ID Q2Y0B2_PROLO Unreviewed; 196 AA. AC Q2Y0B2; DT 20-DEC-2005, integrated into UniProtKB/TrEMBL. DT 20-DEC-2005, sequence version 1. DT 18-MAY-2010, entry version 28. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=1.9.3.1; DE Flags: Fragment; GN Name=COI; OS Procyon lotor (Raccoon). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; OC Procyonidae; Procyon. OX NCBI_TaxID=9654; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=16213754; DOI=10.1016/j.ympev.2005.07.019; RA Bardeleben C., Moore R.L., Wayne R.K.; RT "A molecular phylogeny of the Canidae based on six nuclear loci."; RL Mol. Phylogenet. Evol. 37:815-831(2005). 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 (By similarity). CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase 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; DQ093084; AAZ83630.1; -; Genomic_DNA. DR SMR; Q2Y0B2; 1-196. DR GO; GO:0016021; C:integral to 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:EC. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0009060; P:aerobic respiration; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR000883; Cyt_c_oxidase_su1. DR Gene3D; G3DSA:1.20.210.10; COX1; 1. DR PANTHER; PTHR10422; COX1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; COX1; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Copper; Electron transport; Heme; Iron; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; KW Respiratory chain; Transmembrane; Transport. FT NON_TER 1 1 FT NON_TER 196 196 SQ SEQUENCE 196 AA; 22171 MW; FCBA5798BD585D1E CRC64; FWFFGHPEVY ILILPGFGMI SHIVTYYSGK KEPFGYMGMV WAMMSIGFLG FIVWAHHMFT VGMDVDTRAY FTSATMIIAI PTGVKVFSWL ATLHGGNIKW SPAMLWALGF IFLFTIGGLT GIVLSNSSLD IVLHDTYYVV AHFHYVLSMG AVFAIMGGFA HWFPLFSGYT LNDVWAKIHF TIMFVGVNMT FFPQHF //