ID A0A6G8IZX6_OVIAM Unreviewed; 66 AA. AC A0A6G8IZX6; DT 12-AUG-2020, integrated into UniProtKB/TrEMBL. DT 12-AUG-2020, sequence version 1. DT 14-DEC-2022, entry version 7. DE RecName: Full=ATP synthase protein 8 {ECO:0000256|ARBA:ARBA00019651, ECO:0000256|RuleBase:RU003661}; GN Name=ATP8 {ECO:0000313|EMBL:QIM59236.1}; OS Ovis ammon ammon. OG Mitochondrion {ECO:0000313|EMBL:QIM59236.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Caprinae; Ovis. OX NCBI_TaxID=156212 {ECO:0000313|EMBL:QIM59236.1}; RN [1] {ECO:0000313|EMBL:QIM59236.1} RP NUCLEOTIDE SEQUENCE. RA Cong W., Yongfang Y.; RL Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QIM59236.1} RP NUCLEOTIDE SEQUENCE. RA Wang C., Xu H., Li D., Wu J., Wen A., Xie M., Wang Q., Zhu G., Ni Q., RA Zhang M., Yao Y.; RT "Phylogenetic and characterization of the complete mitochondrial genome RT relationship of Argali sheep (Ovis ammon)."; RL Mitochondrial DNA Part B Resour 5:273-274(2020). CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or CC Complex V) produces ATP from ADP in the presence of a proton gradient CC across the membrane which is generated by electron transport complexes CC of the respiratory chain. F-type ATPases consist of two structural CC domains, F(1) - containing the extramembraneous catalytic core and F(0) CC - containing the membrane proton channel, linked together by a central CC stalk and a peripheral stalk. During catalysis, ATP synthesis in the CC catalytic domain of F(1) is coupled via a rotary mechanism of the CC central stalk subunits to proton translocation. Part of the complex CC F(0) domain. Minor subunit located with subunit a in the membrane. CC {ECO:0000256|ARBA:ARBA00024864}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion CC membrane {ECO:0000256|ARBA:ARBA00004304, CC ECO:0000256|RuleBase:RU003661}; Single-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004304, ECO:0000256|RuleBase:RU003661}. CC -!- SIMILARITY: Belongs to the ATPase protein 8 family. CC {ECO:0000256|ARBA:ARBA00008892, ECO:0000256|RuleBase:RU003661}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MN564883; QIM59236.1; -; Genomic_DNA. DR AlphaFoldDB; A0A6G8IZX6; -. DR GO; GO:0000276; C:mitochondrial proton-transporting ATP synthase complex, coupling factor F(o); IEA:InterPro. DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro. DR InterPro; IPR039017; ATP8_mammal. DR InterPro; IPR001421; ATP8_metazoa. DR PANTHER; PTHR13722; ATP SYNTHASE PROTEIN 8; 1. DR Pfam; PF00895; ATP-synt_8; 1. PE 3: Inferred from homology; KW Acetylation {ECO:0000256|ARBA:ARBA00022990}; KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310}; KW CF(0) {ECO:0000256|ARBA:ARBA00022547, ECO:0000256|RuleBase:RU003661}; KW Hydrogen ion transport {ECO:0000256|RuleBase:RU003661}; KW Ion transport {ECO:0000256|RuleBase:RU003661}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU003661, ECO:0000313|EMBL:QIM59236.1}; KW Transmembrane {ECO:0000256|RuleBase:RU003661, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003661}. FT TRANSMEM 6..24 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 66 AA; 7880 MW; AECCC68AF6499092 CRC64; MPQLDTSTWL TMILSMFLVL FIIFQLKISK HNFYHNPELM TTKAPKQNTP WETKWTKIYL PLSLPL //