P55028 · TYRP1_CARAU
- Protein5,6-dihydroxyindole-2-carboxylic acid oxidase
- Genetyrp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids522 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
Plays a role in melanin biosynthesis. Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid. May regulate or influence the type of melanin synthesized. Also to a lower extent, capable of hydroxylating tyrosine and producing melanin.
Catalytic activity
- 2 5,6-dihydroxyindole-2-carboxylate + O2 = 2 H2O + 2 indole-5,6-quinone-2-carboxylateThis reaction proceeds in the forward direction.
Cofactor
Zn2+ (UniProtKB | Rhea| CHEBI:29105 )