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ATP synthase subunit a

 R9ZP27_HUMAN            Unreviewed;       226 AA.
R9ZP27;
18-SEP-2013, integrated into UniProtKB/TrEMBL.
18-SEP-2013, sequence version 1.
25-APR-2018, entry version 21.
RecName: Full=ATP synthase subunit a {ECO:0000256|RuleBase:RU004450};
Homo sapiens (Human).
Mitochondrion {ECO:0000313|EMBL:AGO43922.1}.
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000313|EMBL:AGO43922.1};
[1] {ECO:0000313|EMBL:AGO43922.1}
NUCLEOTIDE SEQUENCE.
PubMed=24153443;
Aure K., Dubourg O., Jardel C., Clarysse L., Sternberg D.,
Fournier E., Laforet P., Streichenberger N., Petiot P.,
Gervais-Bernard H., Vial C., Bedat-Millet A.L., Drouin-Garraud V.,
Bouillaud F., Vandier C., Fontaine B., Lombes A.;
"Episodic weakness due to mitochondrial DNA MT-ATP6/8 mutations.";
Neurology 81:1810-1818(2013).
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000256|RuleBase:RU004450}; Multi-pass membrane protein
{ECO:0000256|RuleBase:RU004450}.
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EMBL; KC890790; AGO43922.1; -; Genomic_DNA.
PeptideAtlas; R9ZP27; -.
eggNOG; KOG4665; Eukaryota.
eggNOG; COG0356; LUCA.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
Gene3D; 1.20.120.220; -; 1.
InterPro; IPR000568; ATP_synth_F0_asu.
InterPro; IPR035908; F0_ATP_A_sf.
Pfam; PF00119; ATP-synt_A; 1.
PRINTS; PR00123; ATPASEA.
SUPFAM; SSF81336; SSF81336; 1.
TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1.
4: Predicted;
Membrane {ECO:0000256|SAM:Phobius};
Mitochondrion {ECO:0000313|EMBL:AGO43922.1};
Transmembrane {ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAM:Phobius}.
TRANSMEM 6 31 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 67 86 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 98 117 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 137 158 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 164 184 Helical. {ECO:0000256|SAM:Phobius}.
TRANSMEM 191 213 Helical. {ECO:0000256|SAM:Phobius}.
SEQUENCE 226 AA; 24743 MW; 613BFF1429FA5258 CRC64;
MNENLFASFI APTILGLPAA VLIILFPPLL IPTSKYLINN RLITTQQWLI KLTSKQMMTM
HNTKGRTWSL MLVSLIIFIA TTNLLGLLPH SFTPTTQLSM NLAMAIPLWA GAVIMGFRSK
IKNALAHFLP QGTPTPLIPM LVIIETISLL IQPMALAARL TANITAGHLL MHLIGSATLA
MSTINLPSTL IIFTILILLT ILEIAVALIQ AYVFTLLVSP YLHDNT


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Kits Elisa; taq POLYMERASE

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Related Genes :
[ATP5MC2 ATP5G2 PSEC0033] ATP synthase F(0) complex subunit C2, mitochondrial (ATP synthase lipid-binding protein) (ATP synthase membrane subunit c locus 2) (ATP synthase proteolipid P2) (ATP synthase proton-transporting mitochondrial F(0) complex subunit C2) (ATPase protein 9) (ATPase subunit c)
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[aro-1 aro-2 aro-4 aro-5 aro-9 B14H13.20 NCU016321] Pentafunctional AROM polypeptide [Includes: 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4); 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS); Shikimate kinase (SK) (EC 2.7.1.71); 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10); Shikimate dehydrogenase (EC 1.1.1.25)]
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[30888962] ATP Synthase: Structure, Function and Inhibition.
[30883359] Neuronal Apolipoprotein E4 Expression Results in Proteome-Wide Alterations and Compromises Bioenergetic Capacity by Disrupting Mitochondrial Function.
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