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ATP synthase subunit alpha, mitochondrial

 ATPA_HUMAN              Reviewed;         553 AA.
P25705; A8K092; B4DY56; K7ENP3; Q53XX6; Q8IXV2; Q96FB4; Q96HW2;
Q96IR6; Q9BTV8;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
05-DEC-2018, entry version 222.
RecName: Full=ATP synthase subunit alpha, mitochondrial {ECO:0000305};
AltName: Full=ATP synthase F1 subunit alpha {ECO:0000312|HGNC:HGNC:823};
Flags: Precursor;
Name=ATP5F1A {ECO:0000312|HGNC:HGNC:823};
Synonyms=ATP5A, ATP5A1 {ECO:0000312|HGNC:HGNC:823},
ATP5AL2 {ECO:0000312|HGNC:HGNC:823}, ATPM {ECO:0000312|HGNC:HGNC:823};
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=Lung tumor;
PubMed=1830491; DOI=10.1016/0167-4781(91)90183-M;
Kataoka H., Biswas C.;
"Nucleotide sequence of a cDNA for the alpha subunit of human
mitochondrial ATP synthase.";
Biochim. Biophys. Acta 1089:393-395(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Retinoblastoma;
PubMed=8428659; DOI=10.1016/0378-1119(93)90124-L;
Godbout R., Bisgrove D.A., Honore L.H., Day R.S. III;
"Amplification of the gene encoding the alpha-subunit of the
mitochondrial ATP synthase complex in a human retinoblastoma cell
line.";
Gene 123:195-201(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
TISSUE=Colon tumor;
PubMed=8086450; DOI=10.1016/0167-4781(94)90255-0;
Akiyama S., Endo H., Inohara N., Ohta S., Kagawa Y.;
"Gene structure and cell type-specific expression of the human ATP
synthase alpha subunit.";
Biochim. Biophys. Acta 1219:129-140(1994).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Small intestine, and Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lung, Retina, and Uterus;
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]
PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 44-59.
TISSUE=Leukemic T-cell;
PubMed=19892738; DOI=10.1073/pnas.0908958106;
Xu G., Shin S.B., Jaffrey S.R.;
"Global profiling of protease cleavage sites by chemoselective
labeling of protein N-termini.";
Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009).
[9]
PROTEIN SEQUENCE OF 46-83; 89-103; 134-161; 176-182; 219-230; 242-252;
306-316; 335-347; 403-416; 435-463 AND 507-527, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 46-73; 104-123; 134-161; 219-230; 232-239;
306-316; 335-347; 403-416; 442-463 AND 507-527, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (MAR-2005) to UniProtKB.
[11]
PROTEIN SEQUENCE OF 134-141 AND 335-339.
TISSUE=Heart;
PubMed=7498159; DOI=10.1002/elps.11501601192;
Kovalyov L.I., Shishkin S.S., Efimochkin A.S., Kovalyova M.A.,
Ershova E.S., Egorov T.A., Musalyamov A.K.;
"The major protein expression profile and two-dimensional protein
database of human heart.";
Electrophoresis 16:1160-1169(1995).
[12]
INTERACTION WITH PLG, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBCELLULAR LOCATION.
PubMed=10077593; DOI=10.1073/pnas.96.6.2811;
Moser T.L., Stack M.S., Asplin I., Enghild J.J., Hojrup P.,
Everitt L., Hubchak S., Schnaper H.W., Pizzo S.V.;
"Angiostatin binds ATP synthase on the surface of human endothelial
cells.";
Proc. Natl. Acad. Sci. U.S.A. 96:2811-2816(1999).
[13]
INTERACTION WITH ATPAF2.
PubMed=11410595; DOI=10.1074/jbc.M104133200;
Wang Z.-G., White P.S., Ackerman S.H.;
"Atp11p and Atp12p are assembly factors for the F(1)-ATPase in human
mitochondria.";
J. Biol. Chem. 276:30773-30778(2001).
[14]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[15]
INTERACTION WITH HRG, IDENTIFICATION BY MASS SPECTROMETRY, AND
SUBCELLULAR LOCATION.
PubMed=19285951; DOI=10.1016/j.bbamem.2009.03.005;
Ohta T., Ikemoto Y., Usami A., Koide T., Wakabayashi S.;
"High affinity interaction between histidine-rich glycoprotein and the
cell surface type ATP synthase on T-cells.";
Biochim. Biophys. Acta 1788:1099-1107(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-261; LYS-434;
LYS-498; LYS-506 AND LYS-539, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
INTERACTION WITH BLOC1S1, AND ACETYLATION.
