COX2_DROSI
ID COX2_DROSI Reviewed; 228 AA.
AC P50253; C6KI55; Q6UHJ8; Q6UHP0; Q8SGU5; Q9MD62; Q9MD70; Q9MDM7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 130.
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 simulans (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=7240;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8365657; DOI=10.1017/s0016672300031360;
RA Kaneko M., Satta Y., Matsuura E.T., Chigusa S.I.;
RT "Evolution of the mitochondrial ATPase 6 gene in Drosophila: unusually high
RT level of polymorphism in D. melanogaster.";
RL Genet. Res. 61:195-204(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-25; SER-129 AND
RP ILE-130.
RC STRAIN=14021-0251.0;
RX PubMed=11884169; DOI=10.1006/mpev.2001.1053;
RA O'Grady P.M., Kidwell M.G.;
RT "Phylogeny of the subgenus sophophora (Diptera: drosophilidae) based on
RT combined analysis of nuclear and mitochondrial sequences.";
RL Mol. Phylogenet. Evol. 22:442-453(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-129; ILE-130 AND
RP ILE-165.
RC STRAIN=AU023, KY003, KY004, KY005, KY006, KY007, KY009, KY011, KY017,
RC KY019, KY021, KY022, KY025, KY027, KY028, KY032, KY045, KY048, KY052,
RC KY053, KY071, KY201, KY202, KY203, KY204, KY207, KY213, KY214, KY215,
RC KY216, KY217, KY218, KY220, KY224, KY227, KY232, KY234, KY235, KY240,
RC KY242, KY244, KY245, KY249, KY251, KY252, KY257, KY259, KY260, MW13, MW16,
RC MW26, MW34, MW39, MW41, MW42, MW51, MW52, MW61, TZ03a, TZ05a, TZ06a, TZ07a,
RC TZ08a, TZ09a, TZ13a, TZ15a, TZ17a, TZ23, TZ33, TZ35, TZ37, TZ38, TZ39,
RC TZ40, TZ41, TZ42, TZ46, and TZ49;
RX PubMed=14660690; DOI=10.1093/molbev/msh028;
RA Ballard J.W.O.;
RT "Sequential evolution of a symbiont inferred from the host: Wolbachia and
RT Drosophila simulans.";
RL Mol. Biol. Evol. 21:428-442(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-118; SER-129; ILE-130
RP AND ILE-165.
RA Tarnowski H.E., Marshall K., Sinclair B.J.;
RT "Distinguishing Drosophila melanogaster from Drosophila simulans using
RT restriction digest of mitochondrial COII.";
RL Submitted (MAY-2009) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS SER-115;
RP TYR-118; SER-129; ILE-130 AND ILE-165.
RC STRAIN=C167, DSR, DSW, HW00, HW09, MD106, MD111, MD112, MD199, MD221,
RC MD225, MDW86, NC37, NC48, RU00, RU01, RU07, RU259, RU35, Sc00, TT00, and
RC TT01;
RX PubMed=10903373; DOI=10.1007/s002390010067;
RA Ballard J.W.;
RT "Comparative genomics of mitochondrial DNA in Drosophila simulans.";
RL J. Mol. Evol. 51:64-75(2000).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD13956.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; S64977; AAD13956.2; ALT_INIT; Genomic_DNA.
DR EMBL; AF474082; AAL83266.1; -; Genomic_DNA.
DR EMBL; AY370272; AAR21759.1; -; Genomic_DNA.
DR EMBL; AY370273; AAR21760.1; -; Genomic_DNA.
DR EMBL; AY370274; AAR21761.1; -; Genomic_DNA.
DR EMBL; AY370275; AAR21762.1; -; Genomic_DNA.
DR EMBL; AY370276; AAR21763.1; -; Genomic_DNA.
DR EMBL; AY370277; AAR21764.1; -; Genomic_DNA.
DR EMBL; AY370278; AAR21765.1; -; Genomic_DNA.
DR EMBL; AY370279; AAR21766.1; -; Genomic_DNA.
DR EMBL; AY370280; AAR21767.1; -; Genomic_DNA.
DR EMBL; AY370281; AAR21768.1; -; Genomic_DNA.
DR EMBL; AY370282; AAR21769.1; -; Genomic_DNA.
DR EMBL; AY370283; AAR21770.1; -; Genomic_DNA.
DR EMBL; AY370284; AAR21771.1; -; Genomic_DNA.
DR EMBL; AY370285; AAR21772.1; -; Genomic_DNA.
DR EMBL; AY370286; AAR21773.1; -; Genomic_DNA.
DR EMBL; AY370287; AAR21774.1; -; Genomic_DNA.
DR EMBL; AY370288; AAR21775.1; -; Genomic_DNA.
DR EMBL; AY370289; AAR21776.1; -; Genomic_DNA.
DR EMBL; AY370290; AAR21777.1; -; Genomic_DNA.
DR EMBL; AY370291; AAR21778.1; -; Genomic_DNA.
DR EMBL; AY370292; AAR21779.1; -; Genomic_DNA.
