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 10-JUN-2008, entry version 50. DE ATP synthase subunit a (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:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. 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 CF(0); Hydrogen ion transport; Inner membrane; Ion transport; KW Membrane; Mitochondrion; Transmembrane; Transport. FT CHAIN 1 227 ATP synthase subunit a. FT /FTId=PRO_0000082157. 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 //