ID   VATD_CAEEL              Reviewed;         257 AA.
AC   P34462;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=V-type proton ATPase subunit D;
DE            Short=V-ATPase subunit D;
DE   AltName: Full=Vacuolar proton pump subunit D;
GN   Name=vha-14 {ECO:0000312|WormBase:F55H2.2};
GN   ORFNames=F55H2.2 {ECO:0000312|WormBase:F55H2.2};
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=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [2]
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).
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).
CC       {ECO:0000250|UniProtKB:P39942}.
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:P39942}.
CC   -!- SIMILARITY: Belongs to the V-ATPase D subunit family. {ECO:0000305}.
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; BX284603; CAA81600.1; -; Genomic_DNA.
DR   PIR; S40985; S40985.
DR   RefSeq; NP_499094.1; NM_066693.4.
DR   AlphaFoldDB; P34462; -.
DR   SMR; P34462; -.
DR   BioGRID; 41535; 17.
DR   STRING; 6239.F55H2.2.2; -.
DR   TCDB; 3.A.2.2.7; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   iPTMnet; P34462; -.
DR   EPD; P34462; -.
DR   PaxDb; P34462; -.
DR   PeptideAtlas; P34462; -.
DR   EnsemblMetazoa; F55H2.2.1; F55H2.2.1; WBGene00010130.
DR   GeneID; 176338; -.
DR   KEGG; cel:CELE_F55H2.2; -.
DR   UCSC; F55H2.2.1; c. elegans.
DR   CTD; 176338; -.
DR   WormBase; F55H2.2; CE00209; WBGene00010130; vha-14.
DR   eggNOG; KOG1647; Eukaryota.
DR   GeneTree; ENSGT00390000010770; -.
DR   HOGENOM; CLU_069688_0_0_1; -.
DR   InParanoid; P34462; -.
DR   OMA; SKNIMGV; -.
DR   OrthoDB; 1313938at2759; -.
DR   PhylomeDB; P34462; -.
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   PRO; PR:P34462; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00010130; Expressed in larva and 4 other tissues.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; ISS:WormBase.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0051453; P:regulation of intracellular pH; IC:WormBase.
DR   InterPro; IPR002699; V_ATPase_D.
DR   PANTHER; PTHR11671; PTHR11671; 1.
DR   Pfam; PF01813; ATP-synt_D; 1.
DR   TIGRFAMs; TIGR00309; V_ATPase_subD; 1.
PE   3: Inferred from homology;
KW   Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT   CHAIN           1..257
FT                   /note="V-type proton ATPase subunit D"
FT                   /id="PRO_0000144235"
FT   REGION          215..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   257 AA;  28786 MW;  107B2538866BF26B CRC64;
     MSGGGKDRIA VFPSRMAQTL MKTRLKGAQK GHSLLKKKAD ALNLRFRDIL RKIVENKVLM
     GEVMKEAAFS LAEAKFTAGD FSHTVIQNVS QAQYRVRMKK ENVVGVFLPV FDAYQDGPDA
     YDLTGLGKGG ANIARLKKNY NKAIELLVEL ATLQTCFITL DEAIKVTNRR VNAIEHVIIP
     RIENTLTYIV TELDEMEREE FFRMKKIQAN KKKLKEQEAA QKALEGPGPG EDAAHSENNP
     PRNLLASEED NLPVLFN