P54834 · TYRO_CANLF
- ProteinTyrosinase
- GeneTYR
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids530 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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).
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
- 2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone
- 2 5,6-dihydroxyindole-2-carboxylate + O2 = 2 H2O + 2 indole-5,6-quinone-2-carboxylateThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 copper ions per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 180 | Cu cation A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 202 | Cu cation A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 211 | Cu cation A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 363 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 367 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 390 | Cu cation B (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | melanosome | |
Cellular Component | melanosome membrane | |
Molecular Function | metal ion binding | |
Molecular Function | tyrosinase activity | |
Biological Process | melanin biosynthetic process | |
Biological Process | pigmentation | |
Biological Process | response to blue light |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTyrosinase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Carnivora > Caniformia > Canidae > Canis
Accessions
- Primary accessionP54834
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Melanosome membrane ; Single-pass type I membrane protein
Note: Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 19-473 | Lumenal, melanosome | ||||
Sequence: HFPRACASSKSLMEKECCPPWSGDGSPCGQLSGRGACQDIILSNAPFGPQFPFTGVDDRESWPSVFYNRTCQCFGNFMGFNCGNCKFGFWGQNCTEKRLLVRKNIFDLSVPEKNKFLAYLTLAKHTTSPDYVIPTGTYGQMNNGSTPMFNDINIYDLFVWMHYYVSRDTLLGGSEIWKDIDFAHEAPGFLPWHRLFLLLWEQEIQKLTGDENFTIPYWDWRDAKSCDICTDEYMGGRNPANPNLLSPASFFSSWQIVCTRLEEYNSRQALCDGTPEGPLLRNPGNHDKARTPRLPSSADVEFCLSLTQYESDSMDKAANFSFRNTLEGFASPLTGIADASQSSMHNALHIYMNGTMSQVPGSANDPIFLLHHAFVDSIFEQWLRRHHPLREVYPEANAPIGHNRESYMVPFIPLYRNGDLFISSRDLGYDYSNLQESERDIFQDYIKPYLEQASR | ||||||
Transmembrane | 474-494 | Helical | ||||
Sequence: IWPWLIGAAVVGCVVTAVLGG | ||||||
Topological domain | 495-530 | Cytoplasmic | ||||
Sequence: LTSLLCRRNRKQLHEEKQPLLMEKEDYHSLLYQTHL |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MLLAALCCLLWSFRTSTG | ||||||
Chain | PRO_0000035877 | 19-530 | Tyrosinase | |||
Sequence: HFPRACASSKSLMEKECCPPWSGDGSPCGQLSGRGACQDIILSNAPFGPQFPFTGVDDRESWPSVFYNRTCQCFGNFMGFNCGNCKFGFWGQNCTEKRLLVRKNIFDLSVPEKNKFLAYLTLAKHTTSPDYVIPTGTYGQMNNGSTPMFNDINIYDLFVWMHYYVSRDTLLGGSEIWKDIDFAHEAPGFLPWHRLFLLLWEQEIQKLTGDENFTIPYWDWRDAKSCDICTDEYMGGRNPANPNLLSPASFFSSWQIVCTRLEEYNSRQALCDGTPEGPLLRNPGNHDKARTPRLPSSADVEFCLSLTQYESDSMDKAANFSFRNTLEGFASPLTGIADASQSSMHNALHIYMNGTMSQVPGSANDPIFLLHHAFVDSIFEQWLRRHHPLREVYPEANAPIGHNRESYMVPFIPLYRNGDLFISSRDLGYDYSNLQESERDIFQDYIKPYLEQASRIWPWLIGAAVVGCVVTAVLGGLTSLLCRRNRKQLHEEKQPLLMEKEDYHSLLYQTHL | ||||||
Glycosylation | 86 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 111 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 161 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 230 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 337 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 371 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Glycosylated.
Keywords
- PTM
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
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length530
- Mass (Da)60,336
- Last updated2005-04-12 v2
- ChecksumB1C45F6362ACF0E3
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 3 | in Ref. 2; AAA86420 | ||||
Sequence: L → V | ||||||
Sequence conflict | 7 | in Ref. 2; AAA86420 | ||||
Sequence: C → R | ||||||
Sequence conflict | 59 | in Ref. 2; AAA86420 | ||||
Sequence: I → V | ||||||
Sequence conflict | 115 | in Ref. 2; AAA86420 | ||||
Sequence: K → R | ||||||
Sequence conflict | 132 | in Ref. 2; AAA86420 | ||||
Sequence: N → D | ||||||
Sequence conflict | 212 | in Ref. 2; AAA86420 | ||||
Sequence: R → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY336053 EMBL· GenBank· DDBJ | AAQ17535.1 EMBL· GenBank· DDBJ | mRNA | ||
U42219 EMBL· GenBank· DDBJ | AAA86420.1 EMBL· GenBank· DDBJ | Genomic DNA |