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P54834 (TYRO_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Tyrosinase
EC=1.14.18.1
Alternative name(s):
Monophenol monooxygenase
Gene names
Name:TYR
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis ›

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.

L-tyrosine + O2 = 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 processMelanin biosynthesis
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmelanin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

melanosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionmetal 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 530512Tyrosinase
PRO_0000035877

Regions

Topological domain19 – 473455Lumenal, melanosome Potential
Transmembrane474 – 49421Helical; Potential
Topological domain495 – 53036Cytoplasmic Potential

Sites

Metal binding1801Copper A By similarity
Metal binding2021Copper A By similarity
Metal binding2111Copper A By similarity
Metal binding3631Copper B By similarity
Metal binding3671Copper B By similarity
Metal binding3901Copper B By similarity

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation3371N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict31L → V in AAA86420. Ref.2
Sequence conflict71C → R in AAA86420. Ref.2
Sequence conflict591I → V in AAA86420. Ref.2
Sequence conflict1151K → R in AAA86420. Ref.2
Sequence conflict1321N → D in AAA86420. Ref.2
Sequence conflict2121R → T in AAA86420. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P54834 [UniParc].

Last modified April 12, 2005. Version 2.
Checksum: B1C45F6362ACF0E3

FASTA53060,336
        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

« Hide

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

EMBL
GenBank
DDBJ		AY336053 mRNA. Translation: AAQ17535.1.
U42219 Genomic DNA. Translation: AAA86420.1.
RefSeqNP_001002941.1. NM_001002941.1.
UniGeneCfa.104.

3D structure databases

ProteinModelPortalP54834.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403405.
KEGGcfa:403405.

Organism-specific databases

CTD7299.

Phylogenomic databases

eggNOGNOG08919.
HOGENOMHOG000118376.
HOVERGENHBG003553.
InParanoidP54834.
KOK00505.
OrthoDBEOG4D26PK.

Family and domain databases

Gene3D1.10.1280.10. 1 hit.
InterProIPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamPF00264. Tyrosinase. 1 hit.
[Graphical view]
PRINTSPR00092. TYROSINASE.
SUPFAMSSF48056. Di-copper_centre. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816926.

Entry information

Entry nameTYRO_CANFA
AccessionPrimary (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: April 3, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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