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A7BHQ9 (TYRO_PHONA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 25. 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

Names and origin

Protein namesRecommended name:
Tyrosinase

EC=1.14.18.1
Gene names
Name:tyr1
OrganismPholiota nameko
Taxonomic identifier61267 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaAgaricomycetesAgaricomycetidaeAgaricalesStrophariaceaePholiota

Protein attributes

Sequence length625 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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 By similarity. UniProtKB Q92396

Catalytic activity

2 L-dopa + O2 = 2 dopaquinone + 2 H2O. Ref.1

L-tyrosine + O2 = dopaquinone + H2O. Ref.1

Cofactor

Binds 2 copper ions per subunit. Ref.1

Subunit structure

Monomer. Ref.1

Post-translational modification

The N-terminus is blocked. Ref.1

Sequence similarities

Belongs to the tyrosinase family.

Biophysicochemical properties

Kinetic parameters:

KM=1930 µM for L-dopa Ref.1

KM=119 µM for t-butylphenol Ref.1

KM=30.6 µM for p-cresol Ref.1

KM=163 µM for t-butylcatechol Ref.1

KM=1240 µM for 3-(3,4-dihydroxyphenyl) propionic acid Ref.1

KM=122 µM for dopamine Ref.1

Mass spectrometry

Molecular mass is 42424.39 Da from positions 1 - 387. Determined by MALDI. Ref.1

Ontologies

Keywords
   Biological processMelanin biosynthesis
   LigandCopper
Metal-binding
   Molecular functionMonooxygenase
Oxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processmelanin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation-reduction process

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functioncopper ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

monophenol monooxygenase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 387387Tyrosinase Ref.1
PRO_0000352767
Propeptide388 – 625238 Ref.1
PRO_0000352768

Regions

Compositional bias367 – 45185Ala-rich

Sites

Metal binding581Copper A By similarity UniProtKB Q9ZP19
Metal binding861Copper A By similarity UniProtKB Q9ZP19
Metal binding951Copper A By similarity UniProtKB Q9ZP19
Metal binding2581Copper B By similarity UniProtKB Q9ZP19
Metal binding2621Copper B By similarity UniProtKB Q9ZP19
Metal binding2871Copper B By similarity UniProtKB Q9ZP19

Experimental info

Sequence conflict131I → V in BAF74396. Ref.1
Sequence conflict1511V → A in BAF74396. Ref.1
Sequence conflict2721G → A in BAF74396. Ref.1
Sequence conflict4251P → S in BAF74396. Ref.1
Sequence conflict5281S → N in BAF74396. Ref.1

Sequences

Sequence LengthMass (Da)Tools
A7BHQ9 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 26E8AEFA285F871B

FASTA62567,499
        10         20         30         40         50         60 
MSRVVITGVS GTIANRLEIN DFVKNDKFFS LYIQALQVMS SVPPQENVRS FFQIGGIHGL 

        70         80         90        100        110        120 
PYTPWDGITG DQPFDPNTQW GGYCTHGSVL FPTWHRPYVL LYEQILHKHV QDIAATYTTS 

       130        140        150        160        170        180 
DKAAWVQAAA NLRQPYWDWA ANAVPPDQVI VSKKVTITGS NGHKVEVDNP LYHYKFHPID 

       190        200        210        220        230        240 
SSFPRPYSEW PTTLRQPNSS RPNATDNVAK LRNVLRASQE NITSNTYSML TRVHTWKAFS 

       250        260        270        280        290        300 
NHTVGDGGST SNSLEAIHDG IHVDVGGGGH MGDPAVAAFD PIFFLHHCNV DRLLSLWAAI 

       310        320        330        340        350        360 
NPGVWVSPGD SEDGTFILPP EAPVDVSTPL TPFSNTETTF WASGGITDTT KLGYTYPEFN 

       370        380        390        400        410        420 
GLDLGNAQAV KAAIGNIVNR LYGASVFSGF AAATSAIGAG SVASLAADVP LEKAPAPAPE 

       430        440        450        460        470        480 
AAAQPPVPAP AHVEPAVRAV SVHAAAAQPH AEPPVHVSAG GHPSPHGFYD WTARIEFKKY 

       490        500        510        520        530        540 
EFGSSFSVLL FLGPVPEDPE QWLVSPNFVG AHHAFVNSAA GHCANCRSQG NVVVEGFVHL 

       550        560        570        580        590        600 
TKYISEHAGL RSLNPEVVEP YLTNELHWRV LKADGSVGQL ESLEVSVYGT PMNLPVGAMF 

       610        620 
PVPGNRRHFH GITHGRVGGS RHAIV 

« Hide

References

[1]"Purification, characterization, and molecular cloning of tyrosinase from Pholiota nameko."
Kawamura-Konishi Y., Tsuji M., Hatana S., Asanuma M., Kakuta D., Kawano T., Mukouyama E.B., Goto H., Suzuki H.
Biosci. Biotechnol. Biochem. 71:1752-1760(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 154-164; 175-195; 351-362 AND 384-387, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS SPECTROMETRY.
Tissue: Fruiting body.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB275646 mRNA. Translation: BAF74395.1.
AB275647 mRNA. Translation: BAF74396.1.

3D structure databases

ProteinModelPortalA7BHQ9.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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. SSF48056. 1 hit.
PROSITEPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTYRO_PHONA
AccessionPrimary (citable) accession number: A7BHQ9
Secondary accession number(s): A7BHR0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families