{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q07878","secondaryAccessions":["D6VXW6","O00040"],"uniProtkbId":"VPS13_YEAST","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-11-01","entryVersion":190,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Saccharomyces cerevisiae (strain ATCC 204508 / S288c)","commonName":"Baker's yeast","taxonId":559292,"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Saccharomycotina","Saccharomycetes","Saccharomycetales","Saccharomycetaceae","Saccharomyces"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Intermembrane lipid transfer protein VPS13"}},"alternativeNames":[{"fullName":{"value":"Suppression of the onset of impotence protein 1"}},{"fullName":{"value":"Vacuolar protein sorting-associated protein 13"}},{"fullName":{"value":"Vacuolar protein-targeting protein 2"}}]},"genes":[{"geneName":{"value":"VPS13"},"synonyms":[{"value":"SOI1"},{"value":"VPT2"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"27280386"}],"value":"YME3"}],"orderedLocusNames":[{"value":"YLL040C"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22442115"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24036347"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27280386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28122955"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28334785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28404745"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30093493"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32690699"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34830155"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9314526"}],"value":"Mediates the transfer of lipids between membranes at organelle contact sites (PubMed:22442115, PubMed:24036347, PubMed:30093493). Binds phospholipids, including phosphatidic acid (PA), phosphorylated phosphatidylinositol (PI), phosphatidylcholine (PC), phosphatidylethanolamine (PE), ceramide, and phosphatidylserine (PS) (PubMed:28122955, PubMed:28334785, PubMed:30093493, PubMed:34830155). Involved in mitochondrial lipid homeostasis, in a MCP1-dependent manner (PubMed:27280386, PubMed:32690699, PubMed:34830155). Involved in cortical reticulophagy (also known as cortical endoplasmic reticulum (ER) macroautophagy), acting at the late endosome to package ER into autophagosomes (PubMed:32690699). Involved in the formation of the prospore membrane during sporulation, in a SPO71-dependent manner (PubMed:22442115, PubMed:24036347). Involved in Golgi vesicle transport, in a CDC31-dependent and ARF1-dependent manner (PubMed:28122955, PubMed:34830155, PubMed:9314526). Plays a role in sorting at early and late endosomes (PubMed:28404745). Plays a role in actin cytoskeleton organization (PubMed:28334785)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24036347"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28122955"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28334785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28864540"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30018089"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34830155"}],"value":"Interacts (via SHR-BD domain) with SPO71 (via PxP motif); during prospore membrane formation (PubMed:24036347, PubMed:30018089). Interacts (via SHR-BD domain) with YPT35 (via PxP motif) (PubMed:30018089). Interacts (via SHR-BD domain) with MCP1 (via PxP motif) (PubMed:28864540, PubMed:30018089). Interacts with CDC31 (PubMed:28122955). Interacts (via C-terminus) with ARF1; the interaction is direct (PubMed:34830155). Interacts with the actin cytoskeleton (PubMed:28334785)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26370498"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27280386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30018089"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32690699"}],"value":"Found at different interorganellar contact sites depending on the growth state of the cell (PubMed:26370498, PubMed:27280386, PubMed:30018089, PubMed:32690699). Localizes from endosomes to the vacuolar membrane during starvation (PubMed:32690699). Localizes to mitochondrial-endosome contacts (PubMed:27280386). Localizes to nuclear envelope-vacuole contact sites (nuclear-vacuole junction; NVJ) during respiration (PubMed:26370498, PubMed:27280386, PubMed:30018089)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27280386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28334785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28864540"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30018089"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32690699"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"22442115"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"24036347"}],"value":"Endosome membrane","id":"SL-0100"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28122955"}],"value":"Peripheral membrane protein","id":"SL-9903"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26370498"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27280386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30018089"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34830155"}],"value":"Mitochondrion outer membrane","id":"SL-0172"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28122955"}],"value":"Peripheral membrane protein","id":"SL-9903"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22442115"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24036347"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27280386"}],"value":"Prospore membrane","id":"SL-0368"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28122955"}],"value":"Peripheral membrane protein","id":"SL-9903"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26370498"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27280386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30018089"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32690699"}],"value":"Vacuole