ID Q958E0_TINMA Unreviewed; 55 AA. AC Q958E0; DT 01-DEC-2001, integrated into UniProtKB/TrEMBL. DT 01-DEC-2001, sequence version 1. DT 25-APR-2018, entry version 70. DE RecName: Full=ATP synthase protein 8 {ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00400266}; OS Tinamus major (Great tinamou) (Tetrao major). OG Mitochondrion {ECO:0000313|EMBL:AAK53243.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus. OX NCBI_TaxID=30468 {ECO:0000313|EMBL:AAK53243.1}; RN [1] {ECO:0000313|EMBL:AAK53243.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11370967; DOI=10.1098/rspb.2001.1587; RA Haddrath O., Baker A.J.; RT "Complete mitochondrial DNA genome sequences of extinct birds: ratite RT phylogenetics and the vicariance biogeography hypothesis."; RL Proc. R. Soc. B 268:939-945(2001). RN [2] {ECO:0000313|EMBL:AAK53243.1} RP NUCLEOTIDE SEQUENCE. RA Haddrath O.P.; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP CC synthase or Complex V) produces ATP from ADP in the presence of a CC proton gradient across the membrane which is generated by electron CC transport complexes of the respiratory chain. F-type ATPases CC consist of two structural domains, F(1) - containing the CC extramembraneous catalytic core and F(0) - containing the membrane CC proton channel, linked together by a central stalk and a CC peripheral stalk. During catalysis, ATP synthesis in the catalytic CC domain of F(1) is coupled via a rotary mechanism of the central CC stalk subunits to proton translocation. CC {ECO:0000256|SAAS:SAAS00585567}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CC {ECO:0000256|SAAS:SAAS00585553}. CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane CC {ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00400291}; CC Single-pass membrane protein {ECO:0000256|RuleBase:RU003661, CC ECO:0000256|SAAS:SAAS00400291}. CC -!- SIMILARITY: Belongs to the ATPase protein 8 family. CC {ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00585545}. 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; AF338707; AAK53243.1; -; Genomic_DNA. DR PIR; E90620; E90620. DR RefSeq; NP_115393.1; NC_002781.3. DR GeneID; 806282; -. DR CTD; 4509; -. DR HOVERGEN; HBG017400; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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:ATP synthesis coupled proton transport; IEA:InterPro. DR InterPro; IPR001421; ATP8_metazoa. DR Pfam; PF00895; ATP-synt_8; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|SAAS:SAAS00119314}; KW CF(0) {ECO:0000256|RuleBase:RU003661, ECO:0000256|SAAS:SAAS00119302}; KW Hydrogen ion transport {ECO:0000256|RuleBase:RU003661, KW ECO:0000256|SAAS:SAAS00478108}; KW Ion transport {ECO:0000256|RuleBase:RU003661, KW ECO:0000256|SAAS:SAAS00119304}; KW Membrane {ECO:0000256|SAAS:SAAS00119303, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|RuleBase:RU003661, KW ECO:0000256|SAAS:SAAS00119301, ECO:0000313|EMBL:AAK53243.1}; KW Transmembrane {ECO:0000256|RuleBase:RU003661, KW ECO:0000256|SAAS:SAAS00119312, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00119308, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU003661, KW ECO:0000256|SAAS:SAAS00478149}. FT TRANSMEM 6 24 Helical. {ECO:0000256|SAM:Phobius}. SQ SEQUENCE 55 AA; 6505 MW; EDB0347EA9C1BE11 CRC64; MPQLNPNPWF SIMTSLWIIF LLIMQPKSST TYFPNSPSHK TKPTLKPLSW SWPWT //