ID   VA0D1_DANRE             Reviewed;         350 AA.
AC   Q6PGV1;
DT   24-JUL-2013, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=V-type proton ATPase subunit d 1;
DE            Short=V-ATPase subunit d 1;
DE   AltName: Full=Vacuolar proton pump subunit d 1;
GN   Name=atp6v0d1; Synonyms=cto; ORFNames=zgc:63769;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=15256591; DOI=10.1073/pnas.0403929101;
RA   Amsterdam A., Nissen R.M., Sun Z., Swindell E.C., Farrington S.,
RA   Hopkins N.;
RT   "Identification of 315 genes essential for early zebrafish development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12792-12797(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION IN CILIOGENESIS.
RX   PubMed=21844891; DOI=10.1038/cr.2011.134;
RA   Chen Y., Wu B., Xu L., Li H., Xia J., Yin W., Li Z., Shi D., Li S., Lin S.,
RA   Shu X., Pei D.;
RT   "A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in vivo.";
RL   Cell Res. 22:333-345(2012).
CC   -!- FUNCTION: Subunit of the V0 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). May play a
CC       role in coupling of proton transport and ATP hydrolysis (By
CC       similarity). In aerobic conditions, involved in intracellular iron
CC       homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase
CC       (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent
CC       proteasomal degradation (By similarity). May play a role in cilium
CC       biogenesis through regulation of the transport and the localization of
CC       proteins to the cilium (PubMed:21844891).
CC       {ECO:0000250|UniProtKB:P51863, ECO:0000250|UniProtKB:P61421,
CC       ECO:0000269|PubMed:21844891}.
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 ATP6AP1/Ac45 and ATP6AP2/PRR (By
CC       similarity). {ECO:0000250|UniProtKB:P61421}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P61421};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P61421}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:P61421}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:P61421}. Note=Localizes to centrosome and the
CC       base of the cilium. {ECO:0000269|PubMed:21844891}.
CC   -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC       {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; CR356247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY648766; AAT68084.1; -; mRNA.
DR   EMBL; BC056822; AAH56822.1; -; mRNA.
DR   RefSeq; NP_955914.1; NM_199620.1.
DR   AlphaFoldDB; Q6PGV1; -.
DR   SMR; Q6PGV1; -.
DR   STRING; 7955.ENSDARP00000091027; -.
DR   PaxDb; Q6PGV1; -.
DR   PRIDE; Q6PGV1; -.
DR   Ensembl; ENSDART00000100254; ENSDARP00000091027; ENSDARG00000069090.
DR   Ensembl; ENSDART00000180216; ENSDARP00000157519; ENSDARG00000115876.
DR   GeneID; 322811; -.
DR   KEGG; dre:322811; -.
DR   CTD; 9114; -.
DR   ZFIN; ZDB-GENE-030131-1531; atp6v0d1.
DR   eggNOG; KOG2957; Eukaryota.
DR   GeneTree; ENSGT00390000002200; -.
DR   HOGENOM; CLU_051277_0_0_1; -.
DR   InParanoid; Q6PGV1; -.
DR   OMA; MLSRAED; -.
DR   OrthoDB; 910004at2759; -.
DR   PhylomeDB; Q6PGV1; -.
DR   TreeFam; TF300857; -.
DR   Reactome; R-DRE-1222556; ROS and RNS production in phagocytes.
DR   Reactome; R-DRE-77387; Insulin receptor recycling.
DR   Reactome; R-DRE-917977; Transferrin endocytosis and recycling.
DR   Reactome; R-DRE-9639288; Amino acids regulate mTORC1.
DR   Reactome; R-DRE-983712; Ion channel transport.
DR   PRO; PR:Q6PGV1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 7.
DR   Bgee; ENSDARG00000069090; Expressed in brain and 26 other tissues.
DR   ExpressionAtlas; Q6PGV1; baseline.
DR   GO; GO:0005769; C:early endosome; IBA:GO_Central.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro.
DR   GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; IBA:GO_Central.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR   GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
DR   GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0008057; P:eye pigment granule organization; IMP:ZFIN.
DR   GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR   GO; GO:0070986; P:left/right axis specification; IMP:UniProtKB.
DR   GO; GO:0032438; P:melanosome organization; IMP:ZFIN.
DR   GO; GO:0035675; P:neuromast hair cell development; IMP:ZFIN.
DR   GO; GO:0039022; P:pronephric duct development; IMP:ZFIN.
DR   GO; GO:0046688; P:response to copper ion; IMP:ZFIN.
DR   GO; GO:0060041; P:retina development in camera-type eye; IMP:ZFIN.
DR   GO; GO:0003406; P:retinal pigment epithelium development; IMP:ZFIN.
DR   GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central.
DR   GO; GO:0007034; P:vacuolar transport; IBA:GO_Central.
DR   Gene3D; 1.10.132.50; -; 1.
DR   Gene3D; 1.20.1690.10; -; 2.
DR   InterPro; IPR036079; ATPase_su_c/d_sf.
DR   InterPro; IPR002843; ATPase_V0-cplx_csu/dsu.
DR   InterPro; IPR016727; ATPase_V0-cplx_dsu.
DR   InterPro; IPR044911; V-type_ATPase_su_c/d_dom_3.
DR   InterPro; IPR035067; V-type_ATPase_suC/d.
DR   PANTHER; PTHR11028; PTHR11028; 1.
DR   Pfam; PF01992; vATP-synt_AC39; 1.
DR   PIRSF; PIRSF018497; V-ATP_synth_D; 1.
DR   SUPFAM; SSF103486; SSF103486; 1.
PE   1: Evidence at protein level;
KW   Cilium biogenesis/degradation; Hydrogen ion transport; Ion transport;
KW   Lysosome; Membrane; Reference proteome; Transport.
FT   CHAIN           1..350
FT                   /note="V-type proton ATPase subunit d 1"
FT                   /id="PRO_0000423049"
SQ   SEQUENCE   350 AA;  40191 MW;  44722068B54FA921 CRC64;
     MPFSELYFNV DNGYLEGLVR GFKAGILSQA DYLNLVQCET LEDLKLHLQS TDYGSFLANE
     ASPLTVSVID DKLKEKMVVE FRHMRNQSYE PLASFMDFIT YSYMIDNVIL LITGTLHQRA
     ISELVPKCHP LGSFEQMEAV NIAQTPAELY NAILVDTPLA AFFQDCISEQ DLDEMNIEII
     RNTLYKAYLE AFYKFCTTLG GTTADTMCPI LEFEADRRAF IITINSFGTE LSKEDRAKLF
     PHCGKLYPEG LAQLARADDY EQVKAVAEYY PEYKLLFEGA GSNPGDKTLE DRFFEHEVKL
     NKLAFLNQFH FSVFYAYVKL KEQECRNIVW IAECIAQRHR AKIDNYIPIF