wanglab/gogpt-training-data huggingface dataset:
Protein: Clumping factor A (Fibrinogen receptor A) (Fibrinogen-binding protein A) (Q2G015)
Organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)
Function: Cell surface-associated protein implicated in virulence. Promotes bacterial attachment exclusively to the gamma-chain of human fibrinogen. Induces formation of bacterial clumps, which diminish the ability of group IIA phospholipase A2 to cause bacterial phospholipid hydrolysis and killing. Significantly decreases macrophage phagocytosis possibly thanks to the clumps, clumped bacteria being too large to be phagocytosed. Dominant factor responsible for human platelet aggregation, which may be an important mechanism for initiating infective endocarditis. Enhances spleen cell proliferative response in vitro, contributing significantly to the immunostimulatory activity of S.aureus.
Subcellular location: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000269|PubMed:18800056, ECO:0000305|PubMed:11830639}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:11830639}. Note=Found in a ring-like distribution on the cell surface (PubMed:18800056). Does not localize with SasF (PubMed:18800056). Exchanging the ClfA and SasF signal peptides retargets the mature protein on the cell surface (PubMed:18800056). Anchored to the cell wall by sortase A (Probable). {ECO:0000269|PubMed:18800056, ECO:0000305|PubMed:11830639}.
Interaction partners:
- Fibronectin-binding protein A
- Elastin-binding protein EbpS
- Surface protein G
- Alpha-hemolysin
- Iron-regulated surface determinant protein B
- Enolase
- Fibrinogen-binding protein
- Clumping factor B
- Extracellular matrix-binding protein ebh
Sequence:
MNMKKKEKHAIRKKSIGVASVLVGTLIGFGLLSSKEADASENSVTQSDSASNESKSNDSSSVSAAPKTDDTNVSDTKTSSNTNNGETSVAQNPAQQETTQSSSTNATTEETPVTGEATTTTTNQANTPATTQSSNTNAEELVNQTSNETTSNDTNTVSSVNSPQNSTNAENVSTTQDTSTEATPSNNESAPQSTDASNKDVVNQAVNTSAPRMRAFSLAAVAADAPVAGTDITNQLTNVTVGIDSGTTVYPHQAGYVKLNYGFSVPNSAVKGDTFKITVPKELNLNGVTSTAKVPPIMAGDQVLANGVIDSDGNVIYTFTDYVNTKDDVKATLTMPAYIDPENVKKTGNVTLATGIGSTTANKTVLVDYEKYGKFYNLSIKGTIDQIDKTNNTYRQTIYVNPSGDNVIAPVLTGNLKPNTDSNALIDQQNTSIKVYKVDNAADLSESYFVNPENFEDVTNSVNITFPNPNQYKVEFNTPDDQITTPYIVVVNGHIDPNSKGDLALRSTLYGYNSNIIWRSMSWDNEVAFNNGSGSGDGIDKPVVPEQPDEPGEIEPIPEDSDSDPGSDSGSDSNSDSGSDSGSDSTSDSGSDSASDSDSASDSDSASDSDSASDSDSASDSDSDNDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSASDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSDSDSDSDSDSDSDSDSDSDSASDSDSGSDSDSSSDSDSESDSNSDSESVSNNNVVPPNSPKNGTNASNKNEAKDSKEPLPDTGSEDEANTSLIWGLLASIGSLLLFRRKKENKDKK
Protein: Down syndrome cell adhesion molecule 1, isoform BH (Q0E9M4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVPQSYTVNVMDESILRGNSAILKCHIPSFVADFIVVDSWVEDEERVIYPQEDIAESDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPIGSVAPRVNRKDEFNHDRIKSSKTISIQCPAQAFPVPVYRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPHVLPFSFGSEVFNMGDVLSITCVVLKGDLPLRIHWTLNGEPVATGVNGFTVMQLNQRTTYLSVDALEAKHRGSYSCVAQNQAGEAIYSADLQVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPLDDGSGHGNVHTRIRLPAWMPEWLDLNFMVPLIATVVVVAVGICVVCVALSRRRADDMRGGQKDVYYDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Unconventional myosin-Vb (P21271)
Organism: Mus musculus (Mouse)
Function: May be involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation. Required in a complex with RAB11A and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Together with RAB11A participates in CFTR trafficking to the plasma membrane and TF (transferrin) recycling in nonpolarized cells. Together with RAB11A and RAB8A participates in epithelial cell polarization. Together with RAB25 regulates transcytosis. Required for proper localization of bile salt export pump ABCB11 at the apical/canalicular plasma membrane of hepatocytes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P70569}.
