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P61421 (VA0D1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
32 kDa accessory protein
V-ATPase 40 kDa accessory protein
V-ATPase AC39 subunit
Short name=p39
Vacuolar proton pump subunit d 1
Gene names
Name:ATP6V0D1
Synonyms:ATP6D, VPATPD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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 By similarity. May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium By similarity.

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. Ref.7

Tissue specificity

Ubiquitous. Ref.1 Ref.5

Sequence similarities

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

Sequence caution

The sequence CAA50591.1 differs from that shown. Reason: Frameshift at positions 22, 25, 64 and 66.

Ontologies

Keywords
   Biological processCilium biogenesis/degradation
Hydrogen ion transport
Ion transport
Transport
   Cellular componentMembrane
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: InterPro

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

brain development

Inferred from electronic annotation. Source: Ensembl

cellular iron ion homeostasis

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cilium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

interaction with host

Traceable author statement. Source: Reactome

phagosome maturation

Traceable author statement. Source: Reactome

proton transport

Non-traceable author statement Ref.2. Source: UniProtKB

transferrin transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: Ensembl

axon terminus

Inferred from electronic annotation. Source: Ensembl

early endosome

Inferred from electronic annotation. Source: Ensembl

endosome membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

membrane

Inferred from direct assay PubMed 18752060. Source: UniProtKB

phagocytic vesicle membrane

Traceable author statement. Source: Reactome

proton-transporting V-type ATPase, V0 domain

Inferred from electronic annotation. Source: InterPro

synaptic vesicle

Inferred from electronic annotation. Source: Ensembl

vacuolar proton-transporting V-type ATPase complex

Inferred from direct assay PubMed 18752060. Source: UniProtKB

   Molecular_functionhydrogen-exporting ATPase activity, phosphorylative mechanism

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 351351V-type proton ATPase subunit d 1
PRO_0000119350

Amino acid modifications

Modified residue2701Phosphotyrosine By similarity

Experimental info

Sequence conflict271V → E in CAA50591. Ref.1
Sequence conflict266 – 2672NV → KL in CAA50591. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P61421 [UniParc].

Last modified May 24, 2004. Version 1.
Checksum: A720F8A87511203C

FASTA35140,329
        10         20         30         40         50         60 
MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN 

        70         80         90        100        110        120 
EASPLTVSVI DDRLKEKMVV 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]"Cloning and tissue distribution of subunits C, D, and E of the human vacuolar H(+)-ATPase."
van Hille B., Vanek M., Richener H., Green J.R., Bilbe G.
Biochem. Biophys. Res. Commun. 197:15-21(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Osteoclastoma.
[2]"Structure of the VPATPD gene encoding subunit D of the human vacuolar proton ATPase."
Agarwal A.K., White P.C.
Biochem. Biophys. Res. Commun. 279:543-547(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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: Brain.
[4]"Expressed sequence tags from a human cell line."
Bhat K.S.
Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 264-351.
[5]"Molecular cloning and characterization of novel tissue-specific isoforms of the human vacuolar H(+)-ATPase C, G and d subunits, and their evaluation in autosomal recessive distal renal tubular acidosis."
Smith A.N., Borthwick K.J., Karet F.E.
Gene 297:169-177(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"A SNX10/V-ATPase pathway regulates ciliogenesis in vitro and in vivo."
Chen Y., Wu B., Xu L., Li H., Xia J., Yin W., Li Z., Shi D., Li S., Lin S., Shu X., Pei D.
Cell Res. 22:333-345(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X71490 mRNA. Translation: CAA50591.1. Frameshift.
BC008861 mRNA. Translation: AAH08861.1.
L05087 mRNA. Translation: AAC15852.1.
RefSeqNP_004682.2. NM_004691.4.
UniGeneHs.106876.

3D structure databases

ProteinModelPortalP61421.
SMRP61421. Positions 28-55.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114564. 7 interactions.
IntActP61421. 2 interactions.
MINTMINT-5006032.
STRING9606.ENSP00000290949.

Protein family/group databases

TCDB3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteP61421.

Polymorphism databases

DMDM47606646.

Proteomic databases

PaxDbP61421.
PeptideAtlasP61421.
PRIDEP61421.

Protocols and materials databases

DNASU9114.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290949; ENSP00000290949; ENSG00000159720.
GeneID9114.
KEGGhsa:9114.
UCSCuc002ete.1. human.

Organism-specific databases

CTD9114.
GeneCardsGC16M067471.
HGNCHGNC:13724. ATP6V0D1.
HPAHPA016938.
MIM607028. gene.
neXtProtNX_P61421.
PharmGKBPA25150.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1527.
HOGENOMHOG000199065.
HOVERGENHBG018065.
InParanoidP61421.
KOK02146.
OrthoDBEOG7KH9JT.
PhylomeDBP61421.
TreeFamTF300857.

Enzyme and pathway databases

BioCycMetaCyc:HS08417-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP61421.
BgeeP61421.
CleanExHS_ATP6V0D1.
GenevestigatorP61421.

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. human.
GeneWikiATP6V0D1.
GenomeRNAi9114.
NextBio34161.
PROP61421.
SOURCESearch...

Entry information

Entry nameVA0D1_HUMAN
AccessionPrimary (citable) accession number: P61421
Secondary accession number(s): P12953, Q02547
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM