VPP3_CAEEL
ID VPP3_CAEEL Reviewed; 865 AA.
AC G5EGP4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=V-type proton ATPase 116 kDa subunit a 3 {ECO:0000305};
DE Short=V-ATPase 116 kDa isoform a 3 {ECO:0000305};
GN Name=vha-6 {ECO:0000303|PubMed:11441002, ECO:0000312|WormBase:VW02B12L.1};
GN ORFNames=VW02B12L.1 {ECO:0000312|WormBase:VW02B12L.1};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:BAB62292.1}
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH VHA-11, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11441002; DOI=10.1074/jbc.m101652200;
RA Oka T., Toyomura T., Honjo K., Wada Y., Futai M.;
RT "Four subunit a isoforms of Caenorhabditis elegans vacuolar H+-ATPase.
RT Cell-specific expression during development.";
RL J. Biol. Chem. 276:33079-33085(2001).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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 [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=19741196; DOI=10.1152/ajpcell.00284.2009;
RA Allman E., Johnson D., Nehrke K.;
RT "Loss of the apical V-ATPase a-subunit VHA-6 prevents acidification of the
RT intestinal lumen during a rhythmic behavior in C. elegans.";
RL Am. J. Physiol. 297:C1071-C1081(2009).
CC -!- FUNCTION: Subunit of the V0 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 (PubMed:19741196). In the
CC intestine, required for the rhythmic defecation behavior by promoting
CC acidification in the gut lumen following defecation (PubMed:19741196).
CC Also, luminal acidification is required for nutrient uptake
CC (PubMed:19741196). {ECO:0000250|UniProtKB:Q29466,
CC ECO:0000269|PubMed:19741196}.
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 Interacts with V-type proton ATPase subunit C vha-11 (PubMed:11441002).
CC {ECO:0000250|UniProtKB:Q29466, ECO:0000269|PubMed:11441002}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:11441002, ECO:0000269|PubMed:19741196}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Localizes to the apical surface of
CC intestinal cells (PubMed:11441002). Localizes to dot-like structures,
CC possibly P granules, in P2 cells of 4-cell stage embryos
CC (PubMed:11441002). {ECO:0000269|PubMed:11441002}.
CC -!- DEVELOPMENTAL STAGE: Expressed in P2 cell of 4-cell stage embryo (at
CC protein level) (PubMed:11441002). At the comma stage, expressed in
CC cells in the lateral sides (at protein level) (PubMed:11441002).
CC Specifically expressed in intestine from the 2-fold embryonic stage
CC onwards including in the larval and adult stages (at protein level)
CC (PubMed:11441002, PubMed:19741196). {ECO:0000269|PubMed:11441002,
CC ECO:0000269|PubMed:19741196}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes larval lethality
CC at the L1 stage (PubMed:11441002). RNAi-mediated knockdown at the L1
CC larval stage causes reduced growth rate (PubMed:19741196). The progeny
CC of the few that reach adulthood is arrested at the L1 larval stage
CC (PubMed:19741196). Rhythmic defecation behavior is altered; the
CC defecation cycle period is extended and animals have a slight
CC arrhythmia (PubMed:19741196). In the intestinal epithelium, pH
CC oscillates once per cycle as in the wild-type, but the oscillations are
CC diminished in amplitude and cells are relatively acidic
CC (PubMed:19741196). Also, luminal pH oscillations are reduced
CC (PubMed:19741196). RNAi-mediated knockdown at the L2 larval stage
CC causes a reduction of whole body fat mass in young adults
CC (PubMed:19741196). In some animals, the lumen appears swollen, with a
CC reduction of the cytoplasmic contents of intestinal cells
CC (PubMed:19741196). Defect in nutrient absorption (PubMed:19741196).
CC {ECO:0000269|PubMed:11441002, ECO:0000269|PubMed:19741196}.
CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family.
CC {ECO:0000255|RuleBase:RU361189}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB055111; BAB62292.1; -; mRNA.
DR EMBL; BX284602; CAA20334.1; -; Genomic_DNA.
DR PIR; T18565; T18565.
DR RefSeq; NP_496436.1; NM_064035.6.
