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

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P00399 (COX1_DROME)

Last modified June 16, 2009. Version 92. History...

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

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

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) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

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

Hide | Top

Protein attributes

Sequence length	512 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

Hide | Top

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.

Hide | Top

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Ligand	Copper Heme Iron Metal-binding
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	aerobic respiration Inferred from electronic annotation. Source: InterPro electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW sleep Traceable author statement. Source: FlyBase transport Inferred from electronic annotation. Source: UniProtKB-KW
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	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 512

512

Cytochrome c oxidase subunit 1

PRO_0000183325

Regions

Transmembrane

16 – 36

Potential

Transmembrane

55 – 75

Potential

Transmembrane

101 – 121

Potential

Transmembrane

144 – 164

Potential

Transmembrane

182 – 202

Potential

Transmembrane

233 – 253

Potential

Transmembrane

267 – 287

Potential

Transmembrane

304 – 324

Potential

Transmembrane

337 – 357

Potential

Transmembrane

379 – 399

Potential

Transmembrane

413 – 433

Potential

Transmembrane

451 – 471

Potential

Sites

Metal binding

Iron (heme A axial ligand) Probable

Metal binding

239

Copper B Probable

Metal binding

243

Copper B Probable

Metal binding

289

Copper B Probable

Metal binding

290

Copper B Probable

Metal binding

375

Iron (heme A3 axial ligand) Probable

Metal binding

377

Iron (heme A axial ligand) Probable

Amino acid modifications

Cross-link

239 ↔ 243

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

Natural variations

Natural variant

128

Y → F in strain: Zimbabwe 53. Ref.2

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P00399-1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: F7B95FF298EBBA0F
Show »

FASTA

512

56,503

        10         20         30         40         50         60 
MSRQWLFSTN HKDIGTLYFI FGAWAGMVGT SLSILIRAEL GHPGALIGDD QIYNVIVTAH 

        70         80         90        100        110        120 
AFIMIFFMVM PIMIGGFGNW LVPLMLGAPD MAFPRMNNMS FWLLPPALSL LLVSSMVENG 

       130        140        150        160        170        180 
AGTGWTVYPP LSAGIAHGGA SVDLAIFSLH LAGISSILGA VNFITTVINM RSTGISLDRM 

       190        200        210        220        230        240 
PLFVWSVVIT ALLLLLSLPV LAGAITMLLT DRNLNTSFFD PAGGGDPILY QHLFWFFGHP 

       250        260        270        280        290        300 
EVYILILPGF GMISHIISQE SGKKETFGSL GMIYAMLAIG LLGFIVWAHH MFTVGMDVDT 

       310        320        330        340        350        360 
RAYFTSATMI IAVPTGIKIF SWLATLHGTQ LSYSPAILWA LGFVFLFTVG GLTGVVLANS 

       370        380        390        400        410        420 
SVDIILHDTY YVVAHFHYVL SMGAVFAIMA GFIHWYPLFT GLTLNNKWLK SHFIIMFIGV 

       430        440        450        460        470        480 
NLTFFPQHFL GLAGMPRRYS DYPDAYTTWN IVSTIGSTIS LLGILFFFFI IWESLVSQRQ 

       490        500        510 
VIYPIQLNSS IEWYQNTPPA EHSYSELPLL TN

« Hide

Hide | Top

References

[1]	"Drosophila melanogaster mitochondrial DNA, a novel organization and genetic code." de Bruijn M.H.L. Nature 304:234-241(1983) [PubMed: 6408489] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Comparative genomics of mitochondrial DNA in members of the Drosophila melanogaster subgroup." Ballard J.W.O. J. Mol. Evol. 51:48-63(2000) [PubMed: 10903372] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-128. Strain: Oregon-R and Zimbabwe 53.
[3]	"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: 11298822] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Paris.
[4]	"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: 2124697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-499. Strain: SP1.
[5]	"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: 2832697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103.
[6]	"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: 14629361] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-249.
[7]	"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: IND20580636] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 232-391. Strain: Australia 13.

Hide | Top

Cross-references

Sequence databases
	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. 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.
3D structure databases
HSSP	HSSP built from PDB template 2OCC based on UniProtKB P00396.
SMR	P00399. Positions 4-506.
ModBase	Search...
Proteomic databases
PRIDE	P00399.
Genome annotation databases
Ensembl	FBgn0013674. Drosophila melanogaster. [Contig view]
GeneID	192469.
KEGG	dme:COX1.
Organism-specific databases
FlyBase	FBgn0013674. mt:CoI.
Enzyme and pathway databases
BRENDA	1.9.3.1. 48.
Family and domain databases
InterPro	IPR000883. Cyt_c_oxidase_su1. [Graphical view]
Gene3D	G3DSA:1.20.210.10. COX1. 1 hit.
PANTHER	PTHR10422. COX1. 1 hit.
Pfam	PF00115. COX1. 1 hit. [Graphical view]
PRINTS	PR01165. CYCOXIDASEI.
PROSITE	PS50855. COX1. 1 hit. PS00077. COX1_CUB. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	842180.

Hide | Top

Entry information

Entry name

COX1_DROME

Accession

Primary (citable) accession number: P00399
Secondary accession number(s): O21461

Q9MGN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	June 16, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project

Hide | Top

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 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

Genome annotation databases

Organism-specific databases

Enzyme and pathway databases

Family and domain databases

Other Resources

Entry information

Relevant documents