{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P43585","secondaryAccessions":["D6VTM5"],"uniProtkbId":"VTC2_YEAST","entryAudit":{"firstPublicDate":"1995-11-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-11-01","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":"Vacuolar transporter chaperone complex subunit 2"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11102525"}],"value":"Phosphate metabolism protein 1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"28186404"}],"value":"SPX-dependent polyphosphate polymerase VTC subunit 2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19390046"}],"value":"Vacuolar membrane polyphosphate polymerase accessory subunit 2"},"shortNames":[{"value":"PolyP polymerase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10480897"}],"value":"VTC2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11102525"}],"value":"PHM1"}],"orderedLocusNames":[{"value":"YFL004W"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11102525"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11823419"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19390046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"25315834"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27080106"}],"value":"Accessory subunit of the vacuolar transporter chaperone (VTC) complex. The VTC complex acts as a vacuolar polyphosphate polymerase that catalyzes the synthesis of inorganic polyphosphate (polyP) via transfer of phosphate from ATP to a growing polyP chain, releasing ADP. VTC exposes its catalytic domain VTC4 to the cytosol, where the growing polyP chain winds through a tunnel-shaped pocket, integrating cytoplasmic polymer synthesis with polyP membrane translocation (PubMed:19390046). The VTC complex carries 9 vacuolar transmembrane domains, which are likely to constitute the translocation channel into the organelle lumen (PubMed:19390046, PubMed:25315834). PolyP synthesis is tightly coupled to its transport into the vacuole lumen, in order to avoid otherwise toxic intermediates in the cytosol, and it depends on the proton gradient across the membrane, formed by V-ATPase (PubMed:25315834). Binds inositol hexakisphosphate (Ins6P) and similar inositol polyphosphates, such as 5-diphospho-inositol pentakisphosphate (5-InsP7); these are important intracellular signaling molecules (PubMed:27080106). Inositol polyphosphate binding promotes vacuolar polyphosphate synthesis (PubMed:27080106). The VTC complex also plays a role in vacuolar membrane fusion (PubMed:11102525, PubMed:11823419). Required for SEC18/NSF activity in SNARE priming, membrane binding of LMA1 and V(0) trans-complex formation (PubMed:11823419)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11823419"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19390046"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27587415"}],"value":"The VTC core complex is an integral membrane heterooligomer composed of the catalytic subunit VTC4 and the accessory subunits VTC1, VTC2 and VTC3. The complex exists in 2 different sub-complexes: VTC1-VTC2-VCT4 and VCT1-VTC3-VTC4. The VCT1-VTC3-VTC4 subcomplex is mostly found on the vacuolar membrane. The VTC1-VTC2-VCT4 subcomplex is observed in the cell periphery, probably ER and nuclear envelope, but localizes to the vacuole under phosphate starvation. Each subunit contains 3 transmembrane helices. VTC1 is a small membrane protein without hydrophilic domain. VTC2, VTC3 and VTC4 are related and have 2 hydrophilic domains that face the cytosol, an N-terminal SPX domain and the central core domain. The central core in VTC4 is the catalytic domain, with the essential catalytic lysine replaced by isoleucine and leucine in VTC2 and VTC3, respectively (PubMed:19390046). The core complex associates with the accessory subunit VTC5 (PubMed:27587415). The complex interacts with the v-SNARE NYV1 and with the V(0) subunit of V-ATPase VPH1 (PubMed:11823419)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12584253"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19390046"}],"value":"Vacuole membrane","id":"SL-0271"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19390046"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17079729"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19390046"}],"value":"Cytoplasm, cell cortex","id":"SL-0138"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17079729"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19390046"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17079729"}],"value":"Cytoplasmic vesicle, autophagosome membrane","id":"SL-0022"},"topology":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19390046"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11102525"}],"value":"By low phosphate"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"27080106"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"28186404"}],"value":"The SPX domain has very high affinity for inositol polyphosphates, such as myo-inositol hexakisphosphate and 5-diphospho-myo-inositol pentakisphosphate (5-InsP7), and moderate affinity for inorganic pyrophosphate. Its affinity for inorganic phosphate is 2 to 3 orders of magnitude lower (Probable). SPX domains may integrate inositol pyrophosphates (PP-InsP)-dependent signaling to adapt cytosolic phosphate concentrations to different metabolic situations (Probable)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14562106"}],"value":"Present with 2915 molecules/cell in log phase SD medium"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the VTC2/3 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":828,"modifier":"EXACT"}},"description":"Vacuolar transporter chaperone complex subunit 2","featureId":"PRO_0000065935"},{"type":"Topological 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