VATL2_CANGA
ID VATL2_CANGA Reviewed; 164 AA.
AC Q6FUY5;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=V-type proton ATPase subunit c' {ECO:0000250|UniProtKB:P32842};
DE Short=V-ATPase subunit c' {ECO:0000250|UniProtKB:P32842};
DE AltName: Full=Proteolipid protein VMA11;
DE AltName: Full=V-type proton ATPase 16 kDa proteolipid subunit 2;
DE Short=V-ATPase 16 kDa proteolipid subunit 2;
DE AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit 2;
DE AltName: Full=Vacuolar proton pump c' subunit {ECO:0000250|UniProtKB:P32842};
GN Name=VMA11; OrderedLocusNames=CAGL0E06204g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 (By similarity). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments (By similarity). {ECO:0000250|UniProtKB:P32842}.
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) (By similarity). The decameric c-ring forms the proton-conducting
CC pore, and is composed of eight proteolipid subunits c, one subunit c'
CC and one subunit c'' (By similarity). {ECO:0000250|UniProtKB:P32842}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P32842};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; CR380951; CAG58878.1; -; Genomic_DNA.
DR RefSeq; XP_445959.1; XM_445959.1.
DR AlphaFoldDB; Q6FUY5; -.
DR SMR; Q6FUY5; -.
DR STRING; 5478.XP_445959.1; -.
DR EnsemblFungi; CAG58878; CAG58878; CAGL0E06204g.
DR GeneID; 2887351; -.
DR KEGG; cgr:CAGL0E06204g; -.
DR CGD; CAL0128810; CAGL0E06204g.
DR VEuPathDB; FungiDB:CAGL0E06204g; -.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_085752_1_1_1; -.
DR InParanoid; Q6FUY5; -.
DR OMA; MSVCPPY; -.
DR Proteomes; UP000002428; Chromosome E.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:EnsemblFungi.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
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; 2.
DR TIGRFAMs; TIGR01100; V_ATP_synt_C; 1.
PE 3: Inferred from homology;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..164
FT /note="V-type proton ATPase subunit c'"
FT /id="PRO_0000071783"
FT TOPO_DOM 1..16
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..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="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 120..136
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..164
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 145
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P32842"
SQ SEQUENCE 164 AA; 17093 MW; 4AE7668074EB2F76 CRC64;
MDMVASDNVY APLYAPFFGF AGCALAMILS CLGAAIGTAK SGIGIAGIGT FKPELIMKSL
IPVVMSGILA IYGLVVAVLI AGNLSPTEEY TLFNGFMHLS CGLCVGFACL SSGYAIGIVG
DVGVRKYMHQ PRLFVGIVLI LIFSEVLGLY GMIIALILNT KGSE
