[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Body wall muscle, and Egg; PubMed=1551572 [NCBI, ExPASy, EBI, Israel, Japan] Okimoto R., Macfarlane J.L., Clary D.O., Wolstenholme D.R.; "The mitochondrial genomes of two nematodes, Caenorhabditis elegans and Ascaris suum."; Genetics 130:471-498(1992).

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

X54253; CAA38171.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S26022; S26022.

RefSeq

NP_006949.1; -.

3D structure databases

HSSP

P00396; 2OCC. [HSSP ENTRY / PDB]

ModBase

P24881.

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

P24881.

Genome annotation databases

GeneID

807671; -.

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`	`1 525`	`525`	`Cytochrome c oxidase subunit 1.`	`PRO_0000183288`
`TRANSMEM`	`25 45`	`21`	`Potential.`
`TRANSMEM`	`71 91`	`21`	`Potential.`
`TRANSMEM`	`108 128`	`21`	`Potential.`
`TRANSMEM`	`152 172`	`21`	`Potential.`
`TRANSMEM`	`190 210`	`21`	`Potential.`
`TRANSMEM`	`241 261`	`21`	`Potential.`
`TRANSMEM`	`274 294`	`21`	`Potential.`
`TRANSMEM`	`317 337`	`21`	`Potential.`
`TRANSMEM`	`344 364`	`21`	`Potential.`
`TRANSMEM`	`387 407`	`21`	`Potential.`
`TRANSMEM`	`420 440`	`21`	`Potential.`
`TRANSMEM`	`459 479`	`21`	`Potential.`
`METAL`	`69 69`		`Iron (heme A axial ligand) (Probable).`
`METAL`	`247 247`		`Copper B (Probable).`
`METAL`	`251 251`		`Copper B (Probable).`
`METAL`	`297 297`		`Copper B (Probable).`
`METAL`	`298 298`		`Copper B (Probable).`
`METAL`	`383 383`		`Iron (heme A3 axial ligand) (Probable).`
`METAL`	`385 385`		`Iron (heme A axial ligand) (Probable).`
`CROSSLNK`	`247 251`		`1'-histidyl-3'-tyrosine (His-Tyr) (By similarity).`

Sequence information

Length: 525 AA [This is the length of the unprocessed precursor]

Molecular weight: 58529 Da [This is the MW of the unprocessed precursor]

CRC64: 2EFB6A50522F7FBE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSGFYKYQGG LSVWLESSNH KDIGTLYFLF GLWSGMVGTS LSLVIRLELA KPGLLLGSGQ 

        70         80         90        100        110        120 
LYNSVITAHA ILMIFFMVMP TMIGGFGNWM LPLMLGAPDM SFPRLNNLSF WLLPTAMFLI 

       130        140        150        160        170        180 
LDACFVDMGC GTSWTVYPPL STMGHPGGSV DLAIFSLHCA GVSSILGAIN FMTTTKNLRS 

       190        200        210        220        230        240 
SSISLEHMSL FVWTVFVTVF LLVLSLPVLA GAITMLLTDR NLNTSFFDPS TGGNPLIYQH 

       250        260        270        280        290        300 
LFWFFGHPEV YILILPAFGI ISQSSLYLTG KKEVFGSLGM VYAILSIGLI GCVVWAHHMY 

       310        320        330        340        350        360 
TVGMDLDSRA YFTAATMVIA VPTGVKVFSW LATLFGMKMV FQPLLLWVMG FIFLFTIGGL 

       370        380        390        400        410        420 
TGVMLSNSSL DIILHDTYYV VSHFHYVLSL GAVFGIFTGV TLWWSFITGF VYDKMMMSSV 

       430        440        450        460        470        480 
FVLMFVGVNL TFFPLHFAGI HGYPRKYLDY PDVYSVWNIM ASYGSMISVF ALFLFIYVLL 

       490        500        510        520 
ESFVGHRIFL FDYYVNSGPE YSLSGYVFGH SYQSEIFYSS IVFKF

P24881 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