COX1_DROME
ID COX1_DROME Reviewed; 511 AA.
AC P00399; B6E0P3; O21461; Q34349; Q6TXT7; Q7GFY7; Q7GHI7; Q9MGN6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 186.
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 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].
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 [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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-127.
RC STRAIN=Oregon-R, and Zimbabwe;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Alstonville, Brownsville, Dahomey, Japan, Mysore, and W1118;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA], AND IDENTIFICATION OF PROBABLE INITIATION SITE.
RC STRAIN=Oregon-R;
RX PubMed=19540318; DOI=10.1016/j.gene.2009.06.006;
RA Stewart J.B., Beckenbach A.T.;
RT "Characterization of mature mitochondrial transcripts in Drosophila, and
RT the implications for the tRNA punctuation model in arthropods.";
RL Gene 445:49-57(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Barcelona, Hawaii, Israel, Madang, Puerto Montt, and Sweden;
RX PubMed=22863313; DOI=10.1016/j.cub.2012.07.018;
RA Camus M.F., Clancy D.J., Dowling D.K.;
RT "Mitochondria, maternal inheritance, and male aging.";
RL Curr. Biol. 22:1717-1721(2012).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BER1, Canton-S, CO3, Oregon-RC, and QI2;
RX PubMed=22851652; DOI=10.1534/genetics.112.143719;
RA Chen S., Oliveira M.T., Sanz A., Kemppainen E., Fukuoh A., Schlicht B.,
RA Kaguni L.S., Jacobs H.T.;
RT "A cytoplasmic suppressor of a nuclear mutation affecting mitochondrial
RT functions in Drosophila.";
RL Genetics 192:483-493(2012).
RN [9]
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 [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-498.
RC STRAIN=SP1;
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 [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
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 [12]
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 [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-248.
RX PubMed=14629361; DOI=10.1046/j.1365-294x.2003.02014.x;
RA Agusti N., Shayler S.P., Harwood J.D., Vaughan I.P., Sunderland K.D.,
RA Symondson W.O.;
RT "Collembola as alternative prey sustaining spiders in arable ecosystems:
RT prey detection within predators using molecular markers.";
RL Mol. Ecol. 12:3467-3475(2003).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-390.
RC STRAIN=Australia 13;
RX AGRICOLA=IND20580636; DOI=10.2307/2411115;
RA Gleason J.M., Caccone A., Moriyama E.N., White K.P., Powell J.R.;
RT "Mitochondrial DNA phylogenies for the Drosophila obscura group.";
RL Evolution 51:433-440(1997).
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. In PubMed:19540318, further evidence
CC for the presence of the same start codon coding for Ser in
CC D.melanogaster CoI transcript is presented. {ECO:0000305}.
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DR EMBL; J01404; AAB59239.1; -; Genomic_DNA.
DR EMBL; U37541; AAC47812.2; -; Genomic_DNA.
DR EMBL; AF200828; AAF77227.1; -; Genomic_DNA.
DR EMBL; AF200829; AAF77245.1; -; Genomic_DNA.
DR EMBL; AJ400907; CAB91052.2; -; Genomic_DNA.
DR EMBL; FJ190105; ACI28543.1; -; Genomic_DNA.
DR EMBL; FJ190106; ACI28556.1; -; Genomic_DNA.
DR EMBL; FJ190107; ACI28569.1; -; Genomic_DNA.
DR EMBL; FJ190108; ACI28582.1; -; Genomic_DNA.
DR EMBL; FJ190109; ACI28595.1; -; Genomic_DNA.
DR EMBL; FJ190110; ACI28608.1; -; Genomic_DNA.
DR EMBL; GQ229519; ACT21544.1; -; mRNA.
DR EMBL; JX266575; AFR59645.1; -; Genomic_DNA.
DR EMBL; JX266576; AFR59658.1; -; Genomic_DNA.
DR EMBL; JX266577; AFR59671.1; -; Genomic_DNA.
DR EMBL; JX266578; AFR59684.1; -; Genomic_DNA.
DR EMBL; JX266579; AFR59697.1; -; Genomic_DNA.
DR EMBL; JX266580; AFR59710.1; -; Genomic_DNA.
DR EMBL; JQ686694; AFP47060.1; -; Genomic_DNA.
DR EMBL; JQ686695; AFP47073.1; -; Genomic_DNA.
DR EMBL; JQ686696; AFP47086.1; -; Genomic_DNA.
DR EMBL; JQ686698; AFP47112.1; -; Genomic_DNA.
DR EMBL; JQ686699; AFP47125.1; -; Genomic_DNA.
DR EMBL; KJ947872; AIC64005.1; -; Genomic_DNA.
DR EMBL; M57910; AAB02282.1; -; Genomic_DNA.
DR EMBL; M18022; AAA65480.2; -; Genomic_DNA.
DR EMBL; AY383542; AAQ92343.1; -; Genomic_DNA.
DR EMBL; U51619; AAB68481.2; -; Genomic_DNA.
DR PIR; A93307; ODFF1.
DR RefSeq; YP_009047267.1; NC_024511.2.
DR AlphaFoldDB; P00399; -.
DR SMR; P00399; -.
DR BioGRID; 2595062; 1.
DR STRING; 7227.FBpp0100176; -.
DR PaxDb; P00399; -.
DR EnsemblMetazoa; FBtr0100861; FBpp0100176; FBgn0013674.
DR GeneID; 19893533; -.
DR KEGG; dme:Dmel_CG34067; -.
DR CTD; 4512; -.
DR FlyBase; FBgn0013674; mt:CoI.
DR VEuPathDB; VectorBase:FBgn0013674; -.
DR eggNOG; KOG4769; Eukaryota.
DR GeneTree; ENSGT00390000001518; -.
DR HOGENOM; CLU_011899_7_3_1; -.
DR InParanoid; P00399; -.
DR OMA; WAMMSIG; -.
DR OrthoDB; 728231at2759; -.
DR PhylomeDB; P00399; -.
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 UniPathway; UPA00705; -.
DR BioGRID-ORCS; 19893533; 0 hits in 1 CRISPR screen.
DR ChiTaRS; COX1; fly.
DR GenomeRNAi; 19893533; -.
DR PRO; PR:P00399; -.
DR Proteomes; UP000000803; Mitochondrion.
DR Bgee; FBgn0013674; Expressed in Malpighian tubule and 12 other tissues.
DR ExpressionAtlas; P00399; 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; IBA:GO_Central.
DR GO; GO:0045277; C:respiratory chain complex IV; IMP:FlyBase.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IMP:FlyBase.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006123; P:mitochondrial electron transport, cytochrome c to oxygen; IMP:FlyBase.
DR GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR CDD; cd01663; Cyt_c_Oxidase_I; 1.
DR Gene3D; 1.20.210.10; -; 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; PTHR10422; 1.
DR Pfam; PF00115; COX1; 1.
DR PRINTS; PR01165; CYCOXIDASEI.
DR SUPFAM; SSF81442; SSF81442; 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_0000183325"
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 127
FT /note="Y -> F (in strain: Zimbabwe)"
FT /evidence="ECO:0000269|PubMed:10903372"
SQ SEQUENCE 511 AA; 56372 MW; 332DAFF298EBBA13 CRC64;
SRQWLFSTNH 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 HFIIMFIGVN
LTFFPQHFLG LAGMPRRYSD YPDAYTTWNI VSTIGSTISL LGILFFFFII WESLVSQRQV
IYPIQLNSSI EWYQNTPPAE HSYSELPLLT N
