ID D2XBE0_9CUCU Unreviewed; 201 AA. AC D2XBE0; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 20-APR-2010, entry version 2. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=1.9.3.1; DE Flags: Fragment; GN Name=COI; OS Chilocorus renipustulatus (kidney-spot ladybird beetle). OG Mitochondrion. OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia; OC Coccinellidae; Chilocorinae; Chilocorini; Chilocorus. OX NCBI_TaxID=115342; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=F; RX PubMed=19903531; RA Magro A., Lecompte E., Magne F., Hemptinne J.L., Crouau-Roy B.; RT "Phylogeny of ladybirds (Coleoptera: Coccinellidae): Are the RT subfamilies monophyletic?"; RL Mol. Phylogenet. Evol. 0:0-0(2009). 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; GU073961; ADB22588.1; -; Genomic_DNA. 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. 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 201 201 SQ SEQUENCE 201 AA; 21796 MW; 22D50598E885374A CRC64; MIIRLELGTQ SSLIGNDQIY NVIVTAHAFI MIFFMVMPIM IGGFGNWLVP LMIGAPDMAF PRLNNMSFWL LPPSLTLLIL SSMIESGAGT GWTVYPPLSS NLAHGGSSVD LAIFSLHMAG ISSILGAINF ISTILNMRPK GMLLEKTPLF VWSVLITAIL LLLSLPVLAG AITMLLTDRN INTSFFDPTG GGDPILYQHL F //