VA0D1_MOUSE
ID VA0D1_MOUSE Reviewed; 351 AA.
AC P51863; Q54A57; Q9QWJ2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=V-type proton ATPase subunit d 1;
DE Short=V-ATPase subunit d 1;
DE AltName: Full=P39;
DE AltName: Full=Physophilin;
DE AltName: Full=V-ATPase 40 kDa accessory protein;
DE AltName: Full=V-ATPase AC39 subunit;
DE AltName: Full=Vacuolar proton pump subunit d 1;
GN Name=Atp6v0d1 {ECO:0000312|MGI:MGI:1201778}; Synonyms=Atp6d;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Howell M.L., Dean G.E.;
RT "cDNA sequences for mouse vacuolar ATPase subunits.";
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=9753184; DOI=10.1046/j.1460-9568.1998.00130.x;
RA Carrion-Vazquez M., Fernandez A.M., Chowen J., Nieto-Sampedro M.;
RT "Brain Ac39/physophilin: cloning, coexpression and colocalization with
RT synaptophysin.";
RL Eur. J. Neurosci. 10:1153-1166(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12527205; DOI=10.1016/s0378-1119(02)01099-5;
RA Sun-Wada G.-H., Yoshimizu T., Imai-Senga Y., Wada Y., Futai M.;
RT "Diversity of mouse proton-translocating ATPase: presence of multiple
RT isoforms of the C, d and G subunits.";
RL Gene 302:147-153(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP PROTEIN SEQUENCE OF 25-73; 87-128; 188-237; 240-288; 294-300; 304-320;
RP 328-339 AND 344-351, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12963731; DOI=10.1074/jbc.m303924200;
RA Nishi T., Kawasaki-Nishi S., Forgac M.;
RT "Expression and function of the mouse V-ATPase d subunit isoforms.";
RL J. Biol. Chem. 278:46396-46402(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-270, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH PIP4P1.
RX PubMed=29644770; DOI=10.1111/gtc.12583;
RA Hashimoto Y., Shirane M., Nakayama K.I.;
RT "TMEM55B contributes to lysosomal homeostasis and amino acid-induced mTORC1
RT activation.";
RL Genes Cells 23:418-434(2018).
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 (PubMed:12963731). V-ATPase is responsible for acidifying a
CC variety of intracellular compartments in eukaryotic cells, thus
CC providing most of the energy required for transport processes in the
CC vacuolar system (By similarity). May play a role in coupling of proton
CC transport and ATP hydrolysis (PubMed:12963731). In aerobic conditions,
CC involved in intracellular iron homeostasis, thus triggering the
CC activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to
CC HIF1A hydroxylation and subsequent proteasomal degradation (By
CC similarity). May play a role in cilium biogenesis through regulation of
CC the transport and the localization of proteins to the cilium (By
CC similarity). {ECO:0000250|UniProtKB:P61421,
CC ECO:0000250|UniProtKB:Q6PGV1, ECO:0000269|PubMed:12963731}.
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). Interacts with ATP6AP2; ATP6AP2 is a V-ATPase accessory
CC protein and the interaction promotes v-ATPase complex assembly (By
CC similarity). Interacts with TMEM9; TMEM9 is a v-ATPase assembly
CC regulator and the interaction induces the interaction with ATP6AP2 (By
CC similarity). Interacts with PIP4P1 (PubMed:29644770).
CC {ECO:0000250|UniProtKB:P61421, ECO:0000269|PubMed:29644770}.
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}; Peripheral membrane protein
CC {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle membrane
CC {ECO:0000250|UniProtKB:P61420}; Peripheral membrane protein
CC {ECO:0000305}. Note=Localizes to centrosome and the base of the cilium.
CC {ECO:0000250|UniProtKB:Q6PGV1}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12527205,
CC ECO:0000269|PubMed:12963731}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout early development.
CC {ECO:0000269|PubMed:12963731}.
CC -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family.
