[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=CW15-2; DOI=10.1093/nar/14.18.7506; PubMed=3020517 [NCBI, ExPASy, EBI, Israel, Japan] Boer P.H., Gray M.W.; "Nucleotide sequence of a protein coding region in Chlamydomonas reinhardtii mitochondrial DNA."; Nucleic Acids Res. 14:7506-7507(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cw15; DOI=10.1007/BF00355060; PubMed=1831072 [NCBI, ExPASy, EBI, Israel, Japan] Boer P.H., Gray M.W.; "Short dispersed repeats localized in spacer regions of Chlamydomonas reinhardtii mitochondrial DNA."; Curr. Genet. 19:309-312(1991).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=cw15; Vahrenholz C., Pratje E., Michaelis G., Dujon B.; "Mitochondrial DNA of Chlamydomonas reinhardtii: sequence and arrangement of URF5 and the gene for cytochrome oxidase subunit I."; Mol. Gen. Genet. 201:213-224(1985).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 79-234. PubMed=2987921 [NCBI, ExPASy, EBI, Israel, Japan] Boer P.H., Bonen L., Lee R.W., Gray M.W.; "Genes for respiratory chain proteins and ribosomal RNAs are present on a 16-kilobase-pair DNA species from Chlamydomonas reinhardtii mitochondria."; Proc. Natl. Acad. Sci. U.S.A. 82:3340-3344(1985).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30. PubMed=3007117 [NCBI, ExPASy, EBI, Israel, Japan] Boer P.H., Gray M.W.; "The URF 5 gene of Chlamydomonas reinhardtii mitochondria: DNA sequence and mode of transcription."; EMBO J. 5:21-28(1986).

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

U03843; AAB93443.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X54860; CAA38642.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X66484; CAA47114.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X03464; CAA27180.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24707; A24707.

RefSeq

NP_042567.1; -.

3D structure databases

HSSP

P33517; 1M56. [HSSP ENTRY / PDB]

ModBase

P08681.

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).

Genome annotation databases

GeneID

801495; -.

KEGG

cre:ChrepMp04; -.

Other

ProtoNet

P08681.

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`	`1 505`	`505`	`Cytochrome c oxidase subunit 1.`	`PRO_0000183307`
`TRANSMEM`	`14 34`	`21`	`Potential.`
`TRANSMEM`	`55 75`	`21`	`Potential.`
`TRANSMEM`	`98 118`	`21`	`Potential.`
`TRANSMEM`	`143 163`	`21`	`Potential.`
`TRANSMEM`	`180 200`	`21`	`Potential.`
`TRANSMEM`	`229 249`	`21`	`Potential.`
`TRANSMEM`	`261 281`	`21`	`Potential.`
`TRANSMEM`	`302 322`	`21`	`Potential.`
`TRANSMEM`	`332 352`	`21`	`Potential.`
`TRANSMEM`	`374 394`	`21`	`Potential.`
`TRANSMEM`	`408 428`	`21`	`Potential.`
`TRANSMEM`	`446 466`	`21`	`Potential.`
`METAL`	`60 60`		`Iron (heme A axial ligand) (Probable).`
`METAL`	`235 235`		`Copper B (Probable).`
`METAL`	`239 239`		`Copper B (Probable).`
`METAL`	`284 284`		`Copper B (Probable).`
`METAL`	`285 285`		`Copper B (Probable).`
`METAL`	`370 370`		`Iron (heme A3 axial ligand) (Probable).`
`METAL`	`372 372`		`Iron (heme A axial ligand) (Probable).`
`CROSSLNK`	`235 239`		`1'-histidyl-3'-tyrosine (His-Tyr) (By similarity).`
`CONFLICT`	`388 388`		`Y -> C (in Ref. 2; CAA47114).`
`CONFLICT`	`428 428`		`A -> V (in Ref. 2; CAA47114).`

Sequence information

Length: 505 AA [This is the length of the unprocessed precursor]

Molecular weight: 55160 Da [This is the MW of the unprocessed precursor]

CRC64: 042C316203E88B9E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRWLYSTSHK DIGLLYLVFA FFGGLLGTSL SMLIRYELAL PGRGLLDGNG QLYNVIITGH 

        70         80         90        100        110        120 
GIIMLLFMVM PALFGGFGNW LLPIMIGAPD MAFPRLNNIS FWLNPPALAL LLLSTLVEQG 

       130        140        150        160        170        180 
PGTGWTAYPP LSVQHSGTSV DLAILSLHLN GLSSILGAVN MLVTVAGLRA PGMKLLHMPL 

       190        200        210        220        230        240 
FVWAIALTAV LVILAVPVLA AALVMLLTDR NINTAYFCES GDLILYQHLF WFFGHPEVYI 

       250        260        270        280        290        300 
LILPAFGIVS QVVSFFSQKP VFGLTGMICA MGAISLLGFI VWAHHMFTVG LDLDTVAYFT 

       310        320        330        340        350        360 
SATMIIAVPT GMKIFSWMAT IYSGRVWFTT PMWFAVGFIC LFTLGGVTGV VLANAGVDML 

       370        380        390        400        410        420 
VHDTYYVVAH FHYVLSMGAV FGIFAGVYFW GNLITGLGYH EGRAMVHFWL LFIGVNLTFF 

       430        440        450        460        470        480 
PQHFLGLAGM PRRMFDYADC FAGWNAVSSF GASISFISVI VFATTFQEAV RTVPRTATTL 

       490        500 
EWVLLATPAH HALSQVPVLR TASSH

P08681 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