VPS13_YEAST
ID VPS13_YEAST Reviewed; 3144 AA.
AC Q07878; D6VXW6; O00040;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Intermembrane lipid transfer protein VPS13 {ECO:0000305};
DE AltName: Full=Suppression of the onset of impotence protein 1;
DE AltName: Full=Vacuolar protein sorting-associated protein 13;
DE AltName: Full=Vacuolar protein-targeting protein 2;
GN Name=VPS13; Synonyms=SOI1, VPT2, YME3 {ECO:0000303|PubMed:27280386};
GN OrderedLocusNames=YLL040C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9314526; DOI=10.1083/jcb.139.1.23;
RA Brickner J.H., Fuller R.S.;
RT "SOI1 encodes a novel, conserved protein that promotes TGN-endosomal
RT cycling of Kex2p and other membrane proteins by modulating the function of
RT two TGN localization signals.";
RL J. Cell Biol. 139:23-36(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9265642; DOI=10.1083/jcb.138.4.731;
RA Luo W.-J., Chang A.;
RT "Novel genes involved in endosomal traffic in yeast revealed by suppression
RT of a targeting-defective plasma membrane ATPase mutant.";
RL J. Cell Biol. 138:731-746(1997).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1715, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1715, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1715 AND SER-1731, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1364; SER-1382; SER-1715;
RP SER-1729 AND SER-1731, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=22442115; DOI=10.1242/jcs.105114;
RA Park J.S., Neiman A.M.;
RT "VPS13 regulates membrane morphogenesis during sporulation in Saccharomyces
RT cerevisiae.";
RL J. Cell Sci. 125:3004-3011(2012).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP FUNCTION, INTERACTION WITH SPO71, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=24036347; DOI=10.1128/ec.00239-13;
RA Park J.S., Okumura Y., Tachikawa H., Neiman A.M.;
RT "SPO71 encodes a developmental stage-specific partner for Vps13 in
RT Saccharomyces cerevisiae.";
RL Eukaryot. Cell 12:1530-1537(2013).
RN [13]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF ASP-716 AND
RP LEU-1627.
RX PubMed=26370498; DOI=10.1083/jcb.201502105;
RA Lang A.B., John Peter A.T., Walter P., Kornmann B.;
RT "ER-mitochondrial junctions can be bypassed by dominant mutations in the
RT endosomal protein Vps13.";
RL J. Cell Biol. 210:883-890(2015).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP LEU-66; CYS-89; GLY-718; LEU-1107 AND TYR-2702.
RX PubMed=27280386; DOI=10.1091/mbc.e16-02-0112;
RA Park J.S., Thorsness M.K., Policastro R., McGoldrick L.L.,
RA Hollingsworth N.M., Thorsness P.E., Neiman A.M.;
RT "Yeast Vps13 promotes mitochondrial function and is localized at membrane
RT contact sites.";
RL Mol. Biol. Cell 27:2435-2449(2016).
RN [15]
RP FUNCTION, INTERACTION WITH THE ACTIN CYTOSKELETON, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, REGION, AND MUTAGENESIS OF ILE-2749.
RX PubMed=28334785; DOI=10.1093/hmg/ddx054;
RA Rzepnikowska W., Flis K., Kaminska J., Grynberg M., Urbanek A.,
RA Ayscough K.R., Zoladek T.;
RT "Amino acid substitution equivalent to human chorea-acanthocytosis I2771R
RT in yeast Vps13 protein affects its binding to phosphatidylinositol 3-
RT phosphate.";
RL Hum. Mol. Genet. 26:1497-1510(2017).
RN [16]
RP FUNCTION, INTERACTION WITH CDC31, SUBCELLULAR LOCATION, AND REGION.
RX PubMed=28122955; DOI=10.1083/jcb.201606078;
RA De M., Oleskie A.N., Ayyash M., Dutta S., Mancour L., Abazeed M.E.,
RA Brace E.J., Skiniotis G., Fuller R.S.;
RT "The Vps13p-Cdc31p complex is directly required for TGN late endosome
RT transport and TGN homotypic fusion.";
RL J. Cell Biol. 216:425-439(2017).
