COX2_MOUSE
ID COX2_MOUSE Reviewed; 227 AA.
AC P00405; Q85K21;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
GN Name=Mtco2; Synonyms=COII, COX2, mt-Co2;
OS Mus musculus (Mouse).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7332926; DOI=10.1016/0092-8674(81)90300-7;
RA Bibb M.J., van Etten R.A., Wright C.T., Walberg M.W., Clayton D.A.;
RT "Sequence and gene organization of mouse mitochondrial DNA.";
RL Cell 26:167-180(1981).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=12954771; DOI=10.1093/nar/gkg739;
RA Bayona-Bafaluy M.P., Acin-Perez R., Mullikin J.C., Park J.S.,
RA Moreno-Loshuertos R., Hu P., Perez-Martos A., Fernandez-Silva P., Bai Y.,
RA Enriquez J.A.;
RT "Revisiting the mouse mitochondrial DNA sequence.";
RL Nucleic Acids Res. 31:5349-5355(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-63.
RX PubMed=8281018; DOI=10.1007/bf00360907;
RA Nelson I., Gerasimov S., Marsac C., Lestienne P., Boursot P.;
RT "Sequence analysis of a deleted mitochondrial DNA molecule in heteroplasmic
RT mice.";
RL Mamm. Genome 4:680-683(1993).
RN [4]
RP PROTEIN SEQUENCE OF 83-98; 135-171 AND 218-227, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; J01420; AAB48647.1; -; Genomic_DNA.
DR EMBL; V00711; CAA24083.1; -; Genomic_DNA.
DR EMBL; AY172335; AAN85125.1; -; Genomic_DNA.
DR EMBL; S68119; AAP15814.1; -; Genomic_DNA.
DR PIR; A00474; OBMS2.
DR RefSeq; NP_904331.1; NC_005089.1.
DR PDB; 7O37; EM; 3.20 A; b=1-227.
DR PDB; 7O3C; EM; 3.30 A; b=1-227.
DR PDB; 7O3E; EM; 3.60 A; b=1-227.
DR PDBsum; 7O37; -.
DR PDBsum; 7O3C; -.
DR PDBsum; 7O3E; -.
DR AlphaFoldDB; P00405; -.
DR SMR; P00405; -.
DR BioGRID; 201542; 11.
DR CORUM; P00405; -.
DR IntAct; P00405; 14.
DR MINT; P00405; -.
DR STRING; 10090.ENSMUSP00000080994; -.
DR iPTMnet; P00405; -.
DR PhosphoSitePlus; P00405; -.
DR SwissPalm; P00405; -.
DR SWISS-2DPAGE; P00405; -.
DR EPD; P00405; -.
DR jPOST; P00405; -.
DR PaxDb; P00405; -.
DR PeptideAtlas; P00405; -.
DR PRIDE; P00405; -.
DR ProteomicsDB; 284150; -.
DR Antibodypedia; 4262; 252 antibodies from 32 providers.
DR Ensembl; ENSMUST00000082405; ENSMUSP00000080994; ENSMUSG00000064354.
DR GeneID; 17709; -.
DR KEGG; mmu:17709; -.
DR CTD; 4513; -.
DR MGI; MGI:102503; mt-Co2.
DR VEuPathDB; HostDB:ENSMUSG00000064354; -.
DR eggNOG; KOG4767; Eukaryota.
DR GeneTree; ENSGT00390000017410; -.
DR HOGENOM; CLU_036876_2_3_1; -.
DR InParanoid; P00405; -.
DR OMA; WSYEYTD; -.
DR OrthoDB; 1432833at2759; -.
DR PhylomeDB; P00405; -.
DR TreeFam; TF344269; -.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR ChiTaRS; mt-Co2; mouse.
DR PRO; PR:P00405; -.
DR Proteomes; UP000000589; Mitochondrion.
DR RNAct; P00405; protein.
DR Bgee; ENSMUSG00000064354; Expressed in ventricular zone and 60 other tissues.
DR ExpressionAtlas; P00405; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
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; ISO:MGI.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR GO; GO:0007595; P:lactation; IEA:Ensembl.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
DR GO; GO:0010729; P:positive regulation of hydrogen peroxide biosynthetic process; ISO:MGI.
DR GO; GO:0010940; P:positive regulation of necrotic cell death; ISO:MGI.
DR GO; GO:0009409; P:response to cold; IEA:Ensembl.
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 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Electron transport;
KW Magnesium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..227
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183635"
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..59
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P68530"
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:0000250|UniProtKB:P68530"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P68530"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P68530"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P68530"
FT BINDING 198
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P68530"
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:0000250|UniProtKB:P68530"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P68530"
FT BINDING 204
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P68530"
FT BINDING 207
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P68530"
FT MOD_RES 218
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00406"
FT HELIX 15..46
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 62..84
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:7O37"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:7O3C"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:7O37"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:7O37"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:7O37"
FT STRAND 208..214
FT /evidence="ECO:0007829|PDB:7O37"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:7O37"
SQ SEQUENCE 227 AA; 25976 MW; 306C6EAD54802D11 CRC64;
MAYPFQLGLQ DATSPIMEEL MNFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE
VETIWTILPA VILIMIALPS LRILYMMDEI NNPVLTVKTM GHQWYWSYEY TDYEDLCFDS
YMIPTNDLKP GELRLLEVDN RVVLPMELPI RMLISSEDVL HSWAVPSLGL KTDAIPGRLN
QATVTSNRPG LFYGQCSEIC GSNHSFMPIV LEMVPLKYFE NWSASMI
