P51863 (VA0D1_MOUSE) 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):
P39
Physophilin
V-ATPase 40 kDa accessory protein
V-ATPase AC39 subunit
Vacuolar proton pump subunit d 1

Gene names

Name:	Atp6v0d1
Synonyms:	Atp6d

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. Ref.6
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.3 Ref.6
Developmental stage	Expressed throughout early development. Ref.6
Sequence similarities	Belongs to the V-ATPase V0D/AC39 subunit family.
Biophysicochemical properties	Kinetic parameters: KM=0.31 mM for ATP Ref.6

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro
Cellular component	early endosome Inferred from direct assay. Source: MGI proton-transporting V-type ATPase, V0 domain Inferred from electronic annotation. Source: InterPro
Molecular function	hydrogen-exporting ATPase activity, phosphorylative mechanism Inferred from direct assay Ref.3. Source: MGI
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_0000119351
Amino acid modifications
	Modified residue	270	1	Phosphotyrosine Ref.7
	Modified residue	283	1	Phosphoserine Ref.8
Experimental info
	Sequence conflict	23	1	L → M in AAC83085. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P51863 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 62CDF67B982124C9	FASTA	351	40,301
	10 20 30 40 50 60 MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN 70 80 90 100 110 120 EASPLTVSVI DDKLKEKMVV 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]	"cDNA sequences for mouse vacuolar ATPase subunits." Howell M.L., Dean G.E. Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Brain Ac39/physophilin: cloning, coexpression and colocalization with synaptophysin." Carrion-Vazquez M., Fernandez A.M., Chowen J., Nieto-Sampedro M. Eur. J. Neurosci. 10:1153-1166(1998) [PubMed: 9753184] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Brain.
[3]	"Diversity of mouse proton-translocating ATPase: presence of multiple isoforms of the C, d and G subunits." Sun-Wada G.-H., Yoshimizu T., Imai-Senga Y., Wada Y., Futai M. Gene 302:147-153(2003) [PubMed: 12527205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Thymus.
[5]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 25-73; 87-128; 188-237; 240-288; 294-300; 304-320; 328-339 AND 344-351, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[6]	"Expression and function of the mouse V-ATPase d subunit isoforms." Nishi T., Kawasaki-Nishi S., Forgac M. J. Biol. Chem. 278:46396-46402(2003) [PubMed: 12963731] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[7]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-270, MASS SPECTROMETRY. Tissue: Brain.
[8]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, MASS SPECTROMETRY. Tissue: Brain cortex.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U13840 mRNA. Translation: AAC83085.1. U21549 mRNA. Translation: AAA92288.1. AB088408 mRNA. Translation: BAC57954.1. AK083372 mRNA. Translation: BAC38889.1. AK171515 mRNA. Translation: BAE42500.1.
IPI	IPI00313841.
RefSeq	NP_038505.2. NM_013477.3.
UniGene	Mm.17708.
3D structure databases
ProteinModelPortal	P51863.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51863. 6 interactions.
STRING	P51863.
PTM databases
PhosphoSite	P51863.
Proteomic databases
PRIDE	P51863.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000013304; ENSMUSP00000013304; ENSMUSG00000013160.
GeneID	11972.
KEGG	mmu:11972.
UCSC	uc009ndg.1. mouse.
Organism-specific databases
CTD	9114.
MGI	MGI:1201778. Atp6v0d1.
Phylogenomic databases
eggNOG	roNOG08793.
HOGENOM	HBG317755.
HOVERGEN	HBG018065.
InParanoid	P51863.
OMA	QMEAIHV.
OrthoDB	EOG4T4CVN.
PhylomeDB	P51863.
Gene expression databases
ArrayExpress	P51863.
Bgee	P51863.
CleanEx	MM_ATP6V0D1.
Genevestigator	P51863.
GermOnline	ENSMUSG00000013160. Mus musculus.
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	280095.
SOURCE	Search...

Entry information

Entry name

VA0D1_MOUSE

Accession

Primary (citable) accession number: P51863
Secondary accession number(s): Q54A57, Q9QWJ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 11, 2001
Last modified:	November 16, 2011
This is version 98 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program