P54834 · TYRO_CANLF

Function

function

This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds (By similarity).
Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine (By similarity).
In addition to hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to indole-5,6 quinone (By similarity).

Catalytic activity

Cofactor

Cu2+ (UniProtKB | Rhea| CHEBI:29036 )

Note: Binds 2 copper ions per subunit.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site180Cu cation A (UniProtKB | ChEBI)
Binding site202Cu cation A (UniProtKB | ChEBI)
Binding site211Cu cation A (UniProtKB | ChEBI)
Binding site363Cu cation B (UniProtKB | ChEBI)
Binding site367Cu cation B (UniProtKB | ChEBI)
Binding site390Cu cation B (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmelanosome
Cellular Componentmelanosome membrane
Molecular Functionmetal ion binding
Molecular Functiontyrosinase activity
Biological Processmelanin biosynthetic process
Biological Processpigmentation
Biological Processresponse to blue light

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tyrosinase
  • EC number
  • Alternative names
    • Monophenol monooxygenase

Gene names

    • Name
      TYR

Organism names

Accessions

  • Primary accession
    P54834
  • Secondary accessions
    • Q7YRB8

Proteomes

Subcellular Location

Melanosome membrane
; Single-pass type I membrane protein
Melanosome
Note: Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain19-473Lumenal, melanosome
Transmembrane474-494Helical
Topological domain495-530Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for signal, chain, glycosylation.

TypeIDPosition(s)Description
Signal1-18
ChainPRO_000003587719-530Tyrosinase
Glycosylation86N-linked (GlcNAc...) asparagine
Glycosylation111N-linked (GlcNAc...) asparagine
Glycosylation161N-linked (GlcNAc...) asparagine
Glycosylation230N-linked (GlcNAc...) asparagine
Glycosylation337N-linked (GlcNAc...) asparagine
Glycosylation371N-linked (GlcNAc...) asparagine

Post-translational modification

Glycosylated.

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Forms an OPN3-dependent complex with DCT in response to blue light in melanocytes.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the tyrosinase family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    530
  • Mass (Da)
    60,336
  • Last updated
    2005-04-12 v2
  • Checksum
    B1C45F6362ACF0E3
MLLAALCCLLWSFRTSTGHFPRACASSKSLMEKECCPPWSGDGSPCGQLSGRGACQDIILSNAPFGPQFPFTGVDDRESWPSVFYNRTCQCFGNFMGFNCGNCKFGFWGQNCTEKRLLVRKNIFDLSVPEKNKFLAYLTLAKHTTSPDYVIPTGTYGQMNNGSTPMFNDINIYDLFVWMHYYVSRDTLLGGSEIWKDIDFAHEAPGFLPWHRLFLLLWEQEIQKLTGDENFTIPYWDWRDAKSCDICTDEYMGGRNPANPNLLSPASFFSSWQIVCTRLEEYNSRQALCDGTPEGPLLRNPGNHDKARTPRLPSSADVEFCLSLTQYESDSMDKAANFSFRNTLEGFASPLTGIADASQSSMHNALHIYMNGTMSQVPGSANDPIFLLHHAFVDSIFEQWLRRHHPLREVYPEANAPIGHNRESYMVPFIPLYRNGDLFISSRDLGYDYSNLQESERDIFQDYIKPYLEQASRIWPWLIGAAVVGCVVTAVLGGLTSLLCRRNRKQLHEEKQPLLMEKEDYHSLLYQTHL

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict3in Ref. 2; AAA86420
Sequence conflict7in Ref. 2; AAA86420
Sequence conflict59in Ref. 2; AAA86420
Sequence conflict115in Ref. 2; AAA86420
Sequence conflict132in Ref. 2; AAA86420
Sequence conflict212in Ref. 2; AAA86420

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY336053
EMBL· GenBank· DDBJ
AAQ17535.1
EMBL· GenBank· DDBJ
mRNA
U42219
EMBL· GenBank· DDBJ
AAA86420.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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