ID A0A0H3V0W4_ADADE Unreviewed; 202 AA. AC A0A0H3V0W4; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 11-NOV-2015, entry version 2. DE RecName: Full=Cytochrome c oxidase subunit 1 {ECO:0000256|RuleBase:RU000369}; DE EC=1.9.3.1 {ECO:0000256|RuleBase:RU000369}; DE Flags: Fragment; GN Name=COI {ECO:0000313|EMBL:AJA91779.1}; OS Adalia decempunctata (Ten-spotted ladybird beetle). OG Mitochondrion {ECO:0000313|EMBL:AJA91779.1}. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Coleoptera; Polyphaga; OC Cucujiformia; Coccinellidae; Coccinellinae; Coccinellini; Adalia. OX NCBI_TaxID=115343 {ECO:0000313|EMBL:AJA91779.1}; RN [1] {ECO:0000313|EMBL:AJA91779.1} RP NUCLEOTIDE SEQUENCE. RA Pinol J., Mir G., Gomez-Polo P., Agusti N.; RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Cytochrome c oxidase is the component of the respiratory CC chain that catalyzes the reduction of oxygen to water. Subunits 1- CC 3 form the functional core of the enzyme complex. CO I is the CC catalytic subunit of the enzyme. Electrons originating in CC cytochrome c are transferred via the copper A center of subunit 2 CC and heme A of subunit 1 to the bimetallic center formed by heme A3 CC and copper B. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. {ECO:0000256|RuleBase:RU000369}. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000256|RuleBase:RU000369}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000256|RuleBase:RU000369}; Multi-pass membrane protein CC {ECO:0000256|RuleBase:RU000369}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000256|RuleBase:RU000369}. 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; KJ467504; AJA91779.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR Gene3D; 1.20.210.10; -; 1. DR InterPro; IPR000883; COX1. DR InterPro; IPR023616; Cyt_c_Oxase_su1_dom. DR PANTHER; PTHR10422; PTHR10422; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; SSF81442; 1. DR PROSITE; PS50855; COX1; 1. PE 3: Inferred from homology; KW Copper {ECO:0000256|RuleBase:RU000369}; KW Electron transport {ECO:0000256|RuleBase:RU000369}; KW Heme {ECO:0000256|RuleBase:RU000369}; KW Iron {ECO:0000256|RuleBase:RU000369}; KW Membrane {ECO:0000256|RuleBase:RU000369, ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:AJA91779.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000369}; KW Oxidoreductase {ECO:0000256|RuleBase:RU000369}; KW Respiratory chain {ECO:0000256|RuleBase:RU000369}; KW Transmembrane {ECO:0000256|RuleBase:RU000369, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|RuleBase:RU000369}. FT TRANSMEM 29 59 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 80 102 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 122 147 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 159 186 Helical. {ECO:0000256|SAM:Phobius}. FT NON_TER 1 1 {ECO:0000313|EMBL:AJA91779.1}. FT NON_TER 202 202 {ECO:0000313|EMBL:AJA91779.1}. SQ SEQUENCE 202 AA; 21665 MW; 1F0A370F05D7C675 CRC64; WAGMVGTSLS IIIRLELGTT NSLIGNDQIY NVIVTAHAFI MIFFMVMPIM IGGFGNWLVP LMIGAPDMAF PRLNNMSFWL LPPALTLLIS SSIVEMGAGT GWTVYPPLSS NLAHNGPSVD LVIFSLHLAG ISSILGAVNF ISTIMNMRPN GMNLDKTPLF VWSVLITAIL LLLSLPVLAG AITMLLTDRN INTSFFDPTG GG //