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ATP synthase protein 8

 R9ZR79_HUMAN            Unreviewed;        68 AA.
R9ZR79;
18-SEP-2013, integrated into UniProtKB/TrEMBL.
18-SEP-2013, sequence version 1.
31-JAN-2018, entry version 19.
RecName: Full=ATP synthase protein 8 {ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00400266};
Homo sapiens (Human).
Mitochondrion {ECO:0000313|EMBL:AGO43926.1}.
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000313|EMBL:AGO43926.1};
[1] {ECO:0000313|EMBL:AGO43926.1}
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).
-!- 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.
{ECO:0000256|SAAS:SAAS00585567}.
-!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic
core - and CF(0) - the membrane proton channel.
{ECO:0000256|SAAS:SAAS00585553}.
-!- SUBCELLULAR LOCATION: Mitochondrion membrane
{ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00400291};
Single-pass membrane protein {ECO:0000256|RuleBase:RU003661,
ECO:0000256|SAAS:SAAS00400291}.
-!- SIMILARITY: Belongs to the ATPase protein 8 family.
{ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00585545}.
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EMBL; KC890794; AGO43926.1; -; Genomic_DNA.
PeptideAtlas; R9ZR79; -.
eggNOG; ENOG410J587; Eukaryota.
eggNOG; ENOG411154N; LUCA.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro.
GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro.
GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro.
InterPro; IPR001421; ATP8_metazoa.
Pfam; PF00895; ATP-synt_8; 1.
3: Inferred from homology;
ATP synthesis {ECO:0000256|SAAS:SAAS00119314};
CF(0) {ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00119302};
Hydrogen ion transport {ECO:0000256|RuleBase:RU003661,
ECO:0000256|SAAS:SAAS00119302};
Ion transport {ECO:0000256|RuleBase:RU003661,
ECO:0000256|SAAS:SAAS00119302};
Membrane {ECO:0000256|SAAS:SAAS00119308, ECO:0000256|SAM:Phobius};
Mitochondrion {ECO:0000256|RuleBase:RU003661,
ECO:0000256|SAAS:SAAS00119301, ECO:0000313|EMBL:AGO43926.1};
Transmembrane {ECO:0000256|SAAS:SAAS00119308,
ECO:0000256|SAM:Phobius};
Transmembrane helix {ECO:0000256|SAAS:SAAS00119308,
ECO:0000256|SAM:Phobius};
Transport {ECO:0000256|RuleBase:RU003661,
ECO:0000256|SAAS:SAAS00119302}.
TRANSMEM 16 36 Helical. {ECO:0000256|SAM:Phobius}.
SEQUENCE 68 AA; 7996 MW; B175770C3AD76922 CRC64;
MPQLNTTVWP TMTTPMLLTL FLITQLKMLN TNYHLLPSPK PMKMKNYNKP WEPKWTKICS
LHSLPPQS


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