VPS1_YEAST
ID VPS1_YEAST Reviewed; 704 AA.
AC P21576; D6VXT7;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Vacuolar protein sorting-associated protein 1;
GN Name=VPS1; Synonyms=LAM1, SPO15; OrderedLocusNames=YKR001C;
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].
RC STRAIN=J17;
RX PubMed=1825352; DOI=10.1038/349713a0;
RA Yeh E.Y., Driscoll R., Coltrera M., Olins A., Bloom K.S.;
RT "A dynamin-like protein encoded by the yeast sporulation gene SPO15.";
RL Nature 349:713-715(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=J17;
RX PubMed=2112425; DOI=10.1016/0092-8674(90)90070-u;
RA Rothman J.H., Raymond C.K., Gilbert T., O'Hara P.J., Stevens T.H.;
RT "A putative GTP binding protein homologous to interferon-inducible Mx
RT proteins performs an essential function in yeast protein sorting.";
RL Cell 61:1063-1074(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1441752; DOI=10.1002/yea.320080908;
RA Duesterhoeft A., Philippsen P.;
RT "DNA sequencing and analysis of a 24.7 kb segment encompassing centromere
RT CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open
RT reading frames.";
RL Yeast 8:749-759(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [5]
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8344247; DOI=10.1002/j.1460-2075.1993.tb05974.x;
RA Wilsbach K., Payne G.S.;
RT "Vps1p, a member of the dynamin GTPase family, is necessary for Golgi
RT membrane protein retention in Saccharomyces cerevisiae.";
RL EMBO J. 12:3049-3059(1993).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-579 AND SER-599, 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-599, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Essential for protein sorting in meiotic cell division of
CC S.cerevisiae; it binds microtubules. Could also be involved in
CC microtubule-associated motility. Necessary for membrane protein
CC retention in a late Golgi compartment. Interacts with the MVP1 protein.
CC {ECO:0000269|PubMed:8344247}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:8344247}.
CC -!- MISCELLANEOUS: Present with 5960 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. Dynamin/Fzo/YdjA family. {ECO:0000255|PROSITE-
CC ProRule:PRU01055}.
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DR EMBL; X54316; CAA38214.1; -; Genomic_DNA.
DR EMBL; M33315; AAA35216.1; -; Genomic_DNA.
DR EMBL; X65124; CAA46251.1; -; Genomic_DNA.
DR EMBL; Z28226; CAA82071.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09157.1; -; Genomic_DNA.
DR PIR; S25820; S25820.
DR RefSeq; NP_012926.1; NM_001179791.1.
DR AlphaFoldDB; P21576; -.
DR SMR; P21576; -.
DR BioGRID; 34133; 531.
DR DIP; DIP-6290N; -.
DR IntAct; P21576; 60.
DR MINT; P21576; -.
DR STRING; 4932.YKR001C; -.
DR TCDB; 9.A.63.1.1; the retromer-dependent vacuolar protein sorting (r-vps) family.
DR iPTMnet; P21576; -.
DR MaxQB; P21576; -.
DR PaxDb; P21576; -.
DR PRIDE; P21576; -.
DR TopDownProteomics; P21576; -.
DR EnsemblFungi; YKR001C_mRNA; YKR001C; YKR001C.
DR GeneID; 853870; -.
DR KEGG; sce:YKR001C; -.
DR SGD; S000001709; VPS1.
DR VEuPathDB; FungiDB:YKR001C; -.
DR eggNOG; KOG0446; Eukaryota.
DR HOGENOM; CLU_008964_5_2_1; -.
DR InParanoid; P21576; -.
DR OMA; AMDPTNK; -.
DR BioCyc; YEAST:G3O-31979-MON; -.
DR Reactome; R-SCE-169911; Regulation of Apoptosis.
DR Reactome; R-SCE-196025; Formation of annular gap junctions.
DR Reactome; R-SCE-75153; Apoptotic execution phase.
DR PRO; PR:P21576; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P21576; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005777; C:peroxisome; IDA:SGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:SGD.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0060988; P:lipid tube assembly; IDA:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0016559; P:peroxisome fission; IMP:SGD.
DR GO; GO:0007031; P:peroxisome organization; IDA: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:0007034; P:vacuolar transport; IMP:SGD.
DR CDD; cd08771; DLP_1; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR022812; Dynamin.
DR InterPro; IPR001401; Dynamin_GTPase.
DR InterPro; IPR019762; Dynamin_GTPase_CS.
DR InterPro; IPR045063; Dynamin_N.
DR InterPro; IPR000375; Dynamin_stalk.
DR InterPro; IPR030381; G_DYNAMIN_dom.
DR InterPro; IPR003130; GED.
DR InterPro; IPR020850; GED_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11566; PTHR11566; 1.
DR Pfam; PF01031; Dynamin_M; 1.
DR Pfam; PF00350; Dynamin_N; 1.
DR Pfam; PF02212; GED; 1.
DR PRINTS; PR00195; DYNAMIN.
DR SMART; SM00053; DYNc; 1.
DR SMART; SM00302; GED; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00410; G_DYNAMIN_1; 1.
DR PROSITE; PS51718; G_DYNAMIN_2; 1.
DR PROSITE; PS51388; GED; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; GTP-binding; Meiosis;
KW Microtubule; Motor protein; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..704
FT /note="Vacuolar protein sorting-associated protein 1"
FT /id="PRO_0000206588"
FT DOMAIN 26..336
FT /note="Dynamin-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT DOMAIN 618..704
FT /note="GED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00720"
FT REGION 36..43
FT /note="G1 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 62..64
FT /note="G2 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 76..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..181
FT /note="G3 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 247..250
FT /note="G4 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT REGION 277..280
FT /note="G5 motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01055"
FT COMPBIAS 94..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 36..43
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 178..182
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 247..250
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 599
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 33
FT /note="T -> N (in Ref. 2; AAA35216)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="N -> E (in Ref. 2; AAA35216)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="K -> Q (in Ref. 1; CAA38214)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 704 AA; 78737 MW; D9AB527C04B3A977 CRC64;
MDEHLISTIN KLQDALAPLG GGSQSPIDLP QITVVGSQSS GKSSVLENIV GRDFLPRGTG
IVTRRPLVLQ LINRRPKKSE HAKVNQTANE LIDLNINDDD KKKDESGKHQ NEGQSEDNKE
EWGEFLHLPG KKFYNFDEIR KEIVKETDKV TGANSGISSV PINLRIYSPH VLTLTLVDLP
GLTKVPVGDQ PPDIERQIKD MLLKYISKPN AIILSVNAAN TDLANSDGLK LAREVDPEGT
RTIGVLTKVD LMDQGTDVID ILAGRVIPLR YGYIPVINRG QKDIEHKKTI REALENERKF
FENHPSYSSK AHYCGTPYLA KKLNSILLHH IRQTLPEIKA KIEATLKKYQ NELINLGPET
MDSASSVVLS MITDFSNEYA GILDGEAKEL SSQELSGGAR ISYVFHETFK NGVDSLDPFD
QIKDSDIRTI MYNSSGSAPS LFVGTEAFEV LVKQQIRRFE EPSLRLVTLV FDELVRMLKQ
IISQPKYSRY PALREAISNQ FIQFLKDATI PTNEFVVDII KAEQTYINTA HPDLLKGSQA
MVMVEEKLHP RQVAVDPKTG KPLPTQPSSS KAPVMEEKSG FFGGFFSTKN KKKLAALESP
PPVLKATGQM TERETMETEV IKLLISSYFS IVKRTIADII PKALMLKLIV KSKTDIQKVL
LEKLYGKQDI EELTKENDIT IQRRKECKKM VEILRNASQI VSSV
