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 23-FEB-2022, entry version 162. 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; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC 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., Bai Y., RA 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 expression."; RL Cell 143:1174-1189(2010). 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. 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. Component of an ATP synthase complex composed of CC ATP5PB, ATP5MC1, ATP5F1E, ATP5PD, ATP5ME, ATP5PF, ATP5MF, MT-ATP6, MT- CC ATP8, ATP5F1A, ATP5F1B, ATP5F1D, ATP5F1C, ATP5PO, ATP5MG, ATP5MK and CC ATP5MJ (By similarity). Interacts with DNAJC30; interaction is direct CC (By similarity). {ECO:0000250|UniProtKB:P00846, CC ECO:0000250|UniProtKB:P00847}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass membrane CC 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 SMR; P00848; -. DR IntAct; P00848; 1. DR STRING; 10090.ENSMUSP00000080996; -. DR jPOST; P00848; -. DR PaxDb; P00848; -. DR PeptideAtlas; P00848; -. DR PRIDE; P00848; -. DR ProteomicsDB; 265181; -. DR Antibodypedia; 58052; 69 antibodies from 21 providers. DR Ensembl; ENSMUST00000082408; ENSMUSP00000080996; ENSMUSG00000064357. DR GeneID; 17705; -. DR KEGG; mmu:17705; -. DR CTD; 4508; -. DR MGI; MGI:99927; mt-Atp6. DR VEuPathDB; HostDB:ENSMUSG00000064357; -. DR eggNOG; KOG4665; Eukaryota. DR GeneTree; ENSGT00390000005568; -. DR HOGENOM; CLU_041018_0_2_1; -. DR InParanoid; P00848; -. DR OMA; AMAIPLW; -. DR OrthoDB; 1095315at2759; -. DR PhylomeDB; P00848; -. DR TreeFam; TF343395; -. DR Reactome; R-MMU-163210; Formation of ATP by chemiosmotic coupling. DR Reactome; R-MMU-8949613; Cristae formation. DR ChiTaRS; mt-Atp6; mouse. DR PRO; PR:P00848; -. DR Proteomes; UP000000589; Mitochondrion. DR RNAct; P00848; protein. DR Bgee; ENSMUSG00000064357; Expressed in epiblast (generic) and 102 other tissues. DR ExpressionAtlas; P00848; baseline and differential. 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; HDA:MGI. 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:Ensembl. DR GO; GO:0007568; P:aging; IEA:Ensembl. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central. DR GO; GO:0042776; P:mitochondrial ATP synthesis coupled proton transport; ISO:MGI. DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl. DR Gene3D; 1.20.120.220; -; 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 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); Hydrogen ion transport; Ion transport; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..226 FT /note="ATP synthase subunit a" FT /id="PRO_0000082139" FT TRANSMEM 6..26 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 68..88 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 97..117 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 138..158 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 164..184 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 189..209 FT /note="Helical" FT /evidence="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 //