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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 ATPase isoform VA68) (Vacuolar proton pump subunit alpha)

 VATA_HUMAN              Reviewed;         617 AA.
P38606; B2RBR8; B7Z1R5; D3DN75; Q53YD9; Q96DY6; Q9UHY3;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
02-AUG-2002, sequence version 2.
05-DEC-2018, entry version 188.
RecName: Full=V-type proton ATPase catalytic subunit A;
Short=V-ATPase subunit A;
EC=7.1.2.2;
AltName: Full=V-ATPase 69 kDa subunit;
AltName: Full=Vacuolar ATPase isoform VA68;
AltName: Full=Vacuolar proton pump subunit alpha;
Name=ATP6V1A; Synonyms=ATP6A1, ATP6V1A1, VPP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal adrenal gland, and Leukocyte;
PubMed=8463241;
van Hille B., Richener H., Evans D.B., Green J.R., Bilbe G.;
"Identification of two subunit A isoforms of the vacuolar H(+)-ATPase
in human osteoclastoma.";
J. Biol. Chem. 268:7075-7080(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hypothalamus;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Amygdala, and Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Kidney;
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).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2), CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-136 AND SER-384, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
INVOLVEMENT IN ARCL2D, TISSUE SPECIFICITY, AND VARIANTS ARCL2D ASP-72
AND CYS-338.
PubMed=28065471; DOI=10.1016/j.ajhg.2016.12.010;
Van Damme T., Gardeitchik T., Mohamed M., Guerrero-Castillo S.,
Freisinger P., Guillemyn B., Kariminejad A., Dalloyaux D.,
van Kraaij S., Lefeber D.J., Syx D., Steyaert W., De Rycke R.,
Hoischen A., Kamsteeg E.J., Wong S.Y., van Scherpenzeel M., Jamali P.,
Brandt U., Nijtmans L., Korenke G.C., Chung B.H., Mak C.C.,
Hausser I., Kornak U., Fischer-Zirnsak B., Strom T.M., Meitinger T.,
Alanay Y., Utine G.E., Leung P.K., Ghaderi-Sohi S., Coucke P.,
Symoens S., De Paepe A., Thiel C., Haack T.B., Malfait F., Morava E.,
Callewaert B., Wevers R.A.;
"Mutations in ATP6V1E1 or ATP6V1A cause autosomal-recessive cutis
laxa.";
Am. J. Hum. Genet. 100:216-227(2017).
[14]
FUNCTION.
PubMed=28296633; DOI=10.7554/eLife.22693;
Miles A.L., Burr S.P., Grice G.L., Nathan J.A.;
"The vacuolar-ATPase complex and assembly factors, TMEM199 and
CCDC115, control HIF1alpha prolyl hydroxylation by regulating cellular
iron levels.";
Elife 6:E22693-E22693(2017).
[15]
INVOLVEMENT IN IECEE3, VARIANTS IECEE3 ARG-27; TYR-100; ASN-349 AND
GLY-371, VARIANTS ASN-11 AND ARG-249, CHARACTERIZATION OF VARIANTS
IECEE3 TYR-100 AND ASN-349, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=29668857; DOI=10.1093/brain/awy092;
Fassio A., Esposito A., Kato M., Saitsu H., Mei D., Marini C.,
Conti V., Nakashima M., Okamoto N., Olmez Turker A., Albuz B.,
Semerci Guenduez C.N., Yanagihara K., Belmonte E., Maragliano L.,
Ramsey K., Balak C., Siniard A., Narayanan V., Ohba C., Shiina M.,
Ogata K., Matsumoto N., Benfenati F., Guerrini R.;
"De novo mutations of the ATP6V1A gene cause developmental
encephalopathy with epilepsy.";
Brain 141:1703-1718(2018).
-!- 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 (PubMed:28296633). May play a
role in neurite development and synaptic connectivity
(PubMed:29668857). {ECO:0000269|PubMed:28296633,
ECO:0000269|PubMed:29668857}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
EC=7.1.2.2;
-!- 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).
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29668857}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P38606-1; Sequence=Displayed;
Name=2;
IsoId=P38606-2; Sequence=VSP_056408;
Note=No experimental confirmation available. Initiator Met-1 is
removed. Contains a N-acetylalanine at position 2.
{ECO:0000244|PubMed:22814378};
-!- TISSUE SPECIFICITY: High expression in the skin.
{ECO:0000269|PubMed:28065471}.
-!- DISEASE: Cutis laxa, autosomal recessive, 2D (ARCL2D)
[MIM:617403]: A form of cutis laxa, a disorder characterized by an
excessive congenital skin wrinkling, a large fontanelle with
delayed closure, a typical facial appearance with downslanting
palpebral fissures, and a general connective tissue weakness. Most
ARCL2D patients exhibit severe hypotonia as well as cardiovascular
and neurologic involvement. {ECO:0000269|PubMed:28065471}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Epileptic encephalopathy, infantile or early childhood, 3
(IECEE3) [MIM:618012]: A form of epileptic encephalopathy, a
heterogeneous group of severe childhood onset epilepsies
characterized by refractory seizures, neurodevelopmental
impairment, and poor prognosis. Development is normal prior to
seizure onset, after which cognitive and motor delays become
apparent. IECEE3 is an autosomal dominant form characterized by
onset of seizures in the first years of life.The severity of the
phenotype is highly variable: some patients may be non-verbal and
non-ambulatory with spastic quadriparesis and poor eye contact,
whereas others have moderate intellectual disability.
{ECO:0000269|PubMed:29668857}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
{ECO:0000305}.
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EMBL; L09235; AAA83249.1; -; mRNA.
EMBL; AF113129; AAF14870.1; -; mRNA.
EMBL; BT006672; AAP35318.1; -; mRNA.
EMBL; AK293804; BAH11601.1; -; mRNA.
EMBL; AK314779; BAG37315.1; -; mRNA.
EMBL; AC079944; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79625.1; -; Genomic_DNA.
EMBL; CH471052; EAW79626.1; -; Genomic_DNA.
EMBL; BC013138; AAH13138.1; -; mRNA.
CCDS; CCDS2976.1; -. [P38606-1]
PIR; B46091; B46091.
RefSeq; NP_001681.2; NM_001690.3. [P38606-1]
UniGene; Hs.477155; -.
ProteinModelPortal; P38606; -.
SMR; P38606; -.
BioGrid; 107007; 104.
CORUM; P38606; -.
IntAct; P38606; 94.
MINT; P38606; -.
STRING; 9606.ENSP00000273398; -.
DrugBank; DB00630; Alendronic acid.
DrugBank; DB06733; Bafilomycin A1.
DrugBank; DB06734; Bafilomycin B1.
DrugBank; DB01077; Etidronic acid.
DrugBank; DB01133; Tiludronic acid.
TCDB; 3.A.2.2.4; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
iPTMnet; P38606; -.
PhosphoSitePlus; P38606; -.
SwissPalm; P38606; -.
BioMuta; ATP6V1A; -.
DMDM; 22096378; -.
EPD; P38606; -.
MaxQB; P38606; -.
PaxDb; P38606; -.
PeptideAtlas; P38606; -.
PRIDE; P38606; -.
ProteomicsDB; 55303; -.
DNASU; 523; -.
Ensembl; ENST00000273398; ENSP00000273398; ENSG00000114573. [P38606-1]
GeneID; 523; -.
KEGG; hsa:523; -.
UCSC; uc003eao.4; human. [P38606-1]
CTD; 523; -.
DisGeNET; 523; -.
EuPathDB; HostDB:ENSG00000114573.9; -.
GeneCards; ATP6V1A; -.
HGNC; HGNC:851; ATP6V1A.
HPA; CAB006910; -.
HPA; HPA035083; -.
HPA; HPA035084; -.
MalaCards; ATP6V1A; -.
MIM; 607027; gene.
MIM; 617403; phenotype.
MIM; 618012; phenotype.
neXtProt; NX_P38606; -.
OpenTargets; ENSG00000114573; -.
PharmGKB; PA25152; -.
eggNOG; KOG1352; Eukaryota.
eggNOG; COG1155; LUCA.
GeneTree; ENSGT00550000074787; -.
HOGENOM; HOG000161057; -.
HOVERGEN; HBG053351; -.
InParanoid; P38606; -.
KO; K02145; -.
OMA; QQLAKWS; -.
OrthoDB; EOG091G03SR; -.
PhylomeDB; P38606; -.
TreeFam; TF300811; -.
BioCyc; MetaCyc:HS03781-MONOMER; -.
Reactome; R-HSA-1222556; ROS, RNS production in phagocytes.
Reactome; R-HSA-77387; Insulin receptor recycling.
Reactome; R-HSA-917977; Transferrin endocytosis and recycling.
Reactome; R-HSA-983712; Ion channel transport.
ChiTaRS; ATP6V1A; human.
GeneWiki; ATP6V1A; -.
GenomeRNAi; 523; -.
PRO; PR:P38606; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114573; Expressed in 238 organ(s), highest expression level in Brodmann (1909) area 23.
CleanEx; HS_ATP6V1A; -.
ExpressionAtlas; P38606; baseline and differential.
Genevisible; P38606; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0016469; C:proton-transporting two-sector ATPase complex; TAS:ProtInc.
GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro.
GO; GO:0005774; C:vacuolar membrane; IBA:GO_Central.
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; IMP:UniProtKB.
GO; GO:0036295; P:cellular response to increased oxygen levels; IMP:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0016241; P:regulation of macroautophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0033572; P:transferrin transport; TAS:Reactome.
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;
Acetylation; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Disease mutation; Epilepsy; Hydrogen ion transport;
Ion transport; Nucleotide-binding; Phosphoprotein; Polymorphism;
Reference proteome; Translocase; Transport.
CHAIN 1 617 V-type proton ATPase catalytic subunit A.
/FTId=PRO_0000144560.
NP_BIND 250 257 ATP. {ECO:0000255}.
MOD_RES 136 136 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 33 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056408.
VARIANT 11 11 D -> N (found in a patient with autism
spectrum disorder; unknown pathological
significance).
{ECO:0000269|PubMed:29668857}.
/FTId=VAR_080994.
VARIANT 27 27 P -> R (in IECEE3; unknown pathological
significance).
{ECO:0000269|PubMed:29668857}.
/FTId=VAR_080995.
VARIANT 72 72 G -> D (in ARCL2D; dbSNP:rs1060505037).
{ECO:0000269|PubMed:28065471}.
/FTId=VAR_078606.
VARIANT 100 100 D -> Y (in IECEE3; loss-of-function
variant leading to increased pH in
intracellular organelles; affects neurite
arborization and impairs the formation
and maintenance of excitatory synapses,
when tested in a heterologous system; not
effect on subcellular location).
{ECO:0000269|PubMed:29668857}.
/FTId=VAR_080996.
VARIANT 249 249 P -> R (found in a patient with severe
developmental disorder; unknown
pathological significance).
{ECO:0000269|PubMed:29668857}.
/FTId=VAR_080997.
VARIANT 338 338 R -> C (in ARCL2D; dbSNP:rs1060505036).
{ECO:0000269|PubMed:28065471}.
/FTId=VAR_078607.
VARIANT 349 349 D -> N (in IECEE3; gain-of-function
variant leading to decreased pH in
intracellular organelles; affects neurite
arborization and impairs the formation
and maintenance of excitatory synapses,
when tested in a heterologous system; not
effect on subcellular location).
{ECO:0000269|PubMed:29668857}.
/FTId=VAR_080998.
VARIANT 371 371 D -> G (in IECEE3; unknown pathological
significance).
{ECO:0000269|PubMed:29668857}.
/FTId=VAR_080999.
CONFLICT 71 71 S -> C (in Ref. 1; AAA83249).
{ECO:0000305}.
CONFLICT 89 90 EL -> DV (in Ref. 1; AAA83249).
{ECO:0000305}.
CONFLICT 211 211 V -> A (in Ref. 1; AAA83249 and 2;
AAF14870). {ECO:0000305}.
SEQUENCE 617 AA; 68304 MW; DB409A8731D772CB CRC64;
MDFSKLPKIL DEDKESTFGY VHGVSGPVVT ACDMAGAAMY ELVRVGHSEL VGEIIRLEGD
MATIQVYEET SGVSVGDPVL RTGKPLSVEL GPGIMGAIFD GIQRPLSDIS SQTQSIYIPR
GVNVSALSRD IKWDFTPCKN LRVGSHITGG DIYGIVSENS LIKHKIMLPP RNRGTVTYIA
PPGNYDTSDV VLELEFEGVK EKFTMVQVWP 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
LSNMIAFYDM ARRAVETTAQ SDNKITWSII REHMGDILYK LSSMKFKDPL KDGEAKIKSD
YAQLLEDMQN AFRSLED


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