wanglab/gogpt-training-data huggingface dataset:
Protein: Protocadherin gamma C4 (Protocadherin gamma subfamily C, 4) (Q91XX0)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MAAMPSTVRSWVEIWWGATLLFLFCHLGYVYGQIRYPVPEESQEGTFVGNVAQDFLLDTESLSARRLQVAGEVNQRHFRVDLDSGALLIKNPIDREALCGLSASCIVPLEFVTEGPLEMYRAEVEIVDVNDHAPRFPRQQLDLEIGEAAPPGQRFPLEKAQDADVGSNSISSYRLSSNEHFALDVKKRSDGSLVPELLLEKPLDREKQSDYRLVLTAVDGGNPPRSGTAELRVSVLDVNDNAPAFQQSSYRISVLESAPAGMVLIQLNASDPDLGPSGNVTFSFSGHTPDRVRNLFSLHPTTGKLTLQGPLDFESENYYEFDVRARDGGSPAMEQHCSLRVDLLDVNDNAPHITVTSELGTLPESAEPGTVVALISVQDPDSGSNGDVSLRIPDHLPFALKSAFRNQFSLVTAGPLDREARSSYDIMVTASDAGNPPLSTHRTIFLNISDVNDNPPSFFQRSHEVFVPENNRPGDLLCSLAASDPDSGLNALISYSLLEPRNRDVSASSFISLNPQTGAVHATRSFDYEQTQTLQFEVQARDRGSPPLSSTVTVRLFVLDLNDNAPAVLRPRARPGSLCPQALPPSVGAGHLVTKVTAVDLDSGYNAWVSYQLLEAPDPSLFAVSRYAGEVRTAVPIPADLPPQKLVIVVKDSGSPPLSTSVTLLVSLEEDTHPVVPDLRESSAPREGESRLTLYLAVSLVAICFVSFGSFVALLSKCLRGAACGVTCFPAGTCACLTRSRRREGLPPSNGILRIQLGSEDPIKFVDVGGHSHGCTPLASAPTRSDSFMMVKSPSAPMAGEPVRPSCPPSDLLYGLEQAPPNTDWRFSQAQRPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGPQFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK
Protein: Venom prothrombin activator omicarin-C non-catalytic subunit (vPA) (Venom coagulation factor Va-like protein) [Cleaved into: Omicarin-C non-catalytic subunit heavy chain; Omicarin-C non-catalytic subunit light chain] (Q58L90)
Organism: Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota)
Function: Snake prothrombin activator that attacks the hemostatic system of prey. This non-catalytic subunit is functionally similar to blood coagulation factor V. It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X. The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271. Cleavage at Arg-320 produces an active intermediate known as meizothrombin. Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271). Cleavage at Arg-271 releases active thrombin from its pro-fragment. This order of events is reversed if the protease component of prothrombinase is used on its own, suggesting that the 271 site is inherently more accessible to proteolysis.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MGRYSVSPVPKCLLLMFLGWSGLKYYQVNAAQLREYRIAAQLEDWDYNPQPEELSRLSESELTFKKIVYREYELDFKQEKPRDELSGLLGPTLRGEVGDILIIYFKNFATQPVSIHPQSAVYNKWSEGSSYSDGTSDVERLDDAVPPGQSFKYVWNITAEIGPKKADPPCLTYAYYSHVNMVRDFNSGLIGALLICKEGSLNANGAQKFFNREYVLMFSVFDESKNWYRKPSLQYTINGFANGTLPDVQACAYDHISWHLIGMSSSPEIFSVHFNGQTLEQNHYKVSTINLVGGASVTANMSVSRTGKWLISSLVAKHLQAGMYGYLNIKDCGHPNTLTRKLSFRELRRIMNWEYFIAAEEITWDYAPEIPSSVDRRYKAQYLDNFSNFIGKKYKKAVFRQYEDGNFTKPTYAIWPKERGILGPVIKAKVRDTVTIVFKNLASRPYSIYVHGVSVSKDAEGAIYPSDPKENITHGKAVEPGQVYTYKWTVLDTDEPTVKDSECITKLYHSAVDMTRDIASGLIGPLLVCKLKALSVKGVQNKADVEQHAVFAVFDENKSWYLEDNIKKYCSNPSSVKKDDPKFYKSNVMYTLNGYASDRTEVLGFHQSEVVQWHLTSVGTVDEIVPVHLSGHTFLSKGKHQDILNLFPMSGESATVTMDNLGTWLLSSWGSCEMSNGMRLRFLDANYDDEDEGNEEEEEDDGDIFADIFSPPEVVKKKEEVPVNFVPDPESDALAKELGLLDDEDNPEQSRSEQTEDDEEQLMIASVLGLRSFKGSVAEEELKHTALALEEDAHASDPRIDSNSARNSDDIAGRYLRTINRRNKRRYYIAAEEVLWDYSPIGKSQVRSLPAKTTFKKAIFRSYLDDTFQTPSTGGEYEKHLGILGPIIRAEVDDVIEVQFRNLASRPYSLHAHGLLYEKSSEGRSYDDNSPELFKKDDAIMPNGTYTYVWQVPPRSGPTDNTEKCKSWAYYSGVNPEKDIHSGLIGPILICQKGMIDKYNRTIDIREFVLFFMVFDEEKSWYFPKSDKSTCEEKLIGVQSSHHTFPAINGIPYQLQGLMMYKDENVHWHLLNMGGPKDIHVVNFHGQTFTEEGREDNQLGVLPLLPGTFASIKMKPSKIGTWLLETEVGENQERGMQALFTVIDKDCKLPMGLASGIIQDSQISASGHVEYWEPKLARLNNTGMFNAWSIIKKEHEHPWIQIDLQRQVVITGIQTQGTVQLLKHSYTVEYFVTYSKDGQNWITFKGRHSETQMHFEGNSDGTTVKENHIDPPIIARYIRLHPTKFYNTPTFRIELLGCEVEGCSVPLGMESGAIKNSEITASSYKKTWWSSWEPFLARLNLEGGTNAWQPEVNNKDQWLQIDLQHLTKITSIITQGATSMTTAMYVKTFSIHYTDDNSTWKPYLDVRTSMEKVFTGNINSDGHVKHFFKPPILSRFIRIIPKTWNQYIALRIELFGCEVF
Protein: Uncharacterized protein (A0A1D8PJ68)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Nucleoporin NSP1
- Globin family profile domain-containing protein
- F-box domain-containing protein
- Uncharacterized protein
- Probable GPI-anchored adhesin-like protein PGA18
Sequence:
MKFSNVAAATVLASTSSACILPIVEGLLNCVFPRPPPPTIPPSPCGGKKCPPPKPCTTRIPQTHTTIVISTYTTGVVTWGGSVTTVTLTPGTTVATIPPTTVTITPGTETVTLPTPTATVPNTKPGTDTATVPTGPNTTTGTSPTGSNTKPGTDTATVPTGPNTTPGTSPTGPNTKPGTESTPATEPTGPNTKPGTESTPATEPTGPNTKPGTESTPATEPTGPNTKPGTESTPGTSPTGPVTTSVPEQSVITITGPGFTTVFTLTPGTNVITTPTGPATNPSDSESKTTPTGPATEPTGPSTKPTGPGGSVVTVTVTESTVETITGPGFSTTVTLTPGTNVITSPTGPATEPTGPSTKPTGPGGSVVTVTVTESTVETITGPGFSTTVTLTPGTNVITSPTGPATEPTGPSTKPTGPGGSVVTVTVTKPTVQTITGSGYTTTVTLTSGTNVITTPTGPATEPTGPNTKPTGIESKTSPTGPVTTLTTSVPEQSVITITGPGFTTVFTLTPGTNVITSPTGTATKPTGTGSEATPTDPATKPSGSATGPSSPGGSVVTVTVTKPTVQTITGSGYTTTVTLTSGTNVITTPTGPATKPSESNTKTSPTGPNTKPSGTESNTKPSPTGPAGTVVTVTVTKPTSETITGPGYTSTVTYSEGTTVVTVPTGTPSTDKPNTSSAPIPSPSKSTGTGTGATTTTTDDGFPSGSGGVTWTPQPGWICQCVRV
Protein: Adenylate kinase 1, chloroplastic (AK 1) (AtPADK1) (EC 2.7.4.3) (ATP-AMP transphosphorylase 1) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase 1) (AMK1) (Q9ZUU1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis, adenine nucleotide metabolism and plant growth.
Subcellular location: Plastid, chloroplast stroma {ECO:0000305|PubMed:18162585}.
