VATL2_ASHGO
ID VATL2_ASHGO Reviewed; 164 AA.
AC Q755G4;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=AFL141C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016819; AAS53233.1; -; Genomic_DNA.
DR RefSeq; NP_985409.1; NM_210763.1.
DR AlphaFoldDB; Q755G4; -.
DR SMR; Q755G4; -.
DR STRING; 33169.AAS53233; -.
DR EnsemblFungi; AAS53233; AAS53233; AGOS_AFL141C.
DR GeneID; 4621635; -.
DR KEGG; ago:AGOS_AFL141C; -.
DR eggNOG; KOG0232; Eukaryota.
DR HOGENOM; CLU_085752_1_1_1; -.
DR InParanoid; Q755G4; -.
DR OMA; MSVCPPY; -.
DR Proteomes; UP000000591; Chromosome VI.
DR GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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; 1.
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_0000071782"
FT TOPO_DOM 1..15
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..58
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 80..97
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..164
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT SITE 144
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:P32842"
SQ SEQUENCE 164 AA; 16880 MW; 65C6A25772BC55E9 CRC64;
MTDDLVNEYA PAFAPFFGFA GCAAAMILSS LGAAIGTAKS GIGISGIGTF RPELIMKSLI
PVVMSGILAV YGLVVAVLVA GGLSPTEEYT LFNGFMHLAA GLCVGFACLS SGYAIGIVGD
VGVRKFMHQP RLFVGIVLIL IFAEVLGLYG MIIALILNTR GSGN
