ID COX2_WICCA Reviewed; 247 AA. AC P48871; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2002, sequence version 2. DT 02-SEP-2026, entry version 121. DE RecName: Full=Cytochrome c oxidase subunit 2; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide II; DE Flags: Precursor; GN Name=COX2; OS Wickerhamomyces canadensis (Yeast) (Pichia canadensis). OG Mitochondrion. OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Phaffomycetales; Wickerhamomycetaceae; Wickerhamomyces. OX NCBI_TaxID=1156965; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=21; RX PubMed=8536312; DOI=10.1007/bf00311880; RA Sekito T., Okamoto K., Kitano H., Yoshida K.; RT "The complete mitochondrial DNA sequence of Hansenula wingei reveals new RT characteristics of yeast mitochondria."; RL Curr. Genet. 28:39-53(1995). 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] + O2 + 8 H(+)(in) = 4 Fe(III)- CC [cytochrome c] + 2 H2O + 4 H(+)(out); 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 -!- PTM: The signal sequence of COX2 is processed by IMP1. {ECO:0000250}. 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; D31785; BAA06577.2; -; Genomic_DNA. DR PIR; S58754; S58754. DR RefSeq; NP_038222.1; NC_001762.1. DR AlphaFoldDB; P48871; -. DR SMR; P48871; -. DR GeneID; 800566; -. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB. DR GO; GO:0045277; C:respiratory chain complex IV; IEA:UniProtKB-ARBA. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; ISS:UniProtKB. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IEA:UniProtKB-ARBA. DR CDD; cd13912; CcO_II_C; 1. DR FunFam; 1.10.287.90:FF:000004; Cytochrome c oxidase subunit 2; 1. DR FunFam; 2.60.40.420:FF:000001; Cytochrome c oxidase subunit 2; 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; Signal; KW Translocase; Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1..11 FT /evidence="ECO:0000250" FT CHAIN 12..247 FT /note="Cytochrome c oxidase subunit 2" FT /id="PRO_0000006038" FT TOPO_DOM 12..38 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT TRANSMEM 39..59 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 60..78 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000255" FT TRANSMEM 79..101 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 102..247 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000255" FT BINDING 182 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 217 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 217 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 219 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 219 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 221 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 221 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 225 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P00410" FT BINDING 228 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P00410" SQ SEQUENCE 247 AA; 27809 MW; C41D811809897DDD CRC64; MLLIINNIIN NDVPTPWGVY FQDSATPNHE GIIELHDNIM FYLVLILCLV SWLLFSIVKD GSKNPLPHKY LVHGQTIEII WTILPALVLL VIAFPSFILL YLCDEVISPA MTIKAIGLQW YWKYEYSDFI NDSGETIEFE SYVIPEDLLE DGQLPLLDTD TSIVCPVNTH IRFIVSAADV IHDFAVPSLG IKIDACPGRL NQVSALIQRE GVYYGQCSEL CGVAHSAMPI KVEAVSLKEF LTWLNEQ //