[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1016/0378-1119(92)90144-E; PubMed=1446833 [NCBI, ExPASy, EBI, Israel, Japan] Takase M., Miura I., Nakata A., Takeuchi T., Nishioka M.; "Cloning and sequencing of the cDNA encoding tyrosinase of the Japanese pond frog, Rana nigromaculata."; Gene 121:359-363(1992).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-277. TISSUE=Blood; PubMed=7772385 [NCBI, ExPASy, EBI, Israel, Japan] Miura I., Okumoto H., Makino K., Nakata A., Nishioka M.; "Analysis of the tyrosinase gene of the Japanese pond frog, Rana nigromaculata: cloning and nucleotide sequence of the genomic DNA containing the tyrosinase gene and its flanking regions."; Jpn. J. Genet. 70:79-82(1995).

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.
SUBCELLULAR LOCATION: Melanosome membrane; Single-pass type I membrane protein.
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

D12514; BAA02077.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D37779; BAA07034.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JC1392; JC1392.

3D structure databases

ModBase

Q04604.

Ontologies

GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0033162;	Cellular component: melanosome membrane (inferred from electronic annotation from UniProtKB-SubCell).
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.

Phylogenomic databases

HOVERGEN

Q04604; -.

Other

UniRef

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

Keywords

Copper; Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding; Monooxygenase; Oxidoreductase; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`	`Potential.`
`CHAIN`	`20 532`	`513`	`Tyrosinase.`	`PRO_0000035884`
`TOPO_DOM`	`20 475`	`456`	`Lumenal, melanosome (Potential).`
`TRANSMEM`	`476 499`	`24`	`Potential.`
`TOPO_DOM`	`500 532`	`33`	`Cytoplasmic (Potential).`
`METAL`	`184 184`		`Copper A (By similarity).`
`METAL`	`206 206`		`Copper A (By similarity).`
`METAL`	`215 215`		`Copper A (By similarity).`
`METAL`	`367 367`		`Copper B (By similarity).`
`METAL`	`371 371`		`Copper B (By similarity).`
`METAL`	`394 394`		`Copper B (By similarity).`
`CARBOHYD`	`90 90`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`115 115`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`165 165`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`234 234`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`341 341`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`375 375`		`N-linked (GlcNAc...) (Potential).`
`VARIANT`	`10 10`	`1`	`T -> A.`

Sequence information

Length: 532 AA [This is the length of the unprocessed precursor]

Molecular weight: 60116 Da [This is the MW of the unprocessed precursor]

CRC64: B27D3080F0C74B3A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MESTTVLLAT STLLLVLHAS YGQFPRACST AQVLLSKECC PVWPGDNSSC GEVSGRGVCQ 

        70         80         90        100        110        120 
DVVPSNSPVG AQFPFSGIDD RENWPIVFYN RTCQCQGNFM GYNCGECRFG YTGPNCTVRR 

       130        140        150        160        170        180 
NMIRKDIFRM TTAEKDKLIA YLNLAKHTIS PDYVIATGTY EQMNNGSNPM FADISAYDLF 

       190        200        210        220        230        240 
VWIHYYASRD AFLEDGSVWA DIDFAHEAPG FLPWHRFYLL LWEREIQKVT GDDNFTIPFW 

       250        260        270        280        290        300 
DWRDAQQCEL CTDEFFGGTH PTSNNLLSPA SFFSSWQIIC SRPEEYNSLR IICNGTNEGP 

       310        320        330        340        350        360 
LLRSPGRHDR NRTPRLPTSA DVEACLSLTD YETGAMDRSA NFSFRNTLEG FAVPTSGIAN 

       370        380        390        400        410        420 
RSQSSMHNSL HVFLNGSMSS VQGSANDPIF VLHHAFVDSL FEQWLRRHQP SLDVYPEANA 

       430        440        450        460        470        480 
PVGHNREYNM VPFIPLFTNG EFFVQSRDLG YDYDYLAESG SIEDFLLPYL EQARQIWQWL 

       490        500        510        520        530 
LGAAVLGGLI TAVIATIISL TCRRKRKTKI SEETRPLLME AEDYQATYQS NL

Q04604 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