Interaction partners:
- Adenosine kinase 2
- Adenosine kinase 1
- Adenylosuccinate lyase
- Adenylosuccinate lyase
- AMP deaminase
- Thiamine pyrophosphokinase 2
- Thiamine pyrophosphokinase 1
- At5g66005
- Alkaline-phosphatase-like family protein
- 5'-nucleotidase
Sequence:
MARLVRVARSSSLFGFGNRFYSTSAEASHASSPSPFLHGGGASRVAPKDRNVQWVFLGCPGVGKGTYASRLSTLLGVPHIATGDLVREELASSGPLSQKLSEIVNQGKLVSDEIIVDLLSKRLEAGEARGESGFILDGFPRTMRQAEILGDVTDIDLVVNLKLPEEVLVDKCLGRRTCSQCGKGFNVAHINLKGENGRPGISMDPLLPPHQCMSKLVTRADDTEEVVKARLRIYNETSQPLEEYYRTKGKLMEFDLPGGIPESWPRLLEALRLDDYEEKQSVAA
Protein: Microfibrillar-associated protein 5 (MFAP-5) (MP25) (Microfibril-associated glycoprotein 2) (MAGP-2) (Q13361)
Organism: Homo sapiens (Human)
Function: May play a role in hematopoiesis. In the cardiovascular system, could regulate growth factors or participate in cell signaling in maintaining large vessel integrity (By similarity). Component of the elastin-associated microfibrils.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Fibrillin-1
- Fibrillin-2
- Microfibrillar-associated protein 2
- Elastin
- Protein jagged-2
- Fibulin-1
- Fibulin-5
- EGF-containing fibulin-like extracellular matrix protein 2
- Fibulin-2
- Lysyl oxidase homolog 1
Sequence:
MSLLGPKVLLFLAAFIITSDWIPLGVNSQRGDDVTQATPETFTEDPNLVNDPATDETVLAVLADIAPSTDDLASLSEKNTTAECWDEKFTCTRLYSVHRPVKQCIHQLCFTSLRRMYIVNKEICSRLVCKEHEAMKDELCRQMAGLPPRRLRRSNYFRLPPCENVDLQRPNGL
Protein: FKBP12-interacting protein of 37 kDa (FIP-37) (Immunophilin-interacting protein AtFIP37) (Protein WTAP homolog) (Q9ZSZ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable regulatory subunit of the N6-methyltransferase complex, a multiprotein complex that mediates N6-methyladenosine (m6A) methylation at the 5'-[AG]GAC-3' consensus sites of some mRNAs. Associates with MTA, MTB, VIR and HAKAI to form the m6A writer complex which is essential for adenosine methylation at specific mRNA sequences. N6-methyladenosine (m6A) plays a role in mRNA stability, processing, translation efficiency and editing. Essential protein required during endosperm development and embryogenesis. Involved in endoreduplication, especially in trichomes. May play a role in splicing events.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:15047892, ECO:0000269|PubMed:28503769}. Nucleus, nucleoplasm {ECO:0000269|PubMed:28503769}. Note=Nuclear with a speckled distribution pattern. {ECO:0000269|PubMed:15047892}.
Interaction partners:
- Protein virilizer homolog
- N
- E3 ubiquitin-protein ligase HAKAI homolog
- N6-adenosine-methyltransferase non-catalytic subunit MTB
- THO complex subunit 2
- Peptidyl-prolyl cis-trans isomerase FKBP12
- 30-kDa cleavage and polyadenylation specificity factor 30
- RNA demethylase ALKBH10B
- RNA demethylase ALKBH9B
- YTH domain-containing protein ECT4
Sequence:
MEFSSQDDDFGGDDSAANATRASGNRRSFGDLEDDEDDIFGSTTVAPGVRTGMILSLRGSLKNCKDDLASCQNELESAKTEIQKWKSAFQNESFVPAGKSPEPRFLIDYIQNLKSSEKSLKEQLEIAKRKEASCIVQYAKREQEMAELKSAVRDLKSQLKPASMQARRLLLDPAIHEEFSRLKNLVEEKDKKIKELQDNIAAVTFTPQSKNGKMLMAKCRTLQEENEEIGHQAAEGKIHELAIKLAMQKSQNAELRSQFEGLYKHMEELTNDVERSNETVIILQEKLEEKEKEIERVKKGLEIVSELVGDKKDEVDEIDEDAKEEIAGGE
Protein: Ataxin-10 (B7YZJ4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEHVKSETKELVHKLVRLSITENEEEISALLKNLRLLLTKGRENQETLAESAEFSSFLNAVAFSPVMRTEHRLIHNLSLQVLANSVVNNETTQALIWSQHGLKIAEQAYASPLGSSNNVLLMIMYNIYISGHGLITDLVALKTCLQLWRALNEAQCTYNFEYLHFFLEHFIVQNGRACVACYQKLETEDRVAFLDYVAHYLRENSPNGDVTLFLLQHFAKEFRMKSDCLLRETIKLKHELHPREVHTLLRIIASASGSEKYANVYPNDQSLFINVSSLLRCIVSAGKEPDGGGLDKPMTKLEEVALTSDIDAGYEKKVSYELKTLLVRCSANLLYDNKANKGYCLDTQLLPTLLECTTMDARNPLMREWSILAIRNACINCPEAQQVIAGLTMQGSAPNDILTELNLDMGALRISDRQ
Protein: UDP-glucuronate 4-epimerase 3 (EC 5.1.3.6) (UDP-glucuronic acid epimerase 3) (O81312)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the synthesis of the negatively charged monosaccharide that forms the backbone of pectic cell wall components.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- UDP-D-apiose/UDP-D-xylose synthase 1
- UDP-sugar pyrophosphorylase
- UDP-D-apiose/UDP-D-xylose synthase 2
- UTP--glucose-1-phosphate uridylyltransferase 2
- UTP--glucose-1-phosphate uridylyltransferase 1
- Sucrose synthase 3
- Sucrose synthase 1
- Sucrose synthase 2
- Sucrose-phosphate synthase 4
- Sucrose-phosphate synthase 1
Sequence:
MKQMSHLDDIPSTPGKFKPYFHRTRWQSSVAKLAFWSLVFVGLIFIFFYRSPVSSNPADPSRRSLRTYSWGGPAWEKRVRSSARLRTRRGFSVLVTGAAGFVGTHVSAALKRRGDGVLGLDNFNDYYDPSLKRARQALLERSGVFVVEGDINDAALLKKLFEVVPFTHVMHLAAQAGVRYAMENPSSYVHSNIAGFVNLLEVCKSANPQPAIVWASSSSVYGLNTKVPFSEKDRTDQPASLYAATKKAGEEIAHTYNHIYGLSLTGLRFFTVYGPWGRPDMAYFFFTRDILKGKAISIFEGVNHGTVARDFTYIDDIVKGCLGALDTAEKSTGSGGKKRGAAQLRVFNLGNTSPVPVTDLVTILERLLKVKAKRNIMKLPRNGDVQFTHANISSAQRELGYKPTTDLQTGLKKFARWYLGYYNGGKKAAS
Protein: Fructose-1,6-bisphosphatase class 2 (FBPase class 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase class 2) (Q03224)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Can functionally substitute for the FBPase class 3 (Fbp) of B.subtilis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Transketolase
- Probable fructose-bisphosphate aldolase
- Transaldolase
- ATP-dependent 6-phosphofructokinase
- Glucose-6-phosphate isomerase
- Fructose-1,6-bisphosphatase class 3
- 3-hexulose-6-phosphate isomerase
- Putative fructokinase
- Mannitol-1-phosphate 5-dehydrogenase
- Uncharacterized sugar kinase YdjE
Sequence:
MERSLSMELVRVTEAAALASARWMGRGKKDEADEAATSAMRDVFDTVPMKGTVVIGEGEMDEAPMLYIGEKLGNGYGPRVDVAVDPLEGTNILASGGWNALTVIAVADHGTLLNAPDMYMQKIAVGPEAVGCIDIEAPVIDNLKAVAKAKNKDVEDVVATILNRERHAKIISELREAGARIKLINDGDVAGAINTAFDHTGVDILFGSGGAPEGVLSAVALKALGGEIIGKLLPQSEEEITRCHKMGLDLSKVLRMEDLVKGDDAIFAATGVTDGELLKGVQFKGSVGTTESLVIRAKSGTVRFVDGRHSLKKKPNLVIRP
Protein: AP-1 complex subunit sigma-3 (Adaptor protein complex AP-1 subunit sigma-1C) (Adaptor-related protein complex 1 subunit sigma-1C) (Clathrin assembly protein complex 1 sigma-1C small chain) (Golgi adaptor HA1/AP1 adaptin sigma-1C subunit) (Sigma 1C subunit of AP-1 clathrin) (Sigma-adaptin 1C) (Sigma1C-adaptin) (Q96PC3)
Organism: Homo sapiens (Human)
Function: Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. Involved in TLR3 trafficking.
Subcellular location: Golgi apparatus. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.