membrane","id":"SL-0271"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28122955"}],"value":"Peripheral membrane protein","id":"SL-9903"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26370498"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27280386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30018089"}],"value":"Nucleus outer membrane","id":"SL-0183"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28122955"}],"value":"Peripheral membrane protein","id":"SL-9903"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28864540"}],"value":"Peroxisome","id":"SL-0204"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34830155"}],"value":"Golgi apparatus, trans-Golgi network membrane","id":"SL-0267"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28122955"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30018089"}],"value":"The SHR-BD domain binds to PxP motifs found in interaction partners"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22442115"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24036347"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26370498"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27280386"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28334785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28404745"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32690699"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34830155"}],"value":"Compromises mitochondrial function and integrity, increases mitophagy (PubMed:27280386, PubMed:32690699, PubMed:34830155). Vacuolar protein missorting (PubMed:27280386, PubMed:28334785). Decreases number of clathrin-coated vesicles in cell (PubMed:34830155). Abnormal cortical reticulophagy; decreases packaging of endoplasmic reticulum (ER) into autophagosomes (PubMed:32690699). Abnormal sporulation; defective prospore membrane formation (PubMed:22442115, PubMed:24036347, PubMed:27280386). Accumulation of vesicles within the prospore membrane lumen and reduction of phosphatidylinositol and phosphatidic acid in the membrane (PubMed:22442115, PubMed:24036347). Abnormal actin cytoskeleton organization (PubMed:28334785). Sorting at early and late endosomes appears abnormal (PubMed:28404745). Sensitive to the arginine analog canavanine (PubMed:28334785, PubMed:34830155). Synthetic lethal with MMM1 (PubMed:26370498, PubMed:27280386). Localization of SPO71 to the prospore membrane is normal (PubMed:24036347)"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14562106"}],"value":"Present with 125 molecules/cell in log phase SD medium"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the VPS13 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":3144,"modifier":"EXACT"}},"description":"Intermembrane lipid transfer protein VPS13","featureId":"PRO_0000065887"},{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Chorein N-terminal","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Domain","location":{"start":{"value":2206,"modifier":"EXACT"},"end":{"value":2484,"modifier":"EXACT"}},"description":"SHR-BD","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1350,"modifier":"EXACT"}},"description":"Involved in phospholipid binding","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28122955"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30093493"}]},{"type":"Region","location":{"start":{"value":432,"modifier":"EXACT"},"end":{"value":457,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1347,"modifier":"EXACT"},"end":{"value":1393,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":2158,"modifier":"EXACT"},"end":{"value":2177,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":2492,"modifier":"EXACT"},"end":{"value":3144,"modifier":"EXACT"}},"description":"Involved in ARF1 binding and phospholipid binding, including phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3-phosphate; possibly in conjunction with the SHR-BD domain","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28122955"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28334785"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"34830155"}]},{"type":"Compositional bias","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":457,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1369,"modifier":"EXACT"},"end":{"value":1393,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":2160,"modifier":"EXACT"},"end":{"value":2169,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":1364,"modifier":"EXACT"},"end":{"value":1364,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19779198"}]},{"type":"Modified residue","location":{"start":{"value":1382,"modifier":"EXACT"},"end":{"value":1382,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19779198"}]},{"type":"Modified residue","location":{"start":{"value":1715,"modifier":"EXACT"},"end":{"value":1715,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"15665377"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"17330950"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"18407956"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19779198"}]},{"type":"Modified residue","location":{"start":{"value":1729,"modifier":"EXACT"},"end":{"value":1729,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19779198"}]},{"type":"Modified residue","location":{"start":{"value":1731,"modifier":"EXACT"},"end":{"value":1731,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0007744","source":"PubMed","id":"18407956"},{"evidenceCode":"ECO:0007744","source":"PubMed","id":"19779198"}]},{"type":"Mutagenesis","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"Increases localization to nuclear envelope-vacuole contact sites. 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LOCATION":1,"DOMAIN":1,"DISRUPTION PHENOTYPE":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":2,"Region":5,"Compositional bias":3,"Modified residue":5,"Mutagenesis":8},"uniParcId":"UPI0000138B80"}}