ID COX1_DROSI Reviewed; 511 AA. AC Q34388; H9EAT7; H9EAV0; Q34390; Q34393; Q36710; Q9MD75; Q9MDV2; Q9ME63; DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2012, sequence version 3. DT 22-FEB-2023, entry version 120. DE RecName: Full=Cytochrome c oxidase subunit 1; DE EC=7.1.1.9; DE AltName: Full=Cytochrome c oxidase polypeptide I; GN Name=mt:CoI; Synonyms=CoI; 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 [LARGE SCALE GENOMIC DNA], AND VARIANTS ILE-450 AND RP PHE-468. RC STRAIN=C167, DSR, DSW, HW00, HW09, MD106, MD111, MD112, MD119, 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). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Australia, and Kenya; 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Kenya; RX PubMed=23010820; DOI=10.1038/hdy.2012.60; RA Wolff J.N., Nafisinia M., Sutovsky P., Ballard J.W.; RT "Paternal transmission of mitochondrial DNA as an integral part of RT mitochondrial inheritance in metapopulations of Drosophila simulans."; RL Heredity 110:57-62(2013). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-498, AND VARIANTS ILE-450 AND RP PHE-468. RC STRAIN=Hawaii, and Sl3; RX PubMed=2124697; DOI=10.1073/pnas.87.24.9558; RA Satta Y., Takahata N.; RT "Evolution of Drosophila mitochondrial DNA and the history of the RT melanogaster subgroup."; RL Proc. Natl. Acad. Sci. U.S.A. 87:9558-9562(1990). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-101. RC STRAIN=Nairobi; RX PubMed=2832697; DOI=10.1093/oxfordjournals.molbev.a040464; RA Satta Y., Ishiwa H., Chigusa S.I.; RT "Analysis of nucleotide substitutions of mitochondrial DNAs in Drosophila RT melanogaster and its sibling species."; RL Mol. Biol. Evol. 4:638-650(1987). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-10, AND IDENTIFICATION OF PROBABLE RP INITIATION SITE. RX PubMed=19533212; DOI=10.1007/s00239-009-9255-0; RA Montooth K.L., Abt D.N., Hofmann J.W., Rand D.M.; RT "Comparative genomics of Drosophila mtDNA: Novel features of conservation RT and change across functional domains and lineages."; RL J. Mol. Evol. 69:94-114(2009). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-510. 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). 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:P00401}. 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:P00401}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437; CC Evidence={ECO:0000250|UniProtKB:P00401}; CC -!- COFACTOR: CC Name=heme; Xref=ChEBI:CHEBI:30413; CC Evidence={ECO:0000250|UniProtKB:P00401}; CC Note=Binds 2 heme A groups non-covalently per subunit. CC {ECO:0000250|UniProtKB:P00401}; CC -!- COFACTOR: CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; CC Evidence={ECO:0000250|UniProtKB:P00401}; CC Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00401}; CC -!- PATHWAY: Energy metabolism; oxidative phosphorylation. CC {ECO:0000250|UniProtKB:P00401}. 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:P00401}. CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000250|UniProtKB:P00401}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:P00401}. CC -!- SIMILARITY: Belongs to the heme-copper respiratory oxidase family. CC {ECO:0000305}. CC -!- CAUTION: There is no mitochondrial-type translation initiation codon CC present in frame in the sequence. In PubMed:19533212, the authors CC suggest the presence of a novel start codon coding for either Pro or CC Ser in Drosophila CoI transcripts. {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; AF200833; AAF77296.1; -; Genomic_DNA. DR EMBL; AF200834; AAF77310.1; -; Genomic_DNA. DR EMBL; AF200835; AAF77324.1; -; Genomic_DNA. DR EMBL; AF200836; AAF77336.1; -; Genomic_DNA. DR EMBL; AF200837; AAF77349.1; -; Genomic_DNA. DR EMBL; AF200838; AAF77368.1; -; Genomic_DNA. DR EMBL; AF200839; AAF77376.1; -; Genomic_DNA. DR EMBL; AF200840; AAF77393.1; -; Genomic_DNA. DR EMBL; AF200841; AAF77401.1; -; Genomic_DNA. DR EMBL; AF200842; AAF77413.1; -; Genomic_DNA. DR EMBL; AF200843; AAF77427.1; -; Genomic_DNA. DR EMBL; AF200844; AAF77440.1; -; Genomic_DNA. DR EMBL; AF200845; AAF77453.1; -; Genomic_DNA. DR EMBL; AF200846; AAF77466.1; -; Genomic_DNA. DR EMBL; AF200847; AAF77478.1; -; Genomic_DNA. DR EMBL; AF200848; AAF77492.1; -; Genomic_DNA. DR EMBL; AF200849; AAF77506.1; -; Genomic_DNA. DR EMBL; AF200850; AAF77518.1; -; Genomic_DNA. DR EMBL; AF200851; AAF77532.1; -; Genomic_DNA. DR EMBL; AF200852; AAF77544.1; -; Genomic_DNA. DR EMBL; AF200853; AAF77557.1; -; Genomic_DNA. DR EMBL; AF200854; AAF77570.1; -; Genomic_DNA. DR EMBL; AY518670; AAR91400.1; -; Genomic_DNA. DR EMBL; AY518671; AAR91402.1; -; Genomic_DNA. DR EMBL; AY518672; AAR91415.1; -; Genomic_DNA. DR EMBL; AY518673; AAR91428.1; -; Genomic_DNA. DR EMBL; AY518674; AAR91441.1; -; Genomic_DNA. DR EMBL; JQ691660; AFC97648.1; -; Genomic_DNA. DR EMBL; JQ691661; AFC97661.1; -; Genomic_DNA. DR EMBL; M57909; AAB02284.1; -; Genomic_DNA. DR EMBL; M57911; AAA66247.2; -; Genomic_DNA. DR EMBL; M18072; AAA65482.2; -; Genomic_DNA. DR EMBL; S64977; AAD13955.1; -; Genomic_DNA. DR RefSeq; NP_982323.2; NC_005781.1. DR AlphaFoldDB; Q34388; -. DR SMR; Q34388; -. DR STRING; 7240.Q34388; -. DR GeneID; 2760962; -. DR KEGG; dsi:COX1; -. DR CTD; 4512; -. DR UniPathway; UPA00705; -. DR ChiTaRS; COX1; fly. DR Proteomes; UP000000304; Mitochondrion. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0045277; C:respiratory chain complex IV; IEA:InterPro. DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006119; P:oxidative phosphorylation; IEA:UniProtKB-UniPathway. DR CDD; cd01663; Cyt_c_Oxidase_I; 1. DR Gene3D; 1.20.210.10; Cytochrome c oxidase-like, subunit I domain; 1. DR InterPro; IPR023616; Cyt_c_oxase-like_su1_dom. DR InterPro; IPR036927; Cyt_c_oxase-like_su1_sf. DR InterPro; IPR000883; Cyt_C_Oxase_1. DR InterPro; IPR023615; Cyt_c_Oxase_su1_BS. DR InterPro; IPR033944; Cyt_c_oxase_su1_dom. DR PANTHER; PTHR10422; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR PANTHER; PTHR10422:SF18; CYTOCHROME C OXIDASE SUBUNIT 1; 1. DR Pfam; PF00115; COX1; 1. DR PRINTS; PR01165; CYCOXIDASEI. DR SUPFAM; SSF81442; Cytochrome c oxidase subunit I-like; 1. DR PROSITE; PS50855; COX1; 1. DR PROSITE; PS00077; COX1_CUB; 1. PE 2: Evidence at transcript level; KW Calcium; Copper; Electron transport; Heme; Iron; Magnesium; Membrane; KW Metal-binding; Mitochondrion; Mitochondrion inner membrane; KW Reference proteome; Respiratory chain; Translocase; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..511 FT /note="Cytochrome c oxidase subunit 1" FT /id="PRO_0000183328" FT TRANSMEM 15..35 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 54..74 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 100..120 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 143..163 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 181..201 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 232..252 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 266..286 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 303..323 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 336..356 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 378..398 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 412..432 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 450..470 FT /note="Helical" FT /evidence="ECO:0000255" FT BINDING 38 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 43 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 59 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_note="low-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 238 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 242 FT /ligand="O2" FT /ligand_id="ChEBI:CHEBI:15379" FT /evidence="ECO:0000250|UniProtKB:P00396" FT BINDING 288 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 289 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 366 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with subunit 2" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 367 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with subunit 2" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 374 FT /ligand="heme a3" FT /ligand_id="ChEBI:CHEBI:83282" FT /ligand_note="high-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00401" FT BINDING 376 FT /ligand="Fe(II)-heme a" FT /ligand_id="ChEBI:CHEBI:61715" FT /ligand_note="low-spin" FT /ligand_part="Fe" FT /ligand_part_id="ChEBI:CHEBI:18248" FT /note="axial binding residue" FT /evidence="ECO:0000250|UniProtKB:P00401" FT CROSSLNK 238..242 FT /note="1'-histidyl-3'-tyrosine (His-Tyr)" FT /evidence="ECO:0000250|UniProtKB:P00401" FT VARIANT 450 FT /note="V -> I (in strain: Hawaii, New Caledonia and FT Tahiti)" FT /evidence="ECO:0000269|PubMed:10903373, FT ECO:0000269|PubMed:2124697" FT VARIANT 468 FT /note="Y -> F (in strain: Hawaii, New Caledonia and FT Tahiti)" FT /evidence="ECO:0000269|PubMed:10903373, FT ECO:0000269|PubMed:2124697" FT CONFLICT 27 FT /note="V -> I (in Ref. 1; AAF77453/AAF77427/AAF77413 and 3; FT AFC97648)" FT /evidence="ECO:0000305" SQ SEQUENCE 511 AA; 56375 MW; 918CEE06A60210DC CRC64; PRQWLFSTNH KDIGTLYFIF GAWAGMVGTS LSILIRAELG HPGALIGDDQ IYNVIVTAHA FIMIFFMVMP IMIGGFGNWL VPLMLGAPDM AFPRMNNMSF WLLPPALSLL LVSSMVENGA GTGWTVYPPL SAGIAHGGAS VDLAIFSLHL AGISSILGAV NFITTVINMR STGISLDRMP LFVWSVVITA LLLLLSLPVL AGAITMLLTD RNLNTSFFDP AGGGDPILYQ HLFWFFGHPE VYILILPGFG MISHIISQES GKKETFGSLG MIYAMLAIGL LGFIVWAHHM FTVGMDVDTR AYFTSATMII AVPTGIKIFS WLATLHGTQL SYSPAILWAL GFVFLFTVGG LTGVVLANSS VDIILHDTYY VVAHFHYVLS MGAVFAIMAG FIHWYPLFTG LTLNNKWLKS QFIIMFIGVN LTFFPQHFLG LAGMPRRYSD YPDAYTTWNV VSTIGSTISL LGILFFFYII WESLVSQRQV IYPIQLNSSI EWYQNTPPAE HSYSELPLLT N //