DR EMBL; AY370293; AAR21780.1; -; Genomic_DNA.
DR EMBL; AY370294; AAR21781.1; -; Genomic_DNA.
DR EMBL; AY370295; AAR21782.1; -; Genomic_DNA.
DR EMBL; AY370296; AAR21783.1; -; Genomic_DNA.
DR EMBL; AY370297; AAR21784.1; -; Genomic_DNA.
DR EMBL; AY370298; AAR21785.1; -; Genomic_DNA.
DR EMBL; AY370299; AAR21786.1; -; Genomic_DNA.
DR EMBL; AY370300; AAR21787.1; -; Genomic_DNA.
DR EMBL; AY370301; AAR21788.1; -; Genomic_DNA.
DR EMBL; AY370302; AAR21789.1; -; Genomic_DNA.
DR EMBL; AY370303; AAR21790.1; -; Genomic_DNA.
DR EMBL; AY370304; AAR21791.1; -; Genomic_DNA.
DR EMBL; AY370305; AAR21792.1; -; Genomic_DNA.
DR EMBL; AY370306; AAR21793.1; -; Genomic_DNA.
DR EMBL; AY370307; AAR21794.1; -; Genomic_DNA.
DR EMBL; AY370308; AAR21795.1; -; Genomic_DNA.
DR EMBL; AY370309; AAR21796.1; -; Genomic_DNA.
DR EMBL; AY370310; AAR21797.1; -; Genomic_DNA.
DR EMBL; AY370311; AAR21798.1; -; Genomic_DNA.
DR EMBL; AY370312; AAR21799.1; -; Genomic_DNA.
DR EMBL; AY370313; AAR21800.1; -; Genomic_DNA.
DR EMBL; AY370314; AAR21801.1; -; Genomic_DNA.
DR EMBL; AY370315; AAR21802.1; -; Genomic_DNA.
DR EMBL; AY370316; AAR21803.1; -; Genomic_DNA.
DR EMBL; AY370317; AAR21804.1; -; Genomic_DNA.
DR EMBL; AY370318; AAR21805.1; -; Genomic_DNA.
DR EMBL; AY370319; AAR21806.1; -; Genomic_DNA.
DR EMBL; AY370320; AAR21807.1; -; Genomic_DNA.
DR EMBL; AY370321; AAR21808.1; -; Genomic_DNA.
DR EMBL; AY370322; AAR21809.1; -; Genomic_DNA.
DR EMBL; AY370323; AAR21810.1; -; Genomic_DNA.
DR EMBL; AY370324; AAR21811.1; -; Genomic_DNA.
DR EMBL; AY370325; AAR21812.1; -; Genomic_DNA.
DR EMBL; AY370326; AAR21813.1; -; Genomic_DNA.
DR EMBL; AY370327; AAR21814.1; -; Genomic_DNA.
DR EMBL; AY370328; AAR21815.1; -; Genomic_DNA.
DR EMBL; AY370329; AAR21816.1; -; Genomic_DNA.
DR EMBL; AY370330; AAR21817.1; -; Genomic_DNA.
DR EMBL; AY370331; AAR21818.1; -; Genomic_DNA.
DR EMBL; AY370332; AAR21819.1; -; Genomic_DNA.
DR EMBL; AY370333; AAR21820.1; -; Genomic_DNA.
DR EMBL; AY370334; AAR21821.1; -; Genomic_DNA.
DR EMBL; AY370335; AAR21822.1; -; Genomic_DNA.
DR EMBL; AY370336; AAR21823.1; -; Genomic_DNA.
DR EMBL; AY370337; AAR21824.1; -; Genomic_DNA.
DR EMBL; AY370338; AAR21825.1; -; Genomic_DNA.
DR EMBL; AY370339; AAR21826.1; -; Genomic_DNA.
DR EMBL; AY370340; AAR21827.1; -; Genomic_DNA.
DR EMBL; AY370341; AAR21828.1; -; Genomic_DNA.
DR EMBL; AY370342; AAR21829.1; -; Genomic_DNA.
DR EMBL; AY370343; AAR21830.1; -; Genomic_DNA.
DR EMBL; AY370344; AAR21831.1; -; Genomic_DNA.
DR EMBL; AY370345; AAR21832.1; -; Genomic_DNA.
DR EMBL; AY370346; AAR21833.1; -; Genomic_DNA.
DR EMBL; AY370347; AAR21834.1; -; Genomic_DNA.
DR EMBL; AY370348; AAR21835.1; -; Genomic_DNA.
DR EMBL; AY370349; AAR21836.1; -; Genomic_DNA.
DR EMBL; AY370350; AAR21837.1; -; Genomic_DNA.
DR EMBL; AY518670; AAR91395.1; -; Genomic_DNA.
DR EMBL; AY518671; AAR91403.1; -; Genomic_DNA.
DR EMBL; AY518672; AAR91416.1; -; Genomic_DNA.
DR EMBL; AY518673; AAR91429.1; -; Genomic_DNA.
DR EMBL; AY518674; AAR91442.1; -; Genomic_DNA.
DR EMBL; GQ222022; ACT09365.1; -; Genomic_DNA.
DR EMBL; AF200833; AAF77297.1; -; Genomic_DNA.
DR EMBL; AF200834; AAF77311.1; -; Genomic_DNA.
DR EMBL; AF200835; AAF77318.1; -; Genomic_DNA.
DR EMBL; AF200836; AAF77331.1; -; Genomic_DNA.
DR EMBL; AF200837; AAF77344.1; -; Genomic_DNA.
DR EMBL; AF200838; AAF77357.1; -; Genomic_DNA.
DR EMBL; AF200839; AAF77371.1; -; Genomic_DNA.
DR EMBL; AF200840; AAF77383.1; -; Genomic_DNA.
DR EMBL; AF200841; AAF77396.1; -; Genomic_DNA.
DR EMBL; AF200842; AAF77414.1; -; Genomic_DNA.
DR EMBL; AF200843; AAF77422.1; -; Genomic_DNA.
DR EMBL; AF200844; AAF77435.1; -; Genomic_DNA.
DR EMBL; AF200845; AAF77448.1; -; Genomic_DNA.
DR EMBL; AF200846; AAF77461.1; -; Genomic_DNA.
DR EMBL; AF200847; AAF77474.1; -; Genomic_DNA.
DR EMBL; AF200848; AAF77487.1; -; Genomic_DNA.
DR EMBL; AF200849; AAF77501.1; -; Genomic_DNA.
DR EMBL; AF200850; AAF77513.1; -; Genomic_DNA.
DR EMBL; AF200851; AAF77527.1; -; Genomic_DNA.
DR EMBL; AF200852; AAF77539.1; -; Genomic_DNA.
DR EMBL; AF200853; AAF77552.1; -; Genomic_DNA.
DR EMBL; AF200854; AAF77565.1; -; Genomic_DNA.
DR RefSeq; NP_982324.1; NC_005781.1.
DR AlphaFoldDB; P50253; -.
DR SMR; P50253; -.
DR STRING; 7240.P50253; -.
DR GeneID; 2760956; -.
DR KEGG; dsi:COX2; -.
DR CTD; 4513; -.
DR Proteomes; UP000000304; Mitochondrion.
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:0070469; C:respirasome; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
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_0000183585"
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 25
FT /note="D -> A (in strain: 14021-0251.0)"
FT /evidence="ECO:0000269|PubMed:11884169"
FT VARIANT 115
FT /note="N -> S (in strain: HW00, HW09, NC37, NC48, TT00 and
FT TT01)"
FT /evidence="ECO:0000269|PubMed:10903373"
FT VARIANT 118
FT /note="F -> Y (in strain: MD106, MD225 and RU35)"
FT /evidence="ECO:0000269|PubMed:10903373, ECO:0000269|Ref.4"
FT VARIANT 129
FT /note="T -> S (in strain: 14021-0251.0, C167, AU023, DSR,
FT DSW, KY007, KY045, KY201, KY215, MD106, MD111, MD112,
FT MD199, MD221, MD225, MDW86, RU00, RU01, RU07, RU35, RU259
FT and Sc00)"
FT /evidence="ECO:0000269|PubMed:10903373,
FT ECO:0000269|PubMed:11884169, ECO:0000269|PubMed:14660690,
FT ECO:0000269|Ref.4"
FT VARIANT 130
FT /note="T -> I (in strain: 14021-0251.0, C167, AU023, DSR,
FT DSW, KY007, KY045, KY201, KY215, MD106, MD111, MD112,
FT MD199, MD221, MD225, MDW86, RU00, RU01, RU07, RU35, RU259
FT and Sc00)"
FT /evidence="ECO:0000269|PubMed:10903373,
FT ECO:0000269|PubMed:11884169, ECO:0000269|PubMed:14660690,
FT ECO:0000269|Ref.4"
FT VARIANT 165
FT /note="V -> I (in strain: AU023, C167, DSR, DSW, KY007,
FT KY045, KY201, KY215, MD106, MD111, MD112, MD199, MD221,
FT MD225, MDW86, RU00, RU01, RU07, RU35, RU259 and Sc00)"
FT /evidence="ECO:0000269|PubMed:10903373,
FT ECO:0000269|PubMed:14660690, ECO:0000269|Ref.4"
FT VARIANT 218
FT /note="H -> N (in strain: 14021-0251.0)"
SQ SEQUENCE 228 AA; 26148 MW; E7C1A3EE91730B85 CRC64;
MSTWANLGLQ DSASPLMEQL IFFHDHALLI LVMITVLVGY LMFMLFFNNY VNRFLLHGQL
IEMIWTILPA IILLFIALPS LRLLYLLDEI NEPSVTLKSI GHQWYWSYEY SDFNNIEFDS
YMIPTNELTT DGFRLLDVDN RVILPMNSQI RILVTAADVI HSWTVPALGV KVDGTPGRLN
QTNFFINRPG LFYGQCSEIC GANHSFMPIV IESVPVNHFI KWISSNNS
