ID F5HPX7_MERGA Unreviewed; 227 AA. AC F5HPX7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 27-NOV-2024, entry version 35. DE RecName: Full=ATP synthase subunit a {ECO:0000256|ARBA:ARBA00021312, ECO:0000256|RuleBase:RU004450}; GN Name=ATP6 {ECO:0000313|EMBL:BAK38523.1}; OS Merluccius gayi (South Pacific hake) (Merluccius gayi peruanus). OG Mitochondrion {ECO:0000313|EMBL:BAK38523.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Zeiogadaria; Gadariae; Gadiformes; Gadoidei; Merlucciidae; Merluccius. OX NCBI_TaxID=89948 {ECO:0000313|EMBL:BAK38523.1}; RN [1] {ECO:0000313|EMBL:BAK38523.1} RP NUCLEOTIDE SEQUENCE. RA Namikoshi A., Takashima Y., Iguchi J., Yanagimoto T., Yamashita M.; RT "Species identification of Alaska pollock, Gadus spp., and Micromesistius RT spp. in cod roe products using a PCR-based method."; RL Fish. Sci. 77:671-678(2011). 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. Key component of the CC proton channel; it may play a direct role in the translocation of CC protons across the membrane. {ECO:0000256|ARBA:ARBA00002070}. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core CC - and CF(0) - the membrane proton channel. CF(1) has five subunits: CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main CC subunits: a, b and c. {ECO:0000256|ARBA:ARBA00011648}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU004450}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU004450}. Mitochondrion membrane CC {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004225}. CC -!- SIMILARITY: Belongs to the ATPase A chain family. CC {ECO:0000256|ARBA:ARBA00006810}. 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; AB571070; BAK38523.1; -; Genomic_DNA. DR AlphaFoldDB; F5HPX7; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:TreeGrafter. DR CDD; cd00310; ATP-synt_Fo_a_6; 1. DR FunFam; 1.20.120.220:FF:000004; ATP synthase subunit a; 1. DR Gene3D; 1.20.120.220; ATP synthase, F0 complex, subunit A; 1. DR InterPro; IPR000568; ATP_synth_F0_asu. DR InterPro; IPR023011; ATP_synth_F0_asu_AS. DR InterPro; IPR045083; ATP_synth_F0_asu_bact/mt. DR InterPro; IPR035908; F0_ATP_A_sf. DR NCBIfam; TIGR01131; ATP_synt_6_or_A; 1. DR PANTHER; PTHR11410; ATP SYNTHASE SUBUNIT A; 1. DR PANTHER; PTHR11410:SF0; ATP SYNTHASE SUBUNIT A; 1. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR SUPFAM; SSF81336; F1F0 ATP synthase subunit A; 1. DR PROSITE; PS00449; ATPASE_A; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310}; KW CF(0) {ECO:0000256|ARBA:ARBA00022547}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000313|EMBL:BAK38523.1}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 12..31 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 43..63 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 69..92 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 99..118 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 138..159 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 171..199 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 205..223 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 227 AA; 25107 MW; 7A9A6C8D89429664 CRC64; MTLSLFDQFE SPTFMGIPLI MLALALPWLL FPAPTHRWLN SRVLALQGWF ISNFTSQIFS PLNRGGHKWA LLLSALMIFL LTLNTLGLLP YTFTPTTQLA LNMALAVPLW LATVILGLRH QITHALAHFL PEGTPTPLIP VLIIIETISL FIRPLALGVR LTANLTAGHL LIHLVSSAAF VLLPLMPTVA FLTALLLFML TLLEIAVALI QAYVFVLLLS LYLQENV //