wanglab/gogpt-training-data huggingface dataset:
Protein: DIS3-like exonuclease 2 (EC 3.1.13.-) (E7F350)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03045}. Cytoplasm, P-body {ECO:0000256|HAMAP-Rule:MF_03045}.
Interaction partners:
- Exosome complex component 10
- Exosome component 4.
- Exosome component 5.
- Exosome complex component MTR3
- Exosome complex component CSL4
- Exosome component 8.
- Exosome complex component RRP45
- Uncharacterized protein.
- Exosome complex component RRP4
- Nuclear nucleic acid-binding protein C1D
Sequence:
MAFSPKAKRTPKNKDGKGAQNLPKPQKDAYSRLLNQHQNGKFRSYLQEFVEQQSEENATTSVSRSDANRRKKGHSESSYFGDSVSSPQSRPMLADTFNSFHADKTFHQVTCAEDPGTNPGMLEKLHKGSAPKKASAKLKKSEKDIKASTSLVGSEEGDAQQLSGSCGEEKTRKKSKKKSSKGHLEKKDKGACGLEVDAAEKSANKNVKASQALKGSRQIDKKDINAKDGRASGKQVFEQYMSVEDVSAGLKRGELIQGVLRINPKKYKEAYIPSPDGSADIFLDGISARNRALNGDVVVVKVLPLEQSQATKTPDVIVEAHYNGDDEMVSKMEKVSLNDKALLTTQSVEHATTSNTPASSSERTTQKNGKVVFIVEKKHSRAVSGFLKFLPNKRFAMFSPVDHRVPRVNVPLADCPADFTSRPGDYENTLFICRITQWPADSNFAEGRLAKTLGQAGEIEPETEGILTEYGVDFSEFTEEVLNCLPQDLPWSIPAHELSTRRDLRKECIFTIDPATARDLDDALSCKQLSDGNFEVGVHIADVSYFVKEGNALDELAGQRATSVYLVQKVIPMLPRLLCEELCSLNPLTDRLTFSVIWKLSPEGKILSEWFGRTVICSCIKLSYDHAQSMIDAPDKHFSPEELPACSPNHSIIEIQEAVLNLHNIAKQLRAQRFEGGALRLDQLKLSFTLDKESSMPQGCYVYQYRDSNKLVEEFMLLANMAVGHQIYRSYPELALLRRHPPPQTKMVDDMQEFFDQMGLDIDFSSSGALHRSLNENLGDDEYTAARKEVITHMCSRPMQMAVYFCAGALKDEKLFRHYALNVPLYTHFTSPIRRYADVIVHRLLGASLNCGPRLSVSGEEVHQQASHCNDRKTASKRVQELSSELFFAVFVKECGPLDSEAMVMGVLDQSFDVLVLRYGVQKRIYCNSLEGLKEVEFRKVGKKPEMTLVWETDDPSKDSIKQEISIFTLLNVQLKADGAPMKYSATLKRPLAPM
Protein: V-type proton ATPase catalytic subunit A (EC 7.1.2.2) (V-ATPase 69 kDa subunit) (Vacuolar proton pump subunit alpha) (C9JA17)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDIKWDFTPCKNLRVGSHITGGDIYGIVSENSLIKHKIMLPPRNRGTVTYIAPPGNYDTSDVVLELEFEGVKEKFTMVQVWPVRQVRPV
Protein: Benzil reductase ((S)-benzoin forming) IRC24 (EC 1.1.1.320) (Increased recombination centers protein 24) (P40580)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Reduces benzil stereospecifically to (S)-benzoin. Is probably involved in a pathway contributing to genomic integrity.
