ID COX2_STRCA Reviewed; 229 AA. AC O21400; O03894; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 13-SEP-2023, entry version 123. DE RecName: Full=Cytochrome c oxidase subunit 2; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide II; GN Name=MT-CO2; Synonyms=COII, COXII, MTCO2; OS Struthio camelus (Common ostrich). OG Mitochondrion. OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda; OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae; OC Struthio. OX NCBI_TaxID=8801; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9214748; DOI=10.1093/oxfordjournals.molbev.a025815; RA Harlid A., Janke A., Arnason U.; RT "The mtDNA sequence of the ostrich and the divergence between paleognathous RT and neognathous birds."; RL Mol. Biol. Evol. 14:754-761(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Sorenson M.D., Dimcheff D.E., Ast J.C., Yuri T., Mindell D.P.; RT "Primers for a PCR-based approach to complete mitochondrial genome RT sequencing."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11370967; DOI=10.1098/rspb.2001.1587; RA Haddrath O., Baker A.J.; RT "Complete mitochondrial DNA genome sequences of extinct birds: ratite RT phylogenetics and the vicariance biogeography hypothesis."; RL Proc. R. Soc. B 268:939-945(2001). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-229. RA Lee K., Feinstein J., Cracraft J.; RT "Phylogenetic relationships of the ratite birds: resolving conflicts RT between molecular and morphological data sets."; RL (In) Mindell D.P. (eds.); RL Avian molecular evolution and systematics, pp.1-1, Academic Press, New York RL (1997). 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:P68530}; CC Note=Binds a dinuclear copper A center per subunit. CC {ECO:0000250|UniProtKB:P68530}; 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 (By similarity). CC {ECO:0000250|UniProtKB:P00403, ECO:0000250|UniProtKB:P68530}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P68530}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P68530}. 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; Y12025; CAA72747.1; -; Genomic_DNA. DR EMBL; AF069429; AAD09386.1; -; Genomic_DNA. DR EMBL; AF338715; AAK53348.1; -; Genomic_DNA. DR EMBL; U76069; AAB61329.1; ALT_TERM; Genomic_DNA. DR PIR; D90612; D90612. DR PIR; T12412; T12412. DR RefSeq; NP_115444.1; NC_002785.1. DR AlphaFoldDB; O21400; -. DR SMR; O21400; -. DR GeneID; 803280; -. DR CTD; 4513; -. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045277; C:respiratory chain complex IV; ISS:UniProtKB. 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..229 FT /note="Cytochrome c oxidase subunit 2" FT /id="PRO_0000183696" FT TOPO_DOM 1..14 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000250|UniProtKB:P68530" FT TRANSMEM 15..45 FT /note="Helical; Name=I" FT /evidence="ECO:0000250|UniProtKB:P68530" FT TOPO_DOM 46..58 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000250|UniProtKB:P68530" FT TRANSMEM 59..86 FT /note="Helical; Name=II" FT /evidence="ECO:0000250|UniProtKB:P68530" FT TOPO_DOM 87..229 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 160 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 195 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 195 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 197 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 197 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with MT-CO1" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 199 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 199 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 203 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A2" FT /evidence="ECO:0000250|UniProtKB:P68530" FT BINDING 206 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A1" FT /evidence="ECO:0000250|UniProtKB:P68530" SQ SEQUENCE 229 AA; 25700 MW; B9377617BACB14EF CRC64; MANPSQFGFQ DASSPIMEEL VEFHDHALMV ALAICSLVLY LLALMLVEKL SSNTVDAQEV ELIWTILPAI VLILLALPSL QILYMMDEID EPDLTLKAIG HQWYWSYEYT DFKDLTFDSY MIPTSELPPG HFRLLEVDHR VVVPMESPIR VIITAGDVLH SWAVPTLGVK TDAIPGRLNQ TSFITTRPGI FYGQCSEICG ANHSYMPIVV ESTPLTYFES WSSLLSTDS //