ID ATP6_CRIGR Reviewed; 226 AA. AC P14413; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1990, sequence version 1. DT 03-AUG-2022, entry version 100. DE RecName: Full=ATP synthase subunit a; DE AltName: Full=F-ATPase protein 6; GN Name=MT-ATP6; Synonyms=ATP6, ATPASE6, MTATP6; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; OC Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3017940; DOI=10.1016/s0021-9258(18)67297-7; RA Breen G.A.M., Miller D.L., Holmans P.L., Welch G.; RT "Mitochondrial DNA of two independent oligomycin-resistant Chinese hamster RT ovary cell lines contains a single nucleotide change in the ATPase 6 RT gene."; RL J. Biol. Chem. 261:11680-11685(1986). 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; M14311; AAA68616.1; -; Genomic_DNA. DR PIR; B25188; B25188. DR AlphaFoldDB; P14413; -. DR SMR; P14413; -. 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:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW. DR GO; GO:0015078; F:proton transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015986; P:proton motive force-driven ATP synthesis; IEA:InterPro. 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 3: Inferred from homology; KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Membrane; KW Mitochondrion; Mitochondrion inner membrane; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..226 FT /note="ATP synthase subunit a" FT /id="PRO_0000082110" FT TRANSMEM 10..30 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; 25040 MW; E90B091319B533F4 CRC64; MNENLFSSFI TPTLMGLPII ILIIMFPPVI MTSSKRLVNN RFHTFQQWLI KLITKQMMAI HSPKGRTWSL MLASLIIFIG STNLLGLLPH TFTPTTQLSM NLGMAIPPWA GAVILGFRHK MKDSLAHFLP QGTPIPLIPM LVIIETISLF IQPMALAVRL TANITAGHLL MHLIGGATLV LTSISLPTAM ITFIILIMLT ILEFAVALIQ AYVFTLLVSL YLHDNT //