Interaction partners:
- Putative ATP-dependent helicase IRC3
- Uncharacterized ATP-dependent helicase IRC5
- Increased recombination centers protein 21
Sequence:
MGKVILITGASRGIGLQLVKTVIEEDDECIVYGVARTEAGLQSLQREYGADKFVYRVLDITDRSRMEALVEEIRQKHGKLDGIVANAGMLEPVKSISQSNSEHDIKQWERLFDVNFFSIVSLVALCLPLLKSSPFVGNIVFVSSGASVKPYNGWSAYGCSKAALNHFAMDIASEEPSDKVRAVCIAPGVVDTQMQKDIRETLGPQGMTPKALERFTQLYKTSSLLDPKVPAAVLAQLVLKGIPDSLNGQYLRYNDERLGPVQG
Protein: Protein argonaute-3 (Argonaute3) (mAgo3) (EC 3.1.26.n2) (Argonaute RISC catalytic component 3) (Eukaryotic translation initiation factor 2C 3) (eIF-2C 3) (eIF2C 3) (Piwi/argonaute family protein meIF2C3) (Q8CJF9)
Organism: Mus musculus (Mouse)
Function: Required for RNA-mediated gene silencing (RNAi). Binds to short RNAs such as microRNAs (miRNAs) and represses the translation of mRNAs which are complementary to them. Proposed to be involved in stabilization of small RNA derivates (siRNA) derived from processed RNA polymerase III-transcribed Alu repeats containing a DR2 retinoic acid response element (RARE) in stem cells and in the subsequent siRNA-dependent degradation of a subset of RNA polymerase II-transcribed coding mRNAs by recruiting a mRNA decapping complex involving EDC4. Possesses RNA slicer activity but only on select RNAs bearing 5'- and 3'-flanking sequences to the region of guide-target complementarity (By similarity).
Subcellular location: Cytoplasm, P-body {ECO:0000255|HAMAP-Rule:MF_03032}.
Interaction partners:
- Endoribonuclease Dicer
- Protein argonaute-2
- Protein argonaute-1
- Trinucleotide repeat-containing gene 6A protein
- Protein argonaute-4
- RISC-loading complex subunit TARBP2
- Ribonuclease 3
- Trinucleotide repeat-containing gene 6C protein
- Interferon-inducible double-stranded RNA-dependent protein kinase activator A
- Exportin-5
Sequence:
MEIGSAGPIGAQPLFIVPRRPGYGTMGKPIKLLANCFQVEIPKIDVYLYEVDIKPDKCPRRVNREVVDSMVQHFKVTIFGDRRPVYDGKRSLYTANPLPVATTGVDLDVTLPGEGGKDRPFKVSVKFVSRVSWHLLHEALAGGTLPEPLELDKPVSTNPVHAVDVVLRHLPSMKYTPVGRSFFSAPEGYDHPLGGGREVWFGFHQSVRPAMWKMMLNIDVSATAFYKAQPVIQFMCEVLDIHNIDEQPRPLTDSHRVKFTKEIKGLKVEVTHCGTMRRKYRVCNVTRRPASHQTFPLQLENGQTVERTVAQYFREKYTLQLKYPHLPCLQVGQEQKHTYLPLEVCNIVAGQRCIKKLTDNQTSTMIKATARSAPDRQEEISRLVRSANYETDPFVQEFQFKVRDEMAHVTGRVLPAPMLQYGGRNRTVATPSHGVWDMRGKQFHTGVEIKMWAIACFATQRQCREEILKGFTDQLRKISKDAGMPIQGQPCFCKYAQGADSVEPMFRHLKNTYSGLQLIIVILPGKTPVYAEVKRVGDTLLGMATQCVQVKNVIKTSPQTLSNLCLKINVKLGGINNILVPHQRPSVFQQPVIFLGADVTHPPAGDGKKPSIAAVVGSMDAHPSRYCATVRVQRPRQEIIQDLASMVRELLIQFYKSTRFKPTRIIFYRDGVSEGQFRQVLYYELLAIREACISLEKDYQPGITYIVVQKRHHTRLFCADRTERVGRSGNIPAGTTVDTDITHPYEFDFYLCSHAGIQGTSRPSHYHVLWDDNFFTADELQLLTYQLCHTYVRCTRSVSIPAPAYYAHLVAFRARYHLVDKEHDSAEGSHVSGQSNGRDPQALAKAVQIHQDTLRTMYFA
Protein: Envelope glycoprotein B (gB) (P18538)
Organism: Gallid herpesvirus 2 (strain RB-1b) (GaHV-2) (Marek's disease herpesvirus type 1)
Function: Envelope glycoprotein that forms spikes at the surface of virion envelope. Essential for the initial attachment to heparan sulfate moieties of the host cell surface proteoglycans. Involved in fusion of viral and cellular membranes leading to virus entry into the host cell. Following initial binding to its host receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. May be involved in the fusion between the virion envelope and the outer nuclear membrane during virion egress.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-Rule:MF_04032}.
Interaction partners:
Sequence:
MHYFRRNCIFFLIVILYGTNSSPSTQNVTSREVVSSVQLSEEESTFYLCPPPVGSTVIRLEPPRKCPEPRKATEWGEGIAILFKENISPYKFKVTLYYKNIIQTTTWTGTTYRQITNRYTDRTPVSIEEITDLIDGKGRCSSKARYLRNNVYVEAFDRDAGEKQVLLKPSKFNTPESRAWHTTNETYTVWGSPWIYRTGTSVNCIVEEMDARSVFPYSYFAMANGDIANISPFYGLSPPEAAAEPMGYPQDNFKQLDSYFSMDLDKRRKASLPVKRNFLITSHFTVGWDWAPKTTRVCSMTKWKEVTEMLRATVNGRYRFMARELSATFISNTTEFDPNRIILGQCIKREAEAAIEQIFRTKYNDSHVKVGHVQYFLALGGFIVAYQPVLSKSLAHMYLRELMRDNRTDEMLDLVNNKHAIYKKNATSLSRLRRDIRNAPNRKITLDDTTAIKSTSSVQFAMLQFLYDHIQTHINDMFSRIATAWCELQNRELVLWHEGIKINPSATASATLGRRVAAKMLGDVAAVSSCTAIDAESVTLQNSMRVITSTNTCYSRPLVLFSYGENQGNIQGQLGENNELLPTLEAVEPCSANHRRYFLFGSGYALFENYNFVKMVDAADIQIASTFVELNLTLLEDREILPLSVYTKEELRDVGVLDYAEVARRNQLHELKFYDINKVIEVDTNYAFMNGLAELFNGMGQVGQAIGKVVVGAAGAIVSTISGVSAFMSNPFGALAIGLIIIAGLVAAFLAYRYVNKLKSNPMKALYPMTTEVLKAQATRELHGEESDDLERTSIDERKLEEAREMIKYMALVSAEERHEKKLRRKRRGTTAVLSDHLAKMRIKNSNPKYDKLPTTYSDSEDDAV
Protein: Abca12 protein (B2RY21)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MASQFHQLRILVWKNWLGVKRQPLWTLVLILWPVIIFIILAITRTKFPPTAKPTCYLAPRNLPSAGFFPFLQTLLCDTDSKCKDTPYGPRDLLRRKGIDGPLFKESEILKKPSNPKRDSNLSLRSTQVPERSHTSLATVPPRPSYDLEGTGTENFNGSQLLTRILGLEKLLKQNSTPEDIRRELCESYPGYTADYAFSWVTLGKNVFNKFCLSNMTLLESSLQELKYQVSQMSSDPDNQKRVFRGLVQVLSFFSQVQQQREVWQLLSSLPDVFQNGTSLSSLFGVLQKANRVLLVVQKVYPRVQTDEGFSTLQKSVKHLLNTLDSPMQGDNSTHAWSDDDEQTLSPSSLAAQLLILENFEDAILNISSNSPYSPYLACVRNMTDNLAKGSPDNLKLLQSTIHFRKSFLQNGSSEDSFPPFLEILKSKLSQLRNLTELLCESETFSSIKKSCQFSNMSFERLCEDHAFHVQLIEAAELGTDLTTGLLYHDNIISAKLRGLLTGDPSKINLNVDWLLEQALQMNYLENITRLIPTVEAMLHVNTSADASEKPGQLREMFKNIDLLKEDLRAIGMSNTSIDKLLAIPIPDNRAEIISRVFWLHSCDTNVTNPKLEDAMKEFCKLPLPERSHQSYLIGLTLLHYLDIYNFTYKVFFPRKDQKPMERMMELFIKLREILNQLASGTHPLLDKMRSLRQMHLPRSVPLTQAMYRNTRMNSPAGSFSTISQALCSQGITTEYLTAMLPSSQKPKGNHTKDFLTYKLTKEEIASKYGIPLNATPFCFSLYKDIINMPAGPVIWAFLKPMLLGKILYSPYNPTTKAIMEKSNVTLRQLAELREKSQEWMDKSPIFMNSFHLLNQTIPMLQNTLRNPFVQVFVKFSVGLDAVELLKQIDDLDVLRLKLVNNIDIIDQLNTLSSLTVNISSCVLYDRIQASDTVEEMEAVAEQLYKSNELFGSVIFKLPSNGSSHRGFDPEKVSLPPIVRYTIRMSLKTAQTTRSIRTKIWAPGPHNSPSHNQIYGRAFIYLQDSIERAIIELQTGRNSQEVAVQVQAVPYPCFMKDNFLTSVSYSLPIVLMVAWVVFIAAFVKKLVYEKDLRLHEYMKMMGVNSCSHFFAWLIESIGFLLVTIAILIVILKFGNILPKTNGFILFLYFSDYSFSVIAMSYLISVFFNNTNIAALIGSLIYVIAFFPFIVLVTVEDELSYVIKVFMSLLSPTAFSYASQYIARYEEQGVGLQWENMYKSPVQDDTTSFGWLCCLILADSFIYFFIAWYVRNVFPGTYGMAAPWYFPILPSYWKERFGCAEVKHEKSNGLMFTNIMMQNTNPSASKTSPDCAFPSNIEPEPKDLQVGVALHGVTKIYGSKTAVENLNLNFYEGHITSLLGPNGAGKTTTISMLTGLFGATAGTIFVYGKDIKTDLNTVRKNMGVCMQHDVLFSYLTTKEHLLLYGSIKVPHWTKTQLHEEVKRTLKDTGLYSHRHKRVGTLSGGMKRKLSISIALIGGSRVVILDEPSTGVDPCSRRSIWDVISKNKTARTIILSTHHLDEAEVLSDRIAFLEQGGLRCCGSPFYLKEAFGDGYHLTLTKKKSPNLDTNAICDTVAVTAMIQSHLPEAYLKEDIGGELVYVLPPFSTKVSGAYLSLLRALDKGMGKLNIGCYGISDTTVEEVFLNLTKDSQKSSNMSLEHLTQRKVGNPSANGTSTPDDLSVSSSNFTDRDDKVLTRSEKLEGFGLLLKKIMAILIKRFHHTRRNWKGLIAQVILPIVFVATAMGLGTLRDSSNSYPEIMISPSIYGTSEQTAFYANFDPSTSGLVSALWNFPGIDNVCLNTSDLQCLKKDDLGKWNTSGEAIDNFGVCSCSDNVQECPKFNYHPPHRRTYSSQVIYNLTGKHMENYLITTANHFVQKRYGGWSFGMKLTNDLRFDVTAVPDNRTLAKVWYDPEGYHSLPAYLNSLNNFLLRVNMSEYDAARHGIIMYSHPYPGVQDQEQATISSLIDILVALSILMGYSVTTASFVTYIVREHQTKAKQLQHISGIGVTCYWVTNFIYDMVFYLVPVAFSIGVIAIFKLPAFYSGNNLGAVSLLLLLFGYATFSWMYLLAGLFHETGMAFITYVCVNLFFGINSIVSLSVVYFLSKEKPNDPTLELISETLKRIFLIFPQFCFGYGLIELSQQQAVLDFLKAYGVEYPSETFEMDKLGAMFVALVSQGTMFFLLRLLINEWLIKKLRLFFRKFTSSPIMETVDEDEDVRAERLRVESGAAEFDLVQLHRLTKTYQLIHKKIIAVNNISLGIPAGECFGLLGVNGAGKTTIFKMLTGDIIPSSGNILIRNKSGSLGHVDSHSSLVGYCPQEDALDDLVTVEEHLYFYARVHGIPEKDIKDTVHKLLRRLHLMAYKDRSTSMCSYGTKRKLSTALALIGKPSILLLDEPSSGMDPKSKRHLWRIISEEVQNKCSVILTSHSMEECEALCTRLAIMVNGRFQCIGSLQHIKSRFGRGFTVKVHLKNNKVSMETLTKFMQLHFPKTYLKDQHLSMLEYHVPVTAGGVANIFDLLETNKTALNITNFLVSQTTLEEVFINFAKDQKSYENVDTSSQGSTISVDSQEDQLDS
Protein: Uncharacterized protein, isoform F (Uncharacterized protein, isoform G) (Q7KUD8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAALQRKLVHKQFNSPMGLYSQENVKATLNRELKAFGGEGIEVDDQITKPLNLANSAVLRAVEEEEQQAKCGYKRVAWPPASEERIIREFTPQPQTQSPAPGAGGYYPQAHAPTAAAAAPPQQQYGAPSYDGQQPGAQWQQQQQQQQVPQQQYQPQSQAQAPYQPPQWNQPQQQQQQPSYQASPYQQQQQQQPSYYPQQNGGSTYAQPPYNSYSQPQLPYSQDQTDLQQQQQQQQQQYPGAYAGQDSYRGASPGIITLRKEAPVSQKPAPVYTSQPAAVSYQGGSKLRGDLKWPPPEYKEAAARENEERRQLALGPVCRPRRVNRDYTPFFAKHQLNNGYPSYKVPPGTQHIFG
Protein: Phosphotransferase IIC component GlvC (PTS system EIIC component) (P31452)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. This operon may be cryptic in wild-type K12 strains (Probable).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein. Note=When overexpressed using vectors that provide a promoter and ribosome binding site (PubMed:15919996). {ECO:0000269|PubMed:15919996}.
