VATC_CAEEL
ID VATC_CAEEL Reviewed; 384 AA.
AC Q9XXU9; Q869J4; Q9N421;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=V-type proton ATPase subunit C;
DE Short=V-ATPase subunit C;
DE AltName: Full=Vacuolar proton pump subunit C;
GN Name=vha-11 {ECO:0000312|WormBase:Y38F2AL.3a};
GN ORFNames=Y38F2AL.3 {ECO:0000312|WormBase:Y38F2AL.3a};
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 [MRNA] (ISOFORM A), FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9712884; DOI=10.1074/jbc.273.35.22570;
RA Oka T., Yamamoto R., Futai M.;
RT "Multiple genes for vacuolar-type ATPase proteolipids in Caenorhabditis
RT elegans: a new gene, vha-3, has a distinct cell-specific distribution.";
RL J. Biol. Chem. 273:22570-22576(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
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 [3]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10846178; DOI=10.1074/jbc.m002756200;
RA Oka T., Futai M.;
RT "Requirement of V-ATPase for ovulation and embryogenesis in Caenorhabditis
RT elegans.";
RL J. Biol. Chem. 275:29556-29561(2000).
RN [4]
RP INTERACTION WITH VHA-5; VHA-6 AND UNC-32, AND SUBCELLULAR LOCATION.
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).
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 (Probable). 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). Subunit C is
CC necessary for the assembly of the catalytic sector of the enzyme and is
CC likely to have a specific function in its catalytic activity (By
CC similarity). Has roles in embryogenesis and ovulation
CC (PubMed:10846178). {ECO:0000250|UniProtKB:P21282,
CC ECO:0000250|UniProtKB:P31412, ECO:0000269|PubMed:10846178,
CC ECO:0000305|PubMed:9712884}.
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 subunits a1 unc-32, a2 vha-5 and a3
CC vha-6 (PubMed:11441002). {ECO:0000250|UniProtKB:P21282,
CC ECO:0000269|PubMed:11441002}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10846178}. Membrane
CC {ECO:0000269|PubMed:11441002}; Peripheral membrane protein
CC {ECO:0000305}. Note=In embryonic cells, detected in dot-like structures
CC in the cytoplasm around the nuclei. {ECO:0000269|PubMed:10846178}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:Y38F2AL.3a};
CC IsoId=Q9XXU9-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:Y38F2AL.3b};
CC IsoId=Q9XXU9-2; Sequence=VSP_023136, VSP_023137;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously; higher levels are found in
CC gastrointestinal and hypodermal cells, as well as H-shaped excretory
CC cell. {ECO:0000269|PubMed:10846178, ECO:0000269|PubMed:9712884}.
CC -!- DISRUPTION PHENOTYPE: Worms display embryonic lethality. When vha-11 is
CC silenced in adults, they are able to produce eggs but egg numbers
CC gradually decrease and worms become sterile after 24 hours. This
CC sterility continues for about 4 days and then viable eggs are produced
CC again. {ECO:0000269|PubMed:10846178}.
CC -!- MISCELLANEOUS: Vha-11 and vha-3 are transcribed on a dicistronic
CC transcript where vha-3 is the upstream transcript and vha-11 the
CC downstream.
CC -!- SIMILARITY: Belongs to the V-ATPase C subunit family. {ECO:0000305}.
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DR EMBL; AB009567; BAA75067.1; -; mRNA.
DR EMBL; BX284604; CCD66967.1; -; Genomic_DNA.
DR EMBL; BX284604; CCD66968.1; -; Genomic_DNA.
DR PIR; T37271; T37271.
DR RefSeq; NP_001023451.1; NM_001028280.3. [Q9XXU9-1]
DR RefSeq; NP_001023452.1; NM_001028281.3.
DR AlphaFoldDB; Q9XXU9; -.
DR SMR; Q9XXU9; -.
DR BioGRID; 42169; 21.
DR STRING; 6239.Y38F2AL.3a; -.
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; Q9XXU9; -.
DR PaxDb; Q9XXU9; -.
DR PeptideAtlas; Q9XXU9; -.
DR PRIDE; Q9XXU9; -.
DR EnsemblMetazoa; Y38F2AL.3a.1; Y38F2AL.3a.1; WBGene00006920. [Q9XXU9-1]
DR EnsemblMetazoa; Y38F2AL.3b.1; Y38F2AL.3b.1; WBGene00006920. [Q9XXU9-2]
DR GeneID; 177017; -.
DR KEGG; cel:CELE_Y38F2AL.3; -.
DR UCSC; Y38F2AL.3a; c. elegans. [Q9XXU9-1]
DR CTD; 177017; -.
DR WormBase; Y38F2AL.3a; CE29997; WBGene00006920; vha-11. [Q9XXU9-1]
DR WormBase; Y38F2AL.3b; CE38743; WBGene00006920; vha-11. [Q9XXU9-2]
DR eggNOG; KOG2909; Eukaryota.
DR GeneTree; ENSGT00390000004263; -.
DR HOGENOM; CLU_017554_3_0_1; -.
DR InParanoid; Q9XXU9; -.
DR OMA; GEYWLIS; -.
DR OrthoDB; 1016088at2759; -.
DR PhylomeDB; Q9XXU9; -.
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:Q9XXU9; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00006920; Expressed in larva and 4 other tissues.
DR GO; GO:0043229; C:intracellular organelle; IDA:WormBase.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; NAS:UniProtKB.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; NAS:UniProtKB.
DR GO; GO:0015078; F:proton transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0030728; P:ovulation; IMP:UniProtKB.
DR CDD; cd14785; V-ATPase_C; 1.
DR InterPro; IPR004907; ATPase_V1-cplx_csu.
DR InterPro; IPR036132; Vac_ATP_synth_c_sf.
DR PANTHER; PTHR10137; PTHR10137; 1.
DR Pfam; PF03223; V-ATPase_C; 1.
DR SUPFAM; SSF118203; SSF118203; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transport.
FT CHAIN 1..384
FT /note="V-type proton ATPase subunit C"
FT /id="PRO_0000209351"
FT VAR_SEQ 98..133
FT /note="KDMKTYVTKFQWEGAKYPLKQSLKVLSEIIGKQISQ -> RHEDVRDEIPMG
FT RCQISTETIVESAQRDYWQTNQPD (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_023136"
FT VAR_SEQ 134..384
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_023137"
SQ SEQUENCE 384 AA; 43459 MW; FFAC0A9076BEBD42 CRC64;
MSSATSGEYW LISVPGEKGA NDAWDKLNRS TGNTSTNSKY LIPDLKVGTL DQLVGLSDDL
SKLDTSAEAV IRKLVQYFTE VLEEDKSKIA ENLVIGNKDM KTYVTKFQWE GAKYPLKQSL
KVLSEIIGKQ ISQIDNDLKV KSLTYNNLKN ALASMDRKTV GSLLTKDLAD LVKADDFVLN
SEYLQTVIVV VPKISVKEWE QKYATLSSMV VPGSSKLLTE EGEHALYTVT LFKKVIDEFK
NTARENKFIV RDFVYDEETL KAGRTERDKL MAEKQRQYAP LIRWLKINFG EIFAAYIHIK
ALRVFVESVL RYGLPVNFQA AVIEPAKGQQ KKLRQELHKL YIHLDGSAAG PIDTLEDSPA
LMSLGVNEYY PYVFFKLNID FLNK