Interaction partners:
- Rab11 family-interacting protein 2
- Ras-related protein Rab-11A
- Ras-related protein Rab-8A
- Exocyst complex component 6
- Ras-related protein Rab-10
- Rab11 family-interacting protein 5
- Protein spire homolog 1
- Ras-related protein Rab-11B
- Formin-2
- Rab-3A-interacting protein
Sequence:
MSYSELYTRYTRVWIPDPDEVWRSAELTKDYKEGDKSLQLRLEDDTILEYPVDVQNNQVPFLRNPDILVGENDLTALSHLHEPAVLHNLKVRFLESNHIYTYCGIVLVAINPYEQLPIYGQDVIYAYSGQNMGDMDPHIFAVAEEAYKQMARDEKNQSIIVSGESGAGKTVSAKYAMRYFATVGGSASDTNIEEKVLASSPIMEAIGNAKTTRNDNSSRFGKFIEIGFDKKYHIIGANMRTYLLEKSRVVFQADDERNYHIFYQLCAAASLPEFKELALTCAEDFFYTAHGGNTTIEGVNDADDFEKTRQALTLLGVRDSHQISIFKIIASILHLGSVEIQSERDGDSCSISPQDEHLSNFCSLLGIEHSQMEHWLCHRKLVTTSETYVKTMSLQQVVNARDALAKHIYAQLFSWIVEHINKALHTSHKQHSFIGVLDIYGFETFEINSFEQFCINYANEKLQQQFNSHVFKLEQEEYMKEQIPWTLIDFYDNQPCIDLIEAKLGILDLLDEECKVPKGTDQNWAQKLYERHSNSQHFQKPRMSNTAFIVNHFADKVEYLSDGFLEKNRDTVYEEQINILKASKFPLVADLFHDDKDSAPATNTAKNRSSSKINVRSSRPLIKVPNKEHKKSVGYQFRTSLNLLMETLNATTPHYVRCIKPNDEKLPFHFDPKRAVQQLRACGVLETIRISAAGYPSRWTYHDFFNRYRVLMKKRELTNTDKKNICKSVLESLIKDPDKFQFGRTKIFFRAGQVAYLEKLRADKFREATIMIQKSVRGWLQRVKYRRLRAATLSLQRFCRGYLARRLAEHLRRTRAAIVFQKQYRMLKARRAYRRVCRATVIIQSFTRAMFVRRNYRQVLMEHKATIIQKYARGWMARKRFLRERDAAIVIQCAFRRLKARQELKALKIEARSAEHLKRLNVGMENKVVQLQRKIDDQNKEFKTLSEQLSAVTSSHAVEVEKLKKELAHYQQNQEADTSLQLQEEVQSLRTELQKAHSERRVLEDAHNKENGELRKRVADLEHENALLKDEKEYLNNQILCQSKAESSQSSVEENLLMKKELEEERSRYQNLVKEYSQLEQRYENLRDEQTPGHRKNPSNQSSLESDSNYPSISTSEIGDTEDALQQVEEIGIEKAAMDMTVFLKLQKRVRELEQERKKLQAQLEKGQQDSKKGQVEQQNNGLDVDQDADIAYNSLKRQELESENKKLKNDLNELRKAVADQAMQDNSTHSSPDSYSLLLNQLKLANEELEVRKEEVLILRTQIMNADQRRLSGKNMEPNINARTSWPNSEKHVDQEDAIEAYHGVCQTNRLLEAQLQAQSLEHEEEVEHLKAQVEALKEEMDKQQQTFCQTLLLSPEAQVEFGVQQEISRLTNENLDFKELVEKLEKNERKLKKQLKIYMKKVQDLEAAQALAQSDRRHHELTRQVTVQRKEKDFQGMLEYHKEDEALLIRNLVTDLKPQMLSGTVPCLPAYILYMCIRHADYTNDDLKVHSLLSSTINGIKKVLKKHNDDFEMTSFWLSNTCRFLHCLKQYSGDEGFMTQNTAKQNEHCLKNFDLTEYRQVLSDLSIQIYQQLIKIAEGLLQPMIVSAMLENESIQGLSGVRPTGYRKRSSSMVDGENSYCLEAIVRQMNSFHTVLCDQGLDPEIILQVFKQLFYMINAVTLNNLLLRKDACSWSTGMQLRYNISQLEEWLRGKNLHQSGAVQTMEPLIQAAQLLQLKKKTHEDAEAICSLCTSLSTQQIVKILNLYTPLNEFEERVTVSFIRTIQAQLQERNDPQQLLLDSKHVFPVLFPYNPSALTMDSIHIPACLNLEFLNEV
Protein: Cathepsin B (EC 3.4.22.1) (C0H850)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
