNQ | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 39351
Sequence Length: 360
EC: 3.1.3.16
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Q9SUK9 | MLPVRESLQKQVKILIGLGNLGFGGYRGLYTRFTNPNGFLEPASSDLLLINERRNLSVIGAVSRTFSVPSVSGPAFQVCGYHIDLLLSDPCKSMASLGSKSLFVDRHSASLVSKRFTGGMVSGDGPNRGRISMRLRGKDHNEKSTICAYFAYRGAKRWIYLNQQRRGMGFRGLHSSLSNRLSAGNAPDVSLDNSVTDEQVRDSSDSVAAKLCTKPLKLVSGSCYLPHPDKEATGGEDAHFICAEEQALGVADGVGGWAELGIDAGYYSRELMSNSVNAIQDEPKGSIDPARVLEKAHTCTKSQGSSTACIIALTNQGLHAINLGDSGFMVVREGHTVFRSPVQQHDFNFTYQLESGRNGDLPSSGQVFTVAVAPGDVIIAGTDGLFDNLYNNEITAIVVHAVRANIDPQVTAQKIAALARQRAQDKNRQTPFSTAAQDAGFRYYGGKLDDITVVVSYVAASKEEGKH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 50297
Sequence Length: 467
EC: 3.1.3.16
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P49597 | MEEVSPAIAGPFRPFSETQMDFTGIRLGKGYCNNQYSNQDSENGDLMVSLPETSSCSVSGSHGSESRKVLISRINSPNLNMKESAAADIVVVDISAGDEINGSDITSEKKMISRTESRSLFEFKSVPLYGFTSICGRRPEMEDAVSTIPRFLQSSSGSMLDGRFDPQSAAHFFGVYDGHGGSQVANYCRERMHLALAEEIAKEKPMLCDGDTWLEKWKKALFNSFLRVDSEIESVAPETVGSTSVVAVVFPSHIFVANCGDSRAVLCRGKTALPLSVDHKPDREDEAARIEAAGGKVIQWNGARVFGVLAMSRSIGDRYLKPSIIPDPEVTAVKRVKEDDCLILASDGVWDVMTDEEACEMARKRILLWHKKNAVAGDASLLADERRKEGKDPAAMSAAEYLSKLAIQRGSKDNISVVVVDLKPRRKLKSKPLN | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), drought-induced resistance and rhizogenesis, response to glucose, high light stress, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as the actin reorganization in guard cells in response to ABA. Involved in the resistance to the bacterial pathogen Pseudomonas syringae pv. tomato. Controls negatively fibrillin expression that is involved in mediating ABA-induced photoprotection. May be involved in ABA content regulation. Plays a role in the Pro accumulation in response to reduced water availability (low water potential). Required for the ABA negative regulation of the ethylene-induced hyponastic growth. Involved in acquired thermotolerance of root growth and seedling survival. Activates/represses SRK2E/OST1 in response to ABA-dependent stimuli, especially in stomata closure regulation involving SLAC1. Represses MAPKKK18 activity and promotes MAPKKK18 degradation by the proteasome pathway upon abscisic acid (ABA) treatment . Represses KIN10 activity by the specific dephosphorylation of its T-loop Thr-198, leading to a poststress inactivation of SnRK1 signaling . Restricts MAPKKK20 activity by dephosphorylation .
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 47506
Sequence Length: 434
Domain: The 'lock' site stabilizes the complex made of PP2C, ABA and PYR/PYL/RCAR receptor by keeping receptor 'gate' and 'latch' loops in closed positions.