RN [17]
RP INTERACTION WITH MCP1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LEU-1627.
RX PubMed=28864540; DOI=10.1083/jcb.201610055;
RA John Peter A.T., Herrmann B., Antunes D., Rapaport D., Dimmer K.S.,
RA Kornmann B.;
RT "Vps13-Mcp1 interact at vacuole-mitochondria interfaces and bypass ER-
RT mitochondria contact sites.";
RL J. Cell Biol. 216:3219-3229(2017).
RN [18]
RP INTERACTION WITH YPT35; MCP1 AND SPO71, SUBCELLULAR LOCATION, AND DOMAIN
RP SHR-BD.
RX PubMed=30018089; DOI=10.1083/jcb.201804111;
RA Bean B.D.M., Dziurdzik S.K., Kolehmainen K.L., Fowler C.M.S., Kwong W.K.,
RA Grad L.I., Davey M., Schluter C., Conibear E.;
RT "Competitive organelle-specific adaptors recruit Vps13 to membrane contact
RT sites.";
RL J. Cell Biol. 217:3593-3607(2018).
RN [19]
RP FUNCTION, AND REGION.
RX PubMed=30093493; DOI=10.1083/jcb.201807019;
RA Kumar N., Leonzino M., Hancock-Cerutti W., Horenkamp F.A., Li P.,
RA Lees J.A., Wheeler H., Reinisch K.M., De Camilli P.;
RT "VPS13A and VPS13C are lipid transport proteins differentially localized at
RT ER contact sites.";
RL J. Cell Biol. 217:3625-3639(2018).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=32690699; DOI=10.1073/pnas.2008923117;
RA Chen S., Mari M., Parashar S., Liu D., Cui Y., Reggiori F., Novick P.J.,
RA Ferro-Novick S.;
RT "Vps13 is required for the packaging of the ER into autophagosomes during
RT ER-phagy.";
RL Proc. Natl. Acad. Sci. U.S.A. 117:18530-18539(2020).
RN [21]
RP FUNCTION, INTERACTION WITH ARF1, SUBCELLULAR LOCATION, DISRUPTION
RP PHENOTYPE, AND REGION.
RX PubMed=34830155; DOI=10.3390/ijms222212274;
RA Kolakowski D., Rzepnikowska W., Kaniak-Golik A., Zoladek T., Kaminska J.;
RT "The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi
RT Apparatus.";
RL Int. J. Mol. Sci. 22:12274-12274(2021).
CC -!- FUNCTION: Mediates the transfer of lipids between membranes at
CC organelle contact sites (PubMed:30093493, PubMed:24036347,
CC PubMed:22442115). Binds phospholipids, including phosphatidic acid
CC (PA), phosphorylated phosphatidylinositol (PI), phosphatidylcholine
CC (PC), phosphatidylethanolamine (PE), ceramide, and phosphatidylserine
CC (PS) (PubMed:30093493, PubMed:34830155, PubMed:28122955,
CC PubMed:28334785). Involved in mitochondrial lipid homeostasis, in a
CC MCP1-dependent manner (PubMed:27280386, PubMed:34830155,
CC PubMed:32690699). Involved in cortical reticulophagy (also known as
CC cortical endoplasmic reticulum (ER) macroautophagy), acting at the late
CC endosome to package ER into autophagosomes (PubMed:32690699). Involved
CC in the formation of the prospore membrane during sporulation, in a
CC SPO71-dependent manner (PubMed:24036347, PubMed:22442115). Involved in
CC Golgi vesicle transport, in a CDC31-dependent and ARF1-dependent manner
CC (PubMed:28122955, PubMed:9314526, PubMed:34830155). Plays a role in
CC actin cytoskeleton organization (PubMed:28334785).
