ID ATP6_MOUSE Reviewed; 226 AA. AC P00848; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 18-MAR-2008, entry version 62. DE ATP synthase subunit a (ATPase protein 6). GN Name=Mtatp6; Synonyms=Atp6, Atpase6, mt-Atp6; OS Mus musculus (Mouse). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=82137051; PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7; RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.; RT "Sequence and gene organization of mouse mitochondrial DNA."; RL Cell 26:167-180(1981). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=BALB/c; RA Sato M., Matsuki Y., Oguma T., Tadakuma T.; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. 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; J01420; AAB48649.1; -; Genomic_DNA. DR EMBL; V00711; CAA24085.1; -; Genomic_DNA. DR EMBL; AF093677; AAC63375.1; -; mRNA. DR PIR; A01051; PWMS6. DR RefSeq; NP_904333.1; -. DR Ensembl; ENSMUSG00000064357; Mus musculus. DR GeneID; 17705; -. DR KEGG; mmu:17705; -. DR MGI; MGI:99927; mt-Atp6. 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 2: Evidence at transcript level; KW CF(0); Hydrogen ion transport; Inner membrane; Ion transport; KW Membrane; Mitochondrion; Transmembrane; Transport. FT CHAIN 1 226 ATP synthase subunit a. FT /FTId=PRO_0000082139. SQ SEQUENCE 226 AA; 25096 MW; 9941E80F027C4DA7 CRC64; MNENLFASFI TPTMMGFPIV VAIIMFPSIL FPSSKRLINN RLHSFQHWLV KLIIKQMMLI HTPKGRTWTL MIVSLIMFIG STNLLGLLPH TFTPTTQLSM NLSMAIPLWA GAVITGFRHK LKSSLAHFLP QGTPISLIPM LIIIETISLF IQPMALAVRL TANITAGHLL MHLIGGATLV LMNISPPTAT ITFIILLLLT ILEFAVALIQ AYVFTLLVSL YLHDNT //