CC {ECO:0000305}.
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DR EMBL; U13840; AAC83085.1; -; mRNA.
DR EMBL; U21549; AAA92288.1; -; mRNA.
DR EMBL; AB088408; BAC57954.1; -; mRNA.
DR EMBL; AK083372; BAC38889.1; -; mRNA.
DR EMBL; AK171515; BAE42500.1; -; mRNA.
DR CCDS; CCDS22604.1; -.
DR RefSeq; NP_038505.2; NM_013477.3.
DR AlphaFoldDB; P51863; -.
DR SMR; P51863; -.
DR BioGRID; 198264; 11.
DR IntAct; P51863; 10.
DR MINT; P51863; -.
DR STRING; 10090.ENSMUSP00000013304; -.
DR TCDB; 3.A.2.2.6; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR iPTMnet; P51863; -.
DR PhosphoSitePlus; P51863; -.
DR SwissPalm; P51863; -.
DR EPD; P51863; -.
DR jPOST; P51863; -.
DR MaxQB; P51863; -.
DR PaxDb; P51863; -.
DR PeptideAtlas; P51863; -.
DR PRIDE; P51863; -.
DR ProteomicsDB; 297905; -.
DR Antibodypedia; 2185; 198 antibodies from 26 providers.
DR DNASU; 11972; -.
DR Ensembl; ENSMUST00000013304; ENSMUSP00000013304; ENSMUSG00000013160.
DR GeneID; 11972; -.
DR KEGG; mmu:11972; -.
DR UCSC; uc009ndg.1; mouse.
DR CTD; 9114; -.
DR MGI; MGI:1201778; Atp6v0d1.
DR VEuPathDB; HostDB:ENSMUSG00000013160; -.
DR eggNOG; KOG2957; Eukaryota.
DR GeneTree; ENSGT00390000002200; -.
DR HOGENOM; CLU_051277_0_0_1; -.
DR InParanoid; P51863; -.
DR OMA; MLSRAED; -.
DR OrthoDB; 910004at2759; -.
DR PhylomeDB; P51863; -.
DR TreeFam; TF300857; -.
DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-MMU-77387; Insulin receptor recycling.
DR Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
DR Reactome; R-MMU-9639288; Amino acids regulate mTORC1.
DR Reactome; R-MMU-983712; Ion channel transport.
DR BioGRID-ORCS; 11972; 27 hits in 75 CRISPR screens.
DR ChiTaRS; Atp6v0d1; mouse.
DR PRO; PR:P51863; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P51863; protein.
DR Bgee; ENSMUSG00000013160; Expressed in facial nucleus and 268 other tissues.
DR Genevisible; P51863; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0033181; C:plasma membrane proton-transporting V-type ATPase complex; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; ISO:MGI.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IDA:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
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; ISS:UniProtKB.
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; Cytoplasmic vesicle;
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Lysosome;
KW Membrane; Phosphoprotein; Reference proteome; Transport.
FT CHAIN 1..351
FT /note="V-type proton ATPase subunit d 1"
FT /id="PRO_0000119351"
FT MOD_RES 270
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 23
FT /note="L -> M (in Ref. 1; AAC83085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 40301 MW; 62CDF67B982124C9 CRC64;
MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN
EASPLTVSVI DDKLKEKMVV EFRHMRNHAY EPLASFLDFI TYSYMIDNVI LLITGTLHQR
SIAELVPKCH PLGSFEQMEA VNIAQTPAEL YNAILVDTPL AAFFQDCISE QDLDEMNIEI
IRNTLYKAYL ESFYKFCTLL GGTTADAMCP ILEFEADRRA FIITINSFGT ELSKEDRAKL
FPHCGRLYPE GLAQLARADD YEQVKNVADY YPEYKLLFEG AGSNPGDKTL EDRFFEHEVK
LNKLAFLNQF HFGVFYAFVK LKEQECRNIV WIAECIAQRH RAKIDNYIPI F
