ID Q4KNF6_CERNE Unreviewed; 212 AA. AC Q4KNF6; DT 02-AUG-2005, integrated into UniProtKB/TrEMBL. DT 02-AUG-2005, sequence version 1. DT 05-DEC-2018, entry version 64. 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=COXI {ECO:0000313|EMBL:AAY22349.1}; OS Cercopithecus neglectus (De Brazza's monkey). OG Mitochondrion {ECO:0000313|EMBL:AAY22349.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Cercopithecidae; Cercopithecinae; Cercopithecus. OX NCBI_TaxID=36227 {ECO:0000313|EMBL:AAY22349.1}; RN [1] {ECO:0000313|EMBL:AAY22349.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PR00981 {ECO:0000313|EMBL:AAY22349.1}; RC TISSUE=Blood {ECO:0000313|EMBL:AAY22349.1}; 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] {ECO:0000313|EMBL:AAY22349.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PR00981 {ECO:0000313|EMBL:AAY22349.1}; RC TISSUE=Blood {ECO:0000313|EMBL:AAY22349.1}; 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. {ECO:0000256|RuleBase:RU000369}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 [Fe(II)cytochrome c] + 4 H(+) + O2 = 4 CC [Fe(III)cytochrome c] + 2 H2O; Xref=Rhea:RHEA:11436, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, Rhea:RHEA-COMP:10350, CC Rhea:RHEA-COMP:14399; EC=1.9.3.1; CC Evidence={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; AY972783; AAY22349.1; -; Genomic_DNA. DR HOVERGEN; HBG102108; -. 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. 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; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf. DR InterPro; IPR000883; Cyt_C_Oxase_1. 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:AAY22349.1}; 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 43 64 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 85 107 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 127 152 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 164 191 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 1 212 COX1. {ECO:0000259|PROSITE:PS50855}. FT NON_TER 1 1 {ECO:0000313|EMBL:AAY22349.1}. FT NON_TER 212 212 {ECO:0000313|EMBL:AAY22349.1}. 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 //