Subcellular Location: Nucleus
EC: 3.1.3.16
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Q0DBU3 | MARAAGLRALVGIEAAGRGRRVAASPSPGGTPAASRGLPGWPGFCGVGCGSSSSSSFAPPRMQARRAAGSAARTRSPSQSNGWITGGSASEDGRLSWDYSSFKGRRPSMEDRFSIKMTTINEQTVSLFGVFDGHGGSLAAEYLKEHLFENLVNHPELLRDTKLAISQTFLKTDADFLESVSSNPFRDDGSTAVTAILVGNHLYVGNVGDSRVVALKAGKAVPLSEDHKPNRKDEQKRIEDAGGIVVFDDTWRVNGLLAMSRAFGNRALKHYVKAEPDIQEKVVDESLEYLILATDGLWDVMRNEDAVSLLKAQDGPKAAAMKLTEVAHSRLTLDNITCIVLQFHHGKSTNSN | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 37812
Sequence Length: 352
EC: 3.1.3.16
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P49599 | MALLRPHLHRFHSNTLRHSAYPSADAGGGLVVYPTYGRHRCSAIAIDAPSSLTGVTPIRWGYTSVQGFRDEMEDDIVIRSDAVDSFSYAAVFDGHAGSSSVKFLREELYKECVGALQAGSLLNGGDFAAIKEALIKAFESVDRNLLKWLEANGDEEDESGSTATVMIIRNDVSFIAHIGDSCAVLSRSGQIEELTDYHRPYGSSRAAIQEVKRVKEAGGWIVNGRICGDIAVSRAFGDIRFKTKKNDMLKKGVDEGRWSEKFVSRIEFKGDMVVATPDIFQVPLTSDVEFIILASDGLWDYMKSSDVVSYVRDQLRKHGNVQLACESLAQVALDRRSQDNISIIIADLGRTEWKNLPAQRQNVVVELVQAATTIGLVTVGIWMSSHLS | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase specifically required for efficient dephosphorylation of the light-harvesting complex II outer antennae (LCHII) and transition from state 2 to state 1 . State transition plays a central role in response to environmental changes and allows to adjust to changing light conditions via the redistribution of light excitation energy between photosystem II (PSII) and photosystem I (PSI) in a short time by relocating LHCII proteins (Probable). Mainly responsible for the dephosphorylation of Lhcb1 and Lhcb2 but not of the photosystem II core proteins .
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 42719
Sequence Length: 388
Subcellular Location: Membrane
EC: 3.1.3.16
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Q93YW5 | MAGSNILHKIKLKAGFCGSAPDMGRGKSKMWKNITHGFHCVKGKSSHPMEDYVVSEFKKLEGHELGLFAIFDGHLGHDVAKYLQTNLFDNILKEKDFWTDTENAIRNAYRSTDAVILQQSLKLGKGGSTAVTGILIDGKKLVVANVGDSRAVMSKNGVAHQLSVDHEPSKEKKEIESRGGFVSNIPGDVPRVDGQLAVARAFGDKSLKLHLSSEPDITHQTIDDHTEFILFASDGIWKVLSNQEAVDAIKSIKDPHAAAKHLIEEAISRKSKDDISCIVVKFH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 31018
Sequence Length: 283
EC: 3.1.3.16
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Q67UP9 | MGVYLSTPKTEKLSEDGENDKLKFGLSSMQGWRATMEDAHSALLDIDNDTSFFGVFDGHGGRVVAKFCAKYLHREVLRSEAYSAGDLGNAAHKAFFRMDEMMRGQRGWRELQALGDKINQISGMIEGLIWSPRGSDSNDQHDDWAFEEGPHSDFAGPTCGSTACVAIVRNSQLVVANAGDSRCVISRNGQAYNLSRDHKPELEAERERILKAGGYIQMGRVNGTINLSRAIGDIEFKQNKFLSPDKQMLTANPDINTVELCDDDDFLVLACDGIWDCMSSQQLVDFIHEHINTESSLSAVCERVLDRCLAPSTLGGEGCDNMTMILVQFKKPISQNKNVSPAEQSAADKQPTGDTHWSEIHVTEESSS | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 40591
Sequence Length: 368
EC: 3.1.3.16
