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Database: UniProt
Entry: Q9XW92
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ID   VATA_CAEEL              Reviewed;         606 AA.
AC   Q9XW92;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 157.
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:0000312|WormBase:Y49A3A.2};
GN   ORFNames=Y49A3A.2 {ECO:0000312|WormBase:Y49A3A.2};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1] {ECO:0000312|EMBL:CAA22076.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA22076.1};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-33; 97-118; 122-128; 132-152; 192-201; 246-254;
RP   371-377; 449-465; 503-516; 532-541 AND 554-574, AND ACETYLATION AT ALA-2.
RA   Bienvenut W.V.;
RL   Submitted (APR-2006) to UniProtKB.
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=16785323; DOI=10.1083/jcb.200511072;
RA   Liegeois S., Benedetto A., Garnier J.M., Schwab Y., Labouesse M.;
RT   "The V0-ATPase mediates apical secretion of exosomes containing Hedgehog-
RT   related proteins in Caenorhabditis elegans.";
RL   J. Cell Biol. 173:949-961(2006).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=29168500; DOI=10.1038/nature24620;
RA   Bohnert K.A., Kenyon C.;
RT   "A lysosomal switch triggers proteostasis renewal in the immortal C.
RT   elegans germ lineage.";
RL   Nature 551:629-633(2017).
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 (PubMed:29168500). This removal occurs as the oocytes
CC       mature and move to the proximal gonad, is triggered by the introduction
CC       of sperm through mating and occurs before fertilization
CC       (PubMed:29168500). The introduction of sperm triggers V-ATPase
CC       accumulation in proximal oocytes and induces lysosomal acidification
CC       which leads to engulfing of protein aggregates by lysosomes and
CC       subsequent clearance of the aggregates (PubMed:29168500). Lysosomal
CC       acidification also leads to changes in mitochondrial morphology and
CC       function (PubMed:29168500). Mitochondria in distal immature oocytes are
CC       fragmented, produce high levels of reactive oxygen species (ROS) and
CC       have high membrane potential, indicative of metabolic inactivity
CC       (PubMed:29168500). In contrast, mitochondria in proximal mature oocytes
CC       are tubular with lower ROS levels and membrane potential, indicative of
CC       an active metabolic state required for aggregate mobilization before
CC       clearance (PubMed:29168500). Involved in receptor-mediated endocytosis
CC       (PubMed:16785323). {ECO:0000250|UniProtKB:P31404,
CC       ECO:0000269|PubMed:16785323, ECO:0000269|PubMed:29168500, ECO:0000305}.
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   -!- ACTIVITY REGULATION: ATP hydrolysis occurs at the interface between the
CC       nucleotide-binding domains of subunits A and B (By similarity). ATP
CC       hydrolysis triggers a conformational change in the subunits D and F,
CC       which induces a shift of subunit d (By similarity). The c-ring is
CC       subsequently rotated and results in a continuous proton translocation
CC       across the membrane (By similarity). {ECO:0000250|UniProtKB:P31404}.
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:P31404}.
CC   -!- TISSUE SPECIFICITY: Expressed in proximal but not distal germ cells.
CC       {ECO:0000269|PubMed:29168500}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes larval lethality
CC       (PubMed:16785323). Results in increased protein aggregation in the
CC       oocytes of sperm-deficient young adult females which is not eliminated
CC       by mating (PubMed:29168500). Impaired yolk uptake by the oocytes from
CC       the pseudoceolomic cavities (PubMed:16785323). Causes an increase in
CC       the section of the excretory canal, which often has multiple lumens and
CC       abnormal whorls (PubMed:16785323). Does not affect alae formation in
CC       larvae (PubMed:16785323). {ECO:0000269|PubMed:16785323,
CC       ECO:0000269|PubMed:29168500}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255}.
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DR   EMBL; BX284605; CAA22076.1; -; Genomic_DNA.
DR   PIR; T27035; T27035.
DR   RefSeq; NP_506559.1; NM_074158.4.
DR   AlphaFoldDB; Q9XW92; -.
DR   SMR; Q9XW92; -.
DR   BioGRID; 532288; 20.
DR   STRING; 6239.Y49A3A.2.4; -.
DR   TCDB; 3.A.2.2.7; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; Q9XW92; -.
DR   World-2DPAGE; 0020:Q9XW92; -.
DR   EPD; Q9XW92; -.
DR   PaxDb; 6239-Y49A3A-2-3; -.
DR   PeptideAtlas; Q9XW92; -.
DR   EnsemblMetazoa; Y49A3A.2.1; Y49A3A.2.1; WBGene00013025.
DR   GeneID; 3564970; -.
DR   KEGG; cel:CELE_Y49A3A.2; -.
DR   UCSC; Y49A3A.2.2; c. elegans.
DR   AGR; WB:WBGene00013025; -.
DR   WormBase; Y49A3A.2; CE22210; WBGene00013025; vha-13.
DR   eggNOG; KOG1352; Eukaryota.
DR   GeneTree; ENSGT00550000074787; -.
DR   HOGENOM; CLU_008162_3_1_1; -.
DR   InParanoid; Q9XW92; -.
DR   OMA; RIVKTFW; -.
DR   OrthoDB; 5473187at2759; -.
DR   PhylomeDB; Q9XW92; -.
DR   Reactome; R-CEL-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-CEL-77387; Insulin receptor recycling.
DR   Reactome; R-CEL-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-CEL-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-CEL-983712; Ion channel transport.
DR   PRO; PR:Q9XW92; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00013025; Expressed in larva and 4 other cell types or tissues.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IMP:UniProtKB.
DR   GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR   CDD; cd18111; ATP-synt_V_A-type_alpha_C; 1.
DR   CDD; cd18119; ATP-synt_V_A-type_alpha_N; 1.
DR   CDD; cd01134; V_A-ATPase_A; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR01042; V-ATPase_V1_A; 1.
DR   PANTHER; PTHR43607; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 1.
DR   PANTHER; PTHR43607:SF1; V-TYPE PROTON ATPASE CATALYTIC SUBUNIT A; 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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Nucleotide-binding;
KW   Reference proteome; Translocase; Transport.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|Ref.2"
FT   CHAIN           2..606
FT                   /note="V-type proton ATPase catalytic subunit A"
FT                   /id="PRO_0000232903"
FT   BINDING         240..247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   606 AA;  66460 MW;  D1A73ECC57B85892 CRC64;
     MAAESSYGFV YGVSGPVVTA EKMAGSAMYE LVRVGHQELV GEIIRLEGDY ATIQVYEETS
     GVTIGDPVLR TGKPLSVELG PGIMGSIFDG IQRPLKDIAD ITQSIYIPKG VSTNALSREA
     RWDFVVSKDL RVGGHVTGGD IIGTVDENLL IKHKILLPPS ACGTITFVAP SGQYTVEDTL
     LELEFAGRKQ KFSMLQIWPV RSPRPVTEKL AANNPLLCGQ RVLDALFPCV QGGTTAIPGA
     FGCGKTVISQ SLSKYSNSDA IIYVGCGERG NEMSEVLRDF PELTMEVEGV TTSIMKRTAL
     VANTSNMPVA AREASIYTGI TLAEYFRDMG LNVAMMADST SRWAEALREI SGRLGEMPAD
     SGYPAYLAAR LASFYERAGR VKCLGSPERE GSVTIVGAVS PPGGDFADPV TSATLGIVQV
     FWGLDKKLAQ RKHFPSINWL ISYSEYMRAL EEFYEKNYPE FVSLRTKCKE ILQEEEDLSE
     IVQLVGKASL AESDKVTLEV AKIIKDDFLQ QNGYTKYDRF CPFYKTVGML KNMIGFYDLA
     RHAVEATAQS DNKITWNVIK DSMGDLIYQL SAMKFKDPVA DGEAKIRKDY EDLAEAMANA
     FRNLED
//
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