DR AlphaFoldDB; G5EGP4; -.
DR SMR; G5EGP4; -.
DR STRING; 6239.VW02B12L.1.1; -.
DR TCDB; 3.A.2.2.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR EPD; G5EGP4; -.
DR PaxDb; G5EGP4; -.
DR PeptideAtlas; G5EGP4; -.
DR EnsemblMetazoa; VW02B12L.1.1; VW02B12L.1.1; WBGene00006915.
DR GeneID; 174743; -.
DR KEGG; cel:CELE_VW02B12L.1; -.
DR CTD; 174743; -.
DR WormBase; VW02B12L.1; CE18980; WBGene00006915; vha-6.
DR eggNOG; KOG2189; Eukaryota.
DR GeneTree; ENSGT00950000182881; -.
DR HOGENOM; CLU_005230_0_2_1; -.
DR InParanoid; G5EGP4; -.
DR OMA; AIHTVEY; -.
DR OrthoDB; 181796at2759; -.
DR PhylomeDB; G5EGP4; -.
DR Reactome; R-CEL-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
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 Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006915; Expressed in larva and 4 other tissues.
DR GO; GO:0045177; C:apical part of cell; IDA:WormBase.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IPI:WormBase.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR InterPro; IPR002490; V-ATPase_116kDa_su.
DR InterPro; IPR026028; V-type_ATPase_116kDa_su_euka.
DR PANTHER; PTHR11629; PTHR11629; 1.
DR Pfam; PF01496; V_ATPase_I; 2.
DR PIRSF; PIRSF001293; ATP6V0A1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Glycoprotein; Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..865
FT /note="V-type proton ATPase 116 kDa subunit a 3"
FT /id="PRO_0000454082"
FT TOPO_DOM 1..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..453
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 454..474
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 475..556
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 557..577
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 578..583
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 584..604
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 605..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 624..644
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 645..688
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 689..709
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 710..798
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 799..819
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 820..865
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT COILED 51..121
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 865 AA; 98540 MW; F6ED163B72FA9988 CRC64;
MGSIYRSEHM KLCQIFFQSE SAYQCVAELG ELGMAQFIDL NEEQNAYTRK FVNEVRRCDE
MERKINFVED EITKDLVPIP DYDEHIPAPQ PKHMGEMEAN LEKLEEELVQ INKNCKVLKN
NHVQLLEMKA VLEHVTSLLD PHSKREAAMS ISEAARGEAG PISFGMKDEF DKPVKDEKEL
KFVTGVVKRS KAIAFERFLW RLSRAKVFAK FIQIQEQTEL FSNEFEDKCV FILFFSGEQL
RAKVKKICDG FQAKCYTVPE NPAERTKLLL NIKVQTTDMK AVIEKTLDYR SKCIHAAATN
LRKWGIMLLK LKSIFHTLNM FSVDVTQKCL IAECWVPEAD IGQVKNSLHM GTIHSGSTVP
AILNEMETDK YPPTYFKLNK FTQGFQNIVD AYGIANYREV NPAPWTIISF PFLFAVMFGD
AGHGIIMLIA ASAFVIFEKK LISMKIKDEI FNTFFGGRYV VLLMGMFAIY TGFIYNDFYS
KSVNIFGSSW VNPYNQTLLA NMDAQGADSN TDLSLTFPPE IAFNHDYGPY PFGVDPVWNL
AINRLNFLNP MKMKTSILLG ISQMAFGIML SLMNHIGNRS VVDIVFVFIP QCLFLGCIFV
YLCLQVLMKW IFFYVKPAYI FGRLYPGSNC APSLLIGLIN MFMVKSRDAS FAHDVGTAAG
KEWVIVNGQN VTYTINDQCY LQQWYPNQSL VELILLLIAV VSVPVMLLVK PFYIRWRHSR
GLHIDLGHGP DEHGEFNFGD IMVHQAIHTI EFVLGCVSHT ASYLRLWALS LAHAQLSDVL
WTMVLRMSLT MGGWGGSAAI TILFYFIFSI LSVCILILME GLSAFLHAIR LHWVEFQSKF
YGGTGIQFEP FCFTKIIRVY EGLDQ