- NACHT, LRR and PYD domains-containing protein 3-like isoform X2
- NACHT, LRR and PYD domains-containing protein 3-like
- Cathepsin B
- NACHT, LRR and PYD domains-containing protein 3-like
- Cathepsin B
- Cathepsin D-like
- Cathepsin D
- Cathepsin D
- Cathepsin D
- Cathepsin D
Sequence:
MWRVIFLALVSGLSVSWAWPRLPPLSHQMVDYINKANTTWKAGPNFHNVDYSYVKRLCGTLLKGPKLPTMVQYAGDVELPDTFDPRQQWPNCPTLKEIRDQGSCGSCWAFGAAEAISDRVCIHSNAKVSVEISSEDLLSCCDSCGMGCNGGYPSAAWDFWTTEGLVTGGLYDSHVGCRPYSIPPCEHHVNGTRPPCTGEEGDTPQCSNQCETGYTPGYKQDKHFGKNSYSLPSEEQQIMAELLKNGPVEGAFTVYEDFLLYKSGVYQHVSGSAVGGHAIKVLGWGEEGGTPYWLAANSWNTDWGENGFFKILRGKDHCGIESEMVAGVPL
Protein: 2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial (AKB ligase) (EC 2.3.1.29) (Aminoacetone synthase) (Glycine acetyltransferase) (O75600)
Organism: Homo sapiens (Human)
Function: Pyridoxal phosphate (PLP) dependent enzyme, which catalyzes the cleavage of 2-amino-3-oxobutanoate to glycine and acetyl-CoA.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q0P5L8}. Nucleus {ECO:0000269|PubMed:17688197}. Note=Translocates to the nucleus upon cold and osmotic stress. {ECO:0000269|PubMed:17688197}.
Interaction partners:
- Galanin receptor type 3
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- Aminomethyltransferase, mitochondrial
- Sorbitol dehydrogenase
Sequence:
MWPGNAWRAALFWVPRGRRAQSALAQLRGILEGELEGIRGAGTWKSERVITSRQGPHIRVDGVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGALP
Protein: Major capsid protein L1 (P03101)
Organism: Human papillomavirus type 16
Function: Forms an icosahedral capsid with a T=7 symmetry and a 50 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with L2 proteins. Binds to heparan sulfate proteoglycans on cell surface of basal layer keratinocytes to provide initial virion attachment. This binding mediates a conformational change in the virus capsid that facilitates efficient infection. The virion enters the host cell via endocytosis. During virus trafficking, L1 protein dissociates from the viral DNA and the genomic DNA is released to the host nucleus. The virion assembly takes place within the cell nucleus. Encapsulates the genomic DNA together with protein L2.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04002}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04002}.
Interaction partners:
Sequence:
MSLWLPSEATVYLPPVPVSKVVSTDEYVARTNIYYHAGTSRLLAVGHPYFPIKKPNNNKILVPKVSGLQYRVFRIHLPDPNKFGFPDTSFYNPDTQRLVWACVGVEVGRGQPLGVGISGHPLLNKLDDTENASAYAANAGVDNRECISMDYKQTQLCLIGCKPPIGEHWGKGSPCTNVAVNPGDCPPLELINTVIQDGDMVDTGFGAMDFTTLQANKSEVPLDICTSICKYPDYIKMVSEPYGDSLFFYLRREQMFVRHLFNRAGAVGENVPDDLYIKGSGSTANLASSNYFPTPSGSMVTSDAQIFNKPYWLQRAQGHNNGICWGNQLFVTVVDTTRSTNMSLCAAISTSETTYKNTNFKEYLRHGEEYDLQFIFQLCKITLTADVMTYIHSMNSTILEDWNFGLQPPPGGTLEDTYRFVTSQAIACQKHTPPAPKEDPLKKYTFWEVNLKEKFSADLDQFPLGRKFLLQAGLKAKPKFTLGKRKATPTTSSTSTTAKRKKRKL
Protein: Squamosa promoter-binding-like protein 3 (P93015)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3' of AP1 promoter. Binds specifically to the 5'-GTAC-3' core sequence. Promotes both vegetative phase change and flowering. Regulates phase-specific patterns of leaf epidermal differentiation and flowering time, but does not seem to affect leaf shape.
Subcellular location: Nucleus {ECO:0000269|PubMed:16095614}. Cytoplasm {ECO:0000269|PubMed:16095614}. Note=Mostly located in nucleus.
Interaction partners:
- Agamous-like MADS-box protein AGL8
- MADS-box protein SOC1
- Protein LEAFY
- AP2-like ethylene-responsive transcription factor TOE3
- AP2-like ethylene-responsive transcription factor TOE2
- AP2-like ethylene-responsive transcription factor SNZ
- AP2-like ethylene-responsive transcription factor SMZ
- Ethylene-responsive transcription factor RAP2-7
- MADS-box protein AGL24
- Floral homeotic protein APETALA 2
Sequence:
MSMRRSKAEGKRSLRELSEEEEEEEETEDEDTFEEEEALEKKQKGKATSSSGVCQVESCTADMSKAKQYHKRHKVCQFHAKAPHVRISGLHQRFCQQCSRFHALSEFDEAKRSCRRRLAGHNERRRKSTTD
Protein: Forkhead box protein P3 [Cleaved into: Forkhead box protein P3, C-terminally processed; Forkhead box protein P3 41 kDa form] (Q6U8D7)
Organism: Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Function: Transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg). Plays an essential role in maintaining homeostasis of the immune system by allowing the acquisition of full suppressive function and stability of the Treg lineage, and by directly modulating the expansion and function of conventional T-cells. Can act either as a transcriptional repressor or a transcriptional activator depending on its interactions with other transcription factors, histone acetylases and deacetylases. The suppressive activity of Treg involves the coordinate activation of many genes, including CTLA4 and TNFRSF18 by FOXP3 along with repression of genes encoding cytokines such as interleukin-2 (IL2) and interferon-gamma (IFNG). Inhibits cytokine production and T-cell effector function by repressing the activity of two key transcription factors, RELA and NFATC2. Mediates transcriptional repression of IL2 via its association with histone acetylase KAT5 and histone deacetylase HDAC7. Can activate the expression of TNFRSF18, IL2RA and CTLA4 and repress the expression of IL2 and IFNG via its association with transcription factor RUNX1. Inhibits the differentiation of IL17 producing helper T-cells (Th17) by antagonizing RORC function, leading to down-regulation of IL17 expression, favoring Treg development. Inhibits the transcriptional activator activity of RORA (By similarity). Can repress the expression of IL2 and IFNG via its association with transcription factor IKZF4 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9BZS1, ECO:0000255|PROSITE-ProRule:PRU00089}. Cytoplasm {ECO:0000250|UniProtKB:Q9BZS1}. Note=Predominantly expressed in the cytoplasm in activated conventional T-cells whereas predominantly expressed in the nucleus in regulatory T-cells (Treg). The 41 kDa form derived by proteolytic processing is found exclusively in the chromatin fraction of activated Treg cells. {ECO:0000250|UniProtKB:Q99JB6, ECO:0000250|UniProtKB:Q9BZS1}.