PubMed=22309213; DOI=10.1042/BJ20120118;
Scott I., Webster B.R., Li J.H., Sack M.N.;
"Identification of a molecular component of the mitochondrial acetyl
transferase program; a novel role for GCN5L1.";
Biochem. J. 443:655-661(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-53; SER-65; SER-76;
SER-166 AND SER-184, 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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND 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).
[22]
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).
[23]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=30146159; DOI=10.1016/j.cell.2018.07.032;
Qi B., Han M.;
"Microbial Siderophore Enterobactin Promotes Mitochondrial Iron Uptake
and Development of the Host via Interaction with ATP Synthase.";
Cell 0:0-0(2018).
[24]
VARIANT MC5DN4 CYS-329.
PubMed=23599390; DOI=10.1093/brain/awt086;
Jonckheere A.I., Renkema G.H., Bras M., van den Heuvel L.P.,
Hoischen A., Gilissen C., Nabuurs S.B., Huynen M.A., de Vries M.C.,
Smeitink J.A., Rodenburg R.J.;
"A complex V ATP5A1 defect causes fatal neonatal mitochondrial
encephalopathy.";
Brain 136:1544-1554(2013).
[25]
VARIANT COXPD22 CYS-321, AND INVOLVEMENT IN COXPD22.
PubMed=23596069; DOI=10.1212/WNL.0b013e3182918c40;
Lieber D.S., Calvo S.E., Shanahan K., Slate N.G., Liu S.,
Hershman S.G., Gold N.B., Chapman B.A., Thorburn D.R., Berry G.T.,
Schmahmann J.D., Borowsky M.L., Mueller D.M., Sims K.B., Mootha V.K.;
"Targeted exome sequencing of suspected mitochondrial disorders.";
Neurology 80:1762-1770(2013).
-!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP
synthase or Complex V) produces ATP from ADP in the presence of a
proton gradient across the membrane which is generated by electron
transport complexes of the respiratory chain. F-type ATPases
consist of two structural domains, F(1) - containing the
extramembraneous catalytic core, and F(0) - containing the
membrane proton channel, linked together by a central stalk and a
peripheral stalk. During catalysis, ATP synthesis in the catalytic
domain of F(1) is coupled via a rotary mechanism of the central
stalk subunits to proton translocation. Subunits alpha and beta
form the catalytic core in F(1). Rotation of the central stalk
against the surrounding alpha(3)beta(3) subunits leads to
hydrolysis of ATP in three separate catalytic sites on the beta
subunits. Subunit alpha does not bear the catalytic high-affinity
ATP-binding sites (By similarity). Binds the bacterial siderophore
enterobactin and can promote mitochondrial accumulation of
enterobactin-derived iron ions (PubMed:30146159).
{ECO:0000250|UniProtKB:P19483, ECO:0000269|PubMed:30146159}.
-!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
core - and CF(0) - the membrane proton channel. CF(1) has five
subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0)
has three main subunits: a, b and c (By similarity). Interacts
with ATPAF2 (PubMed:11410595). Interacts with HRG; the interaction
occurs on the surface of T-cells and alters the cell morphology
when associated with concanavalin (in vitro) (PubMed:19285951).
Interacts with PLG (angiostatin peptide); the interaction inhibits
most of the angiogenic properties of angiostatin
(PubMed:10077593). Component of an ATP synthase complex composed
of ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-
ATP6, MT-ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG,
ATP5MD and MP68 (By similarity). Interacts with BLOC1S1
(PubMed:22309213). Interacts with BCL2L1 isoform BCL-X(L); the
interaction mediates the association of BCL2L1 isoform BCL-X(L)
with the mitochondrial membrane F(1)F(0) ATP synthase and enhances
neurons metabolic efficency (By similarity). Interacts with CLN5
and PPT1 (By similarity). {ECO:0000250|UniProtKB:P15999,
ECO:0000250|UniProtKB:P19483, ECO:0000250|UniProtKB:Q03265,
ECO:0000269|PubMed:10077593, ECO:0000269|PubMed:11410595,
ECO:0000269|PubMed:19285951, ECO:0000269|PubMed:22309213}.
-!- INTERACTION:
P78537:BLOC1S1; NbExp=2; IntAct=EBI-351437, EBI-348630;
Q9NTG7:SIRT3; NbExp=2; IntAct=EBI-351437, EBI-724621;
P63104:YWHAZ; NbExp=3; IntAct=EBI-351437, EBI-347088;
-!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:30146159}.
Mitochondrion inner membrane {ECO:0000250|UniProtKB:P19483};
Peripheral membrane protein {ECO:0000250|UniProtKB:P19483}; Matrix
side {ECO:0000250|UniProtKB:P19483}. Cell membrane
{ECO:0000269|PubMed:10077593}; Peripheral membrane protein
{ECO:0000269|PubMed:10077593}; Extracellular side
{ECO:0000269|PubMed:10077593}. Note=Colocalizes with HRG on the
cell surface of T-cells (PubMed:19285951).
{ECO:0000269|PubMed:19285951}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P25705-1; Sequence=Displayed;
Name=2;
IsoId=P25705-2; Sequence=VSP_045129;
Name=3;
IsoId=P25705-3; Sequence=VSP_054688;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Fetal lung, heart, liver, gut and kidney.
Expressed at higher levels in the fetal brain, retina and spinal
cord. {ECO:0000269|PubMed:8428659}.
-!- PTM: The N-terminus is blocked.
-!- PTM: Acetylated on lysine residues. BLOC1S1 is required for
acetylation. {ECO:0000269|PubMed:22309213}.
-!- DISEASE: Combined oxidative phosphorylation deficiency 22
(COXPD22) [MIM:616045]: A mitochondrial disorder characterized by
intrauterine growth retardation, microcephaly, hypotonia,
pulmonary hypertension, failure to thrive, encephalopathy, and
heart failure. {ECO:0000269|PubMed:23596069}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Mitochondrial complex V deficiency, nuclear type 4
(MC5DN4) [MIM:615228]: A mitochondrial disorder with heterogeneous
clinical manifestations including dysmorphic features, psychomotor
retardation, hypotonia, growth retardation, cardiomyopathy,
enlarged liver, hypoplastic kidneys and elevated lactate levels in
urine, plasma and cerebrospinal fluid.
{ECO:0000269|PubMed:23599390}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: The siderophore enterobactin (Ent) produced by
enteric bacteria binds Fe(3+) and helps bacteria scavenge iron
ions from the environment (PubMed:30146159). As a consequence, the
mammalian siderocalin LCN2 plays an important role in defense
against bacterial infections by sequestering iron bound to
microbial siderophores. LCN2 can also bind iron bound to
endogenous or nutrient-derived iron chelators and plays an
important role in cellular iron homeostasis. Enterobactin produced
by non-pathogenic E.coli strains can facilitate mitochondrial iron
assimilation, suggesting that iron bound to siderophores from non-
pathogenic bacteria may contribute to iron absorption by the host
(PubMed:30146159). {ECO:0000269|PubMed:30146159, ECO:0000305}.
-!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
{ECO:0000305}.
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EMBL; X59066; CAA41789.1; -; mRNA.
EMBL; X65460; CAA46452.1; -; mRNA.
EMBL; D14710; BAA03531.1; -; mRNA.
EMBL; D28126; BAA05672.1; -; Genomic_DNA.
EMBL; BT007209; AAP35873.1; -; mRNA.
EMBL; AK092735; BAG52604.1; -; mRNA.
EMBL; AK289457; BAF82146.1; -; mRNA.
EMBL; AK302272; BAG63618.1; -; mRNA.
EMBL; AC012569; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003119; AAH03119.1; -; mRNA.
EMBL; BC007299; AAH07299.1; -; mRNA.
EMBL; BC008028; AAH08028.2; -; mRNA.
EMBL; BC011384; AAH11384.1; -; mRNA.
EMBL; BC016046; AAH16046.1; -; mRNA.
EMBL; BC019310; AAH19310.1; -; mRNA.
EMBL; BC039135; AAH39135.2; -; mRNA.
EMBL; BC064562; AAH64562.1; -; mRNA.
EMBL; BC067385; AAH67385.1; -; mRNA.
CCDS; CCDS11927.1; -. [P25705-1]
CCDS; CCDS58620.1; -. [P25705-2]
CCDS; CCDS59315.1; -. [P25705-3]
PIR; S17193; PWHUA.
RefSeq; NP_001001935.1; NM_001001935.2. [P25705-2]
RefSeq; NP_001001937.1; NM_001001937.1. [P25705-1]
RefSeq; NP_001244263.1; NM_001257334.1. [P25705-3]
RefSeq; NP_001244264.1; NM_001257335.1. [P25705-2]
RefSeq; NP_004037.1; NM_004046.5. [P25705-1]
UniGene; Hs.298280; -.
ProteinModelPortal; P25705; -.
SMR; P25705; -.
BioGrid; 106987; 211.
CORUM; P25705; -.
DIP; DIP-32871N; -.
IntAct; P25705; 89.
MINT; P25705; -.
STRING; 9606.ENSP00000282050; -.
ChEMBL; CHEMBL2062351; -.
DrugBank; DB07384; 1-ACETYL-2-CARBOXYPIPERIDINE.
DrugBank; DB07394; AUROVERTIN B.
DrugBank; DB08399; PICEATANNOL.
DrugBank; DB04216; Quercetin.
iPTMnet; P25705; -.
PhosphoSitePlus; P25705; -.
SwissPalm; P25705; -.
BioMuta; ATP5A1; -.
DMDM; 114517; -.
OGP; P25705; -.
REPRODUCTION-2DPAGE; P25705; -.
UCD-2DPAGE; P25705; -.
EPD; P25705; -.
PaxDb; P25705; -.
PeptideAtlas; P25705; -.
PRIDE; P25705; -.
ProteomicsDB; 54283; -.
TopDownProteomics; P25705-1; -. [P25705-1]
DNASU; 498; -.
Ensembl; ENST00000282050; ENSP00000282050; ENSG00000152234. [P25705-1]
Ensembl; ENST00000398752; ENSP00000381736; ENSG00000152234. [P25705-1]
Ensembl; ENST00000590665; ENSP00000467037; ENSG00000152234. [P25705-3]
Ensembl; ENST00000593152; ENSP00000465477; ENSG00000152234. [P25705-2]
GeneID; 498; -.
KEGG; hsa:498; -.
UCSC; uc010dnl.2; human. [P25705-1]
CTD; 498; -.
DisGeNET; 498; -.
EuPathDB; HostDB:ENSG00000152234.15; -.
GeneCards; ATP5F1A; -.
HGNC; HGNC:823; ATP5F1A.
HPA; CAB013067; -.
HPA; HPA040622; -.
HPA; HPA044202; -.
MalaCards; ATP5F1A; -.
MIM; 164360; gene.
MIM; 615228; phenotype.
MIM; 616045; phenotype.
neXtProt; NX_P25705; -.
OpenTargets; ENSG00000152234; -.
Orphanet; 254913; Isolated ATP synthase deficiency.
PharmGKB; PA25115; -.
eggNOG; KOG1353; Eukaryota.
eggNOG; COG0056; LUCA.
GeneTree; ENSGT00550000074846; -.
HOVERGEN; HBG001536; -.
InParanoid; P25705; -.
KO; K02132; -.
OMA; GNAQIKS; -.
OrthoDB; EOG091G0D1M; -.
PhylomeDB; P25705; -.
TreeFam; TF300321; -.
Reactome; R-HSA-1268020; Mitochondrial protein import.
Reactome; R-HSA-163210; Formation of ATP by chemiosmotic coupling.
Reactome; R-HSA-8949613; Cristae formation.
ChiTaRS; ATP5A1; human.
GenomeRNAi; 498; -.
PMAP-CutDB; P25705; -.
PRO; PR:P25705; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000152234; Expressed in 240 organ(s), highest expression level in heart.
CleanEx; HS_ATP5A1; -.
ExpressionAtlas; P25705; baseline and differential.
Genevisible; P25705; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:CAFA.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB.
GO; GO:0000275; C:mitochondrial proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045259; C:proton-transporting ATP synthase complex; IDA:CAFA.
GO; GO:0043531; F:ADP binding; IBA:GO_Central.
GO; GO:0043532; F:angiostatin binding; IPI:CAFA.
GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
GO; GO:0042288; F:MHC class I protein binding; IDA:UniProtKB.
GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IMP:CAFA.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0022857; F:transmembrane transporter activity; IC:UniProtKB.
GO; GO:0006754; P:ATP biosynthetic process; IMP:CAFA.
GO; GO:0046034; P:ATP metabolic process; IBA:GO_Central.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central.
GO; GO:0042407; P:cristae formation; TAS:Reactome.
GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
GO; GO:0006629; P:lipid metabolic process; ISS:UniProtKB.
GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:UniProtKB.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IGI:CAFA.
GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central.
CDD; cd01132; F1_ATPase_alpha; 1.
Gene3D; 1.20.150.20; -; 1.
Gene3D; 2.40.30.20; -; 1.
HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
InterPro; IPR023366; ATP_synth_asu-like_sf.
InterPro; IPR000793; ATP_synth_asu_C.
InterPro; IPR038376; ATP_synth_asu_C_sf.
InterPro; IPR033732; ATP_synth_F1_a.
InterPro; IPR005294; ATP_synth_F1_asu.
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; IPR027417; P-loop_NTPase.
Pfam; PF00006; ATP-synt_ab; 1.
Pfam; PF00306; ATP-synt_ab_C; 1.
Pfam; PF02874; ATP-synt_ab_N; 1.
PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
SUPFAM; SSF50615; SSF50615; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00962; atpA; 1.
PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP synthesis; ATP-binding;
Cell membrane; CF(1); Complete proteome; Direct protein sequencing;
Disease mutation; Glycoprotein; Hydrogen ion transport; Ion transport;
Membrane; Methylation; Mitochondrion; Mitochondrion inner membrane;
Nucleotide-binding; Phosphoprotein; Polymorphism;
Primary mitochondrial disease; Reference proteome; Transit peptide;
Transport.
TRANSIT 1 43 Mitochondrion.
{ECO:0000269|PubMed:19892738}.
CHAIN 44 553 ATP synthase subunit alpha,
mitochondrial.
/FTId=PRO_0000002424.
NP_BIND 213 220 ATP. {ECO:0000250|UniProtKB:P19483}.
NP_BIND 473 475 ATP. {ECO:0000250|UniProtKB:P19483}.
SITE 413 413 Required for activity. {ECO:0000250}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 65 65 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 76 76 Phosphoserine; alternate.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 123 123 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 126 126 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 132 132 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 134 134 Phosphothreonine.
{ECO:0000250|UniProtKB:P15999}.
MOD_RES 161 161 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 161 161 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 166 166 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 167 167 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 167 167 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 204 204 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 230 230 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 230 230 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 239 239 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 239 239 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 240 240 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 261 261 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 261 261 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 305 305 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 305 305 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 427 427 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 427 427 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 434 434 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 498 498 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 498 498 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 506 506 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 506 506 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 531 531 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 531 531 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 539 539 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 539 539 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q03265}.
MOD_RES 541 541 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q03265}.
CARBOHYD 76 76 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
VAR_SEQ 1 50 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045129.
VAR_SEQ 140 161 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_054688.
VARIANT 32 32 A -> S (in dbSNP:rs2228437).
/FTId=VAR_048369.
VARIANT 321 321 Y -> C (in COXPD22; dbSNP:rs587777788).
{ECO:0000269|PubMed:23596069}.
/FTId=VAR_071982.
VARIANT 329 329 R -> C (in MC5DN4; dbSNP:rs587776960).
{ECO:0000269|PubMed:23599390}.
/FTId=VAR_069769.
CONFLICT 162 162 G -> V (in Ref. 5; BAG63618).
{ECO:0000305}.
CONFLICT 183 183 I -> T (in Ref. 5; BAG63618).
{ECO:0000305}.
CONFLICT 329 329 R -> L (in Ref. 5; AAH39135).
{ECO:0000305}.
CONFLICT 356 356 N -> D (in Ref. 5; BAG63618).
{ECO:0000305}.
CONFLICT 510 510 A -> D (in Ref. 5; AAH11384).
{ECO:0000305}.
CONFLICT 529 529 D -> E (in Ref. 5; AAH11384).
{ECO:0000305}.
SEQUENCE 553 AA; 59751 MW; AA47BBB8EDA77EAC CRC64;
MLSVRVAAAV VRALPRRAGL VSRNALGSSF IAARNFHASN THLQKTGTAE MSSILEERIL
GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS GLKGMSLNLE PDNVGVVVFG
NDKLIKEGDI VKRTGAIVDV PVGEELLGRV VDALGNAIDG KGPIGSKTRR RVGLKAPGII
PRISVREPMQ TGIKAVDSLV PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGSDEKK
KLYCIYVAIG QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKMNDAFG
GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF YKGIRPAINV GLSVSRVGSA
AQTRAMKQVA GTMKLELAQY REVAAFAQFG SDLDAATQQL LSRGVRLTEL LKQGQYSPMA
IEEQVAVIYA GVRGYLDKLE PSKITKFENA FLSHVVSQHQ ALLGTIRADG KISEQSDAKL
KEIVTNFLAG FEA


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