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 13-SEP-2023, entry version 133. 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, RC MW16, MW26, MW34, MW39, MW41, MW42, MW51, MW52, MW61, TZ03a, TZ05a, RC TZ06a, TZ07a, TZ08a, TZ09a, TZ13a, TZ15a, TZ17a, TZ23, TZ33, TZ35, RC TZ37, TZ38, TZ39, 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, RC and 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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: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; Cupredoxins - blue copper proteins; 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 NCBIfam; TIGR02866; CoxB; 1. DR PANTHER; PTHR22888:SF9; CYTOCHROME C OXIDASE SUBUNIT 2; 1. DR PANTHER; PTHR22888; CYTOCHROME C OXIDASE, SUBUNIT II; 1. DR Pfam; PF00116; COX2; 1. DR Pfam; PF02790; COX2_TM; 1. DR PRINTS; PR01166; CYCOXIDASEII. DR SUPFAM; SSF49503; Cupredoxins; 1. DR SUPFAM; SSF81464; Cytochrome c oxidase subunit II-like, transmembrane region; 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 //