[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=6092056 [NCBI, ExPASy, EBI, Israel, Japan] Waring R.B., Brown T.A., Ray J.A., Scazzocchio C., Davies R.W.; "Three variant introns of the same general class in the mitochondrial gene for cytochrome oxidase subunit 1 in Aspergillus nidulans."; EMBO J. 3:2121-2128(1984).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 44-133. DOI=10.1093/nar/10.15.4783; PubMed=6290989 [NCBI, ExPASy, EBI, Israel, Japan] Netzker R., Koechel H.G., Basak N., Kuentzel H.; "Nucleotide sequence of Aspergillus nidulans mitochondrial genes coding for ATPase subunit 6, cytochrome oxidase subunit 3, seven unidentified proteins, four tRNAs and L-rRNA."; Nucleic Acids Res. 10:4783-4794(1982).

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

X00790; CAB38220.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A22735; ODAS1.

3D structure databases

HSSP

P00396; 2OCC. [HSSP ENTRY / PDB]

ModBase

P00402.

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

P00402.

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`	`1 567`	`567`	`Cytochrome c oxidase subunit 1.`	`PRO_0000183331`
`TRANSMEM`	`56 76`	`21`	`Potential.`
`TRANSMEM`	`103 123`	`21`	`Potential.`
`TRANSMEM`	`139 159`	`21`	`Potential.`
`TRANSMEM`	`185 205`	`21`	`Potential.`
`TRANSMEM`	`221 241`	`21`	`Potential.`
`TRANSMEM`	`274 294`	`21`	`Potential.`
`TRANSMEM`	`306 326`	`21`	`Potential.`
`TRANSMEM`	`344 364`	`21`	`Potential.`
`TRANSMEM`	`377 397`	`21`	`Potential.`
`TRANSMEM`	`416 436`	`21`	`Potential.`
`TRANSMEM`	`451 471`	`21`	`Potential.`
`TRANSMEM`	`491 511`	`21`	`Potential.`
`METAL`	`101 101`		`Iron (heme A axial ligand) (Probable).`
`METAL`	`280 280`		`Copper B (Probable).`
`METAL`	`284 284`		`Copper B (Probable).`
`METAL`	`329 329`		`Copper B (Probable).`
`METAL`	`330 330`		`Copper B (Probable).`
`METAL`	`415 415`		`Iron (heme A3 axial ligand) (Probable).`
`METAL`	`417 417`		`Iron (heme A axial ligand) (Probable).`
`CROSSLNK`	`280 284`		`1'-histidyl-3'-tyrosine (His-Tyr) (By similarity).`

Sequence information

Length: 567 AA [This is the length of the unprocessed precursor]

Molecular weight: 62621 Da [This is the MW of the unprocessed precursor]

CRC64: 9163AAEA8C02F6A6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIIDLNTNNV LGKKFSTSTK KENIKQIESS SFLTFKQPTE WQERWYLSSN AKDIGTLYLM 

        70         80         90        100        110        120 
FALFSGLLGT AFSVLIRLEL SGPGVQYIAD NQLYNSIITA HAIMMIFFMV MPALIGGFGN 

       130        140        150        160        170        180 
FLLPLLVGGP DMAFPRLNNI SFWLLVPSLL LFVFSATIEN GAGTGWTLYP PLSGIQSHSG 

       190        200        210        220        230        240 
PSVDLAIFGL HLSGISSMLG AMNFITTILN MRSPGIRLHK LALFGWAVII TAVLLLLSLP 

       250        260        270        280        290        300 
VLAGGITMVL TDRNFNTSFF EVAGGGDPIL FQHLFWFFGH PEVYILIIPG FGIISTVIAA 

       310        320        330        340        350        360 
GSGKNVFGYL GMVYAMMSIG VLGFLVWSHH MYTVGLDVDT RAYFTAATLI IAVPTGIKIF 

       370        380        390        400        410        420 
SWLATCYGGS LHLTPPMLFA LGFVVLFTIG GLSGVVLANA SLDVAFHDTY YVVAHFHYVL 

       430        440        450        460        470        480 
SMGAVFALFS GWYLWIPKLL GLSYDQFAAK VHFWILFIGV NLTFFPQHFL GLQLMPRRIS 

       490        500        510        520        530        540 
DYPDAFYGWN LLSSIGSIIS VVATWYFLTI IYKQLTEGKA VSRYPWLTPQ LFSDTFQVLF 

       550        560 
TRNNSSLEWC LTSPPKPHAF ASLPLQS

P00402 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