COX3_CAEEL
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 03-AUG-2022, entry version 138.
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},
GN cox-3 {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}.
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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; -.
DR PaxDb; P24891; -.
DR EnsemblMetazoa; MTCE.23.1; MTCE.23.1; WBGene00010962.
DR GeneID; 2565701; -.
DR KEGG; cel:COX3; -.
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; 1304563at2759; -.
DR PhylomeDB; P24891; -.
DR PRO; PR:P24891; -.
DR Proteomes; UP000001940; Mitochondrion.
DR Bgee; WBGene00010962; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0015453; F:oxidoreduction-driven active transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
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; 1.20.120.80; -; 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; PTHR11403; 1.
DR Pfam; PF00510; COX3; 1.
DR SUPFAM; SSF81452; SSF81452; 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
