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Protein

V-type proton ATPase subunit d 1

Gene

ATP6V0D1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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. 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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cilium biogenesis/degradation, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:HS08417-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_18273. XBP1(S) activates chaperone genes.
REACT_25283. Transferrin endocytosis and recycling.
REACT_25300. Ion channel transport.

Protein family/group databases

TCDBi3.A.2.2.4. 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 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 namesi
Name:ATP6V0D1
Synonyms:ATP6D, VPATPD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:13724. ATP6V0D1.

Subcellular locationi

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • axon terminus Source: Ensembl
  • early endosome Source: Ensembl
  • endosome membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • phagocytic vesicle membrane Source: Reactome
  • proton-transporting V-type ATPase, V0 domain Source: InterPro
  • synaptic vesicle Source: Ensembl
  • vacuolar proton-transporting V-type ATPase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25150.

Polymorphism and mutation databases

BioMutaiATP6V0D1.
DMDMi47606646.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 351351V-type proton ATPase subunit d 1PRO_0000119350Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei270 – 2701PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP61421.
PaxDbiP61421.
PeptideAtlasiP61421.
PRIDEiP61421.

PTM databases

PhosphoSiteiP61421.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

BgeeiP61421.
CleanExiHS_ATP6V0D1.
ExpressionAtlasiP61421. baseline and differential.
GenevestigatoriP61421.

Organism-specific databases

HPAiHPA016938.

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

BioGridi114564. 13 interactions.
IntActiP61421. 3 interactions.
MINTiMINT-5006032.
STRINGi9606.ENSP00000290949.

Structurei

3D structure databases

ProteinModelPortaliP61421.
SMRiP61421. Positions 28-55.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1527.
GeneTreeiENSGT00390000002200.
HOGENOMiHOG000199065.
HOVERGENiHBG018065.
InParanoidiP61421.
KOiK02146.
OrthoDBiEOG7KH9JT.
PhylomeDBiP61421.
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.

P61421-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ
60 70 80 90 100
STDYGNFLAN EASPLTVSVI DDRLKEKMVV EFRHMRNHAY EPLASFLDFI
110 120 130 140 150
TYSYMIDNVI LLITGTLHQR SIAELVPKCH PLGSFEQMEA VNIAQTPAEL
160 170 180 190 200
YNAILVDTPL AAFFQDCISE QDLDEMNIEI IRNTLYKAYL ESFYKFCTLL
210 220 230 240 250
GGTTADAMCP ILEFEADRRA FIITINSFGT ELSKEDRAKL FPHCGRLYPE
260 270 280 290 300
GLAQLARADD YEQVKNVADY YPEYKLLFEG AGSNPGDKTL EDRFFEHEVK
310 320 330 340 350
LNKLAFLNQF HFGVFYAFVK LKEQECRNIV WIAECIAQRH RAKIDNYIPI

F
Length:351
Mass (Da):40,329
Last modified:May 24, 2004 - v1
Checksum:iA720F8A87511203C
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271V → E in CAA50591 (PubMed:8250920).Curated
Sequence conflicti266 – 2672NV → KL in CAA50591 (PubMed:8250920).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71490 mRNA. Translation: CAA50591.1. Frameshift.
BC008861 mRNA. Translation: AAH08861.1.
L05087 mRNA. Translation: AAC15852.1.
CCDSiCCDS10838.1.
RefSeqiNP_004682.2. NM_004691.4.
UniGeneiHs.106876.

Genome annotation databases

EnsembliENST00000290949; ENSP00000290949; ENSG00000159720.
GeneIDi9114.
KEGGihsa:9114.
UCSCiuc002ete.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X71490 mRNA. Translation: CAA50591.1. Frameshift.
BC008861 mRNA. Translation: AAH08861.1.
L05087 mRNA. Translation: AAC15852.1.
CCDSiCCDS10838.1.
RefSeqiNP_004682.2. NM_004691.4.
UniGeneiHs.106876.

3D structure databases

ProteinModelPortaliP61421.
SMRiP61421. Positions 28-55.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114564. 13 interactions.
IntActiP61421. 3 interactions.
MINTiMINT-5006032.
STRINGi9606.ENSP00000290949.

Protein family/group databases

TCDBi3.A.2.2.4. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSiteiP61421.

Polymorphism and mutation databases

BioMutaiATP6V0D1.
DMDMi47606646.

Proteomic databases

MaxQBiP61421.
PaxDbiP61421.
PeptideAtlasiP61421.
PRIDEiP61421.

Protocols and materials databases

DNASUi9114.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000290949; ENSP00000290949; ENSG00000159720.
GeneIDi9114.
KEGGihsa:9114.
UCSCiuc002ete.1. human.

Organism-specific databases

CTDi9114.
GeneCardsiGC16M067471.
HGNCiHGNC:13724. ATP6V0D1.
HPAiHPA016938.
MIMi607028. gene.
neXtProtiNX_P61421.
PharmGKBiPA25150.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1527.
GeneTreeiENSGT00390000002200.
HOGENOMiHOG000199065.
HOVERGENiHBG018065.
InParanoidiP61421.
KOiK02146.
OrthoDBiEOG7KH9JT.
PhylomeDBiP61421.
TreeFamiTF300857.

Enzyme and pathway databases

BioCyciMetaCyc:HS08417-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_18273. XBP1(S) activates chaperone genes.
REACT_25283. Transferrin endocytosis and recycling.
REACT_25300. Ion channel transport.

Miscellaneous databases

ChiTaRSiATP6V0D1. human.
GeneWikiiATP6V0D1.
GenomeRNAii9114.
NextBioi34161.
PROiP61421.
SOURCEiSearch...

Gene expression databases

BgeeiP61421.
CleanExiHS_ATP6V0D1.
ExpressionAtlasiP61421. baseline and differential.
GenevestigatoriP61421.

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. "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. 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.

Entry informationi

Entry nameiVA0D1_HUMAN
AccessioniPrimary (citable) accession number: P61421
Secondary accession number(s): P12953, Q02547
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: May 27, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.