CC {ECO:0000269|PubMed:22442115, ECO:0000269|PubMed:24036347,
CC ECO:0000269|PubMed:27280386, ECO:0000269|PubMed:28122955,
CC ECO:0000269|PubMed:28334785, ECO:0000269|PubMed:30093493,
CC ECO:0000269|PubMed:32690699, ECO:0000269|PubMed:34830155,
CC ECO:0000269|PubMed:9314526}.
CC -!- SUBUNIT: Interacts (via SHR-BD domain) with SPO71 (via PxP motif);
CC during prospore membrane formation (PubMed:24036347, PubMed:30018089).
CC Interacts (via SHR-BD domain) with YPT35 (via PxP motif)
CC (PubMed:30018089). Interacts (via SHR-BD domain) with MCP1 (via PxP
CC motif) (PubMed:30018089, PubMed:28864540). Interacts with CDC31
CC (PubMed:28122955). Interacts (via C-terminus) with ARF1; the
CC interaction is direct (PubMed:34830155). Interacts with the actin
CC cytoskeleton (PubMed:28334785). {ECO:0000269|PubMed:24036347,
CC ECO:0000269|PubMed:28122955, ECO:0000269|PubMed:28334785,
CC ECO:0000269|PubMed:28864540, ECO:0000269|PubMed:30018089,
CC ECO:0000269|PubMed:34830155}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane {ECO:0000269|PubMed:27280386,
CC ECO:0000269|PubMed:28334785, ECO:0000269|PubMed:28864540,
CC ECO:0000269|PubMed:30018089, ECO:0000269|PubMed:32690699,
CC ECO:0000305|PubMed:22442115, ECO:0000305|PubMed:24036347}; Peripheral
CC membrane protein {ECO:0000269|PubMed:28122955}. Mitochondrion outer
CC membrane {ECO:0000269|PubMed:26370498, ECO:0000269|PubMed:27280386,
CC ECO:0000269|PubMed:30018089, ECO:0000269|PubMed:34830155}; Peripheral
CC membrane protein {ECO:0000269|PubMed:28122955}. Prospore membrane
CC {ECO:0000269|PubMed:22442115, ECO:0000269|PubMed:24036347,
CC ECO:0000269|PubMed:27280386}; Peripheral membrane protein
CC {ECO:0000269|PubMed:28122955}. Vacuole membrane
CC {ECO:0000269|PubMed:26370498, ECO:0000269|PubMed:27280386,
CC ECO:0000269|PubMed:30018089, ECO:0000269|PubMed:32690699}; Peripheral
CC membrane protein {ECO:0000269|PubMed:28122955}. Nucleus outer membrane
CC {ECO:0000269|PubMed:26370498, ECO:0000269|PubMed:27280386,
CC ECO:0000269|PubMed:30018089}; Peripheral membrane protein
CC {ECO:0000269|PubMed:28122955}. Peroxisome
CC {ECO:0000269|PubMed:28864540}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000269|PubMed:34830155}; Peripheral membrane protein
CC {ECO:0000269|PubMed:28122955}. Note=Found at different interorganellar
CC contact sites depending on the growth state of the cell
CC (PubMed:26370498, PubMed:27280386, PubMed:30018089, PubMed:32690699).
CC Localizes from endosomes to the vacuolar membrane during starvation
CC (PubMed:32690699). Localizes to mitochondrial-endosome contacts
CC (PubMed:27280386). Localizes to nuclear envelope-vacuole contact sites
CC (nuclear-vacuole junction; NVJ) during respiration (PubMed:26370498,
CC PubMed:27280386, PubMed:30018089). {ECO:0000269|PubMed:26370498,
CC ECO:0000269|PubMed:27280386, ECO:0000269|PubMed:30018089,
CC ECO:0000269|PubMed:32690699}.
CC -!- DOMAIN: The SHR-BD domain binds to PxP motifs found in interaction
CC partners. {ECO:0000269|PubMed:30018089}.
