ID A0A7U0KMR6_CHROW Unreviewed; 226 AA. AC A0A7U0KMR6; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 29-SEP-2021, entry version 2. DE RecName: Full=ATP synthase subunit a {ECO:0000256|ARBA:ARBA00021312, ECO:0000256|RuleBase:RU004450}; GN Name=ATP6 {ECO:0000313|EMBL:QQW47808.1}; OS Chrotogale owstoni (Owston's palm civet). OG Mitochondrion {ECO:0000313|EMBL:QQW47808.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Viverridae; Hemigalinae; OC Chrotogale. OX NCBI_TaxID=94184 {ECO:0000313|EMBL:QQW47808.1}; RN [1] {ECO:0000313|EMBL:QQW47808.1} RP NUCLEOTIDE SEQUENCE. RA Hassanin A.; RL Submitted (NOV-2020) to the EMBL/GenBank/DDBJ databases. 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 {ECO:0000256|ARBA:ARBA00024217}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|RuleBase:RU004450}; Multi-pass membrane CC protein {ECO:0000256|RuleBase:RU004450}. CC -!- SIMILARITY: Belongs to the ATPase A chain family. CC {ECO:0000256|ARBA:ARBA00006810}. 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; MW257222; QQW47808.1; -; Genomic_DNA. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW. DR Gene3D; 1.20.120.220; -; 1. DR InterPro; IPR000568; ATP_synth_F0_asu. DR InterPro; IPR023011; ATP_synth_F0_asu_AS. DR InterPro; IPR035908; F0_ATP_A_sf. 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 {ECO:0000256|ARBA:ARBA00023310}; KW CF(0) {ECO:0000256|ARBA:ARBA00022547}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000313|EMBL:QQW47808.1}; KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}. FT TRANSMEM 6..31 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 67..86 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 98..117 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 137..158 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 164..182 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 189..222 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" SQ SEQUENCE 226 AA; 25041 MW; DADE29908E608A07 CRC64; MNENLFASFI TPTMMGLPIV ILIIMFPSIL FPSPNRLINN RLISLQQWLL QLTTKQMLNI HNYKGQTWAL MLMSLILFIG STNLLGLLPH SFTPTTQLSM NLGMAIPLWA ATVVTGFRHK TKSSLAHFLP QGTPLPLIPM LVIIETISLF IQPMALAVRL TANITAGHLL IHLIGGATLA LMNINMSIAL ITFTILILLT ILEFAVALIQ AYVFTLLVSL YLHDNT //