ID COX1_CAEEL Reviewed; 525 AA. AC P24893; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 2. DT 24-JAN-2024, entry version 150. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide I; GN Name=ctc-1 {ECO:0000312|WormBase:MTCE.26}; GN Synonyms=coI {ECO:0000312|WormBase:MTCE.26}, cox-1 GN {ECO:0000312|WormBase:MTCE.26}; GN ORFNames=MTCE.26 {ECO:0000312|WormBase:MTCE.26}; 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 SER-12 AND MET-466. 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). RN [4] RP SUBCELLULAR LOCATION. RX PubMed=18635357; DOI=10.1016/j.cub.2008.06.065; RA Chen L., McCloskey T., Joshi P.M., Rothman J.H.; RT "ced-4 and proto-oncogene tfg-1 antagonistically regulate cell size and RT apoptosis in C. elegans."; RL Curr. Biol. 18:1025-1033(2008). 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:P00401}. 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:P00401}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000250|UniProtKB:P00401}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000250|UniProtKB:P00401}; CC Note=Binds 2 heme A groups non-covalently per subunit. CC {ECO:0000250|UniProtKB:P00401}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000250|UniProtKB:P00401}; CC Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000250|UniProtKB:P00401}. 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:P00401}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:18635357}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P00401}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase 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; AAO16252.1; -; Genomic_DNA. DR EMBL; AY171194; AAO16256.1; -; Genomic_DNA. DR EMBL; AY171195; AAO16260.1; -; Genomic_DNA. DR EMBL; AY171196; AAO16264.1; -; Genomic_DNA. DR EMBL; AY171197; AAO16268.1; -; Genomic_DNA. DR EMBL; AY171198; AAO16272.1; -; Genomic_DNA. DR EMBL; AY171199; AAO16276.1; -; Genomic_DNA. DR EMBL; AY171200; AAO16280.1; -; Genomic_DNA. DR EMBL; AY171201; AAO16284.1; -; Genomic_DNA. DR EMBL; AY171202; AAO16288.1; -; Genomic_DNA. DR EMBL; AY171203; AAO16292.1; -; Genomic_DNA. DR EMBL; AY171204; AAO16296.1; -; Genomic_DNA. DR EMBL; AY171205; AAO16300.1; -; Genomic_DNA. DR EMBL; AY171206; AAO16304.1; -; Genomic_DNA. DR EMBL; AY171207; AAO16308.1; -; Genomic_DNA. DR EMBL; X54252; CAA38159.1; -; Genomic_DNA. DR PIR; S26034; S26034. DR RefSeq; NP_006961.1; NC_001328.1. DR AlphaFoldDB; P24893; -. DR SMR; P24893; -. DR IntAct; P24893; 1. DR STRING; 6239.MTCE.26.1; -. DR EPD; P24893; -. DR PaxDb; 6239-MTCE-26; -. DR EnsemblMetazoa; MTCE.26.1; MTCE.26.1; WBGene00010964. DR GeneID; 2565700; -. DR KEGG; cel:KEF34_p04; -. DR AGR; WB:WBGene00010964; -. DR CTD; 4512; -. DR WormBase; MTCE.26; CE35350; WBGene00010964; ctc-1. DR eggNOG; KOG4769; Eukaryota. DR GeneTree; ENSGT00390000001518; -. DR HOGENOM; CLU_011899_7_3_1; -. DR InParanoid; P24893; -. DR OrthoDB; 5387269at2759; -. DR PhylomeDB; P24893; -. DR UniPathway; UPA00705; -. DR PRO; PR:P24893; -. DR Proteomes; UP000001940; Mitochondrion. DR Bgee; WBGene00010964; 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:0005751; C:mitochondrial respiratory chain complex IV; IBA:GO_Central. DR GO; GO:0005739; C:mitochondrion; IDA:WormBase. DR GO; GO:0004129; F:cytochrome-c oxidase activity; NAS:UniProtKB. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf. DR InterPro; IPR000883; Cyt_C_Oxase_1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR033944; Cyt_c_oxase_su1_dom. DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 3: Inferred from homology; KW Calcium; Copper; Electron transport; Heme; Iron; Magnesium; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Reference proteome; Respiratory chain; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..525 FT /note="Cytochrome c oxidase subunit 1" FT /id="PRO_0000183298" FT TRANSMEM 25..45 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 71..91 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 108..128 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 152..172 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 190..210 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 241..261 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 274..294 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 317..337 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 344..364 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 387..407 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 420..440 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 459..479 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 48 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 53 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 69 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_note="low-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 247 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 251 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 297 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 298 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 375 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with subunit 2" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 376 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with subunit 2" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 383 FT /ligand="heme a3" FT /ligand_id="ChEBI:CHEBI:83282" FT /ligand_note="high-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 385 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_note="low-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00401" FT CROSSLNK 247..251 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250|UniProtKB:P00401" FT VARIANT 12 FT /note="A -> S (in strain: CB4856 and CB4857)" FT /evidence="ECO:0000269|PubMed:12644560" FT VARIANT 466 FT /note="I -> M (in strain: AB1, AB2, CB4852, CB4853, CB4855, FT CB4857, CB4858, KR314 and PB306)" FT /evidence="ECO:0000269|PubMed:12644560" SQ SEQUENCE 525 AA; 58464 MW; E3D051208B09396F CRC64; MNLYKKYQGG LAVWLESSNH KDIGTLYFIF GLWSGMVGTS FSLLIRLELA KPGFFLSNGQ LYNSVITAHA ILMIFFMVMP TMIGGFGNWL LPLMLGAPDM SFPRLNNLSF WLLPTSMLLI LDACFVDMGC GTSWTVYPPL STMGHPGSSV DLAIFSLHAA GLSSILGGIN FMCTTKNLRS SSISLEHMTL FVWTVFVTVF LLVLSLPVLA GAITMLLTDR NLNTSFFDPS TGGNPLIYQH LFWFFGHPEV YILILPAFGI VSQSTLYLTG KKEVFGALGM VYAILSIGLI GCVVWAHHMY TVGMDLDSRA YFSAATMVIA VPTGVKVFSW LATLFGMKMV FNPLLLWVLG FIFLFTLGGL TGVVLSNSSL DIILHDTYYV VSHFHYVLSL GAVFGIFTGV TLWWSFITGY VLDKLMMSAV FILLFIGVNL TFFPLHFAGL HGFPRKYLDY PDVYSVWNII ASYGSIISTA GLFLFIYVLL ESFFSYRLVI SDYYSNSSPE YCMSNYVFGH SYQSEIYFST TSLKN //