ID COX3_CAEEL Reviewed; 255 AA. AC P24891; DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot. DT 11-APR-2003, sequence version 3. DT 24-JAN-2024, entry version 143. DE RecName: Full=Cytochrome c oxidase subunit 3; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide III; GN Name=ctc-3 {ECO:0000312|WormBase:MTCE.23}; GN Synonyms=coIII {ECO:0000312|WormBase:MTCE.23}, cox-3 GN {ECO:0000312|WormBase:MTCE.23}; GN ORFNames=MTCE.23 {ECO:0000312|WormBase:MTCE.23}; 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 [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 [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96 AND 119-255, AND VARIANTS RP TRP-185; LEU-187; SER-222 AND ASN-235. 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 [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:P00420}. 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:P00420}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000250|UniProtKB:P00420}; 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:P00420}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P00420}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P00420}. CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 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; X54252; CAA38157.1; -; Genomic_DNA. DR EMBL; AY171178; AAO16431.1; -; Genomic_DNA. DR EMBL; AY171179; AAO16433.1; -; Genomic_DNA. DR EMBL; AY171180; AAO16435.1; -; Genomic_DNA. DR EMBL; AY171181; AAO16437.1; -; Genomic_DNA. DR EMBL; AY171182; AAO16439.1; -; Genomic_DNA. DR EMBL; AY171183; AAO16441.1; -; Genomic_DNA. DR EMBL; AY171184; AAO16443.1; -; Genomic_DNA. DR EMBL; AY171185; AAO16445.1; -; Genomic_DNA. DR EMBL; AY171186; AAO16447.1; -; Genomic_DNA. DR EMBL; AY171187; AAO16449.1; -; Genomic_DNA. DR EMBL; AY171188; AAO16451.1; -; Genomic_DNA. DR EMBL; AY171189; AAO16453.1; -; Genomic_DNA. DR EMBL; AY171190; AAO16455.1; -; Genomic_DNA. DR EMBL; AY171191; AAO16457.1; -; Genomic_DNA. DR EMBL; AY171192; AAO16459.1; -; Genomic_DNA. DR EMBL; AY171193; AAO16250.1; -; Genomic_DNA. DR EMBL; AY171194; AAO16254.1; -; Genomic_DNA. DR EMBL; AY171195; AAO16258.1; -; Genomic_DNA. DR EMBL; AY171196; AAO16262.1; -; Genomic_DNA. DR EMBL; AY171197; AAO16266.1; -; Genomic_DNA. DR EMBL; AY171198; AAO16270.1; -; Genomic_DNA. DR EMBL; AY171199; AAO16274.1; -; Genomic_DNA. DR EMBL; AY171200; AAO16278.1; -; Genomic_DNA. DR EMBL; AY171201; AAO16282.1; -; Genomic_DNA. DR EMBL; AY171202; AAO16286.1; -; Genomic_DNA. DR EMBL; AY171203; AAO16290.1; -; Genomic_DNA. DR EMBL; AY171204; AAO16294.1; -; Genomic_DNA. DR EMBL; AY171205; AAO16298.1; -; Genomic_DNA. DR EMBL; AY171206; AAO16302.1; -; Genomic_DNA. DR EMBL; AY171207; AAO16306.1; -; Genomic_DNA. DR PIR; S26032; S26032. DR RefSeq; NP_006959.1; NC_001328.1. DR AlphaFoldDB; P24891; -. DR SMR; P24891; -. DR STRING; 6239.MTCE.23.1; -. DR PaxDb; 6239-MTCE-23; -. DR EnsemblMetazoa; MTCE.23.1; MTCE.23.1; WBGene00010962. DR GeneID; 2565701; -. DR KEGG; cel:KEF34_p06; -. DR AGR; WB:WBGene00010962; -. DR CTD; 4514; -. DR WormBase; MTCE.23; CE34069; WBGene00010962; ctc-3. DR eggNOG; KOG4664; Eukaryota. DR GeneTree; ENSGT00390000013064; -. DR HOGENOM; CLU_044071_0_0_1; -. DR InParanoid; P24891; -. DR OrthoDB; 984876at2759; -. DR PhylomeDB; P24891; -. DR PRO; PR:P24891; -. DR Proteomes; UP000001940; Mitochondrion. DR Bgee; WBGene00010962; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IBA:GO_Central. DR CDD; cd01665; Cyt_c_Oxidase_III; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.80; Cytochrome c oxidase, subunit III, four-helix bundle; 1. DR InterPro; IPR024791; Cyt_c/ubiquinol_Oxase_su3. DR InterPro; IPR033945; Cyt_c_oxase_su3_dom. DR InterPro; IPR000298; Cyt_c_oxidase-like_su3. DR InterPro; IPR035973; Cyt_c_oxidase_su3-like_sf. DR InterPro; IPR013833; Cyt_c_oxidase_su3_a-hlx. DR PANTHER; PTHR11403:SF7; CYTOCHROME C OXIDASE SUBUNIT 3; 1. DR PANTHER; PTHR11403; CYTOCHROME C OXIDASE SUBUNIT III; 1. DR Pfam; PF00510; COX3; 1. DR SUPFAM; SSF81452; Cytochrome c oxidase subunit III-like; 1. DR PROSITE; PS50253; COX3; 1. PE 3: Inferred from homology; KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome; KW Translocase; Transmembrane; Transmembrane helix. FT CHAIN 1..255 FT /note="Cytochrome c oxidase subunit 3" FT /id="PRO_0000183750" FT TRANSMEM 12..32 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 34..54 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 77..97 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 123..143 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 156..176 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 190..210 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 231..251 FT /note="Helical" FT /evidence="ECO:0000255" FT VARIANT 185 FT /note="G -> W (in strain: PB306)" FT /evidence="ECO:0000269|PubMed:12644560" FT VARIANT 187 FT /note="F -> L (in strain: PB306)" FT /evidence="ECO:0000269|PubMed:12644560" FT VARIANT 222 FT /note="N -> S (in strain: CB4854)" FT /evidence="ECO:0000269|PubMed:12644560" FT VARIANT 235 FT /note="Y -> N (in strain: CB4856)" FT /evidence="ECO:0000269|PubMed:12644560" FT CONFLICT 95 FT /note="C -> W (in Ref. 1; CAA38157)" FT /evidence="ECO:0000305" SQ SEQUENCE 255 AA; 29387 MW; 064200C7300696CD CRC64; MFHNFHILSL SSYAYNLFFA SAGMLSSLVM FFKFGLYELF IFTLFSVLFI SFAWGKDIAM EGLSGYHNFF VMDGFKFGVI LFVFSEFMFF FCIFCTFFDA ALVPVHELGE TWSPFGMHLV NPFGVPLLNT IILLSSGVTV TWAHHSLLSN KSCTNSMILT CLLAAYFTGI QLMEYMEASF SIADGVFGSI FYLSTGFHGI HVLCGGLFLA FNFLRLLKNH FNYNHHLGLE FAILYWHFVD VVWLFLFVFV YWWSY //