COX2_CAIMO
ID COX2_CAIMO Reviewed; 228 AA.
AC P50666;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Cairina moschata (Muscovy duck).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Cairina.
OX NCBI_TaxID=8855;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Muscovy shinney duck; TISSUE=Liver;
RA Pan Y.F., Lee Y.H.W., Wei Y.H., Chiang A.N.;
RT "A gene cytochrome C oxidase subunit II in duck mitochondrial DNA:
RT structural features and sequence evolution.";
RL Biochem. Int. 30:479-489(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: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}.
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DR EMBL; X68508; CAA48520.1; -; Genomic_DNA.
DR RefSeq; YP_001974582.1; NC_010965.1.
DR AlphaFoldDB; P50666; -.
DR SMR; P50666; -.
DR GeneID; 6383232; -.
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: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; -; 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; Electron transport; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Respiratory chain;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..228
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183528"
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..228
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 228 AA; 25523 MW; D34E9E93797DBCBB CRC64;
MANHSQLGFQ DASSPIMEEL VEFHDHALIV ALAICSLVLY LLAHMLMEKL SSNAVDAQEV
ELIWTILPAI VLVLLALPSL QILYMMDEID EPDLTLKAIG HQWYWSYEYT DFKDLSFDSY
MIPTTDLPNG HFRLLEVDHR VVVPMESPIR VIITAGDVLH SWAVPTLGVK TDAIPGRLNQ
TSFIATRPGV FYGQCSEICG ANHSYMPIVV ESTPLPYFET WSSLLSAS