Interaction partners:
Sequence:
MLSQIQRFGGAMFTPVLLFPFAGIVVGLAILLQNPMFVGESLTDPNSLFAQIVHIIEEGGWTVFRNMPLIFAVGLPIGLAKQAQGRACLAVMVSFLTWNYFINAMGMTWGSYFGVDFTQDAVAGSGLTMMAGIKTLDTSIIGAIIISGIVTALHNRLFDKKLPVFLGIFQGTSYVVIIAFLVMIPCAWLTLLGWPKVQMGIESLQAFLRSAGALGVWVYTFLERILIPTGLHHFIYGQFIFGPAAVEGGIQMYWAQHLQEFSLSAEPLKSLFPEGGFALHGNSKIFGAVGISLAMYFTAAPENRVKVAGLLIPATLTAMLVGITEPLEFTFLFISPLLFAVHAVLAASMSTVMYLFGVVGNMGGGLID
Protein: Small ribosomal subunit protein uS17 (40S ribosomal protein S11) (Q20206)
Organism: Caenorhabditis elegans
Interaction partners:
- Ribosomal protein
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein eL20
- Large ribosomal subunit protein eL13
- Small ribosomal subunit protein eS19
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein eL15
Sequence:
MSEQTERAFLKQPTVNLNNKARILAGSKKTPRYIREVGLGFKAPRDAVEGTYIDKKCPWAGNVPIRGMILTGVVLKNKMTRTIVVRRDYLHYIKKYRRYEKRHKNVPAHCSPAFRDIHPGDLVTIGECRPLSKTVRFNVLKVNKSGTSKKGFSKF
Protein: S-antigen protein (Q03400)
Organism: Plasmodium falciparum (isolate 3D7)
Function: S antigens are soluble heat-stable proteins present in the sera of some infected individuals.
Subcellular location: Parasitophorous vacuole {ECO:0000250|UniProtKB:P04927}. Note=Localizes to the cell periphery in early schizonts and then to the parasitophorous vacuole in late schizonts. Following schizont rupture, the S-antigen is released in host sera. {ECO:0000250|UniProtKB:P04927}.
Interaction partners:
- Nucleoporin NUP221, putative
- Merozoite surface protein 2
Sequence:
MNRILSVTLCLFFIYLYIYKTYGKVKNTDEGLSNIYGAKYYLRSGLFNEKNGKGQKYEDLEEEKEGENDDEEDSNSEESNNDEENELIKGQEGVEQETHGSEDEVSNGREDKVSNGGEDEVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGREDKVSNGGEDEVSNGREDKVSNGREDKVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGREDEVSNGREDKVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGREDKVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGREDKVSNGREDEVSNGREDKVSNGGEDEVSNGREDKVSNGREDKVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGREDKVSNGREDKVSNGGEDEVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGGEDEVSNGREDKVSNGREDEVSNGREDKGGAGTDGELSHNSESHTKNKKSKNSIINMLIGM
Protein: Netrin receptor unc-40 (Uncoordinated protein 40) (G5EF96)
Organism: Caenorhabditis elegans
Function: Receptor for netrin unc-6 required for asymmetric axon formation, axon guidance and cell migrations. Required during axon formation, in response to unc-6, to initiate, maintain and orient asymmetric neuronal growth, and may signal via phosphoinositide 3-kinase (PI3K). Mediates axon attraction of neuronal growth cones in the developing nervous system upon ligand binding. Axon migration is mediated by the secreted unc-6, which promotes attraction of neurons and axons through binding to