CC -!- DISRUPTION PHENOTYPE: Compromises mitochondrial function and integrity,
CC increases mitophagy (PubMed:27280386, PubMed:34830155,
CC PubMed:32690699). Vacuolar protein missorting (PubMed:27280386,
CC PubMed:28334785). Decreases number of clathrin-coated vesicles in cell
CC (PubMed:34830155). Abnormal cortical reticulophagy; decreases packaging
CC of endoplasmic reticulum (ER) into autophagosomes (PubMed:32690699).
CC Abnormal sporulation; defective prospore membrane formation
CC (PubMed:27280386, PubMed:24036347, PubMed:22442115). Accumulation of
CC vesicles within the prospore membrane lumen and reduction of
CC phosphatidylinositol and phosphatidic acid in the membrane
CC (PubMed:22442115, PubMed:24036347). Abnormal actin cytoskeleton
CC organization (PubMed:28334785). Sensitive to the arginine analog
CC canavanine (PubMed:34830155, PubMed:28334785). Synthetic lethal with
CC MMM1 (PubMed:26370498, PubMed:27280386). Localization of SPO71 to the
CC prospore membrane is normal (PubMed:24036347).
CC {ECO:0000269|PubMed:22442115, ECO:0000269|PubMed:24036347,
CC ECO:0000269|PubMed:26370498, ECO:0000269|PubMed:27280386,
CC ECO:0000269|PubMed:28334785, ECO:0000269|PubMed:32690699,
CC ECO:0000269|PubMed:34830155}.
CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VPS13 family. {ECO:0000305}.
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DR EMBL; AF001317; AAC08284.1; -; Genomic_DNA.
DR EMBL; Z73144; CAA97490.1; -; Genomic_DNA.
DR EMBL; Z73145; CAA97491.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09282.1; -; Genomic_DNA.
DR PIR; S64791; S64791.
DR RefSeq; NP_013060.1; NM_001181860.1.
DR SMR; Q07878; -.
DR BioGRID; 31214; 360.
DR DIP; DIP-6519N; -.
DR IntAct; Q07878; 22.
DR MINT; Q07878; -.
DR STRING; 4932.YLL040C; -.
DR iPTMnet; Q07878; -.
DR MaxQB; Q07878; -.
DR PaxDb; Q07878; -.
DR PRIDE; Q07878; -.
DR EnsemblFungi; YLL040C_mRNA; YLL040C; YLL040C.
DR GeneID; 850619; -.
DR KEGG; sce:YLL040C; -.
DR SGD; S000003963; VPS13.
DR VEuPathDB; FungiDB:YLL040C; -.
DR eggNOG; KOG1809; Eukaryota.
DR GeneTree; ENSGT00950000183083; -.
DR HOGENOM; CLU_000135_0_0_1; -.
DR InParanoid; Q07878; -.
DR OMA; VDVRDWS; -.
DR BioCyc; YEAST:G3O-32142-MON; -.
DR PRO; PR:Q07878; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07878; protein.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005798; C:Golgi-associated vesicle; IMP:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005640; C:nuclear outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071561; C:nucleus-vacuole junction; IDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0005628; C:prospore membrane; IDA:UniProtKB.
DR GO; GO:0005774; C:vacuolar membrane; IDA:UniProtKB.
DR GO; GO:0005773; C:vacuole; IDA:UniProtKB.
DR GO; GO:1990816; C:vacuole-mitochondrion membrane contact site; IDA:SGD.
DR GO; GO:0008289; F:lipid binding; IDA:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0120014; F:phospholipid transfer activity; IDA:UniProtKB.
DR GO; GO:0032120; P:ascospore-type prospore membrane formation; IMP:SGD.
DR GO; GO:0048193; P:Golgi vesicle transport; IDA:UniProtKB.
DR GO; GO:0120009; P:intermembrane lipid transfer; IDA:UniProtKB.
DR GO; GO:0045324; P:late endosome to vacuole transport; IMP:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IGI:SGD.
DR GO; GO:0045053; P:protein retention in Golgi apparatus; IMP:SGD.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0090083; P:regulation of inclusion body assembly; IDA:SGD.
DR GO; GO:0061709; P:reticulophagy; IMP:UniProtKB.
DR InterPro; IPR026847; VPS13.
DR InterPro; IPR026854; VPS13-like_N.
DR InterPro; IPR031645; VPS13_C.
DR InterPro; IPR017148; VPS13_fungi.
DR InterPro; IPR031642; VPS13_mid_rpt.
DR InterPro; IPR031646; VPS13_N2.
DR InterPro; IPR009543; VPS13_VAB.
DR PANTHER; PTHR16166; PTHR16166; 1.
DR Pfam; PF12624; Chorein_N; 1.
DR Pfam; PF06650; SHR-BD; 1.
DR Pfam; PF16908; VPS13; 1.
DR Pfam; PF16909; VPS13_C; 1.
DR Pfam; PF16910; VPS13_mid_rpt; 1.
DR PIRSF; PIRSF037235; VPS13_fungi; 1.
PE 1: Evidence at protein level;
KW Endosome; Golgi apparatus; Lipid transport; Lipid-binding; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Nucleus; Peroxisome;
KW Phosphoprotein; Reference proteome; Transport; Vacuole.
FT CHAIN 1..3144
FT /note="Intermembrane lipid transfer protein VPS13"
FT /id="PRO_0000065887"
FT DOMAIN 2..114
FT /note="Chorein N-terminal"
FT /evidence="ECO:0000255"
FT DOMAIN 2206..2484
FT /note="SHR-BD"
FT /evidence="ECO:0000255"
FT REGION 1..1350
FT /note="Involved in phospholipid binding"
FT /evidence="ECO:0000269|PubMed:28122955,
FT ECO:0000269|PubMed:30093493"
FT REGION 432..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2158..2177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2492..3144
FT /note="Involved in ARF1 binding and phospholipid binding,
FT including phosphatidylinositol 4,5-bisphosphate and
FT phosphatidylinositol 3-phosphate; possibly in conjunction
FT with the SHR-BD domain"
FT /evidence="ECO:0000269|PubMed:28122955,
FT ECO:0000269|PubMed:28334785, ECO:0000269|PubMed:34830155"
FT COMPBIAS 1365..1393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1715
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1731
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 66
FT /note="L->P: Increases localization to nuclear envelope-
FT vacuole contact sites. Synthetic lethal with MMM1. Normal
FT vacuolar protein sorting and normal sporulation."
FT /evidence="ECO:0000269|PubMed:27280386"
FT MUTAGEN 89
FT /note="C->K: Synthetic lethal with MMM1. Normal vacuolar
FT protein sorting and normal sporulation."
FT /evidence="ECO:0000269|PubMed:27280386"
FT MUTAGEN 716
FT /note="D->H: Decreases localization to nuclear envelope-
FT vacuole contact sites."
FT /evidence="ECO:0000269|PubMed:26370498"
FT MUTAGEN 718
FT /note="G->K: Decreases localization to nuclear envelope-
FT vacuole contact sites."
FT /evidence="ECO:0000269|PubMed:27280386"
FT MUTAGEN 1107
FT /note="L->P: Vacuolar protein missorting. Synthetic lethal
FT with MMM1. Normal sporulation."
FT /evidence="ECO:0000269|PubMed:27280386"
FT MUTAGEN 1627
FT /note="L->S: Increases localization to peroxisomes.
FT Decreases localization to nuclear envelope-vacuole contact
FT sites and endosomes."
FT /evidence="ECO:0000269|PubMed:26370498,
FT ECO:0000269|PubMed:28864540"
FT MUTAGEN 2702
FT /note="Y->C: Normal vacuolar protein sorting and normal
FT sporulation."
FT /evidence="ECO:0000269|PubMed:27280386"
FT MUTAGEN 2749
FT /note="I->R: Decreases phosphatidylinositol 3-phosphate
FT binding. Vacuolar protein missorting. Abnormal actin
FT cytoskeleton organization. Sensitive to the arginine analog
FT canavanine."
