VATE_CAEEL
ID VATE_CAEEL Reviewed; 226 AA.
AC Q95X44;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=V-type proton ATPase subunit E {ECO:0000305};
DE Short=V-ATPase subunit E {ECO:0000303|PubMed:12853134};
GN Name=vha-8 {ECO:0000303|PubMed:12853134, ECO:0000312|WormBase:C17H12.14};
GN ORFNames=C17H12.14 {ECO:0000312|WormBase:C17H12.14};
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|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 [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=12853134; DOI=10.1016/s0378-1119(03)00561-4;
RA Choi K.Y., Ji Y.J., Dhakal B.K., Yu J.R., Cho C., Song W.K., Ahnn J.;
RT "Vacuolar-type H+-ATPase E subunit is required for embryogenesis and yolk
RT transfer in Caenorhabditis elegans.";
RL Gene 311:13-23(2003).
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16684534; DOI=10.1016/j.febslet.2006.04.067;
RA Ji Y.J., Choi K.Y., Song H.O., Park B.J., Yu J.R., Kagawa H., Song W.K.,
RA Ahnn J.;
RT "VHA-8, the E subunit of V-ATPase, is essential for pH homeostasis and
RT larval development in C. elegans.";
RL FEBS Lett. 580:3161-3166(2006).
RN [4] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP 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).
CC -!- FUNCTION: Subunit of the V1 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). Regulates pH
CC homeostasis in the intestine (PubMed:16684534). Probably by regulating
CC cytoplasmic pH, required for cell survival in the intestine and
CC hypodermis (PubMed:16684534). Involved in receptor-mediated endocytosis
CC (PubMed:12853134, PubMed:16785323). Involved in embryogenesis and
CC larval development (PubMed:12853134, PubMed:16785323).
CC {ECO:0000250|UniProtKB:P11019, ECO:0000269|PubMed:12853134,
CC ECO:0000269|PubMed:16684534, ECO:0000269|PubMed:16785323}.
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:P11019}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12853134}. Apical
CC cell membrane {ECO:0000269|PubMed:12853134,
CC ECO:0000269|PubMed:16785323}; Peripheral membrane protein
CC {ECO:0000305}. Note=Localizes in clusters in the cytoplasm of the
CC excretory canal (PubMed:12853134). Colocalizes with vha-5 to stacked
CC sheets of the apical cell membrane of syncytial hypodermal cells
CC (PubMed:12853134, PubMed:16785323). {ECO:0000269|PubMed:12853134,
CC ECO:0000269|PubMed:16785323}.
CC -!- TISSUE SPECIFICITY: Expressed in the excretory cell and syncytial
CC hypodermal cells (at protein level) (PubMed:12853134, PubMed:16684534,
CC PubMed:16785323). Expressed in the intestine (at protein level)
CC (PubMed:16684534). {ECO:0000269|PubMed:12853134,
CC ECO:0000269|PubMed:16684534, ECO:0000269|PubMed:16785323}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults (at
CC protein level) (PubMed:12853134, PubMed:16684534). Expressed in the
CC excretory cell, intestine and hypodermis throughout all developmental
CC stages and in adults (at protein level) (PubMed:12853134,
CC PubMed:16684534). {ECO:0000269|PubMed:12853134,
CC ECO:0000269|PubMed:16684534}.
CC -!- DISRUPTION PHENOTYPE: Larvae are arrested at the L1 stage
CC (PubMed:16684534). Larvae exhibit swollen vacuoles in the hypodermis of
CC the head region, gradually spreading throughout the whole body
CC (PubMed:16684534). Pharyngeal pumping ceases at L2 larval stage with
CC many vacuoles covering the entire body (PubMed:16684534). Causes
CC necrotic cell death in intestine and hypodermis (PubMed:16684534).
CC RNAi-mediated knockdown causes sterility, formation of endomitotic
CC oocytes in the proximal gonads, and impaired ovulation
CC (PubMed:12853134). Diakinesis stage oocytes are displaced toward distal
CC gonads (PubMed:12853134). Impaired yolk uptake by the oocytes from the
CC pseudoceolomic cavities (PubMed:12853134, PubMed:16785323). Impaired
CC acidification and food digestion of the intestine (PubMed:16684534).
CC Causes an increase in the section of the excretory canal, which often
CC has multiple lumens and abnormal whorls (PubMed:16785323). Does not
CC affect alae formation in larvae (PubMed:16785323). Progeny is arrested
CC at the embryonic stage or at the L1 larval stage (PubMed:12853134,
CC PubMed:16785323). RNAi-mediated knockdown in embryos causes arrest at
CC the one-cell stage (PubMed:12853134). {ECO:0000269|PubMed:12853134,
CC ECO:0000269|PubMed:16684534, ECO:0000269|PubMed:16785323}.
CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. {ECO:0000305}.
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DR EMBL; BX284604; CCD65002.1; -; Genomic_DNA.
DR RefSeq; NP_501040.1; NM_068639.5.
DR AlphaFoldDB; Q95X44; -.
DR SMR; Q95X44; -.
DR DIP; DIP-24784N; -.
DR IntAct; Q95X44; 5.
DR STRING; 6239.C17H12.14; -.
DR TCDB; 3.A.2.2.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR World-2DPAGE; 0011:Q95X44; -.
DR World-2DPAGE; 0020:Q95X44; -.
DR EPD; Q95X44; -.
DR PaxDb; Q95X44; -.
DR PeptideAtlas; Q95X44; -.
DR EnsemblMetazoa; C17H12.14.1; C17H12.14.1; WBGene00006917.
DR GeneID; 177442; -.
DR KEGG; cel:CELE_C17H12.14; -.
DR UCSC; C17H12.14.1; c. elegans.
DR CTD; 177442; -.
DR WormBase; C17H12.14; CE19362; WBGene00006917; vha-8.
DR eggNOG; KOG1664; Eukaryota.
DR GeneTree; ENSGT00390000002730; -.
DR HOGENOM; CLU_073641_2_0_1; -.
DR InParanoid; Q95X44; -.
DR OMA; AIDTQYE; -.
DR OrthoDB; 1489718at2759; -.
DR PhylomeDB; Q95X44; -.
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:Q95X44; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006917; Expressed in larva and 4 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR GO; GO:0005886; C:plasma membrane; IDA:WormBase.
DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR Gene3D; 3.30.2320.30; -; 1.
DR HAMAP; MF_00311; ATP_synth_E_arch; 1.
DR InterPro; IPR038495; ATPase_E_C.
DR InterPro; IPR002842; ATPase_V1_Esu.
DR PANTHER; PTHR45715; PTHR45715; 1.
DR Pfam; PF01991; vATP-synt_E; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Ion transport; Membrane; Reference proteome;
KW Transport.
FT CHAIN 1..226
FT /note="V-type proton ATPase subunit E"
FT /id="PRO_0000454078"
SQ SEQUENCE 226 AA; 25586 MW; E7F68A74642EE1C8 CRC64;
MGISDNDVQK QLRHMMAFIE QEANEKAEEI DAKAEEEFNI EKGRLVQQQR QKIMEFFEKK
EKQVELQRKI QASNSLNAGR LRCLKAREDH IGAVLDEARS NLSRISGDAA RYPAILKGLV
MQGLLQLLEK EVVLRCREKD LRLVEQLLPE CLDGLQKEWG STTKVVLDKQ NFLPSESAGG
VELSARAGKI KVSSTLESRL ELIANQIVPQ VRTALFGPNP NRSFFD
