Reviewed, UniProtKB/Swiss-Prot P55033 (TYRO_FELCA)

Names and origin

Protein names

Recommended name:
    Tyrosinase
    EC=1.14.18.1
Alternative name(s):
    Monophenol monooxygenase

Gene names

Name:

TYR

Organism

Felis catus (Cat) (Felis silvestris catus)

Taxonomic identifier

9685 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Felidae › Felinae › Felis

Protein attributes

Sequence length	80 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (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.
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.
Sequence similarities	Belongs to the tyrosinase family.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Cellular component	Membrane
Domain	Transmembrane
Ligand	Copper
Molecular function	Monooxygenase Oxidoreductase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	melanin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW monophenol monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – ›80	›80	Tyrosinase		PRO_0000186729
Amino acid modifications
	Glycosylation	59	1	N-linked (GlcNAc...) Potential
Experimental info
	Non-terminal residue	1	1
	Non-terminal residue	80	1

Sequences

	Sequence		Length	Mass (Da)
	P55033-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 926D7C99D49B74D3	FASTA	80	8,694
	10 20 30 40 50 60 LEEYNSRQAL CDGTPEGPLL RNPGNHDKAR TPRLPSSADV EFCLSLTQYE SDSMDKAANF 70 80 SFRNTLEGFA SPLTGIADAS

References

[1]

"Cutaneous malignant melanomas in 57 cats: identification of (amelanotic) signet-ring and balloon cell types and verification of their origin by immunohistochemistry, electron microscopy, and in situ hybridization." van der Linde-Sipman J.S., de Wit M.M., van Garderen E., Molenbeek R.F., van der Velde-Zimmermann D., de Weger R.A. Vet. Pathol. 34:31-38(1997) [PubMed: 9150543] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: European shorthair. Tissue: Melanoma.

Web resources

Protein Spotlight

Snowy stardom - Issue 49 of August 2004

Cross-references

Sequence databases
EMBLGenBankDDBJ	U40716 mRNA. Translation: AAB08729.1.
3D structure databases
ModBase	Search...
Phylogenomic databases
HOVERGEN	P55033.
Enzyme and pathway databases
BRENDA	1.14.18.1. 273949.
Family and domain databases
InterPro	IPR002227. Tyrosinase. [Graphical view]
PROSITE	PS00497. TYROSINASE_1. Partial match. PS00498. TYROSINASE_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TYRO_FELCA

Accession

Primary (citable) accession number: P55033

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	October 13, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)