ID E2DQN9_9CHON Unreviewed; 218 AA. AC E2DQN9; DT 30-NOV-2010, integrated into UniProtKB/TrEMBL. DT 30-NOV-2010, sequence version 1. DT 29-OCT-2014, entry version 20. 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:ADK26838.1}; OS Odontaspis ferox (smalltooth sand tiger). OG Mitochondrion {ECO:0000313|EMBL:ADK26838.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes; OC Elasmobranchii; Galeomorphii; Galeoidea; Lamniformes; Odontaspididae; OC Odontaspis. OX NCBI_TaxID=57989 {ECO:0000313|EMBL:ADK26838.1}; RN [1] {ECO:0000313|EMBL:ADK26838.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S53 {ECO:0000313|EMBL:ADK26838.1}; RX PubMed=20457263; DOI=10.1016/j.ympev.2010.04.042; RA Straube N., Iglesias S.P., Sellos D.Y., Kriwet J., Schliewen U.K.; RT "Molecular phylogeny and node time estimation of bioluminescent RT Lantern Sharks (Elasmobranchii: Etmopteridae)."; RL Mol. Phylogenet. Evol. 56:905-917(2010). 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; GU130673; ADK26838.1; -; Genomic_DNA. DR UniPathway; UPA00705; -. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. 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}; KW Metal-binding {ECO:0000256|RuleBase:RU000369}; KW Mitochondrion {ECO:0000256|RuleBase:RU000369, KW ECO:0000313|EMBL:ADK26838.1}; 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 Transport {ECO:0000256|RuleBase:RU000369}. FT NON_TER 1 1 {ECO:0000313|EMBL:ADK26838.1}. FT NON_TER 218 218 {ECO:0000313|EMBL:ADK26838.1}. SQ SEQUENCE 218 AA; 23311 MW; 24F96DF5DEA04663 CRC64; LYLIFGAWAG MVGMALSLLI RAELGQPGSL LGDDQIYNVI VTAHAFVMIF FMVMPVMIGG FGNWLVPLMI GAPDMAFPRM NNMSFWLLPP SFLLLLASAG VEAGAGTGWT VYPPLAGNLA HAGASVDLAI FSLHLAGISS ILASINFITT IINMKPPAIS QYQTPLFVWS ILVTTILLLL SLPVLAAGIT MLLTDRNLNT TFFDPAGGGD PILYQHLF //