VATD_MOUSE
ID VATD_MOUSE Reviewed; 247 AA.
AC P57746;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=V-type proton ATPase subunit D;
DE Short=V-ATPase subunit D;
DE AltName: Full=V-ATPase 28 kDa accessory protein;
DE AltName: Full=Vacuolar proton pump subunit D;
GN Name=Atp6v1d; Synonyms=Atp6m, Vatd;
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].
RC STRAIN=C57BL/6J;
RX PubMed=11435709; DOI=10.1159/000056924;
RA Kennell J.A., Richards N.W., Schaner P.E., Gumucio D.L.;
RT "cDNA cloning, chromosomal localization and evolutionary analysis of mouse
RT vacuolar ATPase subunit D, Atp6m.";
RL Cytogenet. Cell Genet. 92:337-341(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 7-13; 64-89 AND 183-194, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP IDENTIFICATION BY 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).
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). May play a
CC role in cilium biogenesis through regulation of the transport and the
CC localization of proteins to the cilium (By similarity).
CC {ECO:0000250|UniProtKB:P39942, ECO:0000250|UniProtKB:Q9Y5K8}.
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 SNX10 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y5K8}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Y5K8};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Y5K8}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q9Y5K8}. Cytoplasmic vesicle, clathrin-
CC coated vesicle membrane {ECO:0000250|UniProtKB:P39942}; Peripheral
CC membrane protein {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y5K8}. Cell
CC projection, cilium {ECO:0000250|UniProtKB:Q9Y5K8}. Note=Localizes to
CC centrosome and the base of the cilium. {ECO:0000250|UniProtKB:Q9Y5K8}.
CC -!- SIMILARITY: Belongs to the V-ATPase D subunit family. {ECO:0000305}.
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DR EMBL; AF298810; AAG30225.1; -; mRNA.
DR EMBL; BC033457; AAH33457.1; -; mRNA.
DR CCDS; CCDS26002.1; -.
DR RefSeq; NP_076210.1; NM_023721.2.
DR AlphaFoldDB; P57746; -.
DR SMR; P57746; -.
DR BioGRID; 216291; 12.
DR IntAct; P57746; 3.
DR MINT; P57746; -.
DR STRING; 10090.ENSMUSP00000021536; -.
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; P57746; -.
DR PhosphoSitePlus; P57746; -.
DR EPD; P57746; -.
DR jPOST; P57746; -.
DR PaxDb; P57746; -.
DR PeptideAtlas; P57746; -.
DR PRIDE; P57746; -.
DR ProteomicsDB; 297573; -.
DR Antibodypedia; 24797; 104 antibodies from 30 providers.
DR DNASU; 73834; -.
DR Ensembl; ENSMUST00000021536; ENSMUSP00000021536; ENSMUSG00000021114.
DR GeneID; 73834; -.
DR KEGG; mmu:73834; -.
DR UCSC; uc007nzj.1; mouse.
DR CTD; 51382; -.
DR MGI; MGI:1921084; Atp6v1d.
DR VEuPathDB; HostDB:ENSMUSG00000021114; -.
DR eggNOG; KOG1647; Eukaryota.
DR GeneTree; ENSGT00390000010770; -.
DR HOGENOM; CLU_069688_0_0_1; -.
DR InParanoid; P57746; -.
DR OMA; SKNIMGV; -.
DR OrthoDB; 1313938at2759; -.
DR PhylomeDB; P57746; -.
DR TreeFam; TF300160; -.
DR Reactome; R-MMU-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
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; 73834; 21 hits in 71 CRISPR screens.
DR ChiTaRS; Atp6v1d; mouse.
DR PRO; PR:P57746; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P57746; protein.
DR Bgee; ENSMUSG00000021114; Expressed in motor neuron and 272 other tissues.
DR ExpressionAtlas; P57746; baseline and differential.
DR Genevisible; P57746; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0033176; C:proton-transporting V-type ATPase complex; ISO:MGI.
DR GO; GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; ISS:UniProtKB.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0061512; P:protein localization to cilium; ISS:UniProtKB.
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 1: Evidence at protein level;
KW Cell projection; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing;
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transport.
FT CHAIN 1..247
FT /note="V-type proton ATPase subunit D"
FT /id="PRO_0000144232"
SQ SEQUENCE 247 AA; 28369 MW; 375C7EB2A03E8B08 CRC64;
MSGKDRIEIF PSRMAQTIMK ARLKGAQTGR NLLKKKSDAL TLRFRQILKK IIETKMLMGE
VMREAAFSLA EAKFTAGDFS TTVIQNVNKA QVKIRAKKDN VAGVTLPVFE HYHEGTDSYE
LTGLARGGEQ LAKLKRNYAK AVELLVELAS LQTSFVTLDE AIKITNRRVN AIEHVIIPRI
ERTLAYIITE LDEREREEFY RLKKIQEKKK IIKEKFEKDL ERRRAAGEVM EPANLLAEEK
DEDLLFE
