[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1038/304234a0; PubMed=6408489 [NCBI, ExPASy, EBI, Israel, Japan] de Bruijn M.H.L.; "Drosophila melanogaster mitochondrial DNA, a novel organization and genetic code."; Nature 304:234-241(1983).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PHE-128. STRAIN=Oregon-R, and Zimbabwe 53; PubMed=10903372 [NCBI, ExPASy, EBI, Israel, Japan] Ballard J.W.O.; "Comparative genomics of mitochondrial DNA in members of the Drosophila melanogaster subgroup."; J. Mol. Evol. 51:48-63(2000).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=Paris; DOI=10.1046/j.1365-2540.2001.00814.x; PubMed=11298822 [NCBI, ExPASy, EBI, Israel, Japan] Azou Y., Bregliano J.C.; "I-R system of hybrid dysgenesis in Drosophila melanogaster: analysis of the mitochondrial DNA in reactive strains exhibiting different potentials for I factor transposition."; Heredity 86:110-116(2001).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-499. STRAIN=SP1; PubMed=2124697 [NCBI, ExPASy, EBI, Israel, Japan] Satta Y., Takahata N.; "Evolution of Drosophila mitochondrial DNA and the history of the melanogaster subgroup."; Proc. Natl. Acad. Sci. U.S.A. 87:9558-9562(1990).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103. PubMed=2832697 [NCBI, ExPASy, EBI, Israel, Japan] Satta Y., Ishiwa H., Chigusa S.I.; "Analysis of nucleotide substitutions of mitochondrial DNAs in Drosophila melanogaster and its sibling species."; Mol. Biol. Evol. 4:638-650(1987).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 75-249. DOI=10.1046/j.1365-294X.2003.02014.x; PubMed=14629361 [NCBI, ExPASy, EBI, Israel, Japan] Agusti N., Shayler S.P., Harwood J.D., Vaughan I.P., Sunderland K.D., Symondson W.O.; "Collembola as alternative prey sustaining spiders in arable ecosystems: prey detection within predators using molecular markers."; Mol. Ecol. 12:3467-3475(2003).
[7]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 232-391. STRAIN=Australia 13; DOI=10.2307/2411115; AGRICOLA=IND20580636 Gleason J.M., Caccone A., Moriyama E.N., White K.P., Powell J.R.; "Mitochondrial DNA phylogenies for the Drosophila obscura group."; Evolution 51:433-440(1997).

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.
SIMILARITY: Belongs to the heme-copper respiratory oxidase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

J01404; AAB59239.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U37541; AAC47812.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF200828; AAF77227.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF200829; AAF77245.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ400907; CAB91052.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M57910; AAB02282.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M18022; AAA65480.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY383542; AAQ92343.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U51619; AAB68481.2; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A93307; ODFF1.

RefSeq

NP_008278.1; -.

3D structure databases

HSSP

P00396; 2OCC. [HSSP ENTRY / PDB]

SMR

P00399; 4-506.

ModBase

P00399.

Organism-specific databases

FlyBase

FBgn0013674; mt:CoI.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from InterPro).
GO:0005746;	Cellular component: mitochondrial respiratory chain (inferred from electronic annotation from UniProtKB-KW).
GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004129;	Molecular function: cytochrome-c oxidase activity (inferred from electronic annotation from EC).
GO:0009055;	Molecular function: electron carrier activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0009060;	Biological process: aerobic respiration (inferred from electronic annotation from InterPro).
GO:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
GO:0030431;	Biological process: sleep (traceable author statement from FlyBase).
GO:0006810;	Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000883; COX1.
Graphical view of domain structure.

Gene3D

G3DSA:1.20.210.10; COX1; 1.

PANTHER

PTHR10422; COX1; 1.

Pfam

PF00115; COX1; 1.
Pfam graphical view of domain structure.

PRINTS

PR01165; CYCOXIDASEI.

PROSITE

PS50855; COX1; 1.
PS00077; COX1_CUB; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P00399.

Genome annotation databases

GeneID

192469; -.

KEGG

dme:COX1; -.

Other

NextBio

842180; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Copper; Electron transport; Heme; Iron; Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; Oxidoreductase; Polymorphism; Respiratory chain; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 512`	`512`	`Cytochrome c oxidase subunit 1.`	`PRO_0000183325`
`TRANSMEM`	`16 36`	`21`	`Potential.`
`TRANSMEM`	`55 75`	`21`	`Potential.`
`TRANSMEM`	`101 121`	`21`	`Potential.`
`TRANSMEM`	`144 164`	`21`	`Potential.`
`TRANSMEM`	`182 202`	`21`	`Potential.`
`TRANSMEM`	`233 253`	`21`	`Potential.`
`TRANSMEM`	`267 287`	`21`	`Potential.`
`TRANSMEM`	`304 324`	`21`	`Potential.`
`TRANSMEM`	`337 357`	`21`	`Potential.`
`TRANSMEM`	`379 399`	`21`	`Potential.`
`TRANSMEM`	`413 433`	`21`	`Potential.`
`TRANSMEM`	`451 471`	`21`	`Potential.`
`METAL`	`60 60`		`Iron (heme A axial ligand) (Probable).`
`METAL`	`239 239`		`Copper B (Probable).`
`METAL`	`243 243`		`Copper B (Probable).`
`METAL`	`289 289`		`Copper B (Probable).`
`METAL`	`290 290`		`Copper B (Probable).`
`METAL`	`375 375`		`Iron (heme A3 axial ligand) (Probable).`
`METAL`	`377 377`		`Iron (heme A axial ligand) (Probable).`
`CROSSLNK`	`239 243`		`1'-histidyl-3'-tyrosine (His-Tyr) (By similarity).`
`VARIANT`	`128 128`	`1`	`Y -> F (in strain: Zimbabwe 53).`

Sequence information

Length: 512 AA [This is the length of the unprocessed precursor]

Molecular weight: 56503 Da [This is the MW of the unprocessed precursor]

CRC64: F7B95FF298EBBA0F [This is a checksum on the sequence]

        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

P00399 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools