VATL2_YEAST
ID VATL2_YEAST Reviewed; 164 AA.
AC P32842; D6W3D6; P32365;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=V-type proton ATPase subunit c';
DE Short=V-ATPase subunit c';
DE AltName: Full=Proteolipid protein VMA11;
DE AltName: Full=Trifluoperazine resistance protein 3;
DE AltName: Full=V-ATPase 16 kDa proteolipid subunit 2;
DE AltName: Full=Vacuolar proton pump c' subunit;
GN Name=VMA11; Synonyms=CLS9, TFP3; OrderedLocusNames=YPL234C; ORFNames=P1064;
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 26786 / X2180-1A;
RX PubMed=1837023; DOI=10.1016/s0021-9258(18)54261-7;
RA Umemoto N., Ohya Y., Anraku Y.;
RT "VMA11, a novel gene that encodes a putative proteolipid, is indispensable
RT for expression of yeast vacuolar membrane H(+)-ATPase activity.";
RL J. Biol. Chem. 266:24526-24532(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=2192255; DOI=10.1128/mcb.10.7.3397-3404.1990;
RA Shih C.-K., Kwong J., Montalvo E., Neff N.;
RT "Expression of a proteolipid gene from a high-copy-number plasmid confers
RT trifluoperazine resistance to Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 10:3397-3404(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-145.
RX PubMed=9030535; DOI=10.1074/jbc.272.8.4795;
RA Hirata R., Graham L.A., Takatsuki A., Stevens T.H., Anraku Y.;
RT "VMA11 and VMA16 encode second and third proteolipid subunits of the
RT Saccharomyces cerevisiae vacuolar membrane H+-ATPase.";
RL J. Biol. Chem. 272:4795-4803(1997).
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 TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [9] {ECO:0007744|PDB:5TJ5}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 17-163, AND
RP IDENTIFICATION IN THE V-ATPASE COMPLEX.
RX PubMed=27776355; DOI=10.1038/nature19828;
RA Mazhab-Jafari M.T., Rohou A., Schmidt C., Bueler S.A., Benlekbir S.,
RA Robinson C.V., Rubinstein J.L.;
RT "Atomic model for the membrane-embedded VO motor of a eukaryotic V-
RT ATPase.";
RL Nature 539:118-122(2016).
RN [10] {ECO:0007744|PDB:6C6L}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), AND IDENTIFICATION IN
RP THE V-ATPASE COMPLEX.
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: Proton-conducting pore forming of the V0 complex of
CC vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC complex (V0) that translocates protons (PubMed:1837023,
CC PubMed:9030535). V-ATPase is responsible for acidifying and maintaining
CC the pH of intracellular compartments (PubMed:1837023, PubMed:9030535).
CC {ECO:0000269|PubMed:1837023, ECO:0000269|PubMed:9030535}.
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:27776355, PubMed:29526695). The decameric c-ring forms
CC the proton-conducting pore, and is composed of eight proteolipid
CC subunits c, one subunit c' and one subunit c'' (PubMed:27776355,
CC PubMed:29526695). {ECO:0000269|PubMed:27776355,
CC ECO:0000269|PubMed:29526695}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:9030535};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- MISCELLANEOUS: Present with 538 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35149.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D10486; BAA01367.1; -; Genomic_DNA.
DR EMBL; M32736; AAA35149.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z67751; CAA91610.1; -; Genomic_DNA.
DR EMBL; X94561; CAA64253.1; -; Genomic_DNA.
DR EMBL; Z73590; CAA97951.1; -; Genomic_DNA.
DR EMBL; AY558058; AAS56384.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11202.1; -; Genomic_DNA.
DR PIR; A41712; A41712.
DR RefSeq; NP_015090.1; NM_001184048.1.
DR PDB; 5TJ5; EM; 3.90 A; D=17-163.
DR PDB; 5VOX; EM; 6.80 A; S=1-164.
DR PDB; 5VOY; EM; 7.90 A; S=1-164.
DR PDB; 5VOZ; EM; 7.60 A; S=1-164.
DR PDB; 6C6L; EM; 3.50 A; D=1-164.
DR PDB; 6M0R; EM; 2.70 A; D=7-164.
DR PDB; 6M0S; EM; 3.60 A; D=7-164.
DR PDB; 6O7T; EM; 3.20 A; o=1-164.
DR PDB; 6O7U; EM; 3.10 A; o=1-164.
DR PDB; 6O7V; EM; 6.60 A; o=1-164.
DR PDB; 6O7W; EM; 7.00 A; o=1-164.
DR PDB; 6O7X; EM; 8.70 A; o=1-164.
DR PDB; 6PE4; EM; 3.10 A; H=1-164.
DR PDB; 6PE5; EM; 3.20 A; H=1-164.
DR PDB; 7FDA; EM; 4.20 A; U=1-164.
DR PDB; 7FDB; EM; 4.80 A; U=1-164.
DR PDB; 7FDC; EM; 6.60 A; U=1-164.
DR PDB; 7TAO; EM; 3.20 A; D=1-164.
DR PDB; 7TAP; EM; 2.80 A; D=1-164.
DR PDB; 7TMR; EM; 3.50 A; o=1-164.
DR PDB; 7TMS; EM; 3.80 A; o=1-164.
DR PDBsum; 5TJ5; -.
DR PDBsum; 5VOX; -.
DR PDBsum; 5VOY; -.
DR PDBsum; 5VOZ; -.
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; P32842; -.
DR SMR; P32842; -.
DR BioGRID; 35928; 236.
DR ComplexPortal; CPX-1192; Vacuolar proton translocating ATPase complex, Golgi variant.
DR ComplexPortal; CPX-1193; Vacuolar proton translocating ATPase complex, vacuole variant.
DR DIP; DIP-5394N; -.
DR IntAct; P32842; 7.
DR MINT; P32842; -.
DR STRING; 4932.YPL234C; -.
DR BindingDB; P32842; -.
DR ChEMBL; CHEMBL1795084; -.
DR TCDB; 3.A.2.2.3; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR MaxQB; P32842; -.
DR PaxDb; P32842; -.
DR PRIDE; P32842; -.
DR EnsemblFungi; YPL234C_mRNA; YPL234C; YPL234C.
DR GeneID; 855842; -.
DR KEGG; sce:YPL234C; -.
DR SGD; S000006155; VMA11.
DR VEuPathDB; FungiDB:YPL234C; -.
DR eggNOG; KOG0232; Eukaryota.
DR GeneTree; ENSGT00960000189220; -.
DR HOGENOM; CLU_085752_1_1_1; -.
DR OMA; MSVCPPY; -.
DR BioCyc; YEAST:G3O-34121-MON; -.
DR PRO; PR:P32842; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P32842; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IC:ComplexPortal.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
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; IDA:SGD.
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; TAS:SGD.
DR GO; GO:0048388; P:endosomal lumen acidification; IC:ComplexPortal.
DR GO; GO:0061795; P:Golgi lumen acidification; IC:ComplexPortal.
DR GO; GO:1902600; P:proton transmembrane transport; IDA:ComplexPortal.
DR GO; GO:0007035; P:vacuolar acidification; TAS:SGD.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR000245; ATPase_proteolipid_csu.
DR InterPro; IPR011555; ATPase_proteolipid_su_C_euk.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR PRINTS; PR00122; VACATPASE.
DR SUPFAM; SSF81333; SSF81333; 1.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..164
FT /note="V-type proton ATPase subunit c'"
FT /id="PRO_0000071788"
FT TOPO_DOM 1..14
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 15..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..98
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..164
FT /note="Vacuolar"
FT /evidence="ECO:0000255"
FT SITE 145
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000269|PubMed:9030535"
FT MUTAGEN 145
FT /note="E->D: Partial inactivation."
FT /evidence="ECO:0000269|PubMed:9030535"
FT MUTAGEN 145
FT /note="E->L,Q: Inactivation."
FT /evidence="ECO:0000269|PubMed:9030535"
FT CONFLICT 27..35
FT /note="Missing (in Ref. 2; AAA35149)"
FT /evidence="ECO:0000305"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 15..48
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:6M0R"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 61..82
FT /evidence="ECO:0007829|PDB:6M0R"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 92..127
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:6M0R"
FT HELIX 134..163
FT /evidence="ECO:0007829|PDB:6M0R"
SQ SEQUENCE 164 AA; 17037 MW; C82D165064EEBBF7 CRC64;
MSTQLASNIY APLYAPFFGF AGCAAAMVLS CLGAAIGTAK SGIGIAGIGT FKPELIMKSL
IPVVMSGILA IYGLVVAVLI AGNLSPTEDY TLFNGFMHLS CGLCVGFACL SSGYAIGMVG
DVGVRKYMHQ PRLFVGIVLI LIFSEVLGLY GMIVALILNT RGSE
