Cytochrome c oxidase subunit 1 - Drosophila melanogaster (Fruit fly)

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P00399 (COX1_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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 on

Mitochondrion

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora ›

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	aerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW oxidative phosphorylation Inferred from electronic annotation. Source: UniProtKB-UniPathway sleep Traceable author statement PubMed 14505361. Source: FlyBase
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial inner membrane Inferred from electronic annotation. Source: UniProtKB-SubCell respiratory chain Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	cytochrome-c oxidase activity Inferred from electronic annotation. Source: EC electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 511

511

Cytochrome c oxidase subunit 1

PRO_0000183325

Regions

Transmembrane

15 – 35

Helical; Potential

Transmembrane

54 – 74

Helical; Potential

Transmembrane

100 – 120

Helical; Potential

Transmembrane

143 – 163

Helical; Potential

Transmembrane

181 – 201

Helical; Potential

Transmembrane

232 – 252

Helical; Potential

Transmembrane

266 – 286

Helical; Potential

Transmembrane

303 – 323

Helical; Potential

Transmembrane

336 – 356

Helical; Potential

Transmembrane

378 – 398

Helical; Potential

Transmembrane

412 – 432

Helical; Potential

Transmembrane

450 – 470

Helical; Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

238

Copper B Probable

Metal binding

242

Copper B Probable

Metal binding

288

Copper B Probable

Metal binding

289

Copper B Probable

Metal binding

374

Iron (heme A3 axial ligand) Probable

Metal binding

376

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

238 ↔ 242

1'-histidyl-3'-tyrosine (His-Tyr) By similarity

Natural variations

Natural variant

127

Y → F in strain: Zimbabwe. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P00399 [UniParc].

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

FASTA

511

56,372

        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' referencesShow '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.
PIR	ODFF1. A93307.
RefSeq	NP_008278.1. NC_001709.1.
3D structure databases
ProteinModelPortal	P00399.
SMR	P00399. Positions 3-505.
ModBase	Search...
Proteomic databases
PRIDE	P00399.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	192469.
KEGG	dme:COX1.
Organism-specific databases
CTD	4512.
FlyBase	FBgn0013674. mt:CoI.
Phylogenomic databases
eggNOG	COG0843.
GeneTree	ENSGT00390000001518.
InParanoid	P00399.
KO	K02256.
OMA	HARKPLF.
OrthoDB	EOG4W0VVW.
ProtClustDB	MTH00153.
Enzyme and pathway databases
UniPathway	UPA00705.
Gene expression databases
Bgee	P00399.
Family and domain databases
Gene3D	1.20.210.10. 1 hit.
InterPro	IPR000883. Cyt_c_Oxase_su1. IPR023615. Cyt_c_Oxase_su1_BS. IPR023616. Cyt_c_Oxase_su1_dom. [Graphical view]
PANTHER	PTHR10422. PTHR10422. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
SUPFAM	SSF81442. COX1. 1 hit.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	192469.
NextBio	842180.

Entry information

Entry name

COX1_DROME

Accession

Primary (citable) accession number: P00399
Secondary accession number(s): B6E0P3

Q9MGN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 9, 2013
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project

Relevant documents

Drosophila

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents