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Protein

V-type proton ATPase subunit d 2

Gene

ATP6V0D2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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. May play a role in coupling of proton transport and ATP hydrolysis (By similarity).By similarity

GO - Molecular functioni

  1. hydrogen ion transmembrane transporter activity Source: InterPro

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
  2. cellular iron ion homeostasis Source: Reactome
  3. insulin receptor signaling pathway Source: Reactome
  4. interaction with host Source: Reactome
  5. phagosome maturation Source: Reactome
  6. transferrin transport Source: Reactome
  7. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciMetaCyc:HS07458-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:18266. ATP6V0D2.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. early endosome Source: Ensembl
  3. endosome membrane Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. membrane Source: UniProtKB
  6. phagocytic vesicle membrane Source: Reactome
  7. proton-transporting V-type ATPase, V0 domain Source: InterPro
  8. vacuolar proton-transporting V-type ATPase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38516.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350V-type proton ATPase subunit d 2PRO_0000285657Add
BLAST

Proteomic databases

MaxQBiQ8N8Y2.
PaxDbiQ8N8Y2.
PRIDEiQ8N8Y2.

PTM databases

PhosphoSiteiQ8N8Y2.

Expressioni

Tissue specificityi

Kidney, osteoclast and lung.1 Publication

Gene expression databases

BgeeiQ8N8Y2.
CleanExiHS_ATP6V0D2.
ExpressionAtlasiQ8N8Y2. baseline and differential.
GenevestigatoriQ8N8Y2.

Organism-specific databases

HPAiHPA055327.
HPA058496.

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

BioGridi128858. 8 interactions.
IntActiQ8N8Y2. 4 interactions.
STRINGi9606.ENSP00000285393.

Structurei

3D structure databases

ProteinModelPortaliQ8N8Y2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1527.
GeneTreeiENSGT00390000002200.
HOGENOMiHOG000199065.
HOVERGENiHBG018065.
InParanoidiQ8N8Y2.
KOiK02146.
OMAiFFTYMTC.
PhylomeDBiQ8N8Y2.
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.

Q8N8Y2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLEGAELYFN VDHGYLEGLV RGCKASLLTQ QDYINLVQCE TLEDLKIHLQ
60 70 80 90 100
TTDYGNFLAN HTNPLTVSKI DTEMRKRLCG EFEYFRNHSL EPLSTFLTYM
110 120 130 140 150
TCSYMIDNVI LLMNGALQKK SVKEILGKCH PLGRFTEMEA VNIAETPSDL
160 170 180 190 200
FNAILIETPL APFFQDCMSE NALDELNIEL LRNKLYKSYL EAFYKFCKNH
210 220 230 240 250
GDVTAEVMCP ILEFEADRRA FIITLNSFGT ELSKEDRETL YPTFGKLYPE
260 270 280 290 300
GLRLLAQAED FDQMKNVADH YGVYKPLFEA VGGSGGKTLE DVFYEREVQM
310 320 330 340 350
NVLAFNRQFH YGVFYAYVKL KEQEIRNIVW IAECISQRHR TKINSYIPIL
Length:350
Mass (Da):40,426
Last modified:October 1, 2002 - v1
Checksum:i07658C37F2A10CB7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti272 – 2721G → R.
Corresponds to variant rs10094744 [ dbSNP | Ensembl ].
VAR_032039
Natural varianti295 – 2951E → K.
Corresponds to variant rs4263741 [ dbSNP | Ensembl ].
VAR_032040

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY079172 mRNA. Translation: AAL87000.1.
AK096027 mRNA. Translation: BAC04679.1.
BC065207 mRNA. Translation: AAH65207.1.
CCDSiCCDS6241.1.
RefSeqiNP_689778.1. NM_152565.1.
UniGeneiHs.436360.

Genome annotation databases

EnsembliENST00000285393; ENSP00000285393; ENSG00000147614.
GeneIDi245972.
KEGGihsa:245972.
UCSCiuc003ydp.1. human.

Polymorphism databases

DMDMi74729555.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY079172 mRNA. Translation: AAL87000.1.
AK096027 mRNA. Translation: BAC04679.1.
BC065207 mRNA. Translation: AAH65207.1.
CCDSiCCDS6241.1.
RefSeqiNP_689778.1. NM_152565.1.
UniGeneiHs.436360.

3D structure databases

ProteinModelPortaliQ8N8Y2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi128858. 8 interactions.
IntActiQ8N8Y2. 4 interactions.
STRINGi9606.ENSP00000285393.

PTM databases

PhosphoSiteiQ8N8Y2.

Polymorphism databases

DMDMi74729555.

Proteomic databases

MaxQBiQ8N8Y2.
PaxDbiQ8N8Y2.
PRIDEiQ8N8Y2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000285393; ENSP00000285393; ENSG00000147614.
GeneIDi245972.
KEGGihsa:245972.
UCSCiuc003ydp.1. human.

Organism-specific databases

CTDi245972.
GeneCardsiGC08P086999.
HGNCiHGNC:18266. ATP6V0D2.
HPAiHPA055327.
HPA058496.
neXtProtiNX_Q8N8Y2.
PharmGKBiPA38516.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1527.
GeneTreeiENSGT00390000002200.
HOGENOMiHOG000199065.
HOVERGENiHBG018065.
InParanoidiQ8N8Y2.
KOiK02146.
OMAiFFTYMTC.
PhylomeDBiQ8N8Y2.
TreeFamiTF300857.

Enzyme and pathway databases

BioCyciMetaCyc:HS07458-MONOMER.
ReactomeiREACT_1109. Insulin receptor recycling.
REACT_121256. Phagosomal maturation (early endosomal stage).
REACT_25283. Transferrin endocytosis and recycling.

Miscellaneous databases

GenomeRNAii245972.
NextBioi91831.
PROiQ8N8Y2.

Gene expression databases

BgeeiQ8N8Y2.
CleanExiHS_ATP6V0D2.
ExpressionAtlasiQ8N8Y2. baseline and differential.
GenevestigatoriQ8N8Y2.

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. "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(2001) [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.
    , 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(2003) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.

Entry informationi

Entry nameiVA0D2_HUMAN
AccessioniPrimary (citable) accession number: Q8N8Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: October 1, 2002
Last modified: January 7, 2015
This is version 95 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 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. 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.