{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q14849","secondaryAccessions":["A8MXA4","B4DUY1","F5H0G2","Q53Y53","Q96HM9"],"uniProtkbId":"STAR3_HUMAN","entryAudit":{"firstPublicDate":"2000-05-30","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2006-10-17","entryVersion":217,"sequenceVersion":2},"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:0000305"}],"value":"StAR-related lipid transfer protein 3"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11053434"}],"value":"Metastatic lymph node gene 64 protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11053434"}],"value":"MLN 64"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9270027"}],"value":"Protein CAB1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21322544"}],"value":"START domain-containing protein 3"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"21322544"}],"value":"StARD3"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:17579"}],"value":"STARD3"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9270027"}],"value":"CAB1"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11053434"}],"value":"MLN64"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11053434"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12070139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15930133"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19965586"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21322544"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22514632"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24105263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28377464"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33124732"}],"value":"Sterol-binding protein that mediates cholesterol transport from the endoplasmic reticulum to endosomes (PubMed:11053434, PubMed:15930133, PubMed:22514632, PubMed:28377464, PubMed:33124732). The sterol transport mechanism is triggered by phosphorylation of FFAT motif that leads to membrane tethering between the endoplasmic reticulum and late endosomes via interaction with VAPA and VAPB (PubMed:24105263, PubMed:28377464, PubMed:33124732). Acts as a lipid transfer protein that redirects sterol to the endosome at the expense of the cell membrane and favors membrane formation inside endosomes (PubMed:28377464). May also mediate cholesterol transport between other membranes, such as mitochondria membrane or cell membrane (PubMed:12070139, PubMed:19965586). However, such results need additional experimental evidences; probably mainly mediates cholesterol transport from the endoplasmic reticulum to endosomes (PubMed:28377464). Does not activate transcriptional cholesterol sensing (PubMed:28377464). Able to bind other lipids, such as lutein, a xanthophyll carotenoids that form the macular pigment of the retina (PubMed:21322544)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"cholesterol(in) = cholesterol(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:39747"},{"database":"ChEBI","id":"CHEBI:16113"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11053434"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15930133"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22514632"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28377464"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33124732"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15718238"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16709157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24105263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28377464"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29858488"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33124732"}],"value":"Homodimer (PubMed:15718238, PubMed:16709157). Interacts (via the MENTAL domain) with STARD3NL (PubMed:15718238, PubMed:16709157). Interacts (via phosphorylated FFAT motif) with VAPA (via MSP domain) (PubMed:24105263, PubMed:28377464, PubMed:33124732). Interacts (via phosphorylated FFAT motif) with VAPB (via MSP domain) (PubMed:24105263, PubMed:28377464, PubMed:33124732). Interacts (via phosphorylated FFAT motif) with MOSPD2 (via MSP domain); this interaction allows enrichment of MOSPD2 around endosomes (PubMed:29858488, PubMed:33124732)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q14849","intActId":"EBI-9819324"},"interactantTwo":{"uniProtKBAccession":"P31749","geneName":"AKT1","intActId":"EBI-296087"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14849","intActId":"EBI-9819324"},"interactantTwo":{"uniProtKBAccession":"Q13520","geneName":"AQP6","intActId":"EBI-13059134"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14849","intActId":"EBI-9819324"},"interactantTwo":{"uniProtKBAccession":"Q8N350","geneName":"CBARP","intActId":"EBI-9355611"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14849","intActId":"EBI-9819324"},"interactantTwo":{"uniProtKBAccession":"Q9HD26","geneName":"GOPC","intActId":"EBI-349832"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14849","intActId":"EBI-9819324"},"interactantTwo":{"uniProtKBAccession":"Q8NHP6","geneName":"MOSPD2","intActId":"EBI-2812848"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14849","intActId":"EBI-9819324"},"interactantTwo":{"uniProtKBAccession":"Q96K19-5","geneName":"RNF170","intActId":"EBI-12055631"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"Q14849-1","intActId":"EBI-9819369"},"interactantTwo":{"uniProtKBAccession":"Q9P0L0","geneName":"VAPA","intActId":"EBI-1059156"},"numberOfExperiments":4,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24105263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29858488"}],"value":"Localizes to contact sites between the endoplasmic reticulum and late endosomes: associates with the endoplasmic reticulum membrane via interaction with VAPA, VAPB or MOSPD2"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11053434"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16709157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24105263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28377464"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29858488"}],"value":"Late endosome membrane","id":"SL-0151"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["Q14849-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["Q14849-2"],"sequenceIds":["VSP_042710"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["Q14849-3"],"sequenceIds":["VSP_045361"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21322544"}],"value":"Expressed in retina"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27679500"}],"value":"Not regulated by increases in total cholesterol content, or by marked alterations in cholesterol flux"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24105263"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29858488"}],"value":"The FFAT motif mediates interaction with VAPA, VAPB and MOSPD2"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28377464"}],"value":"The START domain mediates lipid-transfer between membranes. It contains a hydrophobic cavity able to accommodate one lipid molecule, thereby serving as a 'hydrophobic bridge' across the aqueous gap between donor and acceptor organelle membranes"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11053434"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15718238"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16709157"}],"value":"The MENTAL domain anchors the protein in endosome membranes and exposes the START domain in the cytosol (PubMed:11053434). It binds cholesterol and mediates homotypic as well as heterotypic interactions between STARD3 and STARD3NL (PubMed:15718238, PubMed:16709157)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33124732"}],"value":"Phosphorylation at Ser-209 is necessary and sufficient for the direct interaction of the phosphorylated FFAT motif with the MSP domain of MOSPD2, VAPA and VAPB and allows the tethering of two membranes that participates in the formation of ER-endosome contacts (PubMed:33124732). Phosphorylation of the FFAT motif leads to conformation changes (PubMed:33124732). Additional phosphorylations around the core FFAT motif (QFYSPPE) are not essential but strengthen the interaction with MOSPD2, VAPA and VAPB (PubMed:33124732). Phosphorylation at Ser-209 of FFAT motif drives membrane tethering between the endoplasmic reticulum and late endosomes via interaction with VAPA and VAPB that in turn allows the efficient transport of sterol mediated by the START domain (PubMed:33124732)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the STARD3 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11053434"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12070139"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19965586"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28377464"}],"value":"STARD3 was reported to function in cholesterol transport to the mitochondria or to the cell membrane (PubMed:12070139, PubMed:19965586). Other reports however showed that it mediates cholesterol transport from the endoplasmic reticulum to endosomes (PubMed:11053434, PubMed:28377464). Discrepancies may be due to the different cell type used and the cellular physiological state (PubMed:28377464)"}],"commentType":"CAUTION"},{"commentType":"WEB RESOURCE","resourceName":"Atlas of Genetics and Cytogenetics in Oncology and Haematology","resourceUrl":"https://atlasgeneticsoncology.org/gene/202/MLN64","ftp":false}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":445,"modifier":"EXACT"}},"description":"StAR-related lipid transfer protein 3","featureId":"PRO_0000220653"},{"type":"Topological 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