COX2_DROME
ID COX2_DROME Reviewed; 228 AA.
AC P00408; B2L9S3; B6E0V9; Q05GI7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
GN Name=mt:CoII; Synonyms=COII;
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].
RC STRAIN=Oregon-R; TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-39.
RC STRAIN=Alstonvl, Brownsvl, Dahomey, Japan, Mysore, and W1118iso;
RX PubMed=18727704; DOI=10.1111/j.1474-9726.2008.00428.x;
RA Clancy D.J.;
RT "Variation in mitochondrial genotype has substantial lifespan effects which
RT may be modulated by nuclear background.";
RL Aging Cell 7:795-804(2008).
RN [5]
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-225.
RC STRAIN=LHM;
RX PubMed=17151264; DOI=10.1534/genetics.105.052050;
RA Dowling D.K., Friberg U., Hailer F., Arnqvist G.;
RT "Intergenomic epistasis for fitness: within-population interactions between
RT cytoplasmic and nuclear genes in Drosophila melanogaster.";
RL Genetics 175:235-244(2007).
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:P00410}.
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:P00410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00410};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000250|UniProtKB:P00410};
CC Note=Binds a dinuclear copper A center per subunit.
CC {ECO:0000250|UniProtKB:P00410};
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:P00410}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P00410}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P00410}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; J01404; AAB59240.1; -; Genomic_DNA.
DR EMBL; AF200828; AAF77228.1; -; Genomic_DNA.
DR EMBL; AF200829; AAF77240.1; -; Genomic_DNA.
DR EMBL; AJ400907; CAB91053.1; -; Genomic_DNA.
DR EMBL; FJ190105; ACI28544.1; -; Genomic_DNA.
DR EMBL; FJ190106; ACI28557.1; -; Genomic_DNA.
DR EMBL; FJ190107; ACI28570.1; -; Genomic_DNA.
DR EMBL; FJ190108; ACI28583.1; -; Genomic_DNA.
DR EMBL; FJ190109; ACI28596.1; -; Genomic_DNA.
DR EMBL; FJ190110; ACI28609.1; -; Genomic_DNA.
DR EMBL; EU493757; ACC94832.1; -; Genomic_DNA.
DR EMBL; U37541; AAC47813.1; -; Genomic_DNA.
DR EMBL; KJ947872; AIC64006.1; -; Genomic_DNA.
DR EMBL; AM403329; CAL48258.1; -; Genomic_DNA.
DR PIR; A00476; OBFF2.
DR RefSeq; YP_009047268.1; NC_024511.2.
DR AlphaFoldDB; P00408; -.
DR SMR; P00408; -.
DR BioGRID; 2595064; 19.
DR STRING; 7227.FBpp0100177; -.
DR PaxDb; P00408; -.
DR PRIDE; P00408; -.
DR EnsemblMetazoa; FBtr0100863; FBpp0100177; FBgn0013675.
DR GeneID; 19893535; -.
DR KEGG; dme:Dmel_CG34069; -.
DR CTD; 4513; -.
DR FlyBase; FBgn0013675; mt:CoII.
DR VEuPathDB; VectorBase:FBgn0013675; -.
DR eggNOG; KOG4767; Eukaryota.
DR GeneTree; ENSGT00390000017410; -.
DR HOGENOM; CLU_036876_2_3_1; -.
DR InParanoid; P00408; -.
DR OMA; WSYEYTD; -.
DR OrthoDB; 1432833at2759; -.
DR PhylomeDB; P00408; -.
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 GenomeRNAi; 19893535; -.
DR PRO; PR:P00408; -.
DR Proteomes; UP000000803; Mitochondrion.
DR Bgee; FBgn0013675; Expressed in midgut and 14 other tissues.
DR ExpressionAtlas; P00408; baseline and differential.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; ISS:FlyBase.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; ISS:FlyBase.
DR CDD; cd13912; CcO_II_C; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR034210; CcO_II_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR02866; CoxB; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 3: Inferred from homology;
KW Copper; Electron transport; Magnesium; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..228
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183579"
FT TOPO_DOM 1..26
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 49..62
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..228
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 198
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with subunit 1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 204
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT BINDING 207
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000250|UniProtKB:P00410"
FT VARIANT 39
FT /note="G -> S (in strain: Mysore)"
FT /evidence="ECO:0000269|PubMed:18727704"
SQ SEQUENCE 228 AA; 26191 MW; 65FF4502C543335D CRC64;
MSTWANLGLQ DSASPLMEQL IFFHDHALLI LVMITVLVGY LMFMLFFNNY VNRFLLHGQL
IEMIWTILPA IILLFIALPS LRLLYLLDEI NEPSVTLKSI GHQWYWSYEY SDFNNIEFDS
YMIPTNELMT DGFRLLDVDN RVVLPMNSQI RILVTAADVI HSWTVPALGV KVDGTPGRLN
QTNFFINRPG LFYGQCSEIC GANHSFMPIV IESVPVNYFI KWISSNNS
