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V-type proton ATPase catalytic subunit A (V-ATPase subunit A) (EC 3.6.3.14) (V-ATPase 69 kDa subunit) (Vacuolar proton pump subunit alpha)

 VATA_MOUSE              Reviewed;         617 AA.
P50516; Q3TKS0; Q3U5W3; Q3U777; Q3UDZ9; Q3US31; Q8CHX2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
17-APR-2007, sequence version 2.
12-SEP-2018, entry version 165.
RecName: Full=V-type proton ATPase catalytic subunit A;
Short=V-ATPase subunit A;
EC=3.6.3.14;
AltName: Full=V-ATPase 69 kDa subunit;
AltName: Full=Vacuolar proton pump subunit alpha;
Name=Atp6v1a; Synonyms=Atp6a1, Atp6a2, Atp6v1a1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8741845; DOI=10.1091/mbc.7.1.129;
Laitala T., Howell M.L., Dean G.E., Vaananen H.K.;
"Resorption-cycle-dependent polarization of mRNAs for different
subunits of V-ATPase in bone-resorbing osteoclasts.";
Mol. Biol. Cell 7:129-142(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, and Head;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 45-56; 143-163; 242-251; 253-262; 266-280;
324-338; 514-530 AND 599-613, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
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.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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. In aerobic conditions, involved in intracellular iron
homeostasis, thus triggering the activity of Fe(2+) prolyl
hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and
subsequent proteasomal degradation (By similarity).
{ECO:0000250|UniProtKB:P38606}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate +
H(+)(Out).
-!- SUBUNIT: 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).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P50516-1; Sequence=Displayed;
Name=2;
IsoId=P50516-2; Sequence=VSP_024628, VSP_024629;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
{ECO:0000305}.
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EMBL; U13837; AAC52410.1; -; Genomic_DNA.
EMBL; AK140873; BAE24506.1; -; mRNA.
EMBL; AK149833; BAE29112.1; -; mRNA.
EMBL; AK152785; BAE31494.1; -; mRNA.
EMBL; AK153403; BAE31963.1; -; mRNA.
EMBL; AK154869; BAE32890.1; -; mRNA.
EMBL; AK160792; BAE36015.1; -; mRNA.
EMBL; AK166857; BAE39074.1; -; mRNA.
EMBL; AK170721; BAE41978.1; -; mRNA.
EMBL; BC038392; AAH38392.1; -; mRNA.
CCDS; CCDS28182.1; -. [P50516-1]
RefSeq; NP_031534.2; NM_007508.5. [P50516-1]
RefSeq; XP_006521783.1; XM_006521720.3.
RefSeq; XP_006521784.1; XM_006521721.2. [P50516-1]
RefSeq; XP_011244111.1; XM_011245809.2.
UniGene; Mm.217787; -.
ProteinModelPortal; P50516; -.
SMR; P50516; -.
BioGrid; 198261; 9.
IntAct; P50516; 108.
MINT; P50516; -.
STRING; 10090.ENSMUSP00000066886; -.
TCDB; 3.A.2.2.6; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
iPTMnet; P50516; -.
PhosphoSitePlus; P50516; -.
SwissPalm; P50516; -.
EPD; P50516; -.
MaxQB; P50516; -.
PaxDb; P50516; -.
PeptideAtlas; P50516; -.
PRIDE; P50516; -.
TopDownProteomics; P50516-1; -. [P50516-1]
Ensembl; ENSMUST00000063661; ENSMUSP00000066886; ENSMUSG00000052459. [P50516-1]
Ensembl; ENSMUST00000114666; ENSMUSP00000110314; ENSMUSG00000052459. [P50516-1]
GeneID; 11964; -.
KEGG; mmu:11964; -.
UCSC; uc007zgu.1; mouse. [P50516-1]
UCSC; uc007zgw.1; mouse. [P50516-2]
CTD; 523; -.
MGI; MGI:1201780; Atp6v1a.
eggNOG; KOG1352; Eukaryota.
eggNOG; COG1155; LUCA.
GeneTree; ENSGT00550000074787; -.
HOVERGEN; HBG053351; -.
InParanoid; P50516; -.
KO; K02145; -.
OMA; QQLAKWS; -.
OrthoDB; EOG091G03SR; -.
PhylomeDB; P50516; -.
TreeFam; TF300811; -.
Reactome; R-MMU-1222556; ROS, RNS production in phagocytes.
Reactome; R-MMU-77387; Insulin receptor recycling.
