ID   VATA_CAEBR              Reviewed;         606 AA.
AC   Q61VZ4; A8WY40;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=V-type proton ATPase catalytic subunit A;
DE            Short=V-ATPase subunit A;
DE            EC=7.1.2.2 {ECO:0000250|UniProtKB:P50516};
DE   AltName: Full=V-ATPase 69 kDa subunit;
DE   AltName: Full=Vacuolar H ATPase protein 13;
DE   AltName: Full=Vacuolar proton pump subunit alpha;
GN   Name=vha-13 {ECO:0000250|UniProtKB:Q9XW92};
GN   ORFNames=CBG04632 {ECO:0000312|WormBase:CBG04632a};
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: Catalytic subunit of the V1 complex of vacuolar(H+)-ATPase
CC       (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1)
CC       that hydrolyzes ATP and a membrane integral complex (V0) that
CC       translocates protons (By similarity). V-ATPase is responsible for
CC       acidifying and maintaining the pH of intracellular compartments and in
CC       some cell types, is targeted to the plasma membrane, where it is
CC       responsible for acidifying the extracellular environment (By
CC       similarity). Required along with other vacuolar ATPase components for
CC       the removal of protein aggregates which form in immature oocytes in the
CC       distal gonad. This removal occurs as the oocytes mature and move to the
CC       proximal gonad, is triggered by the introduction of sperm through
CC       mating and occurs before fertilization. The introduction of sperm
CC       triggers V-ATPase accumulation in proximal oocytes and induces
CC       lysosomal acidification which leads to engulfing of protein aggregates
CC       by lysosomes and subsequent clearance of the aggregates. Lysosomal
CC       acidification also leads to changes in mitochondrial morphology and
CC       function. Mitochondria in distal immature oocytes are fragmented,
CC       produce high levels of reactive oxygen species (ROS) and have high
CC       membrane potential, indicative of metabolic inactivity. In contrast,
CC       mitochondria in proximal mature oocytes are tubular with lower ROS
CC       levels and membrane potential, indicative of an active metabolic state
CC       required for aggregate mobilization before clearance. Involved in
CC       receptor-mediated endocytosis (By similarity).
CC       {ECO:0000250|UniProtKB:P31404, ECO:0000250|UniProtKB:Q9XW92}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000250|UniProtKB:P50516};
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. {ECO:0000250|UniProtKB:P31404}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255}.
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DR   EMBL; HE601135; CAP25300.3; -; Genomic_DNA.
DR   RefSeq; XP_002637841.1; XM_002637795.1.
DR   AlphaFoldDB; Q61VZ4; -.
DR   SMR; Q61VZ4; -.
DR   STRING; 6238.CBG04632; -.
DR   EnsemblMetazoa; CBG04632a.1; CBG04632a.1; WBGene00027269.
DR   EnsemblMetazoa; CBG04632b.1; CBG04632b.1; WBGene00027269.
DR   GeneID; 8579838; -.
DR   KEGG; cbr:CBG_04632; -.
DR   CTD; 8579838; -.
DR   WormBase; CBG04632a; CBP01281; WBGene00027269; Cbr-vha-13.
DR   eggNOG; KOG1352; Eukaryota.
DR   HOGENOM; CLU_008162_3_1_1; -.
DR   InParanoid; Q61VZ4; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 241249at2759; -.
DR   Proteomes; UP000008549; Chromosome V.
DR   GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR   GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR   GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR   Gene3D; 1.10.1140.10; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00309; ATP_synth_A_arch; 1.
DR   InterPro; IPR031686; ATP-synth_a_Xtn.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR024034; ATPase_F1/V1_b/a_C.
DR   InterPro; IPR005725; ATPase_V1-cplx_asu.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022878; V-ATPase_asu.
DR   PANTHER; PTHR43607; PTHR43607; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   Pfam; PF16886; ATP-synt_ab_Xtn; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   CHAIN           1..606
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000232902"
FT   BINDING         239..246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   606 AA;  66493 MW;  9A235DEA4D7FB08E CRC64;
     MAAESSYGFV YGVSGPVVTA EKMAGSAMYE LVRVGHQELV GEIIRLEGDY ATIQVYEETS
     GVTIGDPVLR TGKPLSVELG PGIMGSIFDG IQRPLKDIAD ITQSIYIPKG VSTNALSREA
     RWDFVVSKDL RVGGHVTGGD IVGTVDENLL IKHKILLPPS ACGTVTFVAP SGQYTVEDTL
     LELEFAGRKQ KFSMLQVWPV RNPRPVTEKL AANNPLLCGQ RVLDALFPCV QGGTTAIPGA
     FGCGKTVISQ SLSKYSNSDA IIYVGCGERG NEMSEVLRDF PELTMEVNGT TTSIMKRTAL
     VANTSNMPVA AREASIYTGI TLAEYFRDMG LNVAMMADST SRWAEALREI SGRLGEMPAD
     SGYPAYLAAR LASFYERAGR VKCLGSPERE GSVTIVGAVS PPGGDFADPV TSATLGIVQV
     FWGLDKKLAQ RKHFPSINWL ISYSKYMRAL EEFYEKNYPE FVHLRTKCKE ILQEEEDLSE
     IVQLVGKASL AESDKITLEV AKIIKDDFLQ QNGYTPYDRF CPFYKTVGML KNMIGFYDLA
     RHSVEATAQS ENKITWNVIK DNMGDLIYQL SAMKFKDPVA DGEAKIRKDY DDLAEAMANG
     FRNLED