VOA1_YEAST
ID VOA1_YEAST Reviewed; 265 AA.
AC P53262; D6VUN8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=V0 assembly protein 1;
DE Flags: Precursor;
GN Name=VOA1; OrderedLocusNames=YGR106C;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 PROTEIN SEQUENCE OF 29-38 AND 144-166, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
RN [4]
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 [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 FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, INTERACTION WITH VMA21, AND ASSOCIATION WITH THE V0 COMPLEX.
RX PubMed=18799613; DOI=10.1091/mbc.e08-06-0629;
RA Ryan M., Graham L.A., Stevens T.H.;
RT "Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum.";
RL Mol. Biol. Cell 19:5131-5142(2008).
RN [7] {ECO:0007744|PDB:6C6L}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), IDENTIFICATION IN THE
RP V-ATPASE COMPLEX, AND DISRUPTION PHENOTYPE.
RX PubMed=29526695; DOI=10.1016/j.molcel.2018.02.006;
RA Roh S.H., Stam N.J., Hryc C.F., Couoh-Cardel S., Pintilie G., Chiu W.,
RA Wilkens S.;
RT "The 3.5-A CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase
RT Vo Proton Channel.";
RL Mol. Cell 69:993-1004.e3(2018).
CC -!- FUNCTION: Accessory component of the V0 complex of vacuolar(H+)-ATPase
CC (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1)
CC that hydrolyzes ATP and a membrane integral complex (V0) that
CC translocates protons (PubMed:29526695). V-ATPase is responsible for
CC acidifying and maintaining the pH of intracellular compartments
CC (PubMed:29526695). Functions with VMA21 in assembly of the V0 complex
CC (PubMed:18799613). {ECO:0000269|PubMed:18799613,
CC ECO:0000269|PubMed:29526695}.
CC -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme composed of a peripheral
CC catalytic V1 complex (components A to H) attached to an integral
CC membrane V0 proton pore complex (components: a, c, c', c'', d, e, f and
CC VOA1) (PubMed:29526695). Interacts with VMA21 (PubMed:18799613).
CC Associates with the assembling V0 complex (PubMed:18799613).
CC {ECO:0000269|PubMed:18799613, ECO:0000269|PubMed:29526695}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:14562095};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:14562095}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:18799613}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:18799613}.
CC -!- DISRUPTION PHENOTYPE: Reduces association of VMA6 with the V-type
CC proton ATPase (PubMed:29526695). Decreases VPH1 protein level
CC (PubMed:29526695). {ECO:0000269|PubMed:29526695}.
CC -!- MISCELLANEOUS: Present with 12764 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the VOA1 family. {ECO:0000305}.
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DR EMBL; Z72891; CAA97110.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08199.1; -; Genomic_DNA.
DR PIR; S64413; S64413.
DR RefSeq; NP_011620.1; NM_001181235.1.
DR PDB; 6C6L; EM; 3.50 A; N=1-265.
DR PDB; 6M0R; EM; 2.70 A; N=212-263.
DR PDB; 6M0S; EM; 3.60 A; N=212-263.
DR PDB; 6O7T; EM; 3.20 A; b=1-265.
DR PDB; 6O7U; EM; 3.10 A; b=1-265.
DR PDB; 6O7V; EM; 6.60 A; b=1-265.
DR PDB; 6O7W; EM; 7.00 A; b=1-265.
DR PDB; 6O7X; EM; 8.70 A; b=1-265.
DR PDB; 6PE4; EM; 3.10 A; B=1-265.
DR PDB; 6PE5; EM; 3.20 A; B=1-265.
DR PDB; 7FDA; EM; 4.20 A; e=1-265.
DR PDB; 7FDB; EM; 4.80 A; e=1-265.
DR PDB; 7FDC; EM; 6.60 A; e=1-265.
DR PDB; 7TAO; EM; 3.20 A; N=1-265.
DR PDB; 7TAP; EM; 2.80 A; N=1-265.
DR PDB; 7TMR; EM; 3.50 A; b=1-265.
DR PDB; 7TMS; EM; 3.80 A; b=1-265.
DR PDBsum; 6C6L; -.
DR PDBsum; 6M0R; -.
DR PDBsum; 6M0S; -.
DR PDBsum; 6O7T; -.
DR PDBsum; 6O7U; -.
DR PDBsum; 6O7V; -.
DR PDBsum; 6O7W; -.
DR PDBsum; 6O7X; -.
DR PDBsum; 6PE4; -.
DR PDBsum; 6PE5; -.
DR PDBsum; 7FDA; -.
DR PDBsum; 7FDB; -.
DR PDBsum; 7FDC; -.
DR PDBsum; 7TAO; -.
DR PDBsum; 7TAP; -.
DR PDBsum; 7TMR; -.
DR PDBsum; 7TMS; -.
DR AlphaFoldDB; P53262; -.
DR SMR; P53262; -.
DR BioGRID; 33349; 473.
DR ComplexPortal; CPX-1192; Vacuolar proton translocating ATPase complex, Golgi variant.
DR ComplexPortal; CPX-1193; Vacuolar proton translocating ATPase complex, vacuole variant.
DR IntAct; P53262; 9.
DR MINT; P53262; -.
DR STRING; 4932.YGR106C; -.
DR MaxQB; P53262; -.
DR PaxDb; P53262; -.
DR PRIDE; P53262; -.
DR EnsemblFungi; YGR106C_mRNA; YGR106C; YGR106C.
DR GeneID; 852998; -.
DR KEGG; sce:YGR106C; -.
DR SGD; S000003338; VOA1.
DR VEuPathDB; FungiDB:YGR106C; -.
DR eggNOG; ENOG502S5C0; Eukaryota.
DR HOGENOM; CLU_1050442_0_0_1; -.
DR InParanoid; P53262; -.
DR OMA; HINSKDY; -.
DR BioCyc; YEAST:G3O-30816-MON; -.
DR PRO; PR:P53262; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53262; protein.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
DR GO; GO:0000139; C:Golgi membrane; IC:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:ComplexPortal.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IC:UniProtKB.
DR GO; GO:0048388; P:endosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:0061795; P:Golgi lumen acidification; IC:ComplexPortal.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:SGD.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0007035; P:vacuolar acidification; IC:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Vacuole.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..265
FT /note="V0 assembly protein 1"
FT /id="PRO_0000042985"
FT TOPO_DOM 25..223
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 224..244
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 245..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 262..265
FT /note="ER retention motif"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 212..215
FT /evidence="ECO:0007829|PDB:6PE4"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 221..245
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:6M0R"
SQ SEQUENCE 265 AA; 29678 MW; 225292CA9DB35F3D CRC64;
MVFGQLYALF IFTLSCCISK TVQADSSKES SSFISFDKES NWDTISTISS TADVISSVDS
AIAVFEFDNF SLLDNLMIDE EYPFFNRFFA NDVSLTVHDD SPLNISQSLS PIMEQFTVDE
LPESASDLLY EYSLDDKSIV LFKFTSDAYD LKKLDEFIDS CLSFLEDKSG DNLTVVINSL
GWAFEDEDGD DEYATEETLS HHDNNKGKEG DDDILSSIWT EGLLMCLIVS ALLLFILIVA
LSWISNLDIT YGALEKSTNP IKKNN