Reactome; R-MMU-917977; Transferrin endocytosis and recycling.
Reactome; R-MMU-983712; Ion channel transport.
ChiTaRS; Atp6v1a; mouse.
PRO; PR:P50516; -.
Proteomes; UP000000589; Chromosome 16.
Bgee; ENSMUSG00000052459; Expressed in 321 organ(s), highest expression level in cingulate cortex.
CleanEx; MM_ATP6V1A; -.
ExpressionAtlas; P50516; baseline and differential.
Genevisible; P50516; MM.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IBA:GO_Central.
GO; GO:0005902; C:microvillus; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central.
GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro.
GO; GO:0046034; P:ATP metabolic process; IEA:InterPro.
GO; GO:0006879; P:cellular iron ion homeostasis; ISS:UniProtKB.
GO; GO:0036295; P:cellular response to increased oxygen levels; ISS:UniProtKB.
Gene3D; 1.10.1140.10; -; 1.
Gene3D; 2.40.30.20; -; 1.
HAMAP; MF_00309; ATP_synth_A_arch; 1.
InterPro; IPR031686; ATP-synth_a_Xtn.
InterPro; IPR023366; ATP_synth_asu-like_sf.
InterPro; IPR020003; ATPase_a/bsu_AS.
InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
InterPro; IPR024034; ATPase_F1/V1_b/a_C.
InterPro; IPR005725; ATPase_V1-cplx_asu.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR022878; V-ATPase_asu.
PANTHER; PTHR43607; PTHR43607; 1.
Pfam; PF00006; ATP-synt_ab; 1.
Pfam; PF02874; ATP-synt_ab_N; 1.
Pfam; PF16886; ATP-synt_ab_Xtn; 1.
SUPFAM; SSF50615; SSF50615; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR01042; V-ATPase_V1_A; 1.
PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome;
Direct protein sequencing; Hydrogen ion transport; Hydrolase;
Ion transport; Nucleotide-binding; Phosphoprotein; Reference proteome;
Transport.
CHAIN 1 617 V-type proton ATPase catalytic subunit A.
/FTId=PRO_0000144561.
NP_BIND 250 257 ATP. {ECO:0000255}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000250|UniProtKB:P38606}.
VAR_SEQ 499 509 ASLAETDKITL -> VRGGCTGCHAG (in isoform
2). {ECO:0000303|PubMed:16141072}.
/FTId=VSP_024628.
VAR_SEQ 510 617 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_024629.
CONFLICT 86 86 L -> R (in Ref. 1; AAC52410).
{ECO:0000305}.
CONFLICT 189 189 D -> N (in Ref. 1; AAC52410).
{ECO:0000305}.
CONFLICT 302 302 V -> A (in Ref. 1; AAC52410).
{ECO:0000305}.
CONFLICT 330 330 G -> V (in Ref. 2; BAE39074).
{ECO:0000305}.
CONFLICT 487 487 E -> G (in Ref. 1; AAC52410).
{ECO:0000305}.
CONFLICT 616 616 E -> G (in Ref. 2; BAE31963).
{ECO:0000305}.
SEQUENCE 617 AA; 68326 MW; D46AC76D9C7580A7 CRC64;
MDFSKLPKIR DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL VGEIIRLEGD
MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD GIQRPLSDIS SQTQSIYIPR
GVNVSALSRD IKWEFIPSKN LRVGSHITGG DIYGIVNENS LIKHKIMLPP RNRGSVTYIA
PPGNYDASDV VLELEFEGVK EKFSMVQVWP VRQVRPVTEK LPANHPLLTG QRVLDALFPC
VQGGTTAIPG AFGCGKTVIS QSLSKYSNSD VIIYVGCGER GNEMSEVLRD FPELTMEVDG
KVESIMKRTA LVANTSNMPV AAREASIYTG ITLSEYFRDM GYHVSMMADS TSRWAEALRE
ISGRLAEMPA DSGYPAYLGA RLASFYERAG RVKCLGNPER EGSVSIVGAV SPPGGDFSDP
VTSATLGIVQ VFWGLDKKLA QRKHFPSVNW LISYSKYMRA LDEYYDKHFT EFVPLRTKAK
EILQEEEDLA EIVQLVGKAS LAETDKITLE VAKLIKDDFL QQNGYTPYDR FCPFYKTVGM
LSNMISFYDM ARRAVETTAQ SDNKITWSII REHMGEILYK LSSMKFKDPV KDGEAKIKAD
YAQLLEDMQN AFRSLED


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