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 16-OCT-2013, entry version 81. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3017940; RA Breen G.A.M., Miller D.L., Holmans P.L., Welch G.; RT "Mitochondrial DNA of two independent oligomycin-resistant Chinese RT hamster ovary cell lines contains a single nucleotide change in the RT ATPase 6 gene."; RL J. Biol. Chem. 261:11680-11685(1986). 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). 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; M14311; AAA68616.1; -; Genomic_DNA. DR PIR; B25188; B25188. DR ProteinModelPortal; P14413; -. DR HOVERGEN; HBG016693; -. DR GO; GO:0016021; C:integral to 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:hydrogen ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IEA:InterPro. 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 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 ATP synthase subunit a. FT /FTId=PRO_0000082110. FT TRANSMEM 10 30 Helical; (Potential). FT TRANSMEM 68 88 Helical; (Potential). FT TRANSMEM 97 117 Helical; (Potential). FT TRANSMEM 138 158 Helical; (Potential). FT TRANSMEM 164 184 Helical; (Potential). FT TRANSMEM 189 209 Helical; (Potential). 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 //