Interaction partners:
- T-cell surface glycoprotein CD4
- Interleukin-2
- Nuclear factor of activated T cells 2.
- Cytotoxic T-lymphocyte protein 4
- Interferon gamma
- Interleukin-10
- Signal transducer and activator of transcription
- Interleukin-4
- Interleukin-6
- GATA binding protein 3
Sequence:
MPNPRPGKPSAPSLALGPSPGASPSWRAAPKASDLLGARGPGGIFQGRDLRGGAHASSSSLNPMPPSQLQLPTLPLVMVAPSGARLGPLPHLQALLQDRPHFMHQLSTVDAHARTPVLQVHPLESPAMISLPPPTTATGVFSLKARPGLPPGINVASLEWVSREPALLCTFPNPGAPRKDSTLSAMPQSSYPLLANGVCKWPGCEKVFEEPEDFLKHCQADHLLDEKGRAQCLLQREMVQSLEQQLVLEKEKLSAMQAHLAGKMALTKASSVASSDKGSCCIVAAGSQGSAVPAWSGPREAPDSLFAVRRHLWGSHGNSTFPEFLHNMDYFKFHNMRPPFTYATLIRWAILEAPEKQRTLNEIYHWFTRMFAFFRNHPATWKNAIRHNLSLHKCFVRVESEKGAVWTVDELEFRKKRSQRPSRCSNPTPGP
Protein: Adenylate cyclase type 1 (EC 4.6.1.1) (D4A3N4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Rap guanine nucleotide exchange factor 3
- Calmodulin-1
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Guanine nucleotide-binding protein G
- Rap guanine nucleotide exchange factor 4
- Protein kinase C beta type
- Protein kinase C gamma type
Sequence:
MAGAPRGQGGGGGAGEPGGAERAAGPGGRRGFRACGEEFACPELEALFRGYTLRLEQAATLKALAVLSLLAGALALAELLGAPGPAPGLAKGSHPVHCILFLALFVVTNVRSLQVSQLQQVGQLALFFSLTFALLCCPFALGGPARSSAGGAMGSAVAEQGVWQLLLVTFVSYALLPVRSLLAIGFGLVVAASHLLVTAALVPAKRPRLWRTLGANALLFFGVNMYGVFVRILTERSQRKAFLQARNCIEDRLRLEDENEKQERLLMSLLPRNVAMEMKEDFLKPPERIFHKIYIQRHDNVSILFADIVGFTGLASQCTAQELVKLLNELFGKFDELATENHCRRIKILGDCYYCVSGLTQPKTDHAHCCVEMGLDMIDTITSVAEATEVDLNMRVGLHTGRVLCGVLGLRKWQYDVWSNDVTLANVMEAAGLPGKVHITKTTLACLNGDYEVEPGHGHERNTFLRTHNIETFFIVPSHRRKIFPGLILSDIKPAKRMKFKTVCYLLVQLMHCRKMFKAEIPFSNVMTCEDDDKRRALRTASEKLRNRSSFSTNVVYTTPGTRVNRYISRLLEARQTELEMADLNFFTLKYKHVEREQKYHQLQDEYFTSAVVLALILATLFGLIYLLVIPQSVAVLLLLVFSICFLVACTLYLHITRVQCFPGCLTIQIRTALCVFIVVLIYSVAQGCVVSCLPWAWSSHSNSSLVVLAAGGRRTVLPALPCESAHHGLLCCLVGTLPLAIFLRVSSLPKMILLSGLTTSYILVLELSGYTKVGGGALSGRSYEPIMAILLFSCTLALHARQVDVRLRLDYLWAAQAEEERDDMERVKLDNKRILFNLLPAHVAQHFLMSNPRNMDLYYQSYSQVGVMFASIPNFNDFYIELDGNNMGVECLRLLNEIIADFDELMDKDFYKDLEKIKTIGSTYMAAVGLAPTAGTRAKKSISSHLSTLADFAIDMFDVLDEINYQSYNDFVLRVGINVGPVVAGVIGARRPQYDIWGNTVNVASRMDSTGVQGRIQVTEEVHRLLNRCSYQFVCRGKVSVKGKGEMLTYFLEGRTDGSSSHSRSLRLERRMFPYGRGGGGQARRPPLCPAAGPPIKPGLSPAPTSQYLSSTAAGKEA
