COX2_MYTED
ID COX2_MYTED Reviewed; 242 AA.
AC Q00227; Q68SR6;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
GN Name=COII;
OS Mytilus edulis (Blue mussel).
OG Mitochondrion.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=6550;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15014161; DOI=10.1093/molbev/msh090;
RA Boore J.L., Medina M., Rosenberg L.A.;
RT "Complete sequences of the highly rearranged molluscan mitochondrial
RT genomes of the scaphopod Graptacme eborea and the bivalve Mytilus edulis.";
RL Mol. Biol. Evol. 21:1492-1503(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-112 AND 162-242.
RX PubMed=1386586; DOI=10.1093/genetics/131.2.397;
RA Hoffmann R.J., Boore J.L., Brown W.M.;
RT "A novel mitochondrial genome organization for the blue mussel, Mytilus
RT edulis.";
RL Genetics 131:397-412(1992).
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: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 -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; AY484747; AAT98406.1; -; Genomic_DNA.
DR PIR; S28747; S28747.
DR RefSeq; YP_073337.1; NC_006161.1.
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:0070469; C:respirasome; IEA:UniProtKB-KW.
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; 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 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..242
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183636"
FT TOPO_DOM 1..30
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..66
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 67..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 84..242
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 176
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 211
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 211
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 213
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 213
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 215
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 215
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 222
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
SQ SEQUENCE 242 AA; 28273 MW; FC3FE2D3D15E4D56 CRC64;
MSFYGSRYFG DIVHGELGKD LFRYHGFVMM VAVAVLVFVM YMGCVILFTK FSYRHFLNRQ
RLEFWWTIVP MLMLVGLWXP SMINLYYMEE VKRPRWNFKA IGKQWYWSYE FCRNLDTPSS
SESAESISCY TIDSYMEDQQ ETFSKGGYRL LDVDNRMVAP ADVQMTAFVS SSDVLHSFAL
PKLLIKVDAI PGRINRLPMK ASQCSIIYGQ CSEICGVNHS FMPIVIEFIP EKYFVMWLEA
LN
