COX2_CAEEL
ID COX2_CAEEL Reviewed; 231 AA.
AC P24894;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
GN Name=ctc-2 {ECO:0000312|WormBase:MTCE.31};
GN Synonyms=coII {ECO:0000312|WormBase:MTCE.31},
GN cox-2 {ECO:0000312|WormBase:MTCE.31};
GN ORFNames=MTCE.31 {ECO:0000312|WormBase:MTCE.31};
OS Caenorhabditis elegans.
OG Mitochondrion.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-132; ILE-143; ASN-186
RP AND MET-216.
RC STRAIN=AB1, AB2, Bristol N2, CB4852, CB4853, CB4854, CB4855, CB4856,
RC CB4857, CB4858, KR314, PB303, PB306, RW7000, and TR403;
RX PubMed=12644560; DOI=10.1093/molbev/msg044;
RA Denver D.R., Morris K., Thomas W.K.;
RT "Phylogenetics in Caenorhabditis elegans: an analysis of divergence and
RT outcrossing.";
RL Mol. Biol. Evol. 20:393-400(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=1551572; DOI=10.1093/genetics/130.3.471;
RA Okimoto R., Macfarlane J.L., Clary D.O., Wolstenholme D.R.;
RT "The mitochondrial genomes of two nematodes, Caenorhabditis elegans and
RT Ascaris suum.";
RL Genetics 130:471-498(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-25.
RX PubMed=2235493; DOI=10.1093/nar/18.20.6113;
RA Okimoto R., Macfarlane J.L., Wolstenholme D.R.;
RT "Evidence for the frequent use of TTG as the translation initiation codon
RT of mitochondrial protein genes in the nematodes, Ascaris suum and
RT Caenorhabditis elegans.";
RL Nucleic Acids Res. 18:6113-6118(1990).
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; AY171193; AAO16253.1; -; Genomic_DNA.
DR EMBL; AY171194; AAO16257.1; -; Genomic_DNA.
DR EMBL; AY171195; AAO16261.1; -; Genomic_DNA.
DR EMBL; AY171196; AAO16265.1; -; Genomic_DNA.
DR EMBL; AY171197; AAO16269.1; -; Genomic_DNA.
DR EMBL; AY171198; AAO16273.1; -; Genomic_DNA.
DR EMBL; AY171199; AAO16277.1; -; Genomic_DNA.
DR EMBL; AY171200; AAO16281.1; -; Genomic_DNA.
DR EMBL; AY171201; AAO16285.1; -; Genomic_DNA.
DR EMBL; AY171202; AAO16289.1; -; Genomic_DNA.
DR EMBL; AY171203; AAO16293.1; -; Genomic_DNA.
DR EMBL; AY171204; AAO16297.1; -; Genomic_DNA.
DR EMBL; AY171205; AAO16301.1; -; Genomic_DNA.
DR EMBL; AY171206; AAO16305.1; -; Genomic_DNA.
DR EMBL; AY171207; AAO16309.1; -; Genomic_DNA.
DR EMBL; X54252; CAA38160.1; -; Genomic_DNA.
DR PIR; S26035; S26035.
DR RefSeq; NP_006962.1; NC_001328.1.
DR AlphaFoldDB; P24894; -.
DR SMR; P24894; -.
DR BioGRID; 57535; 1.
DR STRING; 6239.MTCE.31; -.
DR EPD; P24894; -.
DR PaxDb; P24894; -.
DR EnsemblMetazoa; MTCE.31.1; MTCE.31.1; WBGene00010965.
DR GeneID; 2565697; -.
DR KEGG; cel:COX2; -.
DR CTD; 4513; -.
DR WormBase; MTCE.31; CE35351; WBGene00010965; ctc-2.
DR eggNOG; KOG4767; Eukaryota.
DR GeneTree; ENSGT00390000017410; -.
DR HOGENOM; CLU_036876_2_3_1; -.
DR InParanoid; P24894; -.
DR OrthoDB; 1432833at2759; -.
DR PhylomeDB; P24894; -.
DR PRO; PR:P24894; -.
DR Proteomes; UP000001940; Mitochondrion.
DR Bgee; WBGene00010965; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; NAS:UniProtKB.
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; NAS:UniProtKB.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; NAS:UniProtKB.
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 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; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..231
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183526"
FT TOPO_DOM 1..30
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..69
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..231
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 164
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 199
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 199
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 201
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 201
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 203
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 203
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 207
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 210
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT VARIANT 132
FT /note="S -> N (in strain: PB303)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 143
FT /note="N -> I (in strain: CB4857)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 186
FT /note="S -> N (in strain: AB2, CB4852, CB4853, CB4855,
FT CB4858 and PB306)"
FT /evidence="ECO:0000269|PubMed:12644560"
FT VARIANT 216
FT /note="V -> M (in strain: AB1 and KR314)"
FT /evidence="ECO:0000269|PubMed:12644560"
SQ SEQUENCE 231 AA; 26549 MW; FCD8D458D1B0DDAA CRC64;
MNNFFQGYNL LFQHSLFASY MDWFHSFNCS LLLGVLVFVT LLFGYLIFGT FYFKSKKIEY
QFGELLCSIF PTIILLMQMV PSLSLLYYYG LMNLDSNLTV KVTGHQWYWS YEYSDIPGLE
FDSYMKSLDQ LSLGEPRLLE VDNRCVIPCD TNIRFCITSA DVIHAWALNS LSVKLDAMSG
ILSTFSYSFP MVGVFYGQCS EICGANHSFM PIALEVTLLD NFKSWCFGTM E