Protein: Receptor-type guanylate cyclase gcy-5 (EC 4.6.1.2) (Q23682)
Organism: Caenorhabditis elegans
Function: Guanylate cyclase involved in the production of the second messenger cGMP (By similarity). Unlike other guanylate cyclases expressed in ASE neurons, may not play a role in chemotaxis responses to salt ions mediated by ASE sensory neurons.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Bis
- Inosine triphosphate pyrophosphatase
- Transcription factor che-1
- Homeobox protein ceh-36
- GTP cyclohydrolase 1
- Probable 3',5'-cyclic phosphodiesterase pde-5
- Probable 3',5'-cyclic phosphodiesterase pde-2
- LIM/homeobox protein lim-6
- Uroporphyrinogen-III synthase
Sequence:
MRLLYFSMVLLWVLGASECQVIPSSRRTLRVGIAAAQDTQSGSIGWASCGGTLPIAVQYLKSKGFLTDFDVEYYMEYTECDRASVAKAGMKFMKEMNVDVVVGPSCGDALAIMGTLSAIYKKLVLGWGFVSDTQLADTNRFPYVASVQPTAQTLGLATSRILEMFQFDRVALLYYKDDQDYCKSVMDDVEATLSDPDLYPVRIVWKGELQSDNEALTRSTLQAVKSRARIVLLCAISGPEKRNYLISIAQQNMTTNEYVHILLTMRSIGYGVQTSLGKKTFANGLTPLWESFTVAPDGNETNARRAAEKMLVIDVNSDVQDAEFLQYLTKNIADAVRNPPMKCNTSECINASSTSMGSYARHLFDVFYLYGMAVSKLNSTDPTVYGNLNLLMPQMVTSFDGMTGRVQIGQNLYRVPTYQLYGLDEKYEQVALVNMTFYNSSSQLSRGYSDEGRSVWHFWDGTRPLDTPICGFSGRYCPVQFWDQYGVLIFVASIVLIFLICIMLMCFGFMIRGRRAEQERLNSEWQIPSIQLIMPQKEKRKPNSRRSLQSGPSTITGESKMTIDGGFHENYTVQMFEKDLVLTTKHHSMQMNKEEKEKFVKLRKLEHDNLNKFIGLSIDGPQFVAVWKMCSRGSLQDIIARGNFSMDGFFMFCIITDIAEGMNFLHKSFLHLHGNLRSATCLVNDSWQVKLTDFGLGALLEEHTPSKKRLLWAAPEVLRGSLTIHQMDPSADVYSFAIIASEILTKREAWDISNRKEGADEILYMVKKGGNRTIRPELILDAEVSPRLTTLVKDCWSEQPEDRPKAEQICKLLSEMTPRGNTNLMDHVFNMLEEYTSTLEVDIEERTKELTLEKKKADILLSRMLPKQVAERLKAGQTVEPEGFDTVTVLFSDVVKFTQLAAKCSPFQVVNLLNDLYSNFDTIIEEHGVYKVESIGDGYLCVSGLPTKNGYAHIKQIVDMSLKFMDYCKSFKVPHLPREKVELRIGINSGPCVAGVVGLSMPRYCLFGDTVNTASRMESNGKPSMIHMSEAAHSLLTDHYPHQYETSSRGEVIIKGKGVMETFWVLGKTDSDTKSLSTRTTPPITDENWPPQMKEDLKKRAVTPYPERQRSGKSKMDTLKVV
