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P00399 (COX1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytochrome c oxidase subunit 1

EC=1.9.3.1
Alternative name(s):
Cytochrome c oxidase polypeptide I
Gene names
Name:mt:CoI
Synonyms:CoI
Encoded onMitochondrion
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B.

Catalytic activity

4 ferrocytochrome c + O2 + 4 H+ = 4 ferricytochrome c + 2 H2O.

Pathway

Energy metabolism; oxidative phosphorylation.

Subcellular location

Mitochondrion inner membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the heme-copper respiratory oxidase family.

Caution

There is no mitochondrial-type translation initiation codon present in frame in the sequence. In Ref.11, the authors suggest the presence of a novel start codon coding for either Pro or Ser in Drosophila CoI transcripts. In Ref.6, further evidence for the presence of the same start codon coding for Ser in D.melanogaster CoI transcript is presented.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 511511Cytochrome c oxidase subunit 1
PRO_0000183325

Regions

Transmembrane15 – 3521Helical; Potential
Transmembrane54 – 7421Helical; Potential
Transmembrane100 – 12021Helical; Potential
Transmembrane143 – 16321Helical; Potential
Transmembrane181 – 20121Helical; Potential
Transmembrane232 – 25221Helical; Potential
Transmembrane266 – 28621Helical; Potential
Transmembrane303 – 32321Helical; Potential
Transmembrane336 – 35621Helical; Potential
Transmembrane378 – 39821Helical; Potential
Transmembrane412 – 43221Helical; Potential
Transmembrane450 – 47021Helical; Potential

Sites

Metal binding591Iron (heme A axial ligand) Probable
Metal binding2381Copper B Probable
Metal binding2421Copper B Probable
Metal binding2881Copper B Probable
Metal binding2891Copper B Probable
Metal binding3741Iron (heme A3 axial ligand) Probable
Metal binding3761Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link238 ↔ 2421'-histidyl-3'-tyrosine (His-Tyr) By similarity

Natural variations

Natural variant1271Y → F in strain: Zimbabwe. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P00399 [UniParc].

Last modified January 9, 2013. Version 2.
Checksum: 332DAFF298EBBA13

FASTA51156,372
        10         20         30         40         50         60 
SRQWLFSTNH KDIGTLYFIF GAWAGMVGTS LSILIRAELG HPGALIGDDQ IYNVIVTAHA 

        70         80         90        100        110        120 
FIMIFFMVMP IMIGGFGNWL VPLMLGAPDM AFPRMNNMSF WLLPPALSLL LVSSMVENGA 

       130        140        150        160        170        180 
GTGWTVYPPL SAGIAHGGAS VDLAIFSLHL AGISSILGAV NFITTVINMR STGISLDRMP 

       190        200        210        220        230        240 
LFVWSVVITA LLLLLSLPVL AGAITMLLTD RNLNTSFFDP AGGGDPILYQ HLFWFFGHPE 

       250        260        270        280        290        300 
VYILILPGFG MISHIISQES GKKETFGSLG MIYAMLAIGL LGFIVWAHHM FTVGMDVDTR 

       310        320        330        340        350        360 
AYFTSATMII AVPTGIKIFS WLATLHGTQL SYSPAILWAL GFVFLFTVGG LTGVVLANSS 

       370        380        390        400        410        420 
VDIILHDTYY VVAHFHYVLS MGAVFAIMAG FIHWYPLFTG LTLNNKWLKS HFIIMFIGVN 

       430        440        450        460        470        480 
LTFFPQHFLG LAGMPRRYSD YPDAYTTWNI VSTIGSTISL LGILFFFFII WESLVSQRQV 

       490        500        510 
IYPIQLNSSI EWYQNTPPAE HSYSELPLLT N 

« Hide

References

« Hide 'large scale' references
[1]"Drosophila melanogaster mitochondrial DNA, a novel organization and genetic code."
de Bruijn M.H.L.
Nature 304:234-241(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Drosophila melanogaster mitochondrial DNA: completion of the nucleotide sequence and evolutionary comparisons."
Lewis D.L., Farr C.L., Kaguni L.S.
Insect Mol. Biol. 4:263-278(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Comparative genomics of mitochondrial DNA in members of the Drosophila melanogaster subgroup."
Ballard J.W.O.
J. Mol. Evol. 51:48-63(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-127.
Strain: Oregon-R and Zimbabwe.
[4]"I-R system of hybrid dysgenesis in Drosophila melanogaster: analysis of the mitochondrial DNA in reactive strains exhibiting different potentials for I factor transposition."
Azou Y., Bregliano J.C.
Heredity 86:110-116(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Paris.
[5]"Variation in mitochondrial genotype has substantial lifespan effects which may be modulated by nuclear background."
Clancy D.J.
Aging Cell 7:795-804(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Alstonville, Brownsville, Dahomey, Japan, Mysore and W1118.
[6]"Characterization of mature mitochondrial transcripts in Drosophila, and the implications for the tRNA punctuation model in arthropods."
Stewart J.B., Beckenbach A.T.
Gene 445:49-57(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION OF PROBABLE INITIATION SITE.
Strain: Oregon-R.
[7]"Mitochondria, maternal inheritance, and male aging."
Camus M.F., Clancy D.J., Dowling D.K.
Curr. Biol. 22:1717-1721(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Barcelona, Hawaii, Israel, Madang, Puerto Montt and Sweden.
[8]"A cytoplasmic suppressor of a nuclear mutation affecting mitochondrial functions in Drosophila."
Chen S., Oliveira M.T., Sanz A., Kemppainen E., Fukuoh A., Schlicht B., Kaguni L.S., Jacobs H.T.
Genetics 192:483-493(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BER1, Canton-S, CO3, Oregon-RC and QI2.
[9]"Evolution of Drosophila mitochondrial DNA and the history of the melanogaster subgroup."
Satta Y., Takahata N.
Proc. Natl. Acad. Sci. U.S.A. 87:9558-9562(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-498.
Strain: SP1.
[10]"Analysis of nucleotide substitutions of mitochondrial DNAs in Drosophila melanogaster and its sibling species."
Satta Y., Ishiwa H., Chigusa S.I.
Mol. Biol. Evol. 4:638-650(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-102.
[11]"Comparative genomics of Drosophila mtDNA: Novel features of conservation and change across functional domains and lineages."
Montooth K.L., Abt D.N., Hofmann J.W., Rand D.M.
J. Mol. Evol. 69:94-114(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-10, IDENTIFICATION OF PROBABLE INITIATION SITE.
[12]"Collembola as alternative prey sustaining spiders in arable ecosystems: prey detection within predators using molecular markers."
Agusti N., Shayler S.P., Harwood J.D., Vaughan I.P., Sunderland K.D., Symondson W.O.
Mol. Ecol. 12:3467-3475(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-248.
[13]"Mitochondrial DNA phylogenies for the Drosophila obscura group."
Gleason J.M., Caccone A., Moriyama E.N., White K.P., Powell J.R.
Evolution 51:433-440(1997) [AGRICOLA] [Europe PMC]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 231-390.
Strain: Australia 13.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J01404 Genomic DNA. Translation: AAB59239.1.
U37541 Genomic DNA. Translation: AAC47812.2.
AF200828 Genomic DNA. Translation: AAF77227.1.
AF200829 Genomic DNA. Translation: AAF77245.1.
AJ400907 Genomic DNA. Translation: CAB91052.2.
FJ190105 Genomic DNA. Translation: ACI28543.1.
FJ190106 Genomic DNA. Translation: ACI28556.1.
FJ190107 Genomic DNA. Translation: ACI28569.1.
FJ190108 Genomic DNA. Translation: ACI28582.1.
FJ190109 Genomic DNA. Translation: ACI28595.1.
FJ190110 Genomic DNA. Translation: ACI28608.1.
GQ229519 mRNA. Translation: ACT21544.1.
JX266575 Genomic DNA. Translation: AFR59645.1.
JX266576 Genomic DNA. Translation: AFR59658.1.
JX266577 Genomic DNA. Translation: AFR59671.1.
JX266578 Genomic DNA. Translation: AFR59684.1.
JX266579 Genomic DNA. Translation: AFR59697.1.
JX266580 Genomic DNA. Translation: AFR59710.1.
JQ686694 Genomic DNA. Translation: AFP47060.1.
JQ686695 Genomic DNA. Translation: AFP47073.1.
JQ686696 Genomic DNA. Translation: AFP47086.1.
JQ686698 Genomic DNA. Translation: AFP47112.1.
JQ686699 Genomic DNA. Translation: AFP47125.1.
M57910 Genomic DNA. Translation: AAB02282.1.
M18022 Genomic DNA. Translation: AAA65480.2.
AY383542 Genomic DNA. Translation: AAQ92343.1.
U51619 Genomic DNA. Translation: AAB68481.2.
PIRODFF1. A93307.
RefSeqNP_008278.1. NC_001709.1.

3D structure databases

ProteinModelPortalP00399.
SMRP00399. Positions 3-505.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0100861; FBpp0100176; FBgn0013674.
GeneID192469.
KEGGdme:COX1.

Organism-specific databases

CTD4512.
FlyBaseFBgn0013674. mt:CoI.

Phylogenomic databases

eggNOGCOG0843.
GeneTreeENSGT00390000001518.
InParanoidP00399.
KOK02256.
OMAPGIQIFS.
OrthoDBEOG7Q8CMW.

Enzyme and pathway databases

UniPathwayUPA00705.

Gene expression databases

BgeeP00399.

Family and domain databases

Gene3D1.20.210.10. 1 hit.
InterProIPR000883. Cyt_c_Oxase_su1.
IPR023615. Cyt_c_Oxase_su1_BS.
IPR023616. Cyt_c_Oxase_su1_dom.
[Graphical view]
PANTHERPTHR10422. PTHR10422. 1 hit.
PfamPF00115. COX1. 1 hit.
[Graphical view]
PRINTSPR01165. CYCOXIDASEI.
SUPFAMSSF81442. SSF81442. 1 hit.
PROSITEPS50855. COX1. 1 hit.
PS00077. COX1_CUB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi192469.
NextBio842180.
PROP00399.

Entry information

Entry nameCOX1_DROME
AccessionPrimary (citable) accession number: P00399
Secondary accession number(s): B6E0P3 expand/collapse secondary AC list , O21461, Q34349, Q6TXT7, Q7GFY7, Q7GHI7, Q9MGN6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 9, 2013
Last modified: May 14, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase