VMS1_YEAST
ID VMS1_YEAST Reviewed; 632 AA.
AC Q04311; D6VS36; Q66RH0;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Protein VMS1;
DE AltName: Full=VCP/CDC48-associated mitochondrial stress-responsive protein 1;
GN Name=VMS1; OrderedLocusNames=YDR049W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP DOMAIN.
RX PubMed=9171100; DOI=10.1093/nar/25.12.2464;
RA Boehm S., Frishman D., Mewes H.-W.;
RT "Variations of the C2H2 zinc finger motif in the yeast genome and
RT classification of yeast zinc finger proteins.";
RL Nucleic Acids Res. 25:2464-2469(1997).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
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 [7]
RP SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, FUNCTION, AND INTERACTION WITH
RP CDC48 AND NPL4.
RX PubMed=21070972; DOI=10.1016/j.molcel.2010.10.021;
RA Heo J.M., Livnat-Levanon N., Taylor E.B., Jones K.T., Dephoure N., Ring J.,
RA Xie J., Brodsky J.L., Madeo F., Gygi S.P., Ashrafi K., Glickman M.H.,
RA Rutter J.;
RT "A stress-responsive system for mitochondrial protein degradation.";
RL Mol. Cell 40:465-480(2010).
RN [8]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH CDC48.
RX PubMed=21148305; DOI=10.1074/jbc.m110.179259;
RA Tran J.R., Tomsic L.R., Brodsky J.L.;
RT "A Cdc48p-associated factor modulates endoplasmic reticulum-associated
RT degradation, cell stress, and ubiquitinated protein homeostasis.";
RL J. Biol. Chem. 286:5744-5755(2011).
CC -!- FUNCTION: Involved in the endoplasmic reticulum (ER)-associated
CC degradation (ERAD) pathway. Component of an evolutionarily conserved
CC system for ubiquitin-mediated mitochondria-associated protein
CC degradation (MAD), which is necessary to maintain mitochondrial,
CC cellular, and organismal viability. {ECO:0000269|PubMed:21070972,
CC ECO:0000269|PubMed:21148305}.
CC -!- SUBUNIT: Interacts with CDC48 and NPL4. {ECO:0000269|PubMed:21070972,
CC ECO:0000269|PubMed:21148305}.
CC -!- INTERACTION:
CC Q04311; P25694: CDC48; NbExp=5; IntAct=EBI-784329, EBI-4308;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion. Endoplasmic reticulum
CC membrane; Peripheral membrane protein. Note=translocates from the
CC cytosol to mitochondria upon mitochondrial stress.
CC -!- DISRUPTION PHENOTYPE: Leads to progressive mitochondrial failure,
CC hypersensitivity to oxidative stress, and decreased chronological life
CC span. {ECO:0000269|PubMed:21070972}.
CC -!- MISCELLANEOUS: Present with 3930 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ANKZF1/VMS1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z49209; CAA89079.1; -; Genomic_DNA.
DR EMBL; AY723770; AAU09687.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11896.1; -; Genomic_DNA.
DR PIR; S54034; S54034.
DR RefSeq; NP_010334.1; NM_001180357.1.
DR PDB; 5WHG; X-ray; 2.70 A; A=1-417.
DR PDB; 6R86; EM; 3.40 A; R=13-529.
DR PDB; 6R87; EM; 3.40 A; R=13-529.
DR PDBsum; 5WHG; -.
DR PDBsum; 6R86; -.
DR PDBsum; 6R87; -.
DR AlphaFoldDB; Q04311; -.
DR SMR; Q04311; -.
DR BioGRID; 32103; 428.
DR ComplexPortal; CPX-3069; CDC48-NPL4-VMS1 AAA ATPase complex.
DR DIP; DIP-6303N; -.
DR IntAct; Q04311; 5.
DR MINT; Q04311; -.
DR STRING; 4932.YDR049W; -.
DR iPTMnet; Q04311; -.
DR MaxQB; Q04311; -.
DR PaxDb; Q04311; -.
DR PRIDE; Q04311; -.
DR EnsemblFungi; YDR049W_mRNA; YDR049W; YDR049W.
DR GeneID; 851618; -.
DR KEGG; sce:YDR049W; -.
DR SGD; S000002456; VMS1.
DR VEuPathDB; FungiDB:YDR049W; -.
DR eggNOG; KOG2505; Eukaryota.
DR GeneTree; ENSGT00390000005911; -.
DR HOGENOM; CLU_014293_1_1_1; -.
DR InParanoid; Q04311; -.
DR OMA; GESKWDW; -.
DR BioCyc; YEAST:G3O-29660-MON; -.
DR BRENDA; 3.1.1.29; 984.
DR PRO; PR:Q04311; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q04311; protein.
DR GO; GO:0036266; C:Cdc48p-Npl4p-Vms1p AAA ATPase complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0072671; P:mitochondria-associated ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0071630; P:nuclear protein quality control by the ubiquitin-proteasome system; IMP:SGD.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IC:ComplexPortal.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:SGD.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR041175; VLRF1/Vms1.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF18826; bVLRF1; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ANK repeat; Coiled coil; Cytoplasm; Endoplasmic reticulum;
KW Membrane; Metal-binding; Mitochondrion; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..632
FT /note="Protein VMS1"
FT /id="PRO_0000244435"
FT REPEAT 470..500
FT /note="ANK 1"
FT REPEAT 504..530
FT /note="ANK 2"
FT ZN_FING 72..96
FT /note="C2H2-type"
FT REGION 123..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 544..582
FT /evidence="ECO:0000255"
FT COILED 608..632
FT /evidence="ECO:0000255"
FT COMPBIAS 123..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..632
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 170
FT /note="K -> E (in Ref. 3; AAU09687)"
FT /evidence="ECO:0000305"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:5WHG"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:5WHG"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:5WHG"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:5WHG"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:5WHG"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:5WHG"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:5WHG"
FT HELIX 219..226
FT /evidence="ECO:0007829|PDB:5WHG"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:5WHG"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:5WHG"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:5WHG"
FT STRAND 275..283
FT /evidence="ECO:0007829|PDB:5WHG"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:5WHG"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:5WHG"
FT STRAND 341..344
FT /evidence="ECO:0007829|PDB:5WHG"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:5WHG"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:5WHG"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:5WHG"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:5WHG"
FT HELIX 379..390
FT /evidence="ECO:0007829|PDB:5WHG"
SQ SEQUENCE 632 AA; 72733 MW; 98A2007E5591A220 CRC64;
MNSQKASKMT GSLKKNDLYI FDLSEQLLNS LKLMSFDSTL REVEVEKTSD NDRNKESGDL
QIARKKVTSN VMRCSVCQMS FDSRNEQKAH YQTDYHLMNV KRNLRGLDIL SVEEFDALIS
KEHGIKSEDE NSGGEQTSSD HEESEEASDR DPDLQTNNYM ETIIENDLQK LGFQKDESDA
ISHINTQSPY IYFKSKYLQK NEVLAIYKSL FNKRSLSNPN EALTFWNSQE NPMAISALFM
VGGGHFAGAI VSHQRLNVKG NAHKKDETLI EQAVNFLEHK TFHRYTTRRK QGGSQSAMDN
AKGKANSAGS ALRRYNESAL KTDIQGVLKD WEPYLSKCDN IFIRARNVSD KKIFTDNTVL
NKGDERIKSF PFTTNRPTVL ELKKAWCELS YLKILPKPEP LAVKETVQKL EVSNKKDEFK
EKQEPLLEEI QTEEIISLLK KGRAPLLISF LKKNKLDGNF RLKPESKYSL TPTMLHYASQ
QGMKQMALIL LSNIKCDPTI KNRLGRTAWD LNRNDDVRHA FQIARYNLGE SFTNWDETHI
GQPLSREQVD EINEKKKAIE NEKAEKLIKL ELEAAKEKQR FAKDAERGPG KKLTNIPSIQ
QQNLNSLTDE QRRRLMREQR ARAAEERMKK KY
