[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Spradling T.A., Brant S.V., Hafner M.S., Dickerson C.J.; "DNA data support a rapid radiation of pocket gopher genera."; J. Mammal. Evol. 11:105-125(2004).

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

AY331074; AAR02575.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

SMR

Q6EGJ0; 1-511.

ModBase

Q6EGJ0.

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: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

Q6EGJ0.

Phylogenomic databases

HOVERGEN

Q6EGJ0; -.

Other

UniRef

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`	`1 516`	`516`	`Cytochrome c oxidase subunit 1.`	`PRO_0000254909`
`TRANSMEM`	`17 37`	`21`	`Potential.`
`TRANSMEM`	`63 83`	`21`	`Potential.`
`TRANSMEM`	`102 122`	`21`	`Potential.`
`TRANSMEM`	`145 165`	`21`	`Potential.`
`TRANSMEM`	`183 203`	`21`	`Potential.`
`TRANSMEM`	`234 254`	`21`	`Potential.`
`TRANSMEM`	`268 288`	`21`	`Potential.`
`TRANSMEM`	`310 330`	`21`	`Potential.`
`TRANSMEM`	`338 358`	`21`	`Potential.`
`TRANSMEM`	`380 400`	`21`	`Potential.`
`TRANSMEM`	`414 434`	`21`	`Potential.`
`TRANSMEM`	`453 473`	`21`	`Potential.`
`METAL`	`61 61`		`Iron (heme A axial ligand) (Probable).`
`METAL`	`240 240`		`Copper B (Probable).`
`METAL`	`244 244`		`Copper B (Probable).`
`METAL`	`290 290`		`Copper B (Probable).`
`METAL`	`291 291`		`Copper B (Probable).`
`METAL`	`376 376`		`Iron (heme A3 axial ligand) (Probable).`
`METAL`	`378 378`		`Iron (heme A axial ligand) (Probable).`
`CROSSLNK`	`240 244`		`1'-histidyl-3'-tyrosine (His-Tyr) (By similarity).`

Sequence information

Length: 516 AA [This is the length of the unprocessed precursor]

Molecular weight: 57127 Da [This is the MW of the unprocessed precursor]

CRC64: E15A5B8114E25738 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFINRWLFST NHKDIGTLYM IFGAWAGMVG TGLSILIRAE LGQPGSLLGD DQIYNVVVTA 

        70         80         90        100        110        120 
HAFVMIFFMV MPIMIGGFGN WLVPLMIGAP DMAFPRMNNM SFWLLPPSFL LLLSSSMVEA 

       130        140        150        160        170        180 
GAGTGWTVYP PLAGNLAHAG ASVDLTIFSL HLAGVSSILG AINFITTIIN MKPPAITQYQ 

       190        200        210        220        230        240 
TPLFVWSVMI TAVLLLLSLP VLAAGITMLL TDRNLNTTFF DPAGGGDPIL YQHLFWFFGH 

       250        260        270        280        290        300 
PEVYILILPG FGMISHIVTY YSGKKEPFGY MGMVWAMMSI GFLGFIVWAH HMFTVGMDVD 

       310        320        330        340        350        360 
TRAYFTSATM IIAIPTGVKV FSWLATLHGG NIKWSPAMLW ALGFIFLFTI GGLTGIVLSN 

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFVHWFPLF TGYTLNDTWA KIHFTIMFVG 

       430        440        450        460        470        480 
VNMTFFPQHF LGLAGMPRRY SDYPDAYTTW NTISSMGSFI SLTAVILMVF IIWEALASKR 

       490        500        510 
VVKSIPLTST NLEWMHGCPP PFHTFEEPAF IKSSIK

Q6EGJ0 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