ID   VATL1_CANTR             Reviewed;         160 AA.
AC   Q00607;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=V-type proton ATPase subunit c {ECO:0000303|Ref.1};
DE            Short=V-ATPase subunit c {ECO:0000303|Ref.1};
DE   AltName: Full=V-type proton ATPase 16 kDa proteolipid subunit;
DE            Short=V-ATPase 16 kDa proteolipid subunit;
DE   AltName: Full=Vacuolar proton pump c subunit {ECO:0000250|UniProtKB:P25515};
GN   Name=VMA3;
OS   Candida tropicalis (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Gu H.H., Xu J., Dean G.E.;
RT   "Structure and expression of the vacuolar ATPase subunit c gene from
RT   Candida tropicalis.";
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
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:P25515}.
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:P25515}.
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P25515};
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; U02877; AAA03446.1; -; Unassigned_DNA.
DR   AlphaFoldDB; Q00607; -.
DR   SMR; Q00607; -.
DR   VEuPathDB; FungiDB:CTMYA2_049920; -.
DR   VEuPathDB; FungiDB:CTRG_02310; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
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; Transmembrane;
KW   Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..160
FT                   /note="V-type proton ATPase subunit c"
FT                   /id="PRO_0000071759"
FT   TOPO_DOM        1..6
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..53
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..90
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        112..129
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..160
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   SITE            137
FT                   /note="Essential for proton translocation"
FT                   /evidence="ECO:0000250|UniProtKB:P25515"
SQ   SEQUENCE   160 AA;  16222 MW;  14E52BBA7332B964 CRC64;
     MSDLCPVYAP FFGSIGCAAA IVFTCFGASY GTAKSGVGIC ATSVTRPDLL VKNVVPVVMA
     GIIAIYGLVV SVLVSDSLSQ KQALYTGFIQ LGAGLSVGLS GLAAGFAIGI VGDAGVRGTA
     QQPRLFVGMI LILIFAEVLG LYGLIVALLL NSRASQDVTC