VATA_CAEEL
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 03-AUG-2022, entry version 150.
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; 18.
DR STRING; 6239.Y49A3A.2.3; -.
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; Q9XW92; -.
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 CTD; 3564970; -.
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; 241249at2759; -.
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 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: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 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 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