the unc-40 receptor, while repulsion requires both unc-5 and unc-40 receptors. Involved in dendritic morphogenesis; may act by localizing unc-6 at the tips of growing dendrites for interaction with unc-5 on the apposing branch to induce mutual repulsion. Involved in the ventral-dorsal and anterior-posterior migration of gonadal distal tip cells (DTCs) along the body. Involved in the positioning of ray 1, the most anterior ray sensilium, in the male tail. Positively modulates a TGF-beta-like signaling pathway, independent of its role in unc-6 mediated axon guidance, in association with RGM drag-1. Mediates attraction of muscle plasma membrane extensions, known as muscle arms, towards the secreted madd-4 guidance cue, enhanced by interaction with the coreceptor eva-1.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Netrin unc-6
- Netrin receptor unc-5
- CRAL-TRIO domain-containing protein
- E3 ubiquitin-protein ligase TRIM9
- Repulsive guidance molecule B homolog drag-1
- Slit homolog 1 protein
- Ras-related protein ced-10
- UNC-34
- Protein madd-4
- Inactive tyrosine-protein kinase kin-32
Sequence:
MILRHFGFILIILTVYLSSTHATTRKHHRRSIDNDARNLGFQFVMEPRRNVTVMESSSHLLECSYVLAHERLVHDVRIEWKRDGVLLSERTSSRIKVMSNGSLWIESVSSAEEGTYQCAVHVTTKSDQTSDTWTFLSRKATLRLADLAKFELQAIDRTLAKGQPTAFHCLINSKPTPTAVWLHNDEPIVNGGEYHILPVSNTLEISSTQSRHEGTYRCTVEGAGKRRSSQTARLTVTTETVSNELVFITTPRLQVVEQGDEFLLECLVASLIRPQVRWLKDSRQIIVDGVRIRRVGVSSILVSRASIEDTGLYTCRASNNDDSIDRAVSVEVRAPPRITTRPTTKVAVETADVELECGTAAARPEARVNWYKNGEAIIGSEYFVIEPNRLRILGVVRADQAIYQCIAENDVGSEQASAQLLVDAPDSSSVAASSGVPMTSSAPLGLRSTSSGSRFINVEWDPPVQRNGNIMRYHIFYKDNLIDRERMINSSSTSATLTSLQPSTMYLIRVTAENEAGMGKFSDSLKVTTNKEQAVPGKVASLTTTATGPETIDIRWSPPSGGQPALRYKIFYSHDPLEKNEKETLITTSTTHYTLHGMDKYTGYQIRIEAEGSNGSGLSSDTVKVRTQSDEPSAPPVNIQAEADSSTSVRVSWDEPEEESVNGEITGYRLKYKTKARGAKGNTLVIDATAREYTMGNLEPNTQYLIRMAVVNHNGTGPFSDWVSIDTPGQDKEERTLGAPREIRPHAGIDYILVSWLPPADEQNLVRGYQIGWGLSVPDTETIRVTASTTQYKIARLHSERDYVISLRAFNNLGSGFPIYETVRTLSRETPSHFNEDSDSDDSDVGSSESTPVGVRAEAISATSIRVMWTESDETAFNTQYTVRYSTAVDGNQHRYVNSTETWATVEGLRPATEYEFAVRAVASNGQLSTWSMATRNRTLAAPPSSAPRDLTVLPAESGDPHSSSLHWQPPKYSNGEIEEYLVFYTDRASLADKDWTINYVAGDKLSHQVSNLLPKANYFFKIQARNEKGHGPFSSVVGYTPSGGAILSGKDRHNARGHGSAASGDTVSLVDQLQSLLHSNPLYLILLAAFALILILTLILIIMCCWKRSSGGGRKNGYQSGKKTSAGAGSGGGIGGLGGPPNDLWINGTGSHMRAGASDYMVDGLATAHLTAADIESPTPRYHHLQGQGTLTRSYHQSSQSLEGRQRTPQVVYTGTGRHQPIQRIDFESPYGSSSAIGSASTPPLPMQAPPSGPPTVIDGYRTLRGTPPNSSAANALRSFTQLAGATPPPPHSAASSSSRPTIIAAGGRQVPVGRATAQPRVNVANIYSPFASCSASSDAGESDKKSGECMEMRETTPIKSNTAGSSNGEKMNTNMNPSHSAEDLNAHLENLDTMLDDLQQLQHNLHFETSMDK
