ID ATP6_POLOR Reviewed; 227 AA. AC Q95913; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 04-NOV-2008, entry version 54. DE RecName: Full=ATP synthase subunit a; DE AltName: Full=F-ATPase protein 6; GN Name=mt-atp6; Synonyms=atp6, atpase6, mtatp6; OS Polypterus ornatipinnis (Ornate bichir). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Polypteriformes; Polypteridae; Polypterus. OX NCBI_TaxID=49895; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=97070832; PubMed=8913758; RA Noack K., Zardoya R., Meyer A.; RT "The complete mitochondrial DNA sequence of the bichir (Polypterus RT ornatipinnis), a basal ray-finned fish: ancient establishment of the RT consensus vertebrate gene order."; RL Genetics 144:1165-1180(1996). CC -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(O) 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. Key component of the CC proton channel; it may play a direct role in the translocation of CC protons across the membrane. CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has three main subunits: a, b and c. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein. CC -!- SIMILARITY: Belongs to the ATPase A chain family. 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; U62532; AAC60310.1; -; Genomic_DNA. DR PIR; T11459; T11459. DR RefSeq; NP_008321.1; -. DR GeneID; 808032; -. DR HOVERGEN; Q95913; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, c...; IEA:UniProtKB-KW. DR GO; GO:0015078; F:hydrogen ion transmembrane transporter acti...; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR000568; ATPase_F0_A. DR Gene3D; G3DSA:1.20.120.220; ATPase_F0_A; 1. DR PANTHER; PTHR11410; ATPase_F0_A; 1. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1. DR PROSITE; PS00449; ATPASE_A; 1. PE 3: Inferred from homology; KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Transmembrane; Transport. FT CHAIN 1 227 ATP synthase subunit a. FT /FTId=PRO_0000082157. FT TRANSMEM 14 34 Potential. FT TRANSMEM 69 89 Potential. FT TRANSMEM 98 118 Potential. FT TRANSMEM 139 159 Potential. FT TRANSMEM 165 185 Potential. FT TRANSMEM 189 209 Potential. SQ SEQUENCE 227 AA; 25250 MW; C08D61938B918A4C CRC64; MTLSFLDQFA SQSFLGIPLI AIAILIPWML FPSPYKRWMS NRLITFQSWF IARTTNQLML PLNTGAHKWA MILTALLLFL MTLNLLGLLP YTFTPTTQLS MNMALAVPLW LATVLIGMRN QPTHSLAHLL PEGTPTPLIP ILIIIETISL FIRPLALGVR LTANLTAGHL LIQLISTATF VMLSIMPTIA TLTFIVLALL TILEIAVAMI QAYVLVLLLS LYLQENV //