VA0D2_MOUSE
ID VA0D2_MOUSE Reviewed; 350 AA.
AC Q80SY3; Q3TDQ6; Q5I0V5; Q8BTL3; Q8BW16;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=V-type proton ATPase subunit d 2;
DE Short=V-ATPase subunit d 2;
DE AltName: Full=Osteoclast-specific vacuolar ATP synthase;
DE AltName: Full=Vacuolar proton pump subunit d 2;
GN Name=Atp6v0d2;
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], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=C57BL/6J;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=17128270; DOI=10.1038/nm1514;
RA Lee S.-H., Rho J., Jeong D., Sul J.-Y., Kim T., Kim N., Kang J.-S.,
RA Miyamoto T., Suda T., Lee S.K., Pignolo R.J., Koczon-Jaremko B.,
RA Lorenzo J., Choi Y.;
RT "v-ATPase V0 subunit d2-deficient mice exhibit impaired osteoclast fusion
RT and increased bone formation.";
RL Nat. Med. 12:1403-1409(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Molar;
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).
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. 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 (By similarity). May play a role in coupling
CC of proton transport and ATP hydrolysis (PubMed:12963731). Regulator of
CC osteoclast fusion and bone formation (PubMed:17128270).
CC {ECO:0000250|UniProtKB:P61421, ECO:0000269|PubMed:12963731,
CC ECO:0000269|PubMed:17128270}.
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, subunits e and f, and the accessory
CC subunits ATP6AP1/Ac45 and ATP6AP2/PRR. {ECO:0000250|UniProtKB:P61421}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the kidney. Also
CC expressed in the lung, testis, skeletal muscle and heart. Upr-egulated
CC during osteoclast differentiation and is most abundant in mature
CC osteoclasts. {ECO:0000269|PubMed:12527205, ECO:0000269|PubMed:12963731,
CC ECO:0000269|PubMed:17128270}.
CC -!- DEVELOPMENTAL STAGE: Strongly expressed at day 7 followed by a
CC disappearance and a gradual recovery to original levels by day 17.
CC {ECO:0000269|PubMed:12963731}.
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; AY145896; AAN61104.1; -; mRNA.
DR EMBL; AB088358; BAC57951.1; -; mRNA.
DR EMBL; AY517482; AAR99405.1; -; mRNA.
DR EMBL; AK075745; BAC35925.1; -; mRNA.
DR EMBL; AK089507; BAC40907.1; -; mRNA.
DR EMBL; AK170072; BAE41545.1; -; mRNA.
DR EMBL; AK170405; BAE41772.1; -; mRNA.
DR EMBL; AK170578; BAE41890.1; -; mRNA.
DR EMBL; AK170659; BAE41942.1; -; mRNA.
DR EMBL; AL732527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL773599; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC087899; AAH87899.1; -; mRNA.
DR CCDS; CCDS17994.1; -.
DR RefSeq; NP_780615.2; NM_175406.3.
DR AlphaFoldDB; Q80SY3; -.
DR SMR; Q80SY3; -.
DR BioGRID; 232395; 5.
DR STRING; 10090.ENSMUSP00000029900; -.
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; Q80SY3; -.
DR PhosphoSitePlus; Q80SY3; -.
DR jPOST; Q80SY3; -.
DR MaxQB; Q80SY3; -.
DR PaxDb; Q80SY3; -.
DR PeptideAtlas; Q80SY3; -.
DR PRIDE; Q80SY3; -.
DR ProteomicsDB; 297906; -.
DR Antibodypedia; 25450; 123 antibodies from 24 providers.
DR DNASU; 242341; -.
DR Ensembl; ENSMUST00000029900; ENSMUSP00000029900; ENSMUSG00000028238.
DR GeneID; 242341; -.
DR KEGG; mmu:242341; -.
DR UCSC; uc008sch.2; mouse.
DR CTD; 245972; -.
DR MGI; MGI:1924415; Atp6v0d2.
DR VEuPathDB; HostDB:ENSMUSG00000028238; -.
DR eggNOG; KOG2957; Eukaryota.
DR GeneTree; ENSGT00390000002200; -.
DR HOGENOM; CLU_051277_0_0_1; -.
DR InParanoid; Q80SY3; -.
DR OMA; FCKDHGD; -.
DR OrthoDB; 910004at2759; -.
DR PhylomeDB; Q80SY3; -.
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; 242341; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Atp6v0d2; mouse.
DR PRO; PR:Q80SY3; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80SY3; protein.
DR Bgee; ENSMUSG00000028238; Expressed in lumbar dorsal root ganglion and 60 other tissues.
DR ExpressionAtlas; Q80SY3; baseline and differential.
DR Genevisible; Q80SY3; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; IDA:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
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 2: Evidence at transcript level;
KW Hydrogen ion transport; Ion transport; Reference proteome; Transport.
FT CHAIN 1..350
FT /note="V-type proton ATPase subunit d 2"
FT /id="PRO_0000285658"
FT CONFLICT 309
FT /note="F -> L (in Ref. 1; AAN61104 and 2; BAC57951)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="Y -> C (in Ref. 4; BAE41545)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="E -> G (in Ref. 6; AAH87899)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 350 AA; 40494 MW; 5CC9BC9D2870943D CRC64;
MLETAELYFN VDHGYLEGLV RGCKASLLTQ QDYVNLVQCE TLEDLKIHLQ TTDYGNFLAN
ETNPLTVSKI DTEMRKKLCR EFDYFRNHSL EPLSTFLTYM TCSYMIDNII LLMNGALQKK
SVKEVLAKCH PLGRFTEMEA VNIAETPSDL FKAVLVETPL APFFQDCMSE NTLDELNIEL
LRNKLYKSYL EAFYKFCKDH GDVTADVMCP ILEFEADRRA LIITLNSFGT ELSKEDRETL
FPTCGRLYPE GLRLLAQAED FEQMKRVADN YGVYKPLFDA VGGSGGKTLE DVFYEREVQM
NVLAFNRQFH YGVFYAYVKL KEQEMRNIVW IAECISQRHR TKINSYIPIL
