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Protein

V-type proton ATPase subunit d 2

Gene

Atp6v0d2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-77387. Insulin receptor recycling.
R-RNO-917977. Transferrin endocytosis and recycling.
R-RNO-983712. Ion channel transport.

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
Name:Atp6v0d2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi1306900. Atp6v0d2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 350350V-type proton ATPase subunit d 2PRO_0000285660Add
BLAST

Proteomic databases

PaxDbiQ5FVL0.
PRIDEiQ5FVL0.

Expressioni

Tissue specificityi

Epididymis and vas deferens.1 Publication

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).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009334.

Structurei

3D structure databases

ProteinModelPortaliQ5FVL0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG2957. Eukaryota.
COG1527. LUCA.
GeneTreeiENSGT00390000002200.
HOGENOMiHOG000199065.
HOVERGENiHBG018065.
InParanoidiQ5FVL0.
KOiK02146.
OMAiRETLFPT.
OrthoDBiEOG7KH9JT.
PhylomeDBiQ5FVL0.
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.

Q5FVL0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLETAELYFN VDHGYLEGLV RGCKASLLTQ QDYVNLVQCE TLEDLKIHLQ
60 70 80 90 100
TTDYGNFLAH ETNPLTVSKI DTEMRKKLCR EFDYFRNHSL EPLSTFFTYM
110 120 130 140 150
TCSYMIDNII LLMNGALQKK SVKEVLAKCH PLGRFTEMEA VNIAESASEL
160 170 180 190 200
FKAVLVETPL APFFQDCMSE NTLDELNIEL LRNKLYKSYL EAFYKFCKDH
210 220 230 240 250
GDVTAEVMCP ILEFEADRRA LIITLNSFGT ELSKEDRETL FPTCGKLYPE
260 270 280 290 300
GLRLLAQAED FEHMKRVADN YGVYKPLFDA VGGSGGKTLE DVFYEREVQM
310 320 330 340 350
NVLAFNRQFH YGVFYAYVKL KEQEMRNIVW IAECISQRHR TKINSYIPIL
Length:350
Mass (Da):40,520
Last modified:March 1, 2005 - v1
Checksum:i3B1E7969788BC6FA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC089917 mRNA. Translation: AAH89917.1.
RefSeqiNP_001011972.1. NM_001011972.1.
UniGeneiRn.83540.

Genome annotation databases

EnsembliENSRNOT00000009334; ENSRNOP00000009334; ENSRNOG00000006926.
GeneIDi297932.
KEGGirno:297932.
UCSCiRGD:1306900. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC089917 mRNA. Translation: AAH89917.1.
RefSeqiNP_001011972.1. NM_001011972.1.
UniGeneiRn.83540.

3D structure databases

ProteinModelPortaliQ5FVL0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000009334.

Proteomic databases

PaxDbiQ5FVL0.
PRIDEiQ5FVL0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000009334; ENSRNOP00000009334; ENSRNOG00000006926.
GeneIDi297932.
KEGGirno:297932.
UCSCiRGD:1306900. rat.

Organism-specific databases

CTDi245972.
RGDi1306900. Atp6v0d2.

Phylogenomic databases

eggNOGiKOG2957. Eukaryota.
COG1527. LUCA.
GeneTreeiENSGT00390000002200.
HOGENOMiHOG000199065.
HOVERGENiHBG018065.
InParanoidiQ5FVL0.
KOiK02146.
OMAiRETLFPT.
OrthoDBiEOG7KH9JT.
PhylomeDBiQ5FVL0.
TreeFamiTF300857.

Enzyme and pathway databases

ReactomeiR-RNO-77387. Insulin receptor recycling.
R-RNO-917977. Transferrin endocytosis and recycling.
R-RNO-983712. Ion channel transport.

Miscellaneous databases

NextBioi642854.
PROiQ5FVL0.

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. "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: Ovary.
  2. "Distinct expression patterns of different subunit isoforms of the V-ATPase in the rat epididymis."
    Pietrement C., Sun-Wada G.H., Silva N.D., McKee M., Marshansky V., Brown D., Futai M., Breton S.
    Biol. Reprod. 74:185-194(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiVA0D2_RAT
AccessioniPrimary (citable) accession number: Q5FVL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: March 1, 2005
Last modified: November 11, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.