VA0E_CAEEL
ID VA0E_CAEEL Reviewed; 86 AA.
AC Q20591;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=V-type proton ATPase subunit e;
DE Short=V-ATPase subunit e;
DE AltName: Full=Vacuolar proton pump subunit e;
GN Name=vha-17 {ECO:0000312|WormBase:F49C12.13};
GN Synonyms=fus-1 {ECO:0000303|PubMed:15866168};
GN ORFNames=F49C12.13 {ECO:0000312|WormBase:F49C12.13};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF 52-VAL--ASN-86.
RX PubMed=15866168; DOI=10.1016/j.devcel.2005.02.018;
RA Kontani K., Moskowitz I.P.G., Rothman J.H.;
RT "Repression of cell-cell fusion by components of the C. elegans vacuolar
RT ATPase complex.";
RL Dev. Cell 8:787-794(2005).
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 (By similarity). During
CC embryonic development, the V-ATPase is required to repress fusion of
CC epidermal cells probably by negatively regulating eff-1-mediated cell
CC fusion (PubMed:15866168). {ECO:0000250|UniProtKB:Q2KIB5,
CC ECO:0000269|PubMed:15866168}.
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:Q2KIB5}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:15866168}; Multi-pass membrane protein
CC {ECO:0000255}. Note=In late stage embryos, localizes to the apical cell
CC membrane and partially to apical junctions of epidermal cells
CC (PubMed:15866168). In the gut of 1.5-fold embryo, localizes to puctate
CC structures (PubMed:15866168). {ECO:0000269|PubMed:15866168}.
CC -!- DEVELOPMENTAL STAGE: In the 1.5-fold embryo, expressed in gut cells but
CC not in epidermal cells (at protein level) (PubMed:15866168). In the 3-
CC fold embryo, expressed in dorsal and ventral epidermal cells, but not
CC in seam cells, and in the excretory cell (at protein level)
CC (PubMed:15866168). {ECO:0000269|PubMed:15866168}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes hyperfusion of
CC epidermal cells in embryos. {ECO:0000269|PubMed:15866168}.
CC -!- SIMILARITY: Belongs to the V-ATPase e1/e2 subunit family.
CC {ECO:0000305}.
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DR EMBL; BX284604; CAA92517.2; -; Genomic_DNA.
DR PIR; T22418; T22418.
DR RefSeq; NP_501636.2; NM_069235.6.
DR AlphaFoldDB; Q20591; -.
DR SMR; Q20591; -.
DR STRING; 6239.F49C12.13; -.
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; Q20591; -.
DR PaxDb; Q20591; -.
DR PeptideAtlas; Q20591; -.
DR EnsemblMetazoa; F49C12.13.1; F49C12.13.1; WBGene00009882.
DR GeneID; 177757; -.
DR KEGG; cel:CELE_F49C12.13; -.
DR UCSC; F49C12.13.1; c. elegans.
DR CTD; 177757; -.
DR WormBase; F49C12.13; CE37521; WBGene00009882; vha-17.
DR eggNOG; KOG3500; Eukaryota.
DR GeneTree; ENSGT00940000168530; -.
DR HOGENOM; CLU_170555_0_0_1; -.
DR InParanoid; Q20591; -.
DR OMA; AREWGNP; -.
DR OrthoDB; 1613627at2759; -.
DR PhylomeDB; Q20591; -.
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:Q20591; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00009882; Expressed in larva and 4 other tissues.
DR GO; GO:0043296; C:apical junction complex; 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:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0010172; P:embryonic body morphogenesis; IMP:WormBase.
DR GO; GO:0060142; P:regulation of syncytium formation by plasma membrane fusion; IMP:WormBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR InterPro; IPR008389; ATPase_V0-cplx_e1/e2_su.
DR InterPro; IPR017385; ATPase_V0-cplx_e1/e2_su_met.
DR PANTHER; PTHR12263; PTHR12263; 1.
DR Pfam; PF05493; ATP_synt_H; 1.
DR PIRSF; PIRSF038097; V-ATP_synth_e1/e2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..86
FT /note="V-type proton ATPase subunit e"
FT /id="PRO_0000071741"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 22..32
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 54..86
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MUTAGEN 52..86
FT /note="Missing: Causes hyperfusion of epidermal cells in
FT embryos."
FT /evidence="ECO:0000269|PubMed:15866168"
SQ SEQUENCE 86 AA; 9688 MW; 58A531B414318284 CRC64;
MGILIPLVSV SAFWAIIGFG GPWIVPKGPN RGIIQLMIIM TAVCCWMFWI MVFLHQLNPL
IGPQINVKTI RWISEKWGDA PNVINN