Protein: IRG-type G domain-containing protein (Q3U0K0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MDQFISAFLKGASENSFQQLAKEFLPQYSALISKAGGMLSPETLTGIHKALQEGNLSDVMIQIQKAISAAENAILEVAVIGQSGTGKSSSINALRGLGHEADESADVGTVETTMCKTPYQHPKYPKVIFWDLPGTGTPNFHADAYLDQVGFANYDFFIIISSSRFSLNDALLAQKIKDAGKKFYFVRTKVDSDLYNEQKAKPIAFKKEKVLQQIRDYCVTNLIKTGVTEPCIFLISNLDLGAFDFPKLEETLLKELPGHKRHMFALLLPNISDASIELKKHFLREKIWLEALKSAAVSFIPFMTFFKGFDLPEQEQCLKDYRSYFGLDDQSIKEIAEKLGAPLADIKGELKCLDFWSLVKDNSIIAQATSAAEAFCAVKGGPESSAFQALKVYYRRTQFLNIVVDDAKHLLRKIETVNVA
Protein: Iron-sulfur cluster-binding protein (Q72E92)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Aldehyde:ferredoxin oxidoreductase, tungsten-containing, putative
- Thiosulfate reductase, putative
- Menaquinone reductase, molybdopterin-binding-like subunit
- Molybdopterin oxidoreductase domain protein
- Ribonuclease H
- DUF302 domain-containing protein
- Reductase, transmembrane subunit, putative
- Iron-sulfur protein CooF
- Formate dehydrogenase 2 subunit alpha
- Formate dehydrogenase, alpha subunit, selenocysteine-containing
Sequence:
MERCIGCHACSLACARLVHKRLSWVTAGIRITSAGGLSTGFEARLCLACDPAPCAQACPTGAYAQRKGGGVKVDRSLCIRCGRCAEACPVDAVHMDGETGLPYVCIHCGRCVAFCPHECIELVDQPVADAASDEAGRETGDDKALPRKAGLVNDASEVGHAD
Protein: Phosphatidate phosphatase LPIN3 (EC 3.1.3.4) (Lipin-3) (Lipin-3-like) (Q9BQK8)
Organism: Homo sapiens (Human)
Function: Magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis therefore regulates fatty acid metabolism.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Phosphatidate phosphatase LPIN1
- Phospholipid phosphatase 2
- Phosphatidate phosphatase LPIN2
- Phospholipid phosphatase 3
- Cholinephosphotransferase 1
- Choline/ethanolaminephosphotransferase 1
- Ethanolaminephosphotransferase 1
- Phospholipid phosphatase 4
- Phospholipid phosphatase 5
- Phosphatidate cytidylyltransferase 2
Sequence:
MNYVGQLAETVFGTVKELYRGLNPATLSGGIDVLVVKQVDGSFRCSPFHVRFGKLGVLRSREKVVDIELNGEPVDLHMKLGDSGEAFFVQELESDDEHVPPGLCTSPIPWGGLSGFPSDSQLGTASEPEGLVMAGTASTGRRKRRRRRKPKQKEDAVATDSSPEELEAGAESELSLPEKLRPEPPGVQLEEKSSLQPKDIYPYSDGEWPPQASLSAGELTSPKSDSELEVRTPEPSPLRAESHMQWAWGRLPKVARAERPESSVVLEGRAGATSPPRGGPSTPSTSVAGGVDPLGLPIQQTEAGADLQPDTEDPTLVGPPLHTPETEESKTQSSGDMGLPPASKSWSWATLEVPVPTGQPERVSRGKGSPKRSQHLGPSDIYLDDLPSLDSENAALYFPQSDSGLGARRWSEPSSQKSLRDPNPEHEPEPTLDTVDTIALSLCGGLADSRDISLEKFNQHSVSYQDLTKNPGLLDDPNLVVKINGKHYNWAVAAPMILSLQAFQKNLPKSTMDKLEREKMPRKGGRWWFSWRRRDFLAEERSAQKEKTAAKEQQGEKTEVLSSDDDAPDSPVILEIPSLPPSTPPSTPTYKKSLRLSSDQIRRLNLQEGANDVVFSVTTQYQGTCRCKATIYLWKWDDKVVISDIDGTITKSDALGHILPQLGKDWTHQGITSLYHKIQLNGYKFLYCSARAIGMADLTKGYLQWVSEGGCSLPKGPILLSPSSLFSALHREVIEKKPEVFKVACLSDIQQLFLPHGQPFYAAFGNRPNDVFAYRQVGLPESRIFTVNPRGELIQELIKNHKSTYERLGEVVELLFPPVARGPSTDLANPEYSNFCYWREPLPAVDLDTLD
Protein: Signiferin-4.3 (P86122)
Organism: Crinia signifera (Common eastern froglet)
Function: Inhibits the formation of NO by neuronal nitric oxide synthase with an IC(50) of 40 ug/ml.
