ID   VATD_CAEBR              Reviewed;         259 AA.
AC   Q61IU3; A8XAB2;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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:0000250|UniProtKB:P34462};
GN   ORFNames=CBG10070 {ECO:0000312|WormBase:CBG10070};
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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. V-ATPase is responsible for acidifying and maintaining the pH
CC       of intracellular compartments and in some cell types, is targeted to
CC       the plasma membrane, where it is responsible for acidifying the
CC       extracellular environment. {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. 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, and The proton translocation complex
CC       V0 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:P39942}.
CC   -!- SIMILARITY: Belongs to the V-ATPase D subunit family. {ECO:0000255}.
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DR   EMBL; HE601459; CAP29580.3; -; Genomic_DNA.
DR   RefSeq; XP_002641731.1; XM_002641685.1.
DR   AlphaFoldDB; Q61IU3; -.
DR   SMR; Q61IU3; -.
DR   STRING; 6238.CBG10070; -.
DR   PRIDE; Q61IU3; -.
DR   EnsemblMetazoa; CBG10070.1; CBG10070.1; WBGene00031549.
DR   GeneID; 8583725; -.
DR   KEGG; cbr:CBG_10070; -.
DR   CTD; 8583725; -.
DR   WormBase; CBG10070; CBP08378; WBGene00031549; Cbr-vha-14.
DR   eggNOG; KOG1647; Eukaryota.
DR   HOGENOM; CLU_069688_0_0_1; -.
DR   InParanoid; Q61IU3; -.
DR   OMA; SKNIMGV; -.
DR   OrthoDB; 1313938at2759; -.
DR   Proteomes; UP000008549; Chromosome III.
DR   GO; GO:0033176; C:proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
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..259
FT                   /note="V-type proton ATPase subunit D"
FT                   /id="PRO_0000279719"
FT   REGION          214..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        214..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   259 AA;  29008 MW;  46EEC11DB5D21B0C CRC64;
     MSGGGGKDRI AVFPSRMAQT LMKTRLKGAQ KGHSLLKKKA DALNLRFRDI LKKIVENKVL
     MGEVMKEAAF SLAEAKFTAG DFSHTVIQNV SQAQYRVRMK KENVVGVLLP VFDAYQDGPD
     AYDLTGLGKG GANIARLKKN YNKAIELLVE LATLQTCFIT LDEAIKVTNR RVNAIEHVII
     PRIENTLTYI VTELDEMERE EFFRMKKIQA NKKKLKEQEA AQRALEGPPK EEAGGTHSEN
     QPPRNLLAVE EDNLPVLFN