COX2_SHEEP
ID COX2_SHEEP Reviewed; 227 AA.
AC O78750;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
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, COX2, COXII, MTCO2;
OS Ovis aries (Sheep).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Merinolandschaf {ECO:0000312|Proteomes:UP000002356}; TISSUE=Liver;
RX PubMed=9767689; DOI=10.1007/pl00006401;
RA Hiendleder S., Lewalski H., Wassmuth R., Janke A.;
RT "The complete mitochondrial DNA sequence of the domestic sheep (Ovis aries)
RT and comparison with the other major ovine haplotype.";
RL J. Mol. Evol. 47:441-448(1998).
RN [2]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.80 ANGSTROMS).
RX PubMed=27654913; DOI=10.1038/nature19774;
RA Letts J.A., Fiedorczuk K., Sazanov L.A.;
RT "The architecture of respiratory supercomplexes.";
RL Nature 537:644-648(2016).
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 (By similarity). The complex exists
CC as a monomer or a dimer and forms supercomplexes (SCs) in the inner
CC mitochondrial membrane with NADH-ubiquinone oxidoreductase (complex I,
CC CI) and ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex,
CC complex III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:27654913).
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 ECO:0000269|PubMed:27654913}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:27654913}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:27654913}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; AF010406; AAD10099.1; -; Genomic_DNA.
DR PIR; T11053; T11053.
DR RefSeq; NP_008409.1; NC_001941.1.
DR PDB; 5J4Z; EM; 5.80 A; BO=1-227.
DR PDB; 5J7Y; EM; 6.70 A; BO=1-227.
DR PDBsum; 5J4Z; -.
DR PDBsum; 5J7Y; -.
DR AlphaFoldDB; O78750; -.
DR SMR; O78750; -.
DR STRING; 9940.ENSOARP00000000004; -.
DR BindingDB; O78750; -.
DR ChEMBL; CHEMBL1250404; -.
DR DrugCentral; O78750; -.
DR PRIDE; O78750; -.
DR Ensembl; ENSOART00000000019; ENSOARP00000000004; ENSOARG00000000019.
DR Ensembl; ENSOART00020000020; ENSOARP00020000005; ENSOARG00020000020.
DR GeneID; 808252; -.
DR KEGG; oas:808252; -.
DR CTD; 4513; -.
DR eggNOG; KOG4767; Eukaryota.
DR HOGENOM; CLU_036876_2_3_1; -.
DR OMA; WSYEYTD; -.
DR OrthoDB; 1432833at2759; -.
DR Proteomes; UP000002356; Mitochondrion.
DR Bgee; ENSOARG00000000019; Expressed in heart right ventricle and 56 other tissues.
DR ExpressionAtlas; O78750; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:Ensembl.
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; 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; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Electron transport; Magnesium; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Respiratory chain; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..227
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183689"
FT TOPO_DOM 1..14
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27654913"
FT TRANSMEM 15..45
FT /note="Helical; Name=I"
FT /evidence="ECO:0000250|UniProtKB:P68530"
FT TOPO_DOM 46..59
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:27654913"
FT TRANSMEM 60..87
FT /note="Helical; Name=II"
FT /evidence="ECO:0000250|UniProtKB:P68530"
FT TOPO_DOM 88..227
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27654913"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000269|PubMed:27654913"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000269|PubMed:27654913"
FT BINDING 198
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000269|PubMed:27654913"
FT BINDING 198
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 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000269|PubMed:27654913"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000269|PubMed:27654913"
FT BINDING 204
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000269|PubMed:27654913"
FT BINDING 207
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000269|PubMed:27654913"
FT MOD_RES 218
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00406"
SQ SEQUENCE 227 AA; 25998 MW; CFBD158EAE276829 CRC64;
MAYPMQLGFQ DATSPIMEEL LHFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE
VETIWTILPA IILIMIALPS LRILYMMDEI NNPSLTVKTM GHQWYWSYEY TDYEDLSFDS
YMIPTSELKP GELRLLEVDN RVVLPMEMTV RMLISSEDVL PSWAVPSLGL KTDAIPGRLN
QTTLMSTRPG LFYGQCSEIC GSNHSFMPIV LELVPLKYFE KWSASML
