{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q86UW1","secondaryAccessions":["Q6ZMC7"],"uniProtkbId":"OSTA_HUMAN","entryAudit":{"firstPublicDate":"2008-04-29","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2003-06-01","entryVersion":141,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16317684"}],"value":"Organic solute transporter subunit alpha"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16317684"}],"value":"OST-alpha"}]},"alternativeNames":[{"fullName":{"value":"Solute carrier family 51 subunit alpha"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:29955"}],"value":"SLC51A"},"synonyms":[{"value":"OSTA"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8R000"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q90YM5"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16317684"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606328"}],"value":"Essential component of the OST-alpha/OST-beta complex, a heterotetramer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood (PubMed:16317684, PubMed:41606314, PubMed:41606328). The OST-alpha/OST-beta complex efficiently transports the major species of bile acids (taurocholate) (PubMed:16317684, PubMed:41606314, PubMed:41606328). Taurine conjugates are transported more efficiently across the basolateral membrane than glycine-conjugated bile acids (By similarity). In the complex, SLC51A/OST-alpha adopts a G protein-coupled receptor fold and constitutes a bile acid recognition site (PubMed:41606314, PubMed:41606328). Can also transport steroids such as estrone 3-sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a role in the enterohepatic circulation of sterols (PubMed:16317684). Able to transport eicosanoids such as prostaglandin E2 (By similarity)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"taurocholate(out) = taurocholate(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:71703"},{"database":"ChEBI","id":"CHEBI:36257"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16317684"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606328"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"estrone 3-sulfate(out) = estrone 3-sulfate(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:71835"},{"database":"ChEBI","id":"CHEBI:60050"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16317684"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dehydroepiandrosterone 3-sulfate(out) = dehydroepiandrosterone 3-sulfate(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:71839"},{"database":"ChEBI","id":"CHEBI:57905"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16317684"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tauroursodeoxycholate(out) = tauroursodeoxycholate(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:71843"},{"database":"ChEBI","id":"CHEBI:132028"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8R000"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycoursodeoxycholate(out) = glycoursodeoxycholate(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:71847"},{"database":"ChEBI","id":"CHEBI:132030"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8R000"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycocholate(out) = glycocholate(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:71851"},{"database":"ChEBI","id":"CHEBI:29746"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8R000"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"taurochenodeoxycholate(out) = taurochenodeoxycholate(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:71855"},{"database":"ChEBI","id":"CHEBI:9407"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8R000"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycochenodeoxycholate(out) = glycochenodeoxycholate(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:71859"},{"database":"ChEBI","id":"CHEBI:36252"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8R000"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"taurodeoxycholate(out) = taurodeoxycholate(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:71863"},{"database":"ChEBI","id":"CHEBI:36261"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8R000"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glycodeoxycholate(out) = glycodeoxycholate(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:71867"},{"database":"ChEBI","id":"CHEBI:82982"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8R000"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"prostaglandin E2(out) = prostaglandin E2(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:50984"},{"database":"ChEBI","id":"CHEBI:606564"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q90YM5"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606328"}],"value":"Heterotetramer; the Ost-alpha/Ost-beta complex forms a symmetric dimer of heterodimers of SLC51A and SLC51B"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q86UW1","intActId":"EBI-945738"},"interactantTwo":{"uniProtKBAccession":"P54253","geneName":"ATXN1","intActId":"EBI-930964"},"numberOfExperiments":7,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q86UW1","intActId":"EBI-945738"},"interactantTwo":{"uniProtKBAccession":"Q96LL9","geneName":"DNAJC30","intActId":"EBI-8639143"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8R000"}],"value":"Transported from the endoplasmic reticulum to the plasma membrane upon interacting with SLC51B (By similarity). Mainly restricted to the lateral and basal membranes of ileal enterocytes (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16317684"}],"value":"Basolateral cell membrane","id":"SL-0026"},"topology":{"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12719432"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16317684"}],"value":"Widely expressed with a high expression in ileum. Expressed in testis, colon, liver, small intestine, kidney, ovary and adrenal gland; and at low levels in heart, lung, brain, pituitary, thyroid gland, uterus, prostate, mammary gland and fat"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16251721"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16269519"}],"value":"Positively regulated via NR1H4/FXR in adrenal gland, kidney and intestine"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606328"}],"value":"In the complex, two SLC51A/OST-alpha units form the homodimeric core, with two SLC51B/OST-beta units bound to the periphery (PubMed:41606314, PubMed:41606328). SLC51A/OST-alpha adopts a G protein-coupled receptor fold and contains a unique cysteine-rich loop with seven palmitoylation sites to constitute a bile acid recognition site (PubMed:41606314, PubMed:41606328). A positive cavity in SLC51A/OST-alpha connects the bile acid site and facilitates the transmembrane translocation of bile acids through SLC51B/OST-beta (PubMed:41606314, PubMed:41606328)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606328"}],"value":"The cysteine-rich loop is highly palmitoylated"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"41606328"}],"value":"Palmitoylation of the cysteine-rich loop is required to form a lateral substrate-binding groove for recognition of bile acids"}],"commentType":"PTM"},{"commentType":"DISEASE","disease":{"diseaseId":"Cholestasis, progressive familial intrahepatic, 6","diseaseAccession":"DI-06201","acronym":"PFIC6","description":"An autosomal recessive form of progressive cholestasis, a disorder characterized by early onset of cholestasis that progresses to hepatic fibrosis, cirrhosis, and end-stage liver disease. 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