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Q8RXV3 | MGYLNSVLSSSSQVHSDDGPVSGGGLSQNGKFSYGYASSPGKRSSMEDFYETRIDGVEGEIVGLFGVFDGHGGARAAEYVKQNLFSNLIRHPKFISDTTAAIADAYNQTDSEFLKSENSQNRDAGSTASTAILVGDRLLVANVGDSRAVICRGGNAIAVSRDHKPDQSDERQRIEDAGGFVMWAGTWRVGGVLAVSRAFGDRLLKQYVVADPEIQEEKVDSSLEFLILASDGLWDVVSNEEAVGMIKAIEDPEEGAKRLMMEAYQRGSADNITCVVVRFFSDQAGGIGSSSTNIPIDHGIVPDRISGDSST | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase that modulates defense response to pathogenic bacteria, conferring resistance and promoting salicylic acid (SA) accumulation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 33248
Sequence Length: 311
EC: 3.1.3.16
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Q9SZ53 | MGIYLSTPKTDKFSEDGENHKLRYGLSSMQGWRASMEDAHAAILDLDDNTSFLGVYDGHGGKVVSKFCAKYLHQQVLSDEAYAAGDVGTSLQKAFFRMDEMMQGQRGWRELAVLGDKINKFSGMIEGLIWSPRSGDSANKPDAWAFEEGPHSDFAGPNSGSTACVAVVRDKQLFVANAGDSRCVISRKNQAYNLSRDHKPDLEAEKERILKAGGFIHAGRVNGSLNLSRAIGDMEFKQNKFLPSEKQIVTASPDVNTVELCDDDDFLVLACDGIWDCMTSQQLVDFIHEQLNSETKLSVVCEKVLDRCLAPNTSGGEGCDNMTMILVRFKNPTPSETELKPEASQAEGNHDEPSSSN | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 39203
Sequence Length: 357
EC: 3.1.3.16
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Q9SZT0 | MSKSTSVSTILYLRQRLQGLKIYETSDLIQHINTFDELVGEQVSVDVKIEEKTKDMILLCSLSPLLTTLTCSMVKVAASLRFPNERWLEVITKEPRAFVYHNFLALFFKICKTNEECDHLISLAKPSMARSKVRNALTGLGEESSSRTSSGTFIRSGHDKIVKEIEKRISEFTFIPQENGETLQVINYEVGQKFEPHFDGFQRIATVLMYLSDVDKGGETVFPEAKGIKSKKGVSVRPKKGDALLFWSMRPDGSRDPSSKHGKRHCLSLNLF | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 30754
Sequence Length: 272
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
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Q8GXT7 | MACLSRIFLILMITMSSSSPPFCSGGSRKELRDKEITSKSDDTQASYVLGSKFVDPTRVLQLSWLPRVFLYRGFLSEEECDHLISLRKETTEVYSVDADGKTQLDPVVAGIEEKVSAWTFLPGENGGSIKVRSYTSEKSGKKLDYFGEEPSSVLHESLLATVVLYLSNTTQGGELLFPNSEMKPKNSCLEGGNILRPVKGNAILFFTRLLNASLDGKSTHLRCPVVKGELLVATKLIYAKKQARIEESGECSDEDENCGRWAKLGECKKNPVYMIGSPDYYGTCRKSCNAC | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32173
Sequence Length: 291
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
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F4ILF8 | MRSYGKEKKLVFPYVFIACCFFLAIFGFCFFNLFSQGISFSEIPTTRRSVNDETDSLDHGSSVSNIPFHGLSWNPRVFYLPNFATKQQCEAVIDMAKPKLKPSTLALRKGETAETTQNYRSLHQHTDEDESGVLAAIEEKIALATRFPKDYYESFNILRYQLGQKYDSHYDAFHSAEYGPLISQRVVTFLLFLSSVEEGGETMFPFENGRNMNGRYDYEKCVGLKVKPRQGDAIFFYNLFPNGTIDQTSLHGSCPVIKGEKWVATKWIRDQTYD | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins. Possesses high affinity for leucine-rich repeat and proline-rich extensins of root cell walls that are essential for root hair development. Hydroxyprolines define the subsequent O-glycosylation sites by arabinosyltransferases which elongate the O-arabinosides on extensins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31424
Sequence Length: 274
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
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Q9ZW86 | MAPAMKIVFGLLTFVTVGMVIGSLLQLAFINRLEDSYGTGFPSLRGLRGQNTRYLRDVSRWANDKDAELLRIGNVKPEVVSWSPRIIVLHDFLSPEECEYLKAIARPRLQVSTVVDVKTGKGVKSDVRTSSGMFLTHVERSYPIIQAIEKRIAVFSQVPAENGELIQVLRYEPQQFYKPHHDYFADTFNLKRGGQRVATMLMYLTDDVEGGETYFPLAGDGDCTCGGKIMKGISVKPTKGDAVLFWSMGLDGQSDPRSIHGGCEVLSGEKWSATKWMRQKATS | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxylates preferentially prolines in second positions in the -Pro-Pro-Gly-triplets. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins. Can hydroxylate collagen-like peptides and hypoxia-inducible transcription factor peptides.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31530