FT /evidence="ECO:0000269|PubMed:28334785"
SQ SEQUENCE 3144 AA; 357849 MW; BEE9B55BA2AD515B CRC64;
MLESLAANLL NRLLGSYVEN FDPNQLNVGI WSGDVKLKNL KLRKDCLDSL NLPIDVKSGI
LGDLVLTVPW SSLKNKPVKI IIEDCYLLCS PRSEDHENDE EMIKRAFRLK MRKVSEWELT
NQARILSTQS ENKTSSSSSE KNNAGFMQSL TTKIIDNLQV TIKNIHLRYE DMDGIFTTGP
SSVGLTLNEL SAVSTDSNWA PSFIDITQNI THKLLTLNSL CLYWNTDSPP LISDDDQDRS
LENFVRGFKD MIASKNSTAP KHQYILKPVS GLGKLSINKL GSTEEQPHID LQMFYDEFGL
ELDDTEYNDI LHVLSSIQLR QITKKFKKAR PSFAVSENPT EWFKYIAACV INEIHEKNKM
WTWESMKEKC EQRRLYTKLW VEKLKLKNLE APLRDPIQEA QLSELHKDLT YDEIILFRSV
AKRQYAQYKL GMTEDSPTPT ASSNIEPQTS NKSATKNNGS WLSSWWNGKP TEEVDEDLIM
TEEQRQELYD AIEFDENEDK GPVLQVPRER VELRVTSLLK KGSFTIRKKK QNLNLGSIIF
ENCKVDFAQR PDSFLSSFQL NKFSLEDGSP NALYKHIISV RNSSKDQSSI DNHATGEEEE
EDEPLLRASF ELNPLDGLAD SNLNIKLLGM TVFYHVHFIT EVHKFFKASN QHMETIGNIV
NAAEATVEGW TTQTRMGIES LLEDHKTVNV SLDLQAPLII LPLDPHDWDT PCAIIDAGHM
SILSDLVPKE KIKEIKELSP EEYDKIDGNE INRLMFDRFQ ILSQDTQIFV GPDIQSTIGK
INTASSTNDF RILDKMKLEL TVDLSILPKA YKLPTIRVFG HLPRLSLSIN DIQYKTIMNL
IANSIPSMID DEENNGDYVN YSSGSEKEMK KQIQLQLKNT LKALENMQPL QIEQKFLELH
FDIDQAKIAF FQCIKNDSRN SEKLVDILCQ RLNFNFDKRA KEMNLDLRVH SLDVEDYIEL
TDNKEFKNLI SSGVEKVTRS QKDLFTLKYK RVQRIVPHND TLIELFDQDI VMHMSELQLV
LTPRSVLTLM NYAMLTFTDP NAPEMPADVL RHNKEDRDDA PQKINMKIKM EAVNVIFNDD
SIKLATLVLS AGEFTMVLLP ERYNINLKLG GLELTDETNE SFSRDSVFRK IIQMKGQELV
ELSYESFDPA TNTKDYDSFL KYSTGSMHVN FIESAVNRMV NFFAKFQKSK VSFDRARLAA
YNQAPSIDAV NNMKMDIVIK APIIQFPKLV GTQENNYDTM RFYLGEFFIE NKFSVIDESH
KINHIKLGVR EGQLSSNLNF DGSSQQLYLV ENIGLLFNID RDPLPQDDTP ELKVTSNFES
FALDLTENQL TYLLEISNKV SSAFNITDEN SGESGGKGEI KSPSPDPASL SSESERTATP
QSLQGSNKSN IKNPEQKYLD FSFKAPKIAL TLYNKTKGVT SLNDCGLTRI MFQDIGCSLG
LKNDGTVDGQ AHVAAFRIED VRNIKDNKHT ELIPKSKNKE YQFVANISRK NLEVGRLLNI
