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 05-OCT-2016, entry version 129. DE RecName: Full=ATP synthase subunit a; DE AltName: Full=F-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; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX 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 [MRNA]. RC STRAIN=BALB/cJ; RA Sato M., Matsuki Y., Oguma T., Tadakuma T.; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=12954771; DOI=10.1093/nar/gkg739; RA Bayona-Bafaluy M.P., Acin-Perez R., Mullikin J.C., Park J.S., RA Moreno-Loshuertos R., Hu P., Perez-Martos A., Fernandez-Silva P., RA Bai Y., Enriquez J.A.; RT "Revisiting the mouse mitochondrial DNA sequence."; RL Nucleic Acids Res. 31:5349-5355(2003). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Heart, and Kidney; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). 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. 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. Component of an ATP synthase CC complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, CC ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, CC ATP5L, USMG5 and MP68 (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein. CC -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000305}. 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 EMBL; AY172335; AAN85127.1; -; Genomic_DNA. DR PIR; A01051; PWMS6. DR RefSeq; NP_904333.1; NC_005089.1. DR ProteinModelPortal; P00848; -. DR SMR; P00848; 10-226. DR STRING; 10090.ENSMUSP00000080996; -. DR PaxDb; P00848; -. DR PeptideAtlas; P00848; -. DR PRIDE; P00848; -. DR Ensembl; ENSMUST00000082408; ENSMUSP00000080996; ENSMUSG00000064357. DR GeneID; 17705; -. DR KEGG; mmu:17705; -. DR CTD; 4508; -. DR MGI; MGI:99927; mt-Atp6. DR eggNOG; KOG4665; Eukaryota. DR eggNOG; COG0356; LUCA. DR GeneTree; ENSGT00390000005568; -. DR HOGENOM; HOG000034185; -. DR HOVERGEN; HBG016693; -. DR InParanoid; P00848; -. DR KO; K02126; -. DR OMA; MFIGSTN; -. DR OrthoDB; EOG091G12DP; -. DR PhylomeDB; P00848; -. DR TreeFam; TF343395; -. DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling. DR PRO; PR:P00848; -. DR Proteomes; UP000000589; Mitochondrion. DR Bgee; ENSMUSG00000064357; -. DR ExpressionAtlas; P00848; baseline and differential. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005753; C:mitochondrial proton-transporting ATP synthase complex; ISS:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:Ensembl. DR GO; GO:0015078; F:hydrogen ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl. DR Gene3D; 1.20.120.220; -; 1. DR InterPro; IPR000568; ATPase_F0-cplx_asu. DR InterPro; IPR023011; ATPase_F0-cplx_asu_AS. DR PANTHER; PTHR11410; PTHR11410; 1. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR SUPFAM; SSF81336; SSF81336; 1. DR TIGRFAMs; TIGR01131; ATP_synt_6_or_A; 1. DR PROSITE; PS00449; ATPASE_A; 1. PE 1: Evidence at protein level; KW ATP synthesis; CF(0); Complete proteome; Hydrogen ion transport; KW Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 226 ATP synthase subunit a. FT /FTId=PRO_0000082139. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 97 117 Helical. {ECO:0000255}. FT TRANSMEM 138 158 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 189 209 Helical. {ECO:0000255}. 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 //