Sequence Length: 283
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
|
F4JAU3 | MSMSRLGLLLFVAILLVLLQSSTCLISSPSSIINPSKVKQVSSKPRAFVYEGFLTDLECDHLISLAKENLQRSAVADNDNGESQVSDVRTSSGTFISKGKDPIVSGIEDKLSTWTFLPKENGEDLQVLRYEHGQKYDAHFDYFHDKVNIARGGHRIATVLLYLSNVTKGGETVFPDAQEFSRRSLSENKDDLSDCAKKGIAVKPKKGNALLFFNLQQDAIPDPFSLHGGCPVIEGEKWSATKWIHVDSFDKILTHDGNCTDVNESCERWAVLGECGKNPEYMVGTPEIPGNCRRSCKAC | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins. Possesses high affinity for leucine-rich repeat and proline-rich extensins of root cell walls that are essential for root hair development. Hydroxyprolines define the subsequent O-glycosylation sites by arabinosyltransferases which elongate the O-arabinosides on extensins. Has low affinity for the substrates tested in vitro.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33019
Sequence Length: 299
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
|
Q9LN20 | MAKLRHSRFQARKWSTLMLVLFMLFMLTIVLLMLLAFGVFSLPINNDESSPIDLSYFRRAATERSEGLGKRGDQWTEVLSWEPRAFVYHNFLSKEECEYLISLAKPHMVKSTVVDSETGKSKDSRVRTSSGTFLRRGRDKIIKTIEKRIADYTFIPADHGEGLQVLHYEAGQKYEPHYDYFVDEFNTKNGGQRMATMLMYLSDVEEGGETVFPAANMNFSSVPWYNELSECGKKGLSVKPRMGDALLFWSMRPDATLDPTSLHGGCPVIRGNKWSSTKWMHVGEYKI | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32867
Sequence Length: 287
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
|
Q8LAN3 | MARRGLLISFFAIFSVLLQSSTSLISSSSVFVNPSKVKQVSSKPRAFVYEGFLTELECDHMVSLAKASLKRSAVADNDSGESKFSEVRTSSGTFISKGKDPIVSGIEDKISTWTFLPKENGEDIQVLRYEHGQKYDAHFDYFHDKVNIVRGGHRMATILMYLSNVTKGGETVFPDAEIPSRRVLSENKEDLSDCAKRGIAVKPRKGDALLFFNLHPDAIPDPLSLHGGCPVIEGEKWSATKWIHVDSFDRIVTPSGNCTDMNESCERWAVLGECTKNPEYMVGTTELPGYCRRSCKAC | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 33061
Sequence Length: 298
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
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Q24JN5 | MASKSKQHLRYQPRKSVSRSTQAFTVLILLLVVILILLGLGILSLPNANRNSSKTNDLTNIVRKSETSSGDEEGNGERWVEVISWEPRAVVYHNFLTNEECEHLISLAKPSMVKSTVVDEKTGGSKDSRVRTSSGTFLRRGHDEVVEVIEKRISDFTFIPVENGEGLQVLHYQVGQKYEPHYDYFLDEFNTKNGGQRIATVLMYLSDVDDGGETVFPAARGNISAVPWWNELSKCGKEGLSVLPKKRDALLFWNMRPDASLDPSSLHGGCPVVKGNKWSSTKWFHVHEFKV | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins. Possesses high affinity for leucine-rich repeat and proline-rich extensins of root cell walls that are essential for root hair development. Hydroxyprolines define the subsequent O-glycosylation sites by arabinosyltransferases which elongate the O-arabinosides on extensins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 32691
Sequence Length: 291
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.2
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