ID Q4KNF6_CERNE Unreviewed; 212 AA. AC Q4KNF6; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 19-JAN-2010, entry version 29. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=1.9.3.1; DE Flags: Fragment; GN Name=COXI; OS Cercopithecus neglectus (Debrazza's monkey). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Cercopithecus. OX NCBI_TaxID=36227; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PR00981; TISSUE=Blood; RX PubMed=16214744; DOI=10.1098/rstb.2005.1718; RA Lorenz J.G., Jackson W.E., Beck J.C., Hanner R.; RT "The problems and promise of DNA barcodes for species diagnosis of RT primate biomaterials."; RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 360:1869-1877(2005). RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PR00981; TISSUE=Blood; RA Lorenz J.G., Jackson W.E., Beck J.C., Hanner R.; RT "'Molecular Barcoding' of the Order Primates: Practical Applications RT and Theoretical Concerns."; RL Submitted (MAR-2005) 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 (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; AY972783; AAY22349.1; -; Genomic_DNA. DR SMR; Q4KNF6; 1-212. DR HOVERGEN; Q4KNF6; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-KW. DR GO; GO:0070469; C:respiratory chain; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; 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 PROSITE; PS50855; COX1; 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 212 212 SQ SEQUENCE 212 AA; 22620 MW; ABDBC12852007B9F CRC64; LLFGAWAGIM GTALSLLIRA ELGQPGSLLG SDHIYNVIVT AHAFIMIFFM VMPIMIGGFG NWLVPLMIGA PDMAFPRLNN MSFWLLPPSF LLLMASAMVE AGAGTGWTVY PPLAGNLSHP GASVDLVIFS LHLAGVSSIL GAINFITTII NMKPPAMSQY QTPLFVWSVL ITAILLLLSL PVLAAGITML LTDRNLNTTF FDPTGGGDPI LY //