Subcellular location: Secreted {ECO:0000269|PubMed:15317042}.
Interaction partners:
Sequence:
GFADLFGKAVDFIKSRV
Protein: WAP four-disulfide core domain protein 13 (Q8IUB5)
Organism: Homo sapiens (Human)
Function: Putative acid-stable proteinase inhibitor.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Kunitz-type protease inhibitor 4
- Protein WFDC9
- Protein WFDC11
Sequence:
MKPVLPLQFLVVFCLALQLVPGSPKQRVLKYILEPPPCISAPENCTHLCTMQEDCEKGFQCCSSFCGIVCSSETFQKRNRIKHKGSEVIMPAN
Protein: V-type proton ATPase 16 kDa proteolipid subunit c (V-ATPase 16 kDa proteolipid subunit c) (Vacuolar proton pump 16 kDa proteolipid subunit c) (P63081)
Organism: Rattus norvegicus (Rat)
Function: Proton-conducting pore forming subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:32165585}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase 21 kDa proteolipid subunit c''
- V-type proton ATPase subunit S1
- V-type proton ATPase subunit F
- V-type proton ATPase 116 kDa subunit a 1
- V-type proton ATPase subunit
- V-type proton ATPase subunit D
- V-type proton ATPase subunit B, brain isoform
- V-type proton ATPase subunit C 1
- V-type proton ATPase subunit E 1
Sequence:
MADIKNNPEYSSFFGVMGASSAMVFSAMGAAYGTAKSGTGIAAMSVMRPELIMKSIIPVVMAGIIAIYGLVVAVLIANSLTDGITLYRSFLQLGAGLSVGLSGLAAGFAIGIVGDAGVRGTAQQPRLFVGMILILIFAEVLGLYGLIVALILSTK
Protein: 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid receptor (12-(S)-HETE receptor) (12-HETER) (G-protein coupled receptor 31) (GPR31/12-HETER) (O00270)
Organism: Homo sapiens (Human)
Function: High-affinity receptor for 12-(S)-hydroxy-5,8,10,14-eicosatetraenoic acid (12-S-HETE), with much lower affinities for other HETE isomers. 12-S-HETE is a eicosanoid, a 12-lipoxygenase (ALOX12) metabolite of arachidonic acid, involved in many physiologic and pathologic processes. 12-S-HETE-binding leads to activation of ERK1/2 (MAPK3/MAPK1), MEK, and NF-kappa-B pathways leading to cell growth. Plays a crucial role for proliferation, survival and macropinocytosis of KRAS-dependent cancer cells by mediating the translocation of KRAS from the endoplasmic reticulum to the plasma membrane (PM) and its association with the PM. Contributes to enhanced immune responses by inducing dendrite protrusion of small intestinal CX3CR1(+) phagocytes for the uptake of luminal antigens (By similarity). Acts also as a key receptor for 12-(S)-HETE-mediated liver ischemia reperfusion injury.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21712392, ECO:0000269|PubMed:28619714, ECO:0000269|PubMed:31119277}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Zinc finger protein ZIC 3
- Nodal homolog
- Cryptic protein
Sequence:
MPFPNCSAPSTVVATAVGVLLGLECGLGLLGNAVALWTFLFRVRVWKPYAVYLLNLALADLLLAACLPFLAAFYLSLQAWHLGRVGCWALHFLLDLSRSVGMAFLAAVALDRYLRVVHPRLKVNLLSPQAALGVSGLVWLLMVALTCPGLLISEAAQNSTRCHSFYSRADGSFSIIWQEALSCLQFVLPFGLIVFCNAGIIRALQKRLREPEKQPKLQRAQALVTLVVVLFALCFLPCFLARVLMHIFQNLGSCRALCAVAHTSDVTGSLTYLHSVLNPVVYCFSSPTFRSSYRRVFHTLRGKGQAAEPPDFNPRDSYS