ID A3E4B0_MOUSE Unreviewed; 227 AA. AC A3E4B0; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 15-JAN-2008, entry version 11. DE Cytochrome c oxidase subunit 2 (EC 1.9.3.1). GN Name=COX2; Synonyms=COXII; OS Mus musculus musculus (eastern European house mouse). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=39442; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PWD/Ph; RA Gregorova S., Storchova R., Divina P., Fotopulosova V., Trachtulec Z., RA Paigen B., Forejt J.; RT "A set of inter(sub)-specific mouse chromosomal substitution RT (consomic) strains B6-PWD."; RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE. RC STRAIN=PWD/PhJ; RX PubMed=17284675; DOI=10.1101/gr.5941007; RA Goios A., Pereira L., Bogue M., Macaulay V., Amorim A.; RT "mtDNA phylogeny and evolution of laboratory mouse strains."; RL Genome Res. 17:293-298(2007). 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. Subunit 2 CC transfers the electrons from cytochrome c via its binuclear copper CC A center to the bimetallic center of the catalytic subunit 1 (By CC similarity). CC -!- CATALYTIC ACTIVITY: 4 ferrocytochrome c + O(2) + 4 H(+) = 4 CC ferricytochrome c + 2 H(2)O. CC -!- COFACTOR: Copper A (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Multi-pass CC membrane protein (By similarity). CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 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; DQ874614; ABH09672.1; -; Genomic_DNA. DR EMBL; EF108343; ABK79265.1; -; Genomic_DNA. DR SMR; A3E4B0; 2-227. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR014222; COX2. DR InterPro; IPR002429; COX2_C. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR011759; Cyt_c_oxidase_II_TM. DR Gene3D; G3DSA:1.10.287.90; COX2_TM; 1. DR Gene3D; G3DSA:2.60.40.420; Cupredoxin; 1. DR PANTHER; PTHR22888; COX2_C; 1. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR PRINTS; PR01166; CYCOXIDASEII. DR ProDom; PD000131; Copper_CuA; 1. DR TIGRFAMs; TIGR02866; CoxB; 1. DR PROSITE; PS00078; COX2; 1. DR PROSITE; PS50857; COX2_CUA; 1. DR PROSITE; PS50999; COX2_TM; 1. PE 3: Inferred from homology; KW Copper; Electron transport; Inner membrane; Membrane; Metal-binding; KW Mitochondrion; Oxidoreductase; Respiratory chain; Transmembrane; KW Transport. SQ SEQUENCE 227 AA; 25946 MW; 306C7FAD54912D11 CRC64; MAYPFQLGLQ DATSPIMEEL MNFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE VETIWTILPA VILIMIALPS LRILYMMDEI NNPVLTVKTM GHQWYWSYEY TDYEDLCFDS YMIPTNDLKP GELRLLEVDN RVVLPMELPI RMLISSEDVL HSWAVPSLGL KTDAIPGRLN QATVASNRPG LFYGQCSEIC GSNHSFMPIV LEMVPLKYFE NWSASMI //