Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P51863 (VA0D1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
V-type proton ATPase subunit d 1

Short name=V-ATPase subunit d 1
Alternative name(s):
P39
Physophilin
V-ATPase 40 kDa accessory protein
V-ATPase AC39 subunit
Vacuolar proton pump subunit d 1
Gene names
Name:Atp6v0d1
Synonyms:Atp6d
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length351 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. May play a role in coupling of proton transport and ATP hydrolysis. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium By similarity. Ref.6

Subunit structure

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).

Subcellular location

Membrane; Peripheral membrane protein; Cytoplasmic side Probable. Note: Localizes to centrosome and the base of the cilium By similarity.

Tissue specificity

Ubiquitous. Ref.3 Ref.6

Developmental stage

Expressed throughout early development. Ref.6

Sequence similarities

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

Biophysicochemical properties

Kinetic parameters:

KM=0.31 mM for ATP Ref.6

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351V-type proton ATPase subunit d 1
PRO_0000119351

Amino acid modifications

Modified residue2701Phosphotyrosine Ref.7

Experimental info

Sequence conflict231L → M in AAC83085. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P51863 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 62CDF67B982124C9

FASTA35140,301
        10         20         30         40         50         60 
MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN 

        70         80         90        100        110        120 
EASPLTVSVI DDKLKEKMVV EFRHMRNHAY EPLASFLDFI TYSYMIDNVI LLITGTLHQR 

       130        140        150        160        170        180 
SIAELVPKCH PLGSFEQMEA VNIAQTPAEL YNAILVDTPL AAFFQDCISE QDLDEMNIEI 

       190        200        210        220        230        240 
IRNTLYKAYL ESFYKFCTLL GGTTADAMCP ILEFEADRRA FIITINSFGT ELSKEDRAKL 

       250        260        270        280        290        300 
FPHCGRLYPE GLAQLARADD YEQVKNVADY YPEYKLLFEG AGSNPGDKTL EDRFFEHEVK 

       310        320        330        340        350 
LNKLAFLNQF HFGVFYAFVK LKEQECRNIV WIAECIAQRH RAKIDNYIPI F 

« Hide

References

« Hide 'large scale' references
[1]"cDNA sequences for mouse vacuolar ATPase subunits."
Howell M.L., Dean G.E.
Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Brain Ac39/physophilin: cloning, coexpression and colocalization with synaptophysin."
Carrion-Vazquez M., Fernandez A.M., Chowen J., Nieto-Sampedro M.
Eur. J. Neurosci. 10:1153-1166(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Brain.
[3]"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.
[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. expand/collapse author list , 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.
Tissue: Thymus.
[5]Lubec G., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 25-73; 87-128; 188-237; 240-288; 294-300; 304-320; 328-339 AND 344-351, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain.
[6]"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: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-270, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U13840 mRNA. Translation: AAC83085.1.
U21549 mRNA. Translation: AAA92288.1.
AB088408 mRNA. Translation: BAC57954.1.
AK083372 mRNA. Translation: BAC38889.1.
AK171515 mRNA. Translation: BAE42500.1.
CCDSCCDS22604.1.
RefSeqNP_038505.2. NM_013477.3.
UniGeneMm.17708.

3D structure databases

ProteinModelPortalP51863.
SMRP51863. Positions 28-54.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198264. 2 interactions.
IntActP51863. 8 interactions.
MINTMINT-1858223.

Protein family/group databases

TCDB3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteP51863.

Proteomic databases

MaxQBP51863.
PaxDbP51863.
PRIDEP51863.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000013304; ENSMUSP00000013304; ENSMUSG00000013160.
GeneID11972.
KEGGmmu:11972.
UCSCuc009ndg.1. mouse.

Organism-specific databases

CTD9114.
MGIMGI:1201778. Atp6v0d1.

Phylogenomic databases

eggNOGCOG1527.
GeneTreeENSGT00390000002200.
HOGENOMHOG000199065.
HOVERGENHBG018065.
InParanoidP51863.
KOK02146.
OMAQMEAIHV.
OrthoDBEOG7KH9JT.
PhylomeDBP51863.
TreeFamTF300857.

Gene expression databases

BgeeP51863.
CleanExMM_ATP6V0D1.
GenevestigatorP51863.

Family and domain databases

InterProIPR002843. ATPase_V0-cplx_csu/dsu.
IPR016727. ATPase_V0-cplx_dsu.
[Graphical view]
PANTHERPTHR11028. PTHR11028. 1 hit.
PfamPF01992. vATP-synt_AC39. 1 hit.
[Graphical view]
PIRSFPIRSF018497. V-ATP_synth_D. 1 hit.
SUPFAMSSF103486. SSF103486. 1 hit.
ProtoNetSearch...

Other

ChiTaRSATP6V0D1. mouse.
NextBio280095.
PROP51863.
SOURCESearch...

Entry information

Entry nameVA0D1_MOUSE
AccessionPrimary (citable) accession number: P51863
Secondary accession number(s): Q54A57, Q9QWJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 11, 2001
Last modified: July 9, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot