ID COX2_APILI Reviewed; 225 AA. AC P20375; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1991, sequence version 1. DT 13-SEP-2023, entry version 124. DE RecName: Full=Cytochrome c oxidase subunit 2; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide II; GN Name=COII; OS Apis mellifera ligustica (Common honeybee) (Italian honeybee). OG Mitochondrion. OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea; OC Anthophila; Apidae; Apis. OX NCBI_TaxID=7469; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Thorax; RX PubMed=2559293; DOI=10.1093/oxfordjournals.molbev.a040553; RA Crozier R.H., Crozier Y.C., Mackinlay A.G.; RT "The CO-I and CO-II region of honeybee mitochondrial DNA: evidence for RT variation in insect mitochondrial evolutionary rates."; RL Mol. Biol. Evol. 6:399-411(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Thorax; RX PubMed=8417993; DOI=10.1093/genetics/133.1.97; RA Crozier R.H., Crozier Y.C.; RT "The mitochondrial genome of the honeybee Apis mellifera: complete sequence RT and genome organization."; RL Genetics 133:97-117(1993). 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:0000250|UniProtKB:P00410}. 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:0000250|UniProtKB:P00410}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000250|UniProtKB:P00410}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000250|UniProtKB:P00410}; CC Note=Binds a dinuclear copper A center per subunit. CC {ECO:0000250|UniProtKB:P00410}; CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a CC multisubunit enzyme composed of a catalytic core of 3 subunits and CC several supernumerary subunits. The complex exists as a monomer or a CC dimer and forms supercomplexes (SCs) in the inner mitochondrial CC membrane with ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 CC complex, complex III, CIII). {ECO:0000250|UniProtKB:P00410}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P00410}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P00410}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family. CC {ECO:0000305}. 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; M23409; AAA18477.1; -; Genomic_DNA. DR EMBL; L06178; AAB96800.1; -; Genomic_DNA. DR PIR; B32431; B32431. DR RefSeq; NP_008084.1; NC_001566.1. DR AlphaFoldDB; P20375; -. DR SMR; P20375; -. DR GeneID; 807700; -. DR CTD; 4513; -. 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; Cupredoxins - blue copper proteins; 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 NCBIfam; TIGR02866; CoxB; 1. DR PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1. DR PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR PRINTS; PR01166; CYCOXIDASEII. DR SUPFAM; SSF49503; Cupredoxins; 1. DR SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 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; Magnesium; Membrane; Metal-binding; KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain; KW Translocase; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..225 FT /note="Cytochrome c oxidase subunit 2" FT /id="PRO_0000183499" FT TOPO_DOM 1..25 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT TRANSMEM 26..47 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 48..62 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000255" FT TRANSMEM 63..82 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 83..225 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT BINDING 159 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 194 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 194 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 196 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 196 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with subunit 1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 198 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 198 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 202 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 205 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" SQ SEQUENCE 225 AA; 26664 MW; 2AFCA78E25B3109B CRC64; MSTWFMFMFQ ESNSYYADNL ISFHNMVMMI IIMISTLTVY IILDLFMNKF SNLFLLKNHN IEIIWTIIPI IILLIICFPS LKILYLIDEI VNPFFSIKSI GHQWYWSYEY PEFNNIEFDS YMLNYNNLNQ FRLLETDNRM VIPMKIPLRL ITTSTDVIHS WTVPSLGIKV DAVPGRINQL NLISKRPGIF FGQCSEICGM NHSFMPIMIE STSFQYFLNW VNKQI //