ID   VATL_ASCSU              Reviewed;         161 AA.
AC   Q17046;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=V-type proton ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE            Short=V-ATPase 16 kDa proteolipid subunit c {ECO:0000305};
DE   AltName: Full=Vacuolar proton pump 16 kDa proteolipid subunit c {ECO:0000305};
GN   Name=12;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Denker J.A., Nilsen T.W.;
RL   Submitted (JUN-1990) 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 and in some cell types, is targeted to the plasma
CC       membrane, where it is responsible for acidifying the extracellular
CC       environment (By similarity). {ECO:0000250|UniProtKB:P23956}.
CC   -!- SUBUNIT: V-ATPase is a heteromultimeric enzyme made up of two
CC       complexes: the ATP-hydrolytic V1 complex and the proton translocation
CC       V0 complex (By similarity). The V1 complex consists of three catalytic
CC       AB heterodimers that form a heterohexamer, three peripheral stalks each
CC       consisting of EG heterodimers, one central rotor including subunits D
CC       and F, and the regulatory subunits C and H (By similarity). The proton
CC       translocation complex V0 consists of the proton transport subunit a, a
CC       ring of proteolipid subunits c9c'', rotary subunit d, subunits e and f,
CC       and the accessory subunits vah-19/Ac45 and vah-20/PRR (By similarity).
CC       {ECO:0000250|UniProtKB:P23956}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC       {ECO:0000305}.
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DR   EMBL; M33757; AAA29372.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q17046; -.
DR   SMR; Q17046; -.
DR   EnsemblMetazoa; AgB02_g132_t02; AgB02_g132_t02; AgB02_g132.
DR   EnsemblMetazoa; AgB02_g132_t03; AgB02_g132_t03; AgB02_g132.
DR   EnsemblMetazoa; AgB02_g132_t04; AgB02_g132_t04; AgB02_g132.
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: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; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..161
FT                   /note="V-type proton ATPase 16 kDa proteolipid subunit c"
FT                   /id="PRO_0000071753"
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..98
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        120..137
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..161
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   SITE            145
FT                   /note="Essential for proton translocation"
FT                   /evidence="ECO:0000250|UniProtKB:P63081"
SQ   SEQUENCE   161 AA;  16351 MW;  1D4FE05EE8E1C8A2 CRC64;
     MSYDLATAER AAYAPFFGYM GAASAQIFTV LGAAYGTAKS AVGISSMGVM RPELIMKSVI
     PVIMAGIIGI YGLVVAMVLR GKVTSASAGY TLDKGFAHLA AGLTCGLCGL GAGYAIGIVG
     DAGVRGTAQQ PRLFVGMILI LIFSEVLGLY GMIVALILGT S