ID A0A068LLL7_PHAHR Unreviewed; 221 AA. AC A0A068LLL7; DT 01-OCT-2014, integrated into UniProtKB/TrEMBL. DT 01-OCT-2014, sequence version 1. DT 14-DEC-2022, entry version 23. DE RecName: Full=ATP synthase subunit a {ECO:0000256|ARBA:ARBA00021312, ECO:0000256|RuleBase:RU004450}; DE Flags: Fragment; OS Phalacrocorax harrisi (Flightless cormorant) (Nannopterum harrisi). OG Mitochondrion {ECO:0000313|EMBL:AIE56211.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Phalacrocoracidae; OC Phalacrocorax. OX NCBI_TaxID=473964 {ECO:0000313|EMBL:AIE56211.1}; RN [1] {ECO:0000313|EMBL:AIE56211.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=19523526; DOI=10.1016/j.ympev.2009.06.002; RA Kennedy M., Valle C.A., Spencer H.G.; RT "The phylogenetic position of the Galapagos Cormorant."; RL Mol. Phylogenet. Evol. 53:94-98(2009). RN [2] {ECO:0000313|EMBL:AIE56211.1} RP NUCLEOTIDE SEQUENCE. RA Kennedy M., Valle C.A., Spencer H.G.; RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases. 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. {ECO:0000256|ARBA:ARBA00002070}. 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; GQ205457; AIE56211.1; -; Genomic_DNA. DR AlphaFoldDB; A0A068LLL7; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. 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; ATP SYNTHASE SUBUNIT A; 1. DR Pfam; PF00119; ATP-synt_A; 1. DR PRINTS; PR00123; ATPASEA. DR SUPFAM; SSF81336; F1F0 ATP synthase subunit A; 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:0000313|EMBL:AIE56211.1}; 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 12..32 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 69..93 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 99..118 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 170..189 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 195..219 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT NON_TER 221 FT /evidence="ECO:0000313|EMBL:AIE56211.1" SQ SEQUENCE 221 AA; 24381 MW; 9AE7220A2149AF5B CRC64; MNLSFFDQFT SPHLLGIPLI LLSMLIPALL LPSPDNRWIT NRLSTLQSWL LHLITKQLMM PLNKKGHKWA LILTSLMFLL LMTNLLGLLP YTFTPTTQLS MNMALAFPLW LATLLTGLRN QPTISLGHLL PEGTPTPLIP ALIMIETTSL LIRPLALGVR LTANLTAGHL LIQLISTATT MLLPIMPAIS ILTALILLLL TILEVAVAMI QAYVFVLLLS L //