[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Lee K., Feinstein J., Cracraft J.; "Phylogenetic relationships of the ratite birds: resolving conflicts between molecular and morphological data sets."; (In) Mindell D.P. (eds.); Avian molecular evolution and systematics, pp.1-1, Academic Press, New York (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

U76059; AAB61319.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P18401; 1FFT. [HSSP ENTRY / PDB]

SMR

O03524; 3-337.

ModBase

O03524.

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).

Phylogenomic databases

HOVERGEN

O03524; -.

Other

ProtoNet

O03524.

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 >337`	`>337`	`Cytochrome c oxidase subunit 1.`	`PRO_0000183326`
`TRANSMEM`	`18 38`	`21`	`Potential.`
`TRANSMEM`	`64 84`	`21`	`Potential.`
`TRANSMEM`	`103 123`	`21`	`Potential.`
`TRANSMEM`	`146 166`	`21`	`Potential.`
`TRANSMEM`	`184 204`	`21`	`Potential.`
`TRANSMEM`	`235 255`	`21`	`Potential.`
`TRANSMEM`	`269 289`	`21`	`Potential.`
`TRANSMEM`	`311 331`	`21`	`Potential.`
`METAL`	`62 62`		`Iron (heme A axial ligand) (Probable).`
`METAL`	`241 241`		`Copper B (Probable).`
`METAL`	`245 245`		`Copper B (Probable).`
`METAL`	`291 291`		`Copper B (Probable).`
`METAL`	`292 292`		`Copper B (Probable).`
`CROSSLNK`	`241 245`		`1'-histidyl-3'-tyrosine (His-Tyr) (By similarity).`
`NON_TER`	`337 337`

Sequence information

Length: 337 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 36786 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 662D7FDD03F7BE02 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTFITRWFFS TNHKDIGTLY LIFGAWAGMV GTALSLLIRA ELGQPGTLLG DDQIYNVVVT 

        70         80         90        100        110        120 
AHAFVMIFFM VMPVMIGGFG NWLVPLMIGA PDMAFPRMNN MSFWLLPPSF LLLLASSTVE 

       130        140        150        160        170        180 
AGAGTGWTVY PPLAGNLAHA GASVDLAIFS LHLAGVSSIL GAINFITTAI NMKPPALTQY 

       190        200        210        220        230        240 
QTPLFVWSVL ITAILLLLSL PVLAAGITML LTDRNLNTTF FDPAGGGDPV LYQHLFWFFG 

       250        260        270        280        290        300 
HPEVYILILP GFGMISHVVT YYAGKKEPFG YMGMVWAMLS IGFLGFIVWA HHMFTVGMDV 

       310        320        330 
DTRAYFTSAT MIIAIPTGIK VFSWLATLHG GTIKWDP

O03524 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