Reviewed, UniProtKB/Swiss-Prot P54834 (TYRO_CANFA)

Names and origin

Protein names

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

Gene names

Name:

TYR

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	530 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

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 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.
Sequence similarities	Belongs to the tyrosinase family.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Cellular component	Membrane
Domain	Signal Transmembrane
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	melanin biosynthetic process from tyrosine 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-KW melanosome 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
	Signal peptide	1 – 18	18	Potential
	Chain	19 – 530	512	Tyrosinase		PRO_0000035877
Regions
	Topological domain	19 – 473	455	Lumenal, melanosome Potential
	Transmembrane	474 – 494	21	Potential
	Topological domain	495 – 530	36	Cytoplasmic Potential
Sites
	Metal binding	180	1	Copper A By similarity
	Metal binding	202	1	Copper A By similarity
	Metal binding	211	1	Copper A By similarity
	Metal binding	363	1	Copper B By similarity
	Metal binding	367	1	Copper B By similarity
	Metal binding	390	1	Copper B By similarity
Amino acid modifications
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	111	1	N-linked (GlcNAc...) Potential
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	230	1	N-linked (GlcNAc...) Potential
	Glycosylation	337	1	N-linked (GlcNAc...) Potential
	Glycosylation	371	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	3	1	L → V in AAA86420. Ref.2
	Sequence conflict	7	1	C → R in AAA86420. Ref.2
	Sequence conflict	59	1	I → V in AAA86420. Ref.2
	Sequence conflict	115	1	K → R in AAA86420. Ref.2
	Sequence conflict	132	1	N → D in AAA86420. Ref.2
	Sequence conflict	212	1	R → T in AAA86420. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P54834-1 [UniParc]. Last modified April 12, 2005. Version 2. Checksum: B1C45F6362ACF0E3	FASTA	530	60,336
	10 20 30 40 50 60 MLLAALCCLL WSFRTSTGHF PRACASSKSL MEKECCPPWS GDGSPCGQLS GRGACQDIIL 70 80 90 100 110 120 SNAPFGPQFP FTGVDDRESW PSVFYNRTCQ CFGNFMGFNC GNCKFGFWGQ NCTEKRLLVR 130 140 150 160 170 180 KNIFDLSVPE KNKFLAYLTL AKHTTSPDYV IPTGTYGQMN NGSTPMFNDI NIYDLFVWMH 190 200 210 220 230 240 YYVSRDTLLG GSEIWKDIDF AHEAPGFLPW HRLFLLLWEQ EIQKLTGDEN FTIPYWDWRD 250 260 270 280 290 300 AKSCDICTDE YMGGRNPANP NLLSPASFFS SWQIVCTRLE EYNSRQALCD GTPEGPLLRN 310 320 330 340 350 360 PGNHDKARTP RLPSSADVEF CLSLTQYESD SMDKAANFSF RNTLEGFASP LTGIADASQS 370 380 390 400 410 420 SMHNALHIYM NGTMSQVPGS ANDPIFLLHH AFVDSIFEQW LRRHHPLREV YPEANAPIGH 430 440 450 460 470 480 NRESYMVPFI PLYRNGDLFI SSRDLGYDYS NLQESERDIF QDYIKPYLEQ ASRIWPWLIG 490 500 510 520 530 AAVVGCVVTA VLGGLTSLLC RRNRKQLHEE KQPLLMEKED YHSLLYQTHL

References

[1]	Schmutz S.M., Berryere T.G. Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Doberman pinscher. Tissue: Skin.
[2]	"Cloning and chromosomal in situ hybridization of the dog tyrosinase exon 1." Tang Q., Williams R.W., Hogan D., Valentine V., Goldowitz D. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-273.

Web resources

Protein Spotlight

Snowy stardom - Issue 49 of August 2004

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY336053 mRNA. Translation: AAQ17535.1. U42219 Genomic DNA. Translation: AAA86420.1.
RefSeq	NP_001002941.1.
UniGene	Cfa.104
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSCAFG00000004373. Canis familiaris. [Contig view]
GeneID	403405.
KEGG	cfa:403405.
Phylogenomic databases
HOVERGEN	P54834.
Enzyme and pathway databases
BRENDA	1.14.18.1. 463.
Family and domain databases
InterPro	IPR008922. Di-copper_centre. IPR002227. Tyrosinase. [Graphical view]
Gene3D	G3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
Pfam	PF00264. Tyrosinase. 1 hit. [Graphical view]
PRINTS	PR00092. TYROSINASE.
PROSITE	PS00497. TYROSINASE_1. 1 hit. PS00498. TYROSINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

TYRO_CANFA

Accession

Primary (citable) accession number: P54834
Secondary accession number(s): Q7YRB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	April 12, 2005
Last modified:	January 20, 2009
This is version 59 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)