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Protein

V-type proton ATPase subunit d 2

Gene

Atp6v0d2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). May play a role in coupling of proton transport and ATP hydrolysis. Regulator of osteoclast fusion and bone formation.By similarity2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-MMU-77387. Insulin receptor recycling.
R-MMU-917977. Transferrin endocytosis and recycling.
R-MMU-983712. Ion channel transport.

Protein family/group databases

TCDBi3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase subunit d 2
Short name:
V-ATPase subunit d 2
Alternative name(s):
Osteoclast-specific vacuolar ATP synthase
Vacuolar proton pump subunit d 2
Gene namesi
Name:Atp6v0d2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1924415. Atp6v0d2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350V-type proton ATPase subunit d 2PRO_0000285658Add
BLAST

Proteomic databases

MaxQBiQ80SY3.
PaxDbiQ80SY3.
PRIDEiQ80SY3.

PTM databases

PhosphoSiteiQ80SY3.

Expressioni

Tissue specificityi

Predominantly expressed in the kidney. Also expressed in the lung, testis, skeletal muscle and heart. Upr-egulated during osteoclast differentiation and is most abundant in mature osteoclasts.3 Publications

Developmental stagei

Strongly expressed at day 7 followed by a disappearance and a gradual recovery to original levels by day 17.1 Publication

Gene expression databases

BgeeiQ80SY3.
CleanExiMM_ATP6V0D2.
ExpressionAtlasiQ80SY3. baseline and differential.
GenevisibleiQ80SY3. MM.

Interactioni

Subunit structurei

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d).

Protein-protein interaction databases

BioGridi232395. 2 interactions.
STRINGi10090.ENSMUSP00000029900.

Structurei

3D structure databases

ProteinModelPortaliQ80SY3.
SMRiQ80SY3. Positions 7-349.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the V-ATPase V0D/AC39 subunit family.Curated

Phylogenomic databases

eggNOGiKOG2957. Eukaryota.
COG1527. LUCA.
GeneTreeiENSGT00390000002200.
HOGENOMiHOG000199065.
HOVERGENiHBG018065.
InParanoidiQ80SY3.
KOiK02146.
OMAiRETLFPT.
OrthoDBiEOG7KH9JT.
PhylomeDBiQ80SY3.
TreeFamiTF300857.

Family and domain databases

InterProiIPR002843. ATPase_V0-cplx_csu/dsu.
IPR016727. ATPase_V0-cplx_dsu.
[Graphical view]
PANTHERiPTHR11028. PTHR11028. 1 hit.
PfamiPF01992. vATP-synt_AC39. 1 hit.
[Graphical view]
PIRSFiPIRSF018497. V-ATP_synth_D. 1 hit.
SUPFAMiSSF103486. SSF103486. 1 hit.

Sequencei

Sequence statusi: Complete.

Q80SY3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLETAELYFN VDHGYLEGLV RGCKASLLTQ QDYVNLVQCE TLEDLKIHLQ
60 70 80 90 100
TTDYGNFLAN ETNPLTVSKI DTEMRKKLCR EFDYFRNHSL EPLSTFLTYM
110 120 130 140 150
TCSYMIDNII LLMNGALQKK SVKEVLAKCH PLGRFTEMEA VNIAETPSDL
160 170 180 190 200
FKAVLVETPL APFFQDCMSE NTLDELNIEL LRNKLYKSYL EAFYKFCKDH
210 220 230 240 250
GDVTADVMCP ILEFEADRRA LIITLNSFGT ELSKEDRETL FPTCGRLYPE
260 270 280 290 300
GLRLLAQAED FEQMKRVADN YGVYKPLFDA VGGSGGKTLE DVFYEREVQM
310 320 330 340 350
NVLAFNRQFH YGVFYAYVKL KEQEMRNIVW IAECISQRHR TKINSYIPIL
Length:350
Mass (Da):40,494
Last modified:May 1, 2007 - v2
Checksum:i5CC9BC9D2870943D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti309 – 3091F → L in AAN61104 (PubMed:12963731).Curated
Sequence conflicti309 – 3091F → L in BAC57951 (PubMed:12527205).Curated
Sequence conflicti315 – 3151Y → C in BAE41545 (PubMed:16141072).Curated
Sequence conflicti324 – 3241E → G in AAH87899 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY145896 mRNA. Translation: AAN61104.1.
AB088358 mRNA. Translation: BAC57951.1.
AY517482 mRNA. Translation: AAR99405.1.
AK075745 mRNA. Translation: BAC35925.1.
AK089507 mRNA. Translation: BAC40907.1.
AK170072 mRNA. Translation: BAE41545.1.
AK170405 mRNA. Translation: BAE41772.1.
AK170578 mRNA. Translation: BAE41890.1.
AK170659 mRNA. Translation: BAE41942.1.
AL732527, AL773599 Genomic DNA. Translation: CAM18840.1.
AL773599, AL732527 Genomic DNA. Translation: CAM20936.1.
BC087899 mRNA. Translation: AAH87899.1.
CCDSiCCDS17994.1.
RefSeqiNP_780615.2. NM_175406.3.
UniGeneiMm.19298.

Genome annotation databases

EnsembliENSMUST00000029900; ENSMUSP00000029900; ENSMUSG00000028238.
GeneIDi242341.
KEGGimmu:242341.
UCSCiuc008sch.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY145896 mRNA. Translation: AAN61104.1.
AB088358 mRNA. Translation: BAC57951.1.
AY517482 mRNA. Translation: AAR99405.1.
AK075745 mRNA. Translation: BAC35925.1.
AK089507 mRNA. Translation: BAC40907.1.
AK170072 mRNA. Translation: BAE41545.1.
AK170405 mRNA. Translation: BAE41772.1.
AK170578 mRNA. Translation: BAE41890.1.
AK170659 mRNA. Translation: BAE41942.1.
AL732527, AL773599 Genomic DNA. Translation: CAM18840.1.
AL773599, AL732527 Genomic DNA. Translation: CAM20936.1.
BC087899 mRNA. Translation: AAH87899.1.
CCDSiCCDS17994.1.
RefSeqiNP_780615.2. NM_175406.3.
UniGeneiMm.19298.

3D structure databases

ProteinModelPortaliQ80SY3.
SMRiQ80SY3. Positions 7-349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi232395. 2 interactions.
STRINGi10090.ENSMUSP00000029900.

Protein family/group databases

TCDBi3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteiQ80SY3.

Proteomic databases

MaxQBiQ80SY3.
PaxDbiQ80SY3.
PRIDEiQ80SY3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029900; ENSMUSP00000029900; ENSMUSG00000028238.
GeneIDi242341.
KEGGimmu:242341.
UCSCiuc008sch.2. mouse.

Organism-specific databases

CTDi245972.
MGIiMGI:1924415. Atp6v0d2.

Phylogenomic databases

eggNOGiKOG2957. Eukaryota.
COG1527. LUCA.
GeneTreeiENSGT00390000002200.
HOGENOMiHOG000199065.
HOVERGENiHBG018065.
InParanoidiQ80SY3.
KOiK02146.
OMAiRETLFPT.
OrthoDBiEOG7KH9JT.
PhylomeDBiQ80SY3.
TreeFamiTF300857.

Enzyme and pathway databases

ReactomeiR-MMU-77387. Insulin receptor recycling.
R-MMU-917977. Transferrin endocytosis and recycling.
R-MMU-983712. Ion channel transport.

Miscellaneous databases

ChiTaRSiAtp6v0d2. mouse.
NextBioi385305.
PROiQ80SY3.
SOURCEiSearch...

Gene expression databases

BgeeiQ80SY3.
CleanExiMM_ATP6V0D2.
ExpressionAtlasiQ80SY3. baseline and differential.
GenevisibleiQ80SY3. MM.

Family and domain databases

InterProiIPR002843. ATPase_V0-cplx_csu/dsu.
IPR016727. ATPase_V0-cplx_dsu.
[Graphical view]
PANTHERiPTHR11028. PTHR11028. 1 hit.
PfamiPF01992. vATP-synt_AC39. 1 hit.
[Graphical view]
PIRSFiPIRSF018497. V-ATP_synth_D. 1 hit.
SUPFAMiSSF103486. SSF103486. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Expression and function of the mouse V-ATPase d subunit isoforms."
    Nishi T., Kawasaki-Nishi S., Forgac M.
    J. Biol. Chem. 278:46396-46402(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: C57BL/6J.
  2. "Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d and G subunits."
    Sun-Wada G.-H., Yoshimizu T., Imai-Senga Y., Wada Y., Futai M.
    Gene 302:147-153(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  3. "v-ATPase V0 subunit d2-deficient mice exhibit impaired osteoclast fusion and increased bone formation."
    Lee S.-H., Rho J., Jeong D., Sul J.-Y., Kim T., Kim N., Kang J.-S., Miyamoto T., Suda T., Lee S.K., Pignolo R.J., Koczon-Jaremko B., Lorenzo J., Choi Y.
    Nat. Med. 12:1403-1409(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Placenta.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Molar.

Entry informationi

Entry nameiVA0D2_MOUSE
AccessioniPrimary (citable) accession number: Q80SY3
Secondary accession number(s): Q3TDQ6
, Q5I0V5, Q8BTL3, Q8BW16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: May 1, 2007
Last modified: November 11, 2015
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.