[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Heart; DOI=10.1016/0022-2836(82)90137-1; PubMed=7120390 [NCBI, ExPASy, EBI, Israel, Japan] Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F., Young I.G.; "Complete sequence of bovine mitochondrial DNA. Conserved features of the mammalian mitochondrial genome."; J. Mol. Biol. 156:683-717(1982).
[2]	PROTEIN SEQUENCE. TISSUE=Heart; PubMed=2165784 [NCBI, ExPASy, EBI, Israel, Japan] Hensel S., Buse G.; "Studies on cytochrome-c oxidase, XIV. The amino-acid sequence of subunit I -- proteinchemical methods for the analysis of a large hydrophobic membrane protein."; Biol. Chem. Hoppe-Seyler 371:411-422(1990).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=65, 66, D, and F; Wettstein P.J.; "Bos taurus mitochondrial protein coding regions."; Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[4]	COVALENT BOND. PubMed=10338009 [NCBI, ExPASy, EBI, Israel, Japan] Buse G., Soulimane T., Dewor M., Meyer H.E., Blueggel M.; "Evidence for a copper-coordinated histidine-tyrosine cross-link in the active site of cytochrome oxidase."; Protein Sci. 8:985-990(1999).
[5]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). PubMed=8638158 [NCBI, ExPASy, EBI, Israel, Japan] Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.; "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A."; Science 272:1136-1144(1996).
[6]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). TISSUE=Heart; DOI=10.1107/S0907444998006362; PubMed=10089392 [NCBI, ExPASy, EBI, Israel, Japan] Tomizaki T., Yamashita E., Yamaguchi H., Aoyama H., Tsukihara T., Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.; "Structure analysis of bovine heart cytochrome c oxidase at 2.8 A resolution."; Acta Crystallogr. D 55:31-45(1999).
[7]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). TISSUE=Heart; DOI=10.1107/S0907444900002213; PubMed=10771420 [NCBI, ExPASy, EBI, Israel, Japan] Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T., Shinzawa-Itoh K., Nakashima R., Yoshikawa S.; "X-ray structure of azide-bound fully oxidized cytochrome c oxidase from bovine heart at 2.9 A resolution."; Acta Crystallogr. D 56:529-535(2000).

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.
PTM: His-240 and Tyr-244 are involved in the formation of a copper-coordinated covalent cross-link at the active site of the catalytic subunit I.
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

V00654; CAA23999.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF490528; AAM08330.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF490529; AAM08343.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF493541; AAM12791.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF493542; AAM12804.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A00464; ODBO1.

3D structure databases

PDB

1OCC; X-ray; 2.80 A; A/N=1-514.	[ExPASy / RCSB / EBI]
1OCO; X-ray; 2.80 A; A/N=1-514.	[ExPASy / RCSB / EBI]
1OCR; X-ray; 2.35 A; A/N=1-514.	[ExPASy / RCSB / EBI]
1OCZ; X-ray; 2.90 A; A/N=1-514.	[ExPASy / RCSB / EBI]
1V54; X-ray; 1.80 A; A/N=2-514.	[ExPASy / RCSB / EBI]
1V55; X-ray; 1.90 A; A/N=2-514.	[ExPASy / RCSB / EBI]
2DYR; X-ray; 1.80 A; A/N=1-514.	[ExPASy / RCSB / EBI]
2DYS; X-ray; 2.20 A; A/N=1-514.	[ExPASy / RCSB / EBI]
2EIJ; X-ray; 1.90 A; A/N=1-514.	[ExPASy / RCSB / EBI]
2EIK; X-ray; 2.10 A; A/N=1-514.	[ExPASy / RCSB / EBI]
2EIL; X-ray; 2.10 A; A/N=1-514.	[ExPASy / RCSB / EBI]
2EIM; X-ray; 2.60 A; A/N=1-514.	[ExPASy / RCSB / EBI]
2EIN; X-ray; 2.70 A; A/N=1-514.	[ExPASy / RCSB / EBI]
2OCC; X-ray; 2.30 A; A/N=1-514.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1OCC; -.
1OCO; -.
1OCR; -.
1OCZ; -.
1V54; -.
1V55; -.
2DYR; -.
2DYS; -.
2EIJ; -.
2EIK; -.
2EIL; -.
2EIM; -.
2EIN; -.
2OCC; -.

ModBase

P00396.

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

P00396.

Genome annotation databases

Ensembl

ENSBTAG00000019766; Bos taurus. [Contig view]

Phylogenomic databases

HOVERGEN

P00396; -.

Other

LinkHub

P00396; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Copper; Direct protein sequencing; Electron transport; Formylation; 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`	`1 514`	`514`	`Cytochrome c oxidase subunit 1.`	`PRO_0000183294`
`TOPO_DOM`	`1 11`	`11`	`Mitochondrial matrix.`
`TRANSMEM`	`12 40`	`29`	`I.`
`TOPO_DOM`	`41 50`	`10`	`Mitochondrial intermembrane.`
`TRANSMEM`	`51 86`	`36`	`II.`
`TOPO_DOM`	`87 94`	`8`	`Mitochondrial matrix.`
`TRANSMEM`	`95 117`	`23`	`III.`
`TOPO_DOM`	`118 140`	`23`	`Mitochondrial intermembrane.`
`TRANSMEM`	`141 170`	`30`	`IV.`
`TOPO_DOM`	`171 182`	`12`	`Mitochondrial matrix.`
`TRANSMEM`	`183 212`	`30`	`V.`
`TOPO_DOM`	`213 227`	`15`	`Mitochondrial intermembrane.`
`TRANSMEM`	`228 261`	`34`	`VI.`
`TOPO_DOM`	`262 269`	`8`	`Mitochondrial matrix.`
`TRANSMEM`	`270 286`	`17`	`VII.`
`TOPO_DOM`	`287 298`	`12`	`Mitochondrial intermembrane.`
`TRANSMEM`	`299 327`	`29`	`VIII.`
`TOPO_DOM`	`328 335`	`8`	`Mitochondrial matrix.`
`TRANSMEM`	`336 357`	`22`	`IX.`
`TOPO_DOM`	`358 370`	`13`	`Mitochondrial intermembrane.`
`TRANSMEM`	`371 400`	`30`	`X.`
`TOPO_DOM`	`401 406`	`6`	`Mitochondrial matrix.`
`TRANSMEM`	`407 433`	`27`	`XI.`
`TOPO_DOM`	`434 446`	`13`	`Mitochondrial intermembrane.`
`TRANSMEM`	`447 478`	`32`	`XII.`
`TOPO_DOM`	`479 514`	`36`	`Mitochondrial matrix.`
`METAL`	`61 61`		`Iron (heme A axial ligand).`
`METAL`	`240 240`		`Copper B.`
`METAL`	`290 290`		`Copper B.`
`METAL`	`291 291`		`Copper B.`
`METAL`	`368 368`		`Magnesium; shared with chain II.`
`METAL`	`376 376`		`Iron (heme A3 axial ligand).`
`METAL`	`378 378`		`Iron (heme A axial ligand).`
`BINDING`	`244 244`		`Oxygen (Probable).`
`MOD_RES`	`1 1`		`N-formylmethionine.`
`CROSSLNK`	`240 244`		`1'-histidyl-3'-tyrosine (His-Tyr).`
`HELIX`	`2 6`	`5`
`HELIX`	`12 41`	`30`
`STRAND`	`43 45`	`3`
`STRAND`	`47 50`	`4`
`HELIX`	`51 67`	`17`
`HELIX`	`70 74`	`5`
`HELIX`	`77 86`	`10`
`HELIX`	`95 103`	`9`
`HELIX`	`105 115`	`11`
`TURN`	`125 128`	`4`
`TURN`	`130 133`	`4`
`TURN`	`135 138`	`4`
`HELIX`	`141 170`	`30`
`HELIX`	`178 180`	`3`
`HELIX`	`183 214`	`32`
`HELIX`	`222 224`	`3`
`HELIX`	`228 245`	`18`
`HELIX`	`248 260`	`13`
`TURN`	`261 263`	`3`
`HELIX`	`270 283`	`14`
`HELIX`	`288 291`	`4`
`HELIX`	`299 311`	`13`
`HELIX`	`313 327`	`15`
`HELIX`	`336 357`	`22`
`HELIX`	`361 367`	`7`
`HELIX`	`371 382`	`12`
`HELIX`	`385 401`	`17`
`HELIX`	`407 425`	`19`
`HELIX`	`428 433`	`6`
`STRAND`	`437 439`	`3`
`HELIX`	`445 447`	`3`
`HELIX`	`448 478`	`31`
`HELIX`	`488 490`	`3`
`HELIX`	`492 494`	`3`

Sequence information

Length: 514 AA [This is the length of the unprocessed precursor]

Molecular weight: 57032 Da [This is the MW of the unprocessed precursor]

CRC64: 0D7C807D7FA3996C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFINRWLFST NHKDIGTLYL LFGAWAGMVG TALSLLIRAE LGQPGTLLGD DQIYNVVVTA 

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

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

       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 NIKWSPAMMW ALGFIFLFTV GGLTGIVLAN 

       370        380        390        400        410        420 
SSLDIVLHDT YYVVAHFHYV LSMGAVFAIM GGFVHWFPLF SGYTLNDTWA KIHFAIMFVG 

       430        440        450        460        470        480 
VNMTFFPQHF LGLSGMPRRY SDYPDAYTMW NTISSMGSFI SLTAVMLMVF IIWEAFASKR 

       490        500        510 
EVLTVDLTTT NLEWLNGCPP PYHTFEEPTY VNLK

P00396 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