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 24-JAN-2024, entry version 162. 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}, cox-2 GN {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 2. DR STRING; 6239.MTCE.31.1; -. DR EPD; P24894; -. DR PaxDb; 6239-MTCE-31; -. DR EnsemblMetazoa; MTCE.31.1; MTCE.31.1; WBGene00010965. DR GeneID; 2565697; -. DR KEGG; cel:KEF34_p03; -. DR AGR; WB:WBGene00010965; -. 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; 5390623at2759; -. DR PhylomeDB; P24894; -. DR PRO; PR:P24894; -. DR Proteomes; UP000001940; Mitochondrion. DR Bgee; WBGene00010965; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues. 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; Cupredoxins - blue copper proteins; 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:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1. DR PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1. DR Pfam; PF00116; COX2; 1. DR PRINTS; PR01166; CYCOXIDASEII. DR SUPFAM; SSF49503; Cupredoxins; 1. DR SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 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 //