[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Roe A., Sperling F.A.H.; Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 240-513. STRAIN=Isolate 15; PubMed=8078404 [NCBI, ExPASy, EBI, Israel, Japan] Sperling F.A.H., Hickey D.A.; "Mitochondrial DNA sequence variation in the spruce budworm species complex (Choristoneura: Lepidoptera)."; Mol. Biol. Evol. 11:656-665(1994).

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

L19095; AAA53644.2; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

P67794; 2-506.

ModBase

P67794.

Ontologies

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:0022900;	Biological process: electron transport chain (inferred from electronic annotation from UniProtKB-KW).
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).

Other

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 513`	`513`	`Cytochrome c oxidase subunit 1.`	`PRO_0000183311`
`TRANSMEM`	`16 36`	`21`	`Potential.`
`TRANSMEM`	`62 82`	`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`	`384 404`	`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).`

Sequence information

Length: 513 AA [This is the length of the unprocessed precursor]

Molecular weight: 57047 Da [This is the MW of the unprocessed precursor]

CRC64: EE6CE68666FE3878 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MMRKWLYSTN HKDIGTLYFM FGIWAGMVGT SLSLLIRAEL GNPGSLIGDD QIYNTIVTAH 

        70         80         90        100        110        120 
AFIMIFFMVM PIMIGGFGNW LVPLMLGAPD MAFPRMNNMS FWLLPPSIML LISSSIVENG 

       130        140        150        160        170        180 
AGTGWTVYPP LSSNIAHSGS SVDLAIFSLH LAGISSILGA VNFITTIINM RPNNMSLDQM 

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

       250        260        270        280        290        300 
EVYILILPGF GMISHIISQE SGKKETFGCL GMIYAMMAIG LLGFVVWAHH MFTVGMDIDT 

       310        320        330        340        350        360 
RAYFTSATMI IAVPTGIKIF SWLATLHGTQ INYSPSMLWS LGFVFLFTVG GLTGVILANS 

       370        380        390        400        410        420 
SIDVTLHDTY YVVAHFHYVL SMGAVFAIMG GFVHWYPLFT GLALNPYLLK IQFFTMFIGV 

       430        440        450        460        470        480 
NLTFFPQHFL GLAGMPRRYS DYPDTYTSWN IISSLGSYIS LIATMLMLMI IWESLINKRI 

       490        500        510 
ILFPLNMNSS IEWYQNLPPA EHSYNELPIL SNF

P67794 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