Q8N8Y2 (VA0D2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

ATP6V0D2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Hydrogen ion transport Ion transport Transport
Coding sequence diversity	Polymorphism
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP 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_component	apical plasma membrane Inferred from direct assay PubMed 15800125. Source: UniProtKB early endosome Inferred from electronic annotation. Source: Compara endosome membrane Traceable author statement. Source: Reactome 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_function	hydrogen ion transmembrane transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 350	350	V-type proton ATPase subunit d 2		PRO_0000285657
Natural variations
	Natural variant	272	1	G → R. Corresponds to variant rs10094744 [ dbSNP | Ensembl ].		VAR_032039
	Natural variant	295	1	E → K. Corresponds to variant rs4263741 [ dbSNP | Ensembl ].		VAR_032040

Sequences

	Sequence		Length	Mass (Da)
	Q8N8Y2 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 07658C37F2A10CB7	FASTA	350	40,426
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00167639.
RefSeq	NP_689778.1. NM_152565.1.
UniGene	Hs.436360.
3D structure databases
ProteinModelPortal	Q8N8Y2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8N8Y2. 4 interactions.
STRING	9606.ENSP00000285393.
PTM databases
PhosphoSite	Q8N8Y2.
Polymorphism databases
DMDM	74729555.
Proteomic databases
PaxDb	Q8N8Y2.
PRIDE	Q8N8Y2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000285393; ENSP00000285393; ENSG00000147614.
GeneID	245972.
KEGG	hsa:245972.
UCSC	uc003ydp.1. human.
Organism-specific databases
CTD	245972.
GeneCards	GC08P086999.
HGNC	HGNC:18266. ATP6V0D2.
neXtProt	NX_Q8N8Y2.
PharmGKB	PA38516.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1527.
HOGENOM	HOG000199065.
HOVERGEN	HBG018065.
InParanoid	Q8N8Y2.
KO	K02146.
OMA	FFTYMTC.
OrthoDB	EOG4T4CVN.
PhylomeDB	Q8N8Y2.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_116125. Disease. REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	Q8N8Y2.
Bgee	Q8N8Y2.
CleanEx	HS_ATP6V0D2.
Genevestigator	Q8N8Y2.
Family and domain databases
InterPro	IPR002843. ATPase_V0-cplx_csu/dsu. IPR016727. ATPase_V0-cplx_dsu. [Graphical view]
PANTHER	PTHR11028. PTHR11028. 1 hit.
Pfam	PF01992. vATP-synt_AC39. 1 hit. [Graphical view]
PIRSF	PIRSF018497. V-ATP_synth_D. 1 hit.
SUPFAM	SSF103486. ATPase_V0/A0_c/d. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	245972.
NextBio	91831.

Entry information

Entry name

VA0D2_HUMAN

Accession

Primary (citable) accession number: Q8N8Y2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 2007
Last sequence update:	October 1, 2002
Last modified:	April 3, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.