VATO_CAEEL
ID VATO_CAEEL Reviewed; 214 AA.
AC G5EDB8;
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 21 kDa proteolipid subunit c'' {ECO:0000305};
DE Short=V-ATPase 21 kDa proteolipid subunit c'' {ECO:0000305};
GN Name=vha-4 {ECO:0000303|PubMed:9305897, ECO:0000312|WormBase:T01H3.1};
GN ORFNames=T01H3.1 {ECO:0000312|WormBase:T01H3.1};
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:BAA22597.1}
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=9305897;
RA Oka T., Yamamoto R., Futai M.;
RT "Three vha genes encode proteolipids of Caenorhabditis elegans vacuolar-
RT type ATPase. Gene structures and preferential expression in an H-shaped
RT excretory cell and rectal cells.";
RL J. Biol. Chem. 272:24387-24392(1997).
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, 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).
CC -!- FUNCTION: Proton-conducting pore forming of the V0 complex of
CC vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a
CC peripheral complex (V1) that hydrolyzes ATP and a membrane integral
CC complex (V0) that translocates protons (By similarity). V-ATPase is
CC responsible for acidifying and maintaining the pH of intracellular
CC compartments and in some cell types, is targeted to the plasma
CC membrane, where it is responsible for acidifying the extracellular
CC environment (By similarity). The V-ATPase is required for the function
CC of the excretory canal (PubMed:16785323). Involved in receptor-mediated
CC endocytosis (PubMed:16785323). {ECO:0000250|UniProtKB:Q2TA24,
CC 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 (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:Q2TA24}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the H-shaped excretory cell, rectum,
CC and a pair of cells posterior to the anus.
CC {ECO:0000269|PubMed:9305897}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes embryonic
CC lethality (PubMed:16785323). Causes defects in alae formation in the
CC few surviving larvae and impairs yolk uptake by the oocytes from the
CC pseudoceolomic cavities (PubMed:16785323). Causes an increase in the
CC section of the excretory canal, which often has multiple lumens and
CC abnormal whorls (PubMed:16785323). {ECO:0000269|PubMed:16785323}.
CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family.
CC {ECO:0000305}.
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DR EMBL; AB000919; BAA22597.1; -; mRNA.
DR EMBL; BX284602; CAA92686.1; -; Genomic_DNA.
DR PIR; T37237; T37237.
DR RefSeq; NP_495659.1; NM_063258.6.
DR AlphaFoldDB; G5EDB8; -.
DR SMR; G5EDB8; -.
DR IntAct; G5EDB8; 1.
DR STRING; 6239.T01H3.1.1; -.
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; G5EDB8; -.
DR PaxDb; G5EDB8; -.
DR PeptideAtlas; G5EDB8; -.
DR EnsemblMetazoa; T01H3.1.1; T01H3.1.1; WBGene00006913.
DR GeneID; 174272; -.
DR KEGG; cel:CELE_T01H3.1; -.
DR CTD; 174272; -.
DR WormBase; T01H3.1; CE03595; WBGene00006913; vha-4.
DR eggNOG; KOG0233; Eukaryota.
DR GeneTree; ENSGT00550000075120; -.
DR HOGENOM; CLU_085752_0_1_1; -.
DR InParanoid; G5EDB8; -.
DR OMA; PYAWAST; -.
DR OrthoDB; 1408246at2759; -.
DR PhylomeDB; G5EDB8; -.
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 Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006913; Expressed in larva and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0033177; C:proton-transporting two-sector ATPase complex, proton-transporting domain; IEA:InterPro.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR Gene3D; 1.20.120.610; -; 1.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR Pfam; PF00137; ATP-synt_C; 2.
DR SUPFAM; SSF81333; SSF81333; 2.
PE 2: Evidence at transcript level;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..214
FT /note="V-type proton ATPase 21 kDa proteolipid subunit c''"
FT /id="PRO_0000454080"
FT TOPO_DOM 1..9
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..93
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 94..114
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 115..144
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..183
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..214
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT SITE 100
FT /note="Essential for proton translocation"
FT /evidence="ECO:0000250|UniProtKB:Q2TA24"
SQ SEQUENCE 214 AA; 22108 MW; 597D13E55416AEA8 CRC64;
MAAGAILKTT ATLTVITTLI ILGTGLFYML SGQGHRFDIG WFLTSTSPHM WAGLGIGFSL
SLSVLGAGWG IFTTGSSILG GGVKAPRIRT KNLVSIIFCE AVAIFGIIMA FVFVGKLAEF
RREDLPDTED GMAILARNLA SGYMIFGGGL TVGLSNLVCG LAVGIVGSGA AIADAANPAL
FVKILIIEIF ASAIGLFGMI IGIVQTNKAS FGNK
