COX1_CAEEL
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 03-AUG-2022, entry version 145.
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},
GN cox-1 {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}.
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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; -.
DR EPD; P24893; -.
DR PaxDb; P24893; -.
DR EnsemblMetazoa; MTCE.26.1; MTCE.26.1; WBGene00010964.
DR GeneID; 2565700; -.
DR KEGG; cel:COX1; -.
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; 728231at2759; -.
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 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: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:0009060; P:aerobic respiration; IBA:GO_Central.
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 GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; -; 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; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 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
