P61421 (VA0D1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ATP6V0D1
Synonyms:	ATP6D, VPATPD

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	351 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 an 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	Ubiquitous. Ref.1 Ref.5
Sequence similarities	Belongs to the V-ATPase V0D/AC39 subunit family.
Sequence caution	The sequence CAA50591.1 differs from that shown. Reason: Frameshift at positions 22, 25, 64 and 66.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
PTM	Phosphoprotein
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 transferrin transport Traceable author statement. Source: Reactome
Cellular component	clathrin sculpted glutamate transport vesicle membrane Traceable author statement. Source: Reactome endosome 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. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 351	351	V-type proton ATPase subunit d 1		PRO_0000119350
Amino acid modifications
	Modified residue	270	1	Phosphotyrosine By similarity
	Modified residue	283	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	27	1	V → E in CAA50591. Ref.1
	Sequence conflict	266 – 267	2	NV → KL in CAA50591. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P61421 [UniParc]. Last modified May 24, 2004. Version 1. Checksum: A720F8A87511203C	FASTA	351	40,329
	10 20 30 40 50 60 MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN 70 80 90 100 110 120 EASPLTVSVI DDRLKEKMVV EFRHMRNHAY EPLASFLDFI TYSYMIDNVI LLITGTLHQR 130 140 150 160 170 180 SIAELVPKCH PLGSFEQMEA VNIAQTPAEL YNAILVDTPL AAFFQDCISE QDLDEMNIEI 190 200 210 220 230 240 IRNTLYKAYL ESFYKFCTLL GGTTADAMCP ILEFEADRRA FIITINSFGT ELSKEDRAKL 250 260 270 280 290 300 FPHCGRLYPE GLAQLARADD YEQVKNVADY YPEYKLLFEG AGSNPGDKTL EDRFFEHEVK 310 320 330 340 350 LNKLAFLNQF HFGVFYAFVK LKEQECRNIV WIAECIAQRH RAKIDNYIPI F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8250920] [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: 11118322] [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: 15489334] [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: 12384298] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X71490 mRNA. Translation: CAA50591.1. Frameshift. BC008861 mRNA. Translation: AAH08861.1. L05087 mRNA. Translation: AAC15852.1.
IPI	IPI00034159.
RefSeq	NP_004682.2. NM_004691.4.
UniGene	Hs.106876.
3D structure databases
ProteinModelPortal	P61421.
ModBase	Search...
Protein-protein interaction databases
IntAct	P61421. 1 interaction.
MINT	MINT-5006032.
STRING	P61421.
Protein family/group databases
TCDB	3.A.2.2.4. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.
PTM databases
PhosphoSite	P61421.
Polymorphism databases
DMDM	47606646.
Proteomic databases
PeptideAtlas	P61421.
PRIDE	P61421.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000290949; ENSP00000290949; ENSG00000159720.
GeneID	9114.
KEGG	hsa:9114.
UCSC	uc002ete.1. human.
Organism-specific databases
CTD	9114.
GeneCards	GC16M067471.
H-InvDB	HIX0013148.
HGNC	HGNC:13724. ATP6V0D1.
HPA	HPA016938.
MIM	607028. gene.
neXtProt	NX_P61421.
PharmGKB	PA25150.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16262.
GeneTree	ENSGT00390000002200.
HOGENOM	HBG317755.
HOVERGEN	HBG018065.
InParanoid	P61421.
OMA	QMEAIHV.
OrthoDB	EOG4T4CVN.
PhylomeDB	P61421.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_15380. Diabetes pathways. REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	P61421.
Bgee	P61421.
CleanEx	HS_ATP6V0D1.
Genevestigator	P61421.
GermOnline	ENSG00000159720. Homo sapiens.
Family and domain databases
InterPro	IPR016727. ATPase_V0-cplx_dsu. IPR002843. ATPase_V0/A0-cplx_csu/dsu. [Graphical view]
KO	K02146.
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
NextBio	34161.
SOURCE	Search...

Entry information

Entry name

VA0D1_HUMAN

Accession

Primary (citable) accession number: P61421
Secondary accession number(s): P12953, Q02547

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 24, 2004
Last sequence update:	May 24, 2004
Last modified:	January 25, 2012
This is version 77 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.