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Q8N8Y2 (VA0D2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 2

Short name=V-ATPase subunit d 2
Alternative name(s):
Vacuolar proton pump subunit d 2
Gene names
Name:ATP6V0D2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

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).

Tissue specificity

Kidney, osteoclast and lung. Ref.1

Sequence similarities

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

Ontologies

Keywords
   Biological processHydrogen ion transport
Ion transport
Transport
   Coding sequence diversityPolymorphism
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: InterPro

cellular iron ion homeostasis

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

transferrin transport

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentapical plasma membrane

Inferred from direct assay PubMed 15800125. Source: UniProtKB

early endosome

Inferred from electronic annotation. Source: Ensembl

endosome membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

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

vacuolar proton-transporting V-type ATPase complex

Inferred from direct assay PubMed 18752060. Source: UniProtKB

   Molecular_functionhydrogen ion transmembrane transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350V-type proton ATPase subunit d 2
PRO_0000285657

Natural variations

Natural variant2721G → R.
Corresponds to variant rs10094744 [ dbSNP | Ensembl ].
VAR_032039
Natural variant2951E → K.
Corresponds to variant rs4263741 [ dbSNP | Ensembl ].
VAR_032040

Sequences

Sequence LengthMass (Da)Tools
Q8N8Y2 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 07658C37F2A10CB7

FASTA35040,426
        10         20         30         40         50         60 
MLEGAELYFN VDHGYLEGLV RGCKASLLTQ QDYINLVQCE TLEDLKIHLQ TTDYGNFLAN 

        70         80         90        100        110        120 
HTNPLTVSKI DTEMRKRLCG EFEYFRNHSL EPLSTFLTYM TCSYMIDNVI LLMNGALQKK 

       130        140        150        160        170        180 
SVKEILGKCH PLGRFTEMEA VNIAETPSDL FNAILIETPL APFFQDCMSE NALDELNIEL 

       190        200        210        220        230        240 
LRNKLYKSYL EAFYKFCKNH GDVTAEVMCP ILEFEADRRA FIITLNSFGT ELSKEDRETL 

       250        260        270        280        290        300 
YPTFGKLYPE GLRLLAQAED FDQMKNVADH YGVYKPLFEA VGGSGGKTLE DVFYEREVQM 

       310        320        330        340        350 
NVLAFNRQFH YGVFYAYVKL KEQEIRNIVW IAECISQRHR TKINSYIPIL 

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[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: Colon.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY079172 mRNA. Translation: AAL87000.1.
AK096027 mRNA. Translation: BAC04679.1.
BC065207 mRNA. Translation: AAH65207.1.
RefSeqNP_689778.1. NM_152565.1.
UniGeneHs.436360.

3D structure databases

ProteinModelPortalQ8N8Y2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128858. 5 interactions.
IntActQ8N8Y2. 4 interactions.
STRING9606.ENSP00000285393.

PTM databases

PhosphoSiteQ8N8Y2.

Polymorphism databases

DMDM74729555.

Proteomic databases

PaxDbQ8N8Y2.
PRIDEQ8N8Y2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000285393; ENSP00000285393; ENSG00000147614.
GeneID245972.
KEGGhsa:245972.
UCSCuc003ydp.1. human.

Organism-specific databases

CTD245972.
GeneCardsGC08P086999.
HGNCHGNC:18266. ATP6V0D2.
HPAHPA055327.
HPA058496.
neXtProtNX_Q8N8Y2.
PharmGKBPA38516.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1527.
HOGENOMHOG000199065.
HOVERGENHBG018065.
InParanoidQ8N8Y2.
KOK02146.
OMAFFTYMTC.
PhylomeDBQ8N8Y2.
TreeFamTF300857.

Enzyme and pathway databases

BioCycMetaCyc:HS07458-MONOMER.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressQ8N8Y2.
BgeeQ8N8Y2.
CleanExHS_ATP6V0D2.
GenevestigatorQ8N8Y2.

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

GenomeRNAi245972.
NextBio91831.
PROQ8N8Y2.

Entry information

Entry nameVA0D2_HUMAN
AccessionPrimary (citable) accession number: Q8N8Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 88 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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM