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P50516

- VATA_MOUSE

UniProt

P50516 - VATA_MOUSE

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Protein
V-type proton ATPase catalytic subunit A
Gene
Atp6v1a, Atp6a1, Atp6a2, Atp6v1a1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi250 – 2578ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. proton-transporting ATPase activity, rotational mechanism Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. ATP hydrolysis coupled proton transport Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198515. Transferrin endocytosis and recycling.

Protein family/group databases

TCDBi3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
V-type proton ATPase catalytic subunit A (EC:3.6.3.14)
Short name:
V-ATPase subunit A
Alternative name(s):
V-ATPase 69 kDa subunit
Vacuolar proton pump subunit alpha
Gene namesi
Name:Atp6v1a
Synonyms:Atp6a1, Atp6a2, Atp6v1a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 16

Organism-specific databases

MGIiMGI:1201780. Atp6v1a.

Subcellular locationi

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. lysosomal membrane Source: Ensembl
  4. microvillus Source: UniProtKB
  5. mitochondrion Source: MGI
  6. plasma membrane Source: UniProtKB
  7. proton-transporting V-type ATPase, V1 domain Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 617617V-type proton ATPase catalytic subunit AUniRule annotation
PRO_0000144561Add
BLAST

Proteomic databases

MaxQBiP50516.
PaxDbiP50516.
PRIDEiP50516.

PTM databases

PhosphoSiteiP50516.

Expressioni

Gene expression databases

ArrayExpressiP50516.
BgeeiP50516.
CleanExiMM_ATP6V1A.
GenevestigatoriP50516.

Interactioni

Subunit structurei

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).

Protein-protein interaction databases

BioGridi198261. 6 interactions.
IntActiP50516. 108 interactions.
MINTiMINT-1866559.

Structurei

3D structure databases

ProteinModelPortaliP50516.
SMRiP50516. Positions 40-587.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1155.
GeneTreeiENSGT00550000074787.
HOVERGENiHBG053351.
InParanoidiP50516.
KOiK02145.
OMAiENKITWN.
OrthoDBiEOG7Q8CMM.
PhylomeDBiP50516.
TreeFamiTF300811.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 2 hits.
HAMAPiMF_00309. ATP_synth_A_arch.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR005725. ATPase_V1-cplx_asu.
IPR027417. P-loop_NTPase.
IPR022878. V-ATPase_asu.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01042. V-ATPase_V1_A. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P50516-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MDFSKLPKIR DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL    50
VGEIIRLEGD MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD 100
GIQRPLSDIS SQTQSIYIPR GVNVSALSRD IKWEFIPSKN LRVGSHITGG 150
DIYGIVNENS LIKHKIMLPP RNRGSVTYIA PPGNYDASDV VLELEFEGVK 200
EKFSMVQVWP VRQVRPVTEK LPANHPLLTG QRVLDALFPC VQGGTTAIPG 250
AFGCGKTVIS QSLSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTMEVDG 300
KVESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYHVSMMADS 350
TSRWAEALRE ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPER 400
EGSVSIVGAV SPPGGDFSDP VTSATLGIVQ VFWGLDKKLA QRKHFPSVNW 450
LISYSKYMRA LDEYYDKHFT EFVPLRTKAK EILQEEEDLA EIVQLVGKAS 500
LAETDKITLE VAKLIKDDFL QQNGYTPYDR FCPFYKTVGM LSNMISFYDM 550
ARRAVETTAQ SDNKITWSII REHMGEILYK LSSMKFKDPV KDGEAKIKAD 600
YAQLLEDMQN AFRSLED 617
Length:617
Mass (Da):68,326
Last modified:April 17, 2007 - v2
Checksum:iD46AC76D9C7580A7
GO
Isoform 2 (identifier: P50516-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     499-509: ASLAETDKITL → VRGGCTGCHAG
     510-617: Missing.

Note: No experimental confirmation available.

Show »
Length:509
Mass (Da):55,595
Checksum:i55D9F7CCEF00CC89
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei499 – 50911ASLAETDKITL → VRGGCTGCHAG in isoform 2.
VSP_024628Add
BLAST
Alternative sequencei510 – 617108Missing in isoform 2.
VSP_024629Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861L → R in AAC52410. 1 Publication
Sequence conflicti189 – 1891D → N in AAC52410. 1 Publication
Sequence conflicti302 – 3021V → A in AAC52410. 1 Publication
Sequence conflicti330 – 3301G → V in BAE39074. 1 Publication
Sequence conflicti487 – 4871E → G in AAC52410. 1 Publication
Sequence conflicti616 – 6161E → G in BAE31963. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS28182.1. [P50516-1]
RefSeqiNP_031534.2. NM_007508.5. [P50516-1]
XP_006521783.1. XM_006521720.1. [P50516-1]
XP_006521784.1. XM_006521721.1. [P50516-1]
UniGeneiMm.217787.

Genome annotation databases

EnsembliENSMUST00000063661; ENSMUSP00000066886; ENSMUSG00000052459. [P50516-1]
ENSMUST00000114666; ENSMUSP00000110314; ENSMUSG00000052459. [P50516-1]
GeneIDi11964.
KEGGimmu:11964.
UCSCiuc007zgu.1. mouse. [P50516-1]
uc007zgw.1. mouse. [P50516-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS28182.1. [P50516-1 ]
RefSeqi NP_031534.2. NM_007508.5. [P50516-1 ]
XP_006521783.1. XM_006521720.1. [P50516-1 ]
XP_006521784.1. XM_006521721.1. [P50516-1 ]
UniGenei Mm.217787.

3D structure databases

ProteinModelPortali P50516.
SMRi P50516. Positions 40-587.
ModBasei Search...

Protein-protein interaction databases

BioGridi 198261. 6 interactions.
IntActi P50516. 108 interactions.
MINTi MINT-1866559.

Protein family/group databases

TCDBi 3.A.2.2.6. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

PTM databases

PhosphoSitei P50516.

Proteomic databases

MaxQBi P50516.
PaxDbi P50516.
PRIDEi P50516.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000063661 ; ENSMUSP00000066886 ; ENSMUSG00000052459 . [P50516-1 ]
ENSMUST00000114666 ; ENSMUSP00000110314 ; ENSMUSG00000052459 . [P50516-1 ]
GeneIDi 11964.
KEGGi mmu:11964.
UCSCi uc007zgu.1. mouse. [P50516-1 ]
uc007zgw.1. mouse. [P50516-2 ]

Organism-specific databases

CTDi 523.
MGIi MGI:1201780. Atp6v1a.

Phylogenomic databases

eggNOGi COG1155.
GeneTreei ENSGT00550000074787.
HOVERGENi HBG053351.
InParanoidi P50516.
KOi K02145.
OMAi ENKITWN.
OrthoDBi EOG7Q8CMM.
PhylomeDBi P50516.
TreeFami TF300811.

Enzyme and pathway databases

Reactomei REACT_198345. Phagosomal maturation (early endosomal stage).
REACT_198515. Transferrin endocytosis and recycling.

Miscellaneous databases

ChiTaRSi ATP6V1A. mouse.
NextBioi 280087.
PROi P50516.
SOURCEi Search...

Gene expression databases

ArrayExpressi P50516.
Bgeei P50516.
CleanExi MM_ATP6V1A.
Genevestigatori P50516.

Family and domain databases

Gene3Di 1.10.1140.10. 1 hit.
3.40.50.300. 2 hits.
HAMAPi MF_00309. ATP_synth_A_arch.
InterProi IPR020003. ATPase_a/bsu_AS.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR005725. ATPase_V1-cplx_asu.
IPR027417. P-loop_NTPase.
IPR022878. V-ATPase_asu.
[Graphical view ]
Pfami PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01042. V-ATPase_V1_A. 1 hit.
PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain and Hippocampus.
  5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  6. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiVATA_MOUSE
AccessioniPrimary (citable) accession number: P50516
Secondary accession number(s): Q3TKS0
, Q3U5W3, Q3U777, Q3UDZ9, Q3US31, Q8CHX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: April 17, 2007
Last modified: September 3, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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