ID A3E4B0_MOUSE Unreviewed; 227 AA. AC A3E4B0; DT 20-MAR-2007, integrated into UniProtKB/TrEMBL. DT 20-MAR-2007, sequence version 1. DT 03-AUG-2022, entry version 98. DE RecName: Full=Cytochrome c oxidase subunit 2 {ECO:0000256|ARBA:ARBA00015946, ECO:0000256|RuleBase:RU000457}; GN Name=COX2 {ECO:0000313|EMBL:ABH09672.1}; GN Synonyms=COXII {ECO:0000313|EMBL:ABK79265.1}; OS Mus musculus musculus (eastern European house mouse). OG Mitochondrion {ECO:0000313|EMBL:ABH09672.1}. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=39442 {ECO:0000313|EMBL:ABH09672.1}; RN [1] {ECO:0000313|EMBL:ABK79265.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PWD/PhJ {ECO:0000313|EMBL:ABK79265.1}; 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). RN [2] {ECO:0000313|EMBL:ABH09672.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PWD/Ph {ECO:0000313|EMBL:ABH09672.1}; RX PubMed=18256238; DOI=10.1101/gr.7160508; RA Gregorova S., Divina P., Storchova R., Trachtulec Z., Fotopulosova V., RA Svenson K.L., Donahue L.R., Paigen B., Forejt J.; RT "Mouse consomic strains: exploiting genetic divergence between Mus m. RT musculus and Mus m. domesticus subspecies."; RL Genome Res. 18:509-515(2008). CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the CC mitochondrial electron transport chain which drives oxidative CC phosphorylation. The respiratory chain contains 3 multisubunit CC complexes succinate dehydrogenase (complex II, CII), ubiquinol- CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to CC transfer electrons derived from NADH and succinate to molecular oxygen, CC creating an electrochemical gradient over the inner membrane that CC drives transmembrane transport and the ATP synthase. Cytochrome c CC oxidase is the component of the respiratory chain that catalyzes the CC reduction of oxygen to water. Electrons originating from reduced CC cytochrome c in the intermembrane space (IMS) are transferred via the CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 CC to the active site in subunit 1, a binuclear center (BNC) formed by CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 CC water molecules using 4 electrons from cytochrome c in the IMS and 4 CC protons from the mitochondrial matrix. {ECO:0000256|RuleBase:RU000457}. CC -!- CATALYTIC ACTIVITY: CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)- CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, CC ChEBI:CHEBI:29034; EC=7.1.1.9; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000256|ARBA:ARBA00029331}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000256|RuleBase:RU000457}; CC Note=Binds a copper A center. {ECO:0000256|RuleBase:RU000457}; CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a CC multisubunit enzyme composed of 14 subunits. The complex is composed of CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in CC the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A, CC COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which CC are encoded in the nuclear genome. The complex exists as a monomer or a CC dimer and forms supercomplexes (SCs) in the inner mitochondrial CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex CC III, CIII), resulting in different assemblies (supercomplex CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (By similarity). CC Found in a complex with TMEM177, COA6, COX18, COX20, SCO1 and SCO2. CC Interacts with TMEM177 in a COX20-dependent manner. Interacts with CC COX20. Interacts with COX16. {ECO:0000256|ARBA:ARBA00025842}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion CC inner membrane {ECO:0000256|ARBA:ARBA00004448, CC ECO:0000256|RuleBase:RU000457}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004448, ECO:0000256|RuleBase:RU000457}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000256|ARBA:ARBA00007866, ECO:0000256|RuleBase:RU000457}. 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 RefSeq; YP_001686701.1; NC_010339.1. DR SMR; A3E4B0; -. DR PRIDE; A3E4B0; -. DR GeneID; 5912281; -. DR CTD; 4513; -. 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:respirasome; IEA:UniProtKB-KW. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR CDD; cd13912; CcO_II_C; 1. DR Gene3D; 1.10.287.90; -; 1. DR Gene3D; 2.60.40.420; -; 1. DR InterPro; IPR045187; CcO_II. DR InterPro; IPR002429; CcO_II-like_C. DR InterPro; IPR034210; CcO_II_C. DR InterPro; IPR001505; Copper_CuA. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR014222; Cyt_c_oxidase_su2. DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom. DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf. DR PANTHER; PTHR22888; PTHR22888; 1. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR SUPFAM; SSF49503; SSF49503; 1. DR SUPFAM; SSF81464; SSF81464; 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 {ECO:0000256|ARBA:ARBA00023008, ECO:0000256|RuleBase:RU000457}; KW Electron transport {ECO:0000256|ARBA:ARBA00022982, KW ECO:0000256|RuleBase:RU000457}; Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU000457}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU000457}; KW Mitochondrion {ECO:0000256|RuleBase:RU000457, ECO:0000313|EMBL:ABH09672.1}; KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457}; KW Oxidoreductase {ECO:0000313|EMBL:ABK79265.1}; KW Respiratory chain {ECO:0000256|ARBA:ARBA00022660, KW ECO:0000256|RuleBase:RU000457}; KW Translocase {ECO:0000256|ARBA:ARBA00022967}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU000457}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU000457}. FT TRANSMEM 27..46 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 66..85 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 1..91 FT /note="COX2_TM" FT /evidence="ECO:0000259|PROSITE:PS50999" FT DOMAIN 92..225 FT /note="COX2_CUA" FT /evidence="ECO:0000259|PROSITE:PS50857" 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 //