[1]	NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN ALBINISM. STRAIN=White Galloway; DOI=10.1007/s00335-002-2249-5; PubMed=14727143 [NCBI, ExPASy, EBI, Israel, Japan] Schmutz S.M., Berryere T.G., Ciobanu D.C., Mileham A.J., Schmidtz B.H., Fredholm M.; "A form of albinism in cattle is caused by a tyrosinase frameshift mutation."; Mamm. Genome 15:62-67(2004).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Skin; Guibert S., Julien R., Oulmouden A.; "Transcriptional regulation of bovine TYR gene."; Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone (By similarity).
CATALYTIC ACTIVITY: L-tyrosine + L-dopa + O₂ = L-dopa + dopaquinone + H₂O.
COFACTOR: Binds 2 copper ions per subunit (By similarity).
SUBCELLULAR LOCATION: Melanosome membrane; Single-pass type I membrane protein (By similarity).
DISEASE: Defects in TYR are the cause of a form of albinism in Braunvieh calf.
SIMILARITY: Belongs to the tyrosinase family.
WEB RESOURCE: Name=Protein Spotlight; Note=Snowy stardom - Issue 49 of August 2004; URL="http://www.expasy.org/spotlight/back_issues/sptlt049.shtml";.

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

AY046527; AAL02331.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF445639; AAL38168.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_851344.1; -.

UniGene

Bt.9028

3D structure databases

ModBase

Q8MIU0.

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:0046982;	Molecular function: protein heterodimerization activity (inferred from sequence or structural similarity from UniProtKB).
GO:0042803;	Molecular function: protein homodimerization activity (inferred from sequence or structural similarity from UniProtKB).
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.

ProtoNet

Q8MIU0.

Genome annotation databases

Ensembl

ENSBTAG00000011813; Bos taurus. [Contig view]

GeneID

280951; -.

KEGG

bta:280951; -.

Phylogenomic databases

HOVERGEN

Q8MIU0; -.

Other

UniRef

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

Keywords

Albinism; 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 17`	`17`	`Potential.`
`CHAIN`	`18 530`	`513`	`Tyrosinase.`	`PRO_0000035876`
`TOPO_DOM`	`19 473`	`455`	`Lumenal, melanosome (Potential).`
`TRANSMEM`	`474 494`	`21`	`Potential.`
`TOPO_DOM`	`495 530`	`36`	`Cytoplasmic (Potential).`
`METAL`	`180 180`		`Copper A (By similarity).`
`METAL`	`202 202`		`Copper A (By similarity).`
`METAL`	`211 211`		`Copper A (By similarity).`
`METAL`	`363 363`		`Copper B (By similarity).`
`METAL`	`367 367`		`Copper B (By similarity).`
`METAL`	`390 390`		`Copper B (By similarity).`
`CARBOHYD`	`86 86`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`230 230`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`290 290`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`337 337`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`371 371`		`N-linked (GlcNAc...) (Potential).`
`CONFLICT`	`172 172`		`V -> A (in Ref. 2; AAL38168).`

Sequence information

Length: 530 AA [This is the length of the unprocessed precursor]

Molecular weight: 60304 Da [This is the MW of the unprocessed precursor]

CRC64: 1C0CEF3D8CB1356C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLLAALYCLL WSFRTSAGHF PRACASSKSL TEKECCPPWA GDGSPCGRLS GRGSCQDVIL 

        70         80         90        100        110        120 
STAPLGPQFP FTGVDDRESW PSIFYNRTCQ CFSNFMGFNC GSCKFGFRGP RCTERRLLVR 

       130        140        150        160        170        180 
RNIFDLSVPE KNKFLAYLTL AKHTTSPDYV IPTGTYGQMN HGTTPLFNDV SVYDLFVWMH 

       190        200        210        220        230        240 
YYVSRDTLLG DSEVWRDIDF AHEAPGFLPW HRLFLLLWEQ EIQKLTGDEN FTIPYWDWRD 

       250        260        270        280        290        300 
AENCDVCTDE YMGGRNPANP NLLSPASFFS SWQIVCSRLE EYNSRQALCN GTSEGPLLRN 

       310        320        330        340        350        360 
PGNHDKARTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFADP VTGIADASQS 

       370        380        390        400        410        420 
SMHNALHIYM NGTMSQVPGS ANDPIFLLHH AFVDSIFEQW LRKYHPLQDV YPEANAPIGH 

       430        440        450        460        470        480 
NRESYMVPFI PLYRNGDFFI SSKDXGYDYS YLQDSEPDIF QDYIKPYLEQ AQRIWPWLIG 

       490        500        510        520        530 
AAVVGSVLTA VLGGLTSLLC RRKRNQLPEE KQPLLMEKED YHNLMYQSHL

Q8MIU0 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