SMTMDSPKMI LAMDYLVSLK EFFDAIMSKS HENNLYYPEN TNQKPENKAI VESVQEGGDV
TKIQYSVNII ETALILLADP CDMNSEAISF KIGQFLVTDQ NIMTVAANNV GIFLFKMNSS
EEKLRLLDDF SSSLTIDKRN STPQTLMTNI QLSVQPLLMR ISLRDIRLAM LIFKRVTTLL
NKMTEKEDNG EEEESTDKIQ FSHEFERKLA VLDPSILGER SRASQSSDSE SIEVPTAILK
NETFNADLGG LRFILIGDVH EMPILDMNVN EITASAKDWS TDFEALASLE TYVNIFNYSR
SSWEPLLEMI PITFHLSKGH SEMDPAFSFD ILTQRIAEIT LSARSIAMLS HIPASLTEEL
PLASRVSQKP YQLVNDTELD FDVWIQDKTT EDNKNEVVLL KANTSLPWEF EDWRSIREKL
DIDKSKNILG VCVSGQNYKT IMNIDATTEG ENLHVLSPPR NNVHNRIVCE ARCDENNVKI
ITFRSTLVIE NTTSTEIELL VDSKDPNKPS LKYAIKPHQS KSVPVEYAYD SDIRIRPASE
DIYDWSQQTL SWKSLLSNQM SIFCSSKEDS NQRFHFEIGA KYDEREPLAK IFPHMKIVVS
ASMTIENLLP ADINFSIFDK REEKRTDFLK TGESMEVHHI SLDSFLLMSV QPLQDEASAS
KPSIVNTPHK SPLNPEDSLS LTLSGGQNLL LKLDYKNIDG TRSKVIRIYS PYIIMNSTDR
ELYIQSSLLN IAQSKILLEN EKRYTIPKMF SFDKEDDKSN RARIRFKESE WSSKLSFDAI
GQSFDASVRI KNKEQESNLG INISEGKGKY LLSKVIEIAP RYIISNTLDI PIEVCETGSM
DVQQIESNIT KPLYRMRNIV DKQLVLKFLG GDSNWSQPFF IKNVGVTYLK VLKNSRHKLL
KIEILLDKAT IFIRIKDGGD RWPFSIRNFS DHDFIFYQRD PRKVSDPYKD DQSNESSSRS
FKPIFYRIPS KSIMPYAWDF PTAKEKYLVL ESGTRTREVR LAEIGELPPL RLDKRSKDKP
APIVGLHVVA DDDMQALVIV NYKANVGLYK LKTASATTTS SVSVNSSVTD GFVQKDEDEK
VNTQIVVSFK GVGISLINGR LQELLYINMR GIELRYNESK AYQTFSWKMK WMQIDNQLFS
GNYSNILYPT EIPYTEKEIE NHPVISGSIS KVNDSLQAVP YFKHVTLLIQ EFSIQLDEDM
LYAMMDFIKF PGSPWIMDSR DYKYDEEIQL PDVSELKTAG DIYFEIFHIQ PTVLHLSFIR
SDEISPGLAE ETEESFSSSL YYVHMFAMTL GNINEAPVKV NSLFMDNVRV PLPILMDHIE
RHYTTQFVYQ IHKILGSADC FGNPVGLFNT ISSGVWDLFY EPYQGYMMND RPQEIGIHLA
KGGLSFAKKT VFGLSDSMSK FTGSMAKGLS VTQDLEFQRV RRLQQRINKN NRNALANSAQ
SFASTLGSGL SGIALDPYKA MQKEGAAGFL KGLGKGIVGL PTKTAIGFLD LTSNLSQGVK
STTTVLDMQK GCRVRLPRYV DHDQIIKPYD LREAQGQYWL KTVNGGVFMN DEYLSHVILP
GKELAVIVSM QHIAEVQMAT QELMWSTGYP SIQGITLERS GLQIKLKSQS EYFIPISDPE
ERRSLYRNIA IAVREYNKYC EAIL
