COX3_LOXAF
ID COX3_LOXAF Reviewed; 261 AA.
AC Q2I3F5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Cytochrome c oxidase subunit 3;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide III;
GN Name=MT-CO3; Synonyms=COIII, COXIII, MTCO3;
OS Loxodonta africana (African elephant).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=16448217; DOI=10.1371/journal.pbio.0040073;
RA Rogaev E.I., Moliaka Y.K., Malyarchuk B.A., Kondrashov F.A., Derenko M.V.,
RA Chumakov I., Grigorenko A.P.;
RT "Complete mitochondrial genome and phylogeny of Pleistocene mammoth
RT Mammuthus primigenius.";
RL PLoS Biol. 4:403-410(2006).
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 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I, COX5A,
CC COX5B, COX6A, COX6B, COX6C, COX7A, COX7B, COX7C, COX8 and NDUFA4, which
CC are encoded in the nuclear genome. The complex exists as a monomer or a
CC dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)).
CC {ECO:0000250|UniProtKB:P00415}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00415}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00415}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 3 family.
CC {ECO:0000305}.
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DR EMBL; DQ316069; ABC17910.1; -; Genomic_DNA.
DR RefSeq; NP_009285.2; NC_000934.1.
DR AlphaFoldDB; Q2I3F5; -.
DR SMR; Q2I3F5; -.
DR STRING; 9785.ENSLAFP00000029497; -.
DR Ensembl; ENSLAFT00000038057; ENSLAFP00000029497; ENSLAFG00000033291.
DR GeneID; 808787; -.
DR KEGG; lav:808787; -.
DR CTD; 4514; -.
DR eggNOG; KOG4664; Eukaryota.
DR GeneTree; ENSGT00390000013064; -.
DR HOGENOM; CLU_044071_0_0_1; -.
DR InParanoid; Q2I3F5; -.
DR OMA; SIYWWGS; -.
DR OrthoDB; 1304563at2759; -.
DR TreeFam; TF343435; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:Ensembl.
DR GO; GO:0045277; C:respiratory chain complex IV; ISS:UniProtKB.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR GO; GO:0008535; P:respiratory chain complex IV assembly; ISS:UniProtKB.
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..261
FT /note="Cytochrome c oxidase subunit 3"
FT /id="PRO_0000232860"
FT TOPO_DOM 1..15
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 16..34
FT /note="Helical; Name=I"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 35..40
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 41..66
FT /note="Helical; Name=II"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 67..72
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 73..105
FT /note="Helical; Name=III"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 106..128
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 129..152
FT /note="Helical; Name=IV"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 153..155
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 156..183
FT /note="Helical; Name=V"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 184..190
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 191..223
FT /note="Helical; Name=VI"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 224..232
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TRANSMEM 233..256
FT /note="Helical; Name=VII"
FT /evidence="ECO:0000250|UniProtKB:P00415"
FT TOPO_DOM 257..261
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:P00415"
SQ SEQUENCE 261 AA; 30096 MW; 4019FFBACD2D3AEA CRC64;
MTHQTHAYHM VDPSPWPLTG ALSALLMTSG LTMWFHYHSV TLLLLGLTTN ILTMFQWWRD
VVREGTFQGH HTPVVQESLR YGMILFITSE VLFFTGFFWA FYHSSLAPTP ELGSYWPPVG
VYPLNPLEVP LLNTSVLLAS GVTITWAHHS LMEGNRKNML QALLITILLG VYFTLLQMFE
YYEASFTISD GIYGSTFFVT TGFHGLHVII GSTFLLTCFI RQLKFHFTSN HHFGFEAAAW
YWHFVDVVWL FLYLSIYWWG S
