Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q04604 (TYRO_PELNI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 27, 2011. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosinase
EC=1.14.18.1
Alternative name(s):
Monophenol monooxygenase
Gene names
Name:TYR
Synonyms:TYRS
OrganismPelophylax nigromaculatus (Black-spotted frog) (Rana nigromaculata)
Taxonomic identifier8409 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Neobatrachia › Ranoidea › Ranidae › Raninae › Rana › Pelophylax

Protein attributes

Sequence length532 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.

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 processMelanin biosynthesis
   Cellular componentMembrane
   DomainSignal
Transmembrane
Transmembrane helix
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   PTMGlycoprotein
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 – 1919 Potential
Chain20 – 532513Tyrosinase
PRO_0000035884

Regions

Topological domain20 – 475456Lumenal, melanosome Potential
Transmembrane476 – 49924Helical; Potential
Topological domain500 – 53233Cytoplasmic Potential

Sites

Metal binding1841Copper A By similarity
Metal binding2061Copper A By similarity
Metal binding2151Copper A By similarity
Metal binding3671Copper B By similarity
Metal binding3711Copper B By similarity
Metal binding3941Copper B By similarity

Amino acid modifications

Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation3411N-linked (GlcNAc...) Potential
Glycosylation3751N-linked (GlcNAc...) Potential

Natural variations

Natural variant101T → A.

Sequences

Sequence LengthMass (Da)Tools
Q04604 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: B27D3080F0C74B3A

FASTA53260,116
        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

« Hide

References

[1]"Cloning and sequencing of the cDNA encoding tyrosinase of the Japanese pond frog, Rana nigromaculata."
Takase M., Miura I., Nakata A., Takeuchi T., Nishioka M.
Gene 121:359-363(1992) [PubMed: 1446833] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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."
Miura I., Okumoto H., Makino K., Nakata A., Nishioka M.
Jpn. J. Genet. 70:79-92(1995) [PubMed: 7772385] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-277.
Tissue: Blood.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D12514 mRNA. Translation: BAA02077.1.
D37779 Genomic DNA. Translation: BAA07034.1.
PIRJC1392.

3D structure databases

ProteinModelPortalQ04604.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG003553.

Family and domain databases

InterProIPR002227. Tyrosinase.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
Gene3DG3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
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...

Entry information

Entry nameTYRO_PELNI
AccessionPrimary (citable) accession number: Q04604
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 27, 2011
This is version 65 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents