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P50516 (VATA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
V-type proton ATPase catalytic subunit A
Short name=V-ATPase subunit A
EC=3.6.3.14
Alternative name(s):
V-ATPase 69 kDa subunit
Vacuolar proton pump subunit alpha
Gene names
Name:Atp6v1a
Synonyms:Atp6a1, Atp6a2, Atp6v1a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length617 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).

Subunit structure

V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein).

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P50516-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P50516-2)

The sequence of this isoform differs from the canonical sequence as follows:
     499-509: ASLAETDKITL → VRGGCTGCHAG
     510-617: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 617617V-type proton ATPase catalytic subunit A
PRO_0000144561

Regions

Nucleotide binding250 – 2578ATP Potential

Amino acid modifications

Modified residue3741Phosphotyrosine Ref.5
Modified residue3841Phosphoserine Ref.6

Natural variations

Alternative sequence499 – 50911ASLAETDKITL → VRGGCTGCHAG in isoform 2.
VSP_024628
Alternative sequence510 – 617108Missing in isoform 2.
VSP_024629

Experimental info

Sequence conflict861L → R in AAC52410. Ref.1
Sequence conflict1891D → N in AAC52410. Ref.1
Sequence conflict3021V → A in AAC52410. Ref.1
Sequence conflict3301G → V in BAE39074. Ref.2
Sequence conflict4871E → G in AAC52410. Ref.1
Sequence conflict6161E → G in BAE31963. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 17, 2007. Version 2.
Checksum: D46AC76D9C7580A7

FASTA61768,326
        10         20         30         40         50         60 
MDFSKLPKIR DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL VGEIIRLEGD 

        70         80         90        100        110        120 
MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD GIQRPLSDIS SQTQSIYIPR 

       130        140        150        160        170        180 
GVNVSALSRD IKWEFIPSKN LRVGSHITGG DIYGIVNENS LIKHKIMLPP RNRGSVTYIA 

       190        200        210        220        230        240 
PPGNYDASDV VLELEFEGVK EKFSMVQVWP VRQVRPVTEK LPANHPLLTG QRVLDALFPC 

       250        260        270        280        290        300 
VQGGTTAIPG AFGCGKTVIS QSLSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTMEVDG 

       310        320        330        340        350        360 
KVESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYHVSMMADS TSRWAEALRE 

       370        380        390        400        410        420 
ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPER EGSVSIVGAV SPPGGDFSDP 

       430        440        450        460        470        480 
VTSATLGIVQ VFWGLDKKLA QRKHFPSVNW LISYSKYMRA LDEYYDKHFT EFVPLRTKAK 

       490        500        510        520        530        540 
EILQEEEDLA EIVQLVGKAS LAETDKITLE VAKLIKDDFL QQNGYTPYDR FCPFYKTVGM 

       550        560        570        580        590        600 
LSNMISFYDM ARRAVETTAQ SDNKITWSII REHMGEILYK LSSMKFKDPV KDGEAKIKAD 

       610 
YAQLLEDMQN AFRSLED

« Hide

Isoform 2 [UniParc].

Checksum: 55D9F7CCEF00CC89
Show »

FASTA50955,595

References

« Hide 'large scale' references
[1]"Resorption-cycle-dependent polarization of mRNAs for different subunits of V-ATPase in bone-resorbing osteoclasts."
Laitala T., Howell M.L., Dean G.E., Vaananen H.K.
Mol. Biol. Cell 7:129-142(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J and NOD.
Tissue: Bone marrow and Head.
[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] (ISOFORM 1).
Strain: Czech II.
Tissue: Mammary tumor.
[4]Lubec G., Klug S., Kang S.U.
Submitted (APR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 45-56; 143-163; 242-251; 253-262; 266-280; 324-338; 514-530 AND 599-613, MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[5]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-374, MASS SPECTROMETRY.
Tissue: Brain.
[6]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, MASS SPECTROMETRY.
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U13837 Genomic DNA. Translation: AAC52410.1.
AK140873 mRNA. Translation: BAE24506.1.
AK149833 mRNA. Translation: BAE29112.1.
AK152785 mRNA. Translation: BAE31494.1.
AK153403 mRNA. Translation: BAE31963.1.
AK154869 mRNA. Translation: BAE32890.1.
AK160792 mRNA. Translation: BAE36015.1.
AK166857 mRNA. Translation: BAE39074.1.
AK170721 mRNA. Translation: BAE41978.1.
BC038392 mRNA. Translation: AAH38392.1.
IPIIPI00407692.
IPI00844689.
RefSeqNP_031534.2. NM_007508.5.
UniGeneMm.217787.

3D structure databases

ProteinModelPortalP50516.
SMRP50516. Positions 40-587.
ModBaseSearch...

Protein-protein interaction databases

IntActP50516. 106 interactions.

PTM databases

PhosphoSiteP50516.

Proteomic databases

PaxDbP50516.
PRIDEP50516.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063661; ENSMUSP00000066886; ENSMUSG00000052459.
ENSMUST00000114666; ENSMUSP00000110314; ENSMUSG00000052459.
GeneID11964.
KEGGmmu:11964.
UCSCuc007zgu.1. mouse.
uc007zgw.1. mouse.

Organism-specific databases

CTD523.
MGIMGI:1201780. Atp6v1a.

Phylogenomic databases

eggNOGCOG1155.
GeneTreeENSGT00550000074787.
HOVERGENHBG053351.
InParanoidP50516.
KOK02145.
OMAWALDAKL.
OrthoDBEOG4TTGHG.

Gene expression databases

ArrayExpressP50516.
BgeeP50516.
CleanExMM_ATP6V1A.
GenevestigatorP50516.
GermOnlineENSMUSG00000052459. Mus musculus.

Family and domain databases

Gene3D1.10.1140.10. 1 hit.
InterProIPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_a/bsu_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR024034. ATPase_F1_bsu/V1_C.
IPR005725. ATPase_V1-cplx_asu.
IPR022878. V-ATPase_su_A/alpha.
[Graphical view]
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMSSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMsTIGR01042. V-ATPase_V1_A. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP6V1A. mouse.
NextBio280087.
SOURCESearch...

Entry information

Entry nameVATA_MOUSE
AccessionPrimary (citable) accession number: P50516
Secondary accession number(s): Q3TKS0 expand/collapse secondary AC list , Q3U5W3, Q3U777, Q3UDZ9, Q3US31, Q8CHX2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 17, 2007
Last modified: May 1, 2013
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents