[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. STRAIN=DSM 40716 / ETH 22794 / GLA.0; DOI=10.1021/bi00343a003; PubMed=3002431 [NCBI, ExPASy, EBI, Israel, Japan] Huber M., Hintermann G., Lerch K.; "Primary structure of tyrosinase from Streptomyces glaucescens."; Biochemistry 24:6038-6044(1985).
[2]	COPPER-LIGANDS, AND MUTAGENESIS. STRAIN=DSM 40716 / ETH 22794 / GLA.0; DOI=10.1021/bi00415a032; PubMed=2846043 [NCBI, ExPASy, EBI, Israel, Japan] Huber M., Lerch K.; "Identification of two histidines as copper ligands in Streptomyces glaucescens tyrosinase."; Biochemistry 27:5610-5615(1988).
[3]	COPPER-LIGANDS, AND MUTAGENESIS. STRAIN=DSM 40716 / ETH 22794 / GLA.0; PubMed=1901488 [NCBI, ExPASy, EBI, Israel, Japan] Jackman M.P., Hajnal A., Lerch K.; "Albino mutants of Streptomyces glaucescens tyrosinase."; Biochem. J. 274:707-713(1991).

Comments

FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.
CATALYTIC ACTIVITY: L-tyrosine + L-dopa + O₂ = L-dopa + dopaquinone + H₂O.
COFACTOR: Binds 2 copper ions per subunit.
MISCELLANEOUS: The extra- and intra-cellular tyrosinases are identical.
SIMILARITY: Belongs to the tyrosinase 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

M11302; AAA26834.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24089; A24089.

3D structure databases

HSSP

O61363; 1JS8. [HSSP ENTRY / PDB]

SMR

P06845; 2-272.

ModBase

P06845.

Ontologies

GO:0005507;	Molecular function: copper ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004503;	Molecular function: monophenol monooxygenase activity (inferred from electronic annotation from EC).
GO:0006583;	Biological process: melanin biosynthetic process from tyrosine (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR008922; Di-copper_centre.
IPR002227; Tyrosinase.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.1280.10; Di-copper_centre; 1.

Pfam

PF00264; Tyrosinase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00092; TYROSINASE.

PROSITE

PS00497; TYROSINASE_1; 1.
PS00498; TYROSINASE_2; 1.

Other

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

Keywords

Copper; Direct protein sequencing; Melanin biosynthesis; Metal-binding; Monooxygenase; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 274`	`273`	`Tyrosinase.`	`PRO_0000186738`
`METAL`	`38 38`		`Copper A.`
`METAL`	`54 54`		`Copper A.`
`METAL`	`63 63`		`Copper A.`
`METAL`	`190 190`		`Copper B.`
`METAL`	`194 194`		`Copper B.`
`METAL`	`216 216`		`Copper B.`
`MUTAGEN`	`38 38`		`H->Q: Loss of activity.`
`MUTAGEN`	`54 54`		`H->Q: Loss of activity.`
`MUTAGEN`	`63 63`		`H->N: Loss of activity.`
`MUTAGEN`	`190 190`		`H->N: Loss of activity.`
`MUTAGEN`	`191 191`		`N->Q: Loss of activity.`
`MUTAGEN`	`194 194`		`H->Q: Loss of activity.`
`MUTAGEN`	`216 216`		`H->Q: Loss of activity.`
`CONFLICT`	`216 216`		`H -> N (in Ref. 1; AAA26834).`

Sequence information

Length: 274 AA [This is the length of the unprocessed precursor]

Molecular weight: 30874 Da [This is the MW of the unprocessed precursor]

CRC64: 0FDC67DC2739AA79 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTVRKNQATL TADEKRRFVA AVLELKRSGR YDEFVTTHNA FIIGDTDAGE RTGHRSPSFL 

        70         80         90        100        110        120 
PWHRRYLLEF ERALQSVDAS VALPYWDWSA DRTARASLWA PDFLGGTGRS LDGRVMDGPF 

       130        140        150        160        170        180 
AASAGNWPIN VRVDGRAYLR RSLGTAVREL PTRAEVESVL GMATYDTAPW NSASDGFRNH 

       190        200        210        220        230        240 
LEGWRGVNLH NRVHVWVGGQ MATGMSPNDP VFWLHHAYVD KLWAEWQRRH PGSGYLPAAG 

       250        260        270 
TPDVVDLNDR MKPWNDTSPA DLLDHTAHYT FDTD

P06845 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