Interaction partners:
- AP-1 complex subunit gamma-1
- AP-1 complex subunit beta-1
- AP-1 complex subunit mu-1
- AP-1 complex subunit mu-2
- AP-1 complex subunit gamma-like 2
- HLA class I histocompatibility antigen, A alpha chain
- ADP-ribosylation factor 1
- AP-1 complex subunit sigma-1A
- AP-1 complex subunit sigma-2
- AP-2 complex subunit beta
Sequence:
MIHFILLFSRQGKLRLQKWYITLPDKERKKITREIVQIILSRGHRTSSFVDWKELKLVYKRYASLYFCCAIENQDNELLTLEIVHRYVELLDKYFGNVCELDIIFNFEKAYFILDEFIIGGEIQETSKKIAVKAIEDSDMLQEVSTVSQTMGER
Protein: Regulator of rDNA transcription protein 5 (P43607)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in the modulation of rDNA transcription.
Interaction partners:
- Uncharacterized protein YFL012W
- Uncharacterized protein YGL138C
- FAS1 domain-containing protein YDR262W
- Endoplasmic reticulum chaperone BiP
- Outer spore wall protein 4
- Small ribosomal subunit protein eS21B
Sequence:
MTEQVNNDTTSDTTTTITTVYISNLPFTASERDLHAFLNNYGASSVLIPTQTVRRFSKRHNSNPRKPLGIAFAQFANNTLALKAIQDLNGTVFQNQKLFLKLHVPYEADSTPDTDVKKPKEKNKVKKTPETAADTVYCHDLPDDITDSEIRELFQLYSPQEIWIYRSKVYRRKCIPFAPHQITAALVTLQSETPIGDICDSVAKTATLRGKSIIVKPAYVSKIQEIKQLVKDNLTNARDPPPAALAEPAPAPAPVEPAEQVQEGQDNAETNDVPPPPASSSDRPTVAAT
Protein: Protein YzcX (CyaX) (O161) (P11291)
Organism: Escherichia coli (strain K12)
Interaction partners:
Sequence:
MVAALFGCQPYLVQRLLAVDNDFAAILKGNGQYAAVDFAVDIAVAIPVVQAFFNGQPELISQAMKFTVVHCCILFLSDGGSIAAWGQGFKVCTSAAAFRHDSSVTGIMMSLCSERFVSSLGRSYTTSFPVSGKHYDQVYRASILTLTELKKTTNKPHCDSA
Protein: Periplasmic [NiFeSe] hydrogenase, large subunit, selenocysteine-containing (EC 1.12.7.2) (Q72AS3)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
- cytochrome-c3 hydrogenase
- Periplasmic [NiFe] hydrogenase small subunit 2
- Periplasmic [NiFe] hydrogenase small subunit 1
- Heterodisulfide reductase, iron-sulfur-binding subunit, putative
- Hydrogenase expression/formation protein, putative
- Pyruvate:ferredoxin oxidoreductase
- Sulfite reductase, dissimilatory-type subunit alpha
- Sulfite reductase, dissimilatory-type subunit beta
- Iron-sulfur protein CooF
- Carbon monoxide dehydrogenase
Sequence:
MSGCTPKAAPAGATGRTTIAIDPVTRIEGHLKAEVVVENGKVVDARLSGGMYRGFETILRGRDPRDASQIVQRICGVCPTAHSTASVLALDEAFGAKVPNNGRITRNLIFGANYLQSHILHFYHLSAQDFVQGPDTAPFVPRFPKSDLRLSKELNKAGVDQYIEALEVRRICHEMVALFGGRMPHVQGQVVGGATEIPTKEKLVEYAARFKKVRDFVEQKYVPVVYTIGSKYKDMFKVGQGFKAALCVGAFPLDNSGKKHLFMPGVYAKGKDMPFDPSKIKEYVKYSWFAEETTGLNYKEGKTIPAPDKAGAYSFVKAPRYDGLSLEVGPLARMWVNNPELSPVGKKLLKDLFGISAKKFRDLGEEAAFSLMGRHVARAEETYYMLGAIEGWLKEIKAGEDTVVMPAVPASAEGTGFTEAPRGSLLHYVKVKDSKIDNYQIVSASLWNCNPRDDMGQRGAVEEALIGIPVDDIQNPVNVARLIRAFDPULGCAVHVLHAESGKVAVIEVK
Protein: Otoancorin (Q8K561)
Organism: Mus musculus (Mouse)
Function: May act as an adhesion molecule.
Subcellular location: Apical cell membrane {ECO:0000305|PubMed:11972037}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:11972037}; Extracellular side {ECO:0000305|PubMed:11972037}. Secreted, extracellular space, extracellular matrix {ECO:0000305|PubMed:11972037}. Note=At the interface between the apical surface of the epithelia and the overlying acellular gel of the tectorial and otoconial membranes.
Interaction partners:
- Alpha-tectorin
- Otogelin
Sequence:
MSQGPRTCSLLLVLLLSHGGAYQREPSPRQDLHPLLQKMAEEIIEGSYLNALLDLTLFERSHVWTADLSHRVLAYLNSKNVAFTIPSLQAVMEAHLEQYLYQPQKLLEDLRATDNQQFHTAMKCLLEDKWGHLDLEDVVINLGDIRDEALQSPGVNRSLFLITLERCFQVLNALECVEVLGRVLRGSSGSFLQPDITERLPQDLHEDAFKNLSAVFKDLYDQTSAHTQRALYSWMTGILRTPFNVTDGSVSWVSAEKLWILGRYMVHLSFEEIMNISPIEIGLFISYDNATKQLDMVYDITPELAQAFLERIRCSSFDVRNISTIHRLGLLVCFYDGLELLDATLAQVLLHQMLKCSRLRGFQAGVQKLKANLLDIATENQTLNETLGSLSDAVVGLTSSQLESLSSDAVHSAISTLNQVTGWGRSQIVILSAKYLAQEKVLSFYNVCQMGVLLAGVGTQAFYSMDHKDLWQVLRSPLSQDMSDLSPVQQQGVLGKLMEAEDATSGIAEVPRALFKEVSLYDLWKESRFNATVLKAKELRRSQALFLYEFLGKTTERPEELLSAGQLVKGVPCSHIDAMSDHLFLALFQYFDNNFSLLSPDQVNCLAWKYWEVSRSSMPPFLLATLPSRFLSSIPPSRCVRFLISLGKRRLETLVLDSDKRSVVVRKVQQCLDGVIADEYTVDIVGHLLCHLPASFIERGISPRAWAAALHGLRSCTALSSEQKAAVRVRLLEQWGPPENWTAETTKDLAPFLAFFSGDELHTVATKFPEILQQTASKMVGVLLPKEFLWAVFESVQNSSNESPSFDPTFGCHGVVTPSSDDIFKLAEANACWDPEVLLCMEEDTFIRNVELLGAVKGFSRAQLMALKEKAIQVWDLPSRWKEHHIVSLGRIALALSESELEQLDLSSIDTVASLGQQTEWTPGQAKSILQAFLEDSGYGIQDLKSFHLVGFGPTLCAMDPTEIQLIKTSEFRAVVARIGTLFCSTPVLAGFKKKAEVVFGRPTEWTSSILQELGTIAAGITKAELRMLNKELMTYFQPSAIRCLPGEVFKELSTEQIASLGPQNAASVTHSQRLQLSSAQLQSLQRALDGAKTHSWQTDPLSSSPTWPASTGSPTGEPASQALWLGCTLLLLTAKS
Protein: Endothelial protein C receptor (Activated protein C receptor) (APC receptor) (Endothelial cell protein C receptor) (CD antigen CD201) (Q4V8I1)
Organism: Rattus norvegicus (Rat)
Function: Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation (By similarity).
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Vitamin K-dependent protein C
- Thrombomodulin
- Prothrombin
- Proteinase-activated receptor 1
- Platelet factor 4
- Tissue factor pathway inhibitor
- Tissue factor pathway inhibitor
- Sphingosine 1-phosphate receptor 1
- Proteinase 3
- Vitamin K-dependent protein S
Sequence:
MLTKFLSLLLLLLLLGCAFCNSDGSQSLHMLQISYFPDPYHGRHQGNASLGKLLTHTLEGPSNNVTILQLQDWQDPDSWARTESGLKIYLSQFNSLVQLIYRERKNDVVFPLTVSCSVGCELPPEEGSEPHVFFDVAVNGSAFVSFQPKTAIWVTGSQEPSEAINFTLKQLNTYNRTRYELQEFLQDTCVQYLENHITTQNTKGSQTGRSYTSLVLGILMGCFIIAGVAVGIFLCTGGRRC
Protein: Putative phosphatidate phosphatase (EC 3.1.3.4) (Germ cell guidance factor) (Phosphatidic acid phosphatase type 2) (Protein wunen) (Q9V576)
Organism: Drosophila melanogaster (Fruit fly)
Function: Responsible for guiding the germ cells early in the process of migration from the lumen of the developing gut towards the overlying mesoderm, where the germ cells enter the gonads. May be involved in lipid metabolism.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- sphingosine kinase
- O-acyltransferase
- sphingosine kinase
- Sphingosine-1-phosphate lyase
- LD18904p
- 3-dehydrosphinganine reductase
- Phosphatidate cytidylyltransferase, photoreceptor-specific
- Neutral ceramidase
- Alkaline ceramidase
- FI05338p
Sequence:
MPAVKIIMSTETSASETTPLRRSENETPDHKELAQSNSNSRQTTVNSNNNNYSNSVQVRLQEQDRDSDSEQQQHTATITMDTNKRILCRVGLDVLILLCAGFPILLFFLLGEPYKRGFFCDDESLKHPFHDSTVRNWMLYFIGAVIPVGVIFIVEVIISQNKAKQDNGNATSRRYVFMNYELPDWMIECYKKIGIYAFGAVLSQLTTDIAKYSIGRLRPHFIAVCQPQMADGSTCDDAINAGKYIQEFTCKGVGSSARMLKEMRLSFPSGHSSFTFFAMVYLALYLQARMTWRGSKLLRHLLQFLFIMVAWYTALSRVSDYKHHWSDVLAGSLIGSISALVVANYVSDLFQKPNTKPYLARTVQDMNASPAQAITITTN
Protein: DNA topoisomerase 2 (EC 5.6.2.2) (DNA topoisomerase II) (P06786)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands. Topoisomerase II makes double-strand breaks. Essential during mitosis and meiosis for proper segregation of daughter chromosomes.
Subcellular location: Nucleus.
Interaction partners:
- DNA topoisomerase 1
- DNA topoisomerase 3
- ATP-dependent helicase SGS1
- Structural maintenance of chromosomes protein 2
- Structural maintenance of chromosomes protein 6
- Tyrosyl-DNA phosphodiesterase 1
- Sister chromatid cohesion protein PDS5
- Ubiquitin-like protein SMT3
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 4
Sequence:
MSTEPVSASDKYQKISQLEHILKRPDTYIGSVETQEQLQWIYDEETDCMIEKNVTIVPGLFKIFDEILVNAADNKVRDPSMKRIDVNIHAEEHTIEVKNDGKGIPIEIHNKENIYIPEMIFGHLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTEFILETADLNVGQKYVQKWENNMSICHPPKITSYKKGPSYTKVTFKPDLTRFGMKELDNDILGVMRRRVYDINGSVRDINVYLNGKSLKIRNFKNYVELYLKSLEKKRQLDNGEDGAAKSDIPTILYERINNRWEVAFAVSDISFQQISFVNSIATTMGGTHVNYITDQIVKKISEILKKKKKKSVKSFQIKNNMFIFINCLIENPAFTSQTKEQLTTRVKDFGSRCEIPLEYINKIMKTDLATRMFEIADANEENALKKSDGTRKSRITNYPKLEDANKAGTKEGYKCTLVLTEGDSALSLAVAGLAVVGRDYYGCYPLRGKMLNVREASADQILKNAEIQAIKKIMGLQHRKKYEDTKSLRYGHLMIMTDQDHDGSHIKGLIINFLESSFPGLLDIQGFLLEFITPIIKVSITKPTKNTIAFYNMPDYEKWREEESHKFTWKQKYYKGLGTSLAQEVREYFSNLDRHLKIFHSLQGNDKDYIDLAFSKKKADDRKEWLRQYEPGTVLDPTLKEIPISDFINKELILFSLADNIRSIPNVLDGFKPGQRKVLYGCFKKNLKSELKVAQLAPYVSECTAYHHGEQSLAQTIIGLAQNFVGSNNIYLLLPNGAFGTRATGGKDAAAARYIYTELNKLTRKIFHPADDPLYKYIQEDEKTVEPEWYLPILPMILVNGAEGIGTGWSTYIPPFNPLEIIKNIRHLMNDEELEQMHPWFRGWTGTIEEIEPLRYRMYGRIEQIGDNVLEITELPARTWTSTIKEYLLLGLSGNDKIKPWIKDMEEQHDDNIKFIITLSPEEMAKTRKIGFYERFKLISPISLMNMVAFDPHGKIKKYNSVNEILSEFYYVRLEYYQKRKDHMSERLQWEVEKYSFQVKFIKMIIEKELTVTNKPRNAIIQELENLGFPRFNKEGKPYYGSPNDEIAEQINDVKGATSDEEDEESSHEDTENVINGPEELYGTYEYLLGMRIWSLTKERYQKLLKQKQEKETELENLLKLSAKDIWNTDLKAFEVGYQEFLQRDAEARGGNVPNKGSKTKGKGKRKLVDDEDYDPSKKNKKSTARKGKKIKLEDKNFERILLEQKLVTKSKAPTKIKKEKTPSVSETKTEEEENAPSSTSSSSIFDIKKEDKDEGELSKISNKFKKISTIFDKMGSTSATSKENTPEQDDVATKKNQTTAKKTAVKPKLAKKPVRKQQKVVELSGESDLEILDSYTDREDSNKDEDDAIPQRSRRQRSSRAASVPKKSYVETLELSDDSFIEDDEEENQGSDVSFNEED
Protein: Protein disulfide-isomerase (PDI) (EC 5.3.4.1) (Thioredoxin-related glycoprotein 1) (P17967)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bonds. Forms a complex with MNL1 to process unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2, promoting degradation in unfolded protein response.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Endoplasmic oxidoreductin-1
- Endoplasmic reticulum chaperone BiP
- ER degradation-enhancing alpha-mannosidase-like protein 1
- Calnexin homolog
- Protein disulfide isomerase MPD2
- Heat shock protein 70 homolog LHS1
- DnaJ-related protein SCJ1
- Protein disulfide-isomerase EUG1
- Transcriptional activator HAC1
- Protein transport protein SEC61
Sequence:
MKFSAGAVLSWSSLLLASSVFAQQEAVAPEDSAVVKLATDSFNEYIQSHDLVLAEFFAPWCGHCKNMAPEYVKAAETLVEKNITLAQIDCTENQDLCMEHNIPGFPSLKIFKNSDVNNSIDYEGPRTAEAIVQFMIKQSQPAVAVVADLPAYLANETFVTPVIVQSGKIDADFNATFYSMANKHFNDYDFVSAENADDDFKLSIYLPSAMDEPVVYNGKKADIADADVFEKWLQVEALPYFGEIDGSVFAQYVESGLPLGYLFYNDEEELEEYKPLFTELAKKNRGLMNFVSIDARKFGRHAGNLNMKEQFPLFAIHDMTEDLKYGLPQLSEEAFDELSDKIVLESKAIESLVKDFLKGDASPIVKSQEIFENQDSSVFQLVGKNHDEIVNDPKKDVLVLYYAPWCGHCKRLAPTYQELADTYANATSDVLIAKLDHTENDVRGVVIEGYPTIVLYPGGKKSESVVYQGSRSLDSLFDFIKENGHFDVDGKALYEEAQEKAAEEADADAELADEEDAIHDEL
Protein: Methylthioribose kinase 1 (MTR kinase 1) (OsMTK1) (EC 2.7.1.100) (Q7XR61)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the phosphorylation of methylthioribose into methylthioribose-1-phosphate.
Interaction partners:
- Os01g0101200 protein
- Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1
- Methylthioribose-1-phosphate isomerase
- Os06g0112200 protein
- Os07g0675000 protein
- Translation initiation factor eIF2B subunit beta
- Acireductone dioxygenase 2-requiring) 2)
- Eukaryotic translation initiation factor 2 alpha subunit family protein, expressed
- Os07g0692800 protein.
- Translation initiation factor eIF2B subunit delta
Sequence:
MAAAAEQQQQQQQQGFRPLDEASLVAYIKATPALAARLGGSLDALTIKEVGDGNLNFVYIVLSDAGSVVIKQALPYIRCVGDSWPMTRERAYFEASALQKHRGLCPDHVPEVYHFDRAMSLIGMRYIEPPHIILRKGLIAGVEYPLLAEHMADYMAKTLFFTSLLYNSTTDHKKGVAQYCDNVEMCRLTEQVVFSDPYMLAKYNRCTSPFLDNDAAAVREDAELKLEIAELKSMFIERAQALLHGDLHTGSIMVTPDSTQVIDPEFAFYGPMGYDIGAFLGNLILAYFSQDGHADQANDRKAYKKWILKTIEDSWNLFHKKFVELWNKHKDGNGEAYLPPIYNSSELLCLAQKKYMTSLFHDSLGFGSAKMIRRIVGIAHVEDFESIEDASKRASCERRALNCAKAILKGRRQFESIGQVIVHVQSFDRD