ID   COX3_DROME              Reviewed;         262 AA.
AC   P00417; B1PTQ2; Q7HMA0; Q9MGN4;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   24-JAN-2024, entry version 174.
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:CoIII; Synonyms=CoIII;
OS   Drosophila melanogaster (Fruit fly).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT MET-170.
RC   STRAIN=Oregon-R, and Zimbabwe 53;
RX   PubMed=10903372; DOI=10.1007/s002390010066;
RA   Ballard J.W.O.;
RT   "Comparative genomics of mitochondrial DNA in members of the Drosophila
RT   melanogaster subgroup.";
RL   J. Mol. Evol. 51:48-63(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Paris;
RX   PubMed=11298822; DOI=10.1046/j.1365-2540.2001.00814.x;
RA   Azou Y., Bregliano J.C.;
RT   "I-R system of hybrid dysgenesis in Drosophila melanogaster: analysis of
RT   the mitochondrial DNA in reactive strains exhibiting different potentials
RT   for I factor transposition.";
RL   Heredity 86:110-116(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=18296276; DOI=10.1098/rsbl.2007.0575;
RA   O'Grady P.M., DeSalle R.;
RT   "Out of Hawaii: the origin and biogeography of the genus Scaptomyza
RT   (Diptera: Drosophilidae).";
RL   Biol. Lett. 4:195-199(2008).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8825764; DOI=10.1111/j.1365-2583.1995.tb00032.x;
RA   Lewis D.L., Farr C.L., Kaguni L.S.;
RT   "Drosophila melanogaster mitochondrial DNA: completion of the nucleotide
RT   sequence and evolutionary comparisons.";
RL   Insect Mol. Biol. 4:263-278(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RA   Wan K., Celniker S.;
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-179.
RC   STRAIN=Oregon-R;
RX   PubMed=6408489; DOI=10.1038/304234a0;
RA   de Bruijn M.H.L.;
RT   "Drosophila melanogaster mitochondrial DNA, a novel organization and
RT   genetic code.";
RL   Nature 304:234-241(1983).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-262.
RX   PubMed=6304652; DOI=10.1093/nar/11.8.2411;
RA   Clary D.O., Wahleithner J.A., Wolstenholme D.R.;
RT   "Transfer RNA genes in Drosophila mitochondrial DNA: related 5' flanking
RT   sequences and comparisons to mammalian mitochondrial tRNA genes.";
RL   Nucleic Acids Res. 11:2411-2425(1983).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 179-262.
RC   STRAIN=Bretagne;
RX   PubMed=3130291; DOI=10.1093/genetics/118.4.649;
RA   Garesse R.;
RT   "Drosophila melanogaster mitochondrial DNA: gene organization and
RT   evolutionary considerations.";
RL   Genetics 118:649-663(1988).
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; AF200828; AAF77231.1; -; Genomic_DNA.
DR   EMBL; AF200829; AAF77243.1; -; Genomic_DNA.
DR   EMBL; AJ400907; CAB91056.1; -; Genomic_DNA.
DR   EMBL; EU493887; ACA62455.1; -; Genomic_DNA.
DR   EMBL; KJ947872; AIC64009.1; -; Genomic_DNA.
DR   EMBL; U37541; AAC47816.1; -; Genomic_DNA.
DR   EMBL; J01404; AAB59243.1; -; Genomic_DNA.
DR   EMBL; M37275; AAA69708.1; -; Genomic_DNA.
DR   PIR; A00485; OTFF3.
DR   RefSeq; YP_009047271.1; NC_024511.2.
DR   AlphaFoldDB; P00417; -.
DR   SMR; P00417; -.
DR   STRING; 7227.FBpp0100180; -.
DR   PaxDb; 7227-FBpp0100180; -.
DR   EnsemblMetazoa; FBtr0100868; FBpp0100180; FBgn0013676.
DR   GeneID; 19893540; -.
DR   KEGG; dme:Dmel_CG34074; -.
DR   AGR; FB:FBgn0013676; -.
DR   CTD; 4514; -.
DR   FlyBase; FBgn0013676; mt:CoIII.
DR   VEuPathDB; VectorBase:FBgn0013676; -.
DR   eggNOG; KOG4664; Eukaryota.
DR   GeneTree; ENSGT00390000013064; -.
DR   HOGENOM; CLU_044071_0_0_1; -.
DR   InParanoid; P00417; -.
DR   OMA; SIYWWGS; -.
DR   OrthoDB; 984876at2759; -.
DR   PhylomeDB; P00417; -.
DR   Reactome; R-DME-5628897; TP53 Regulates Metabolic Genes.
DR   Reactome; R-DME-611105; Respiratory electron transport.
DR   Reactome; R-DME-9707564; Cytoprotection by HMOX1.
DR   BioGRID-ORCS; 19893540; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 19893540; -.
DR   PRO; PR:P00417; -.
DR   Proteomes; UP000000803; Mitochondrion.
DR   Bgee; FBgn0013676; Expressed in brain and 11 other cell types or tissues.
DR   ExpressionAtlas; P00417; baseline and differential.
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..262
FT                   /note="Cytochrome c oxidase subunit 3"
FT                   /id="PRO_0000183767"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        198..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VARIANT         170
FT                   /note="L -> M (in strain: Zimbabwe 53)"
FT                   /evidence="ECO:0000269|PubMed:10903372"
SQ   SEQUENCE   262 AA;  30064 MW;  68D5AEFC2297C130 CRC64;
     MSTHSNHPFH LVDYSPWPLT GAIGAMTTVS GMVKWFHQYD ISLFVLGNII TILTVYQWWR
     DVSREGTYQG LHTYAVTIGL RWGMILFILS EVLFFVSFFW AFFHSSLSPA IELGASWPPM
     GIISFNPFQI PLLNTAILLA SGVTVTWAHH SLMENNHSQT TQGLFFTVLL GIYFTILQAY
     EYIEAPFTIA DSIYGSTFFM ATGFHGIHVL IGTTFLLVCL LRHLNNHFSK NHHFGFEAAA
     WYWHFVDVVW LFLYITIYWW GG
//