Protein: Alpha-amylase (EC 3.2.1.1) (Q7LV45)
Organism: Aspergillus flavus
Interaction partners:
Sequence:
MMVAWWSLFLYGLQVAAPALAATPADWRSQSIYFLLTDRFARTDGSTTATCNTADRKYCGGTWQGIIDKLDYIQGMGFTAIWITPVTAQLPQTTAYGDAYHGYWQQDIYSLNENYGTADDLKALSSALHERGMYLMVDVVANHMGYDGAGSSVDYSVFKPFSSQDYFHPFCLIQNYEDQTQVEDCWLGDNTVSLPDLDTTKDVVKNEWYDWVGSLVSNYSIDGLRIDTVKHVQKDFWPGYNKAAGVYCIGEVLDGDPAYTCPYQNVMDGVLNYPIYYPLLNAFKSTSGSMDDLYNMINTVKSDCPDSTLLGTFVENHDNPRFASYTNDIALAKNVAAFIILNDGIPIIYAGQEQHYAGGNDPANREATWLSGYPTDSELYKLIASANAIRNYAISKDTGFVTYKNWPIYKDDTTIAMRKGTDGSQIVTILSNKGASGDSYTLSLSGAGYTAGQQLTEVIGCTTVTVGSDGNVPVPMAGGLPRVLYPTEKLAGSKICSSS
Protein: ER lumen protein-retaining receptor 2 (KDEL endoplasmic reticulum protein retention receptor 2) (KDEL receptor 2) (Q5ZKX9)
Organism: Gallus gallus (Chicken)
Function: Membrane receptor that binds the K-D-E-L sequence motif in the C-terminal part of endoplasmic reticulum resident proteins and maintains their localization in that compartment by participating to their vesicle-mediated recycling back from the Golgi (By similarity). Binding is pH dependent, and is optimal at pH 5-5.4.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33947}; Multi-pass membrane protein {ECO:0000269|PubMed:30846601}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P33947}; Multi-pass membrane protein {ECO:0000269|PubMed:30846601}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250|UniProtKB:P33947}; Multi-pass membrane protein {ECO:0000269|PubMed:30846601}. Note=Localized in the Golgi in the absence of bound proteins with the sequence motif K-D-E-L. Trafficks back to the endoplasmic reticulum together with cargo proteins containing the sequence motif K-D-E-L. {ECO:0000250|UniProtKB:P33947}.
Interaction partners:
- Coiled-coil domain containing 6
- Coatomer subunit beta
- Uncharacterized protein.
- Centrosomal protein 85 like.
- Coiled-coil domain containing 134
- Coatomer subunit delta
- Uncharacterized protein.
- Uncharacterized protein
Sequence:
MNIFRLTGDLSHLAAIIILLLKIWKSRSCAGISGKSQLLFALVFTTRYLDLFTSFISLYNTSMKLIYIACSYATVYLIYMKFKATYDGNHDTFRVEFLIVPVGGLSFLVNHDFSPLEILWTFSIYLESVAILPQLFMISKTGEAETITTHYLFFLGLYRALYLVNWIWRYYFEGFFDLIAVVAGVVQTVLYCDFFYLYVTKVLKGKKLSLPA
Protein: Enterotoxin type D (SED) (P20723)
Organism: Staphylococcus aureus
Function: Staphylococcal enterotoxin that activates the host immune system by binding as unprocessed molecules to major histocompatibility (MHC) complex class II and T-cell receptor (TCR) molecules. In turn, this ternary complex activates a large number of T-lymphocytes initiating a systemic release of pro-inflammatory cytokines. In addition, induces B-cell proliferation and differentiation in the presence of T-cells. Causes also the intoxication staphylococcal food poisoning syndrome.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MKKFNILIALLFFTSLVISPLNVKANENIDSVKEKELHKKSELSSTALNNMKHSYADKNPIIGENKSTGDQFLENTLLYKKFFTDLINFEDLLINFNSKEMAQHFKSKNVDVYPIRYSINCYGGEIDRTACTYGGVTPHEGNKLKERKKIPINLWINGVQKEVSLDKVQTDKKNVTVQELDAQARRYLQKDLKLYNNDTLGGKIQRGKIEFDSSDGSKVSYDLFDVKGDFPEKQLRIYSDNKTLSTEHLHIDIYLYEK
Protein: Tapasin long form (Tapasin short form) (Q3SAV0)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MANISTIYKLSFLAFTYFIQVYGTSCPVLECWFVQEKPGRGGGFPAAMIQEKSLLYINTDPESEQTKSQQGPSADISHDRVYYITDPAAILCSSSLHPPEGSVHKPQCEINPFMPQPSTVQWAVPLTDSAHSPIYLQADWYSAALQGLDGQLALSSVMRAPTATKEPTVVLSVSSRTPLVRSRLGEPVVLDCGFWAETSSPLSGSGFAVEWRYQFRGDGRLVLAYDGKTDRFAETKEKGAGLDFTALHETGNASLILQEAEVRHTGTYICTVYLPYLLAQVAVELEIVEPPSLSIFPSPLPLSVPGQVVKVQCEASGFFPLSLEFYWELTGPDGKVRPLGQGSVTGHRQGPDNTYSQTTRLELDSAKLDLGRGGEVTCVAVHPGGTRRARVTLNVIGVNGPSIEDSMAMVAVALGLYGLIKIVSWTFSSGSDDTNSQEKKVK
Protein: Uncharacterized mitochondrial carrier C19G12.05 (O13844)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable citrate synthase, mitochondrial
- mRNA-capping enzyme subunit beta
- mRNA-capping enzyme subunit alpha
- Anthranilate phosphoribosyltransferase
- Probable ATP-citrate synthase subunit 2
- DNA polymerase epsilon subunit B
Sequence:
MSTVAKTNPKSSNKPGPVKSIIAGGVAGAIEISITYPAEFAKTRLQLYRNVEGTKAKLPPFGLEWYRGCSTVIVGNSLKAAVRFFAFDSIKKSLSDEHGHLTGPRTVLAGLGAGVAESVLVLTPFESIKTAIIDDRKRPNPRLKGFLQASRIIVHENGIRGLYRGLAATVARQAANSGVRFTAYNSIKQSLQSRLPPDEKLSTVTTFLVGSVAGIITVYCTQPIDTVKSRMQSLSASKEYKNSIHCAYKILTQDGLLRFWSGATPRLARLILSGGIVFTVYEKVMEILKPF
Protein: Uncharacterized protein (Q66YX3)
Organism: Borreliella burgdorferi (Lyme disease spirochete) (Borrelia burgdorferi)
Interaction partners:
Sequence:
LKNFKLNIIKLNVITAILTSICISCAPFGKVNPNKLKNPITSKNLKKTKRSNNSRNLKNTSNHTNSENLTGNSTKNPSENNQNLENESQNSKSSNQNSQEETTISKLKNIGKDLEAQKKKEDTGITKMSKIDNAKYDFLENFKLHNYDYFMHNAKMKLKRIIYPSLNYDTKKILVLKEILEKLDTEDNNRRIAGQFLETSRDIQLHLEDTYLKKIQDTLQTLSEKEAEKLLQGVKLDLKKKQNFAKSLNATIDAYNKNVDNIKIDNKALAKHIKDKYSHPLYLLNQAD