ID   VATC_CAEBR              Reviewed;         385 AA.
AC   Q612A4; A8XPW4;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=V-type proton ATPase subunit C;
DE            Short=V-ATPase subunit C;
DE   AltName: Full=Vacuolar proton pump subunit C;
GN   Name=vha-11 {ECO:0000250|UniProtKB:Q9XXU9};
GN   ORFNames=CBG16826 {ECO:0000312|WormBase:CBG16826};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
CC   -!- FUNCTION: Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase),
CC       a multisubunit enzyme composed of a peripheral complex (V1) that
CC       hydrolyzes ATP and a membrane integral complex (V0) that translocates
CC       protons (By similarity). V-ATPase is responsible for acidifying and
CC       maintaining the pH of intracellular compartments and in some cell
CC       types, is targeted to the plasma membrane, where it is responsible for
CC       acidifying the extracellular environment (By similarity). Subunit C is
CC       necessary for the assembly of the catalytic sector of the enzyme and is
CC       likely to have a specific function in its catalytic activity (By
CC       similarity). Has roles in embryogenesis and ovulation (By similarity).
CC       {ECO:0000250|UniProtKB:P21282, ECO:0000250|UniProtKB:P31412,
CC       ECO:0000250|UniProtKB:Q9XXU9}.
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. The V1 complex consists of three catalytic AB heterodimers
CC       that form a heterohexamer, three peripheral stalks each consisting of
CC       EG heterodimers, one central rotor including subunits D and F, and the
CC       regulatory subunits C and H. The proton translocation complex V0
CC       consists of the proton transport subunit a, a ring of proteolipid
CC       subunits c9c'', rotary subunit d, subunits e and f, and the accessory
CC       subunits vah-19/Ac45 and vah-20/PRR (By similarity). Interacts with V-
CC       type proton ATPase subunits a1 unc-32, a2 vha-5 and a3 vha-6 (By
CC       similarity). {ECO:0000250|UniProtKB:P21282,
CC       ECO:0000250|UniProtKB:Q9XXU9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9XXU9}.
CC       Membrane {ECO:0000250|UniProtKB:Q9XXU9}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9XXU9}. Note=In embryonic cells, detected in
CC       dot-like structures in the cytoplasm around the nuclei.
CC       {ECO:0000250|UniProtKB:Q9XXU9}.
CC   -!- MISCELLANEOUS: Vha-11 and vha-3 are transcribed on a dicistronic
CC       transcript where vha-3 is the upstream transcript and vha-11 the
CC       downstream. {ECO:0000250|UniProtKB:Q9XXU9}.
CC   -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000255}.
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DR   EMBL; HE600944; CAP34690.1; -; Genomic_DNA.
DR   RefSeq; XP_002645132.1; XM_002645086.1.
DR   AlphaFoldDB; Q612A4; -.
DR   SMR; Q612A4; -.
DR   STRING; 6238.CBG16826; -.
DR   EnsemblMetazoa; CBG16826.1; CBG16826.1; WBGene00036659.
DR   GeneID; 8587130; -.
DR   KEGG; cbr:CBG_16826; -.
DR   CTD; 8587130; -.
DR   WormBase; CBG16826; CBP10353; WBGene00036659; Cbr-vha-11.
DR   eggNOG; KOG2909; Eukaryota.
DR   HOGENOM; CLU_017554_3_0_1; -.
DR   InParanoid; Q612A4; -.
DR   OMA; GEYWLIS; -.
DR   OrthoDB; 1016088at2759; -.
DR   Proteomes; UP000008549; Chromosome IV.
DR   GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; ISS:UniProtKB.
DR   GO; GO:0030728; P:ovulation; ISS:UniProtKB.
DR   CDD; cd14785; V-ATPase_C; 1.
DR   InterPro; IPR004907; ATPase_V1-cplx_csu.
DR   InterPro; IPR036132; Vac_ATP_synth_c_sf.
DR   PANTHER; PTHR10137; PTHR10137; 1.
DR   Pfam; PF03223; V-ATPase_C; 1.
DR   SUPFAM; SSF118203; SSF118203; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Developmental protein; Hydrogen ion transport; Ion transport;
KW   Membrane; Reference proteome; Transport.
FT   CHAIN           1..385
FT                   /note="V-type proton ATPase subunit C"
FT                   /id="PRO_0000278180"
SQ   SEQUENCE   385 AA;  43463 MW;  02B68289FD9A1BAF CRC64;
     MSSAATSGEY WLISVPGEKG ANDAWDKLNR ATGNISTNSK YLIPDLKVGT LDQLVGLSDD
     LSKLDTSAEG VIRKLVQYFT EVLEEDKSKI AENLVIGNKD MKTYVTKFQW EGAKYPLKQS
     LKVLSEIIGK QITQIDNDLK MKSLAYNNLK NALASMDRKT TGSLLTKDLA DLVKAEDFVL
     NSEYLQTIIV VVPKILVKEW ETKYATLSSM VVPGSSKLLT EEGEHALYTV TLFKKVIDEF
     KNIARENKFI VRDFVYDEET LKAGRTERDK LLAEKQKQYA PLIRWLKINF GEIFSAYIHI
     KALRVFVESV LRYGLPVNFQ AAVIEPAKGQ SKKLRQELQK LYIHLDGSAA GPIDTLEDSP
     ALMSLGVNEY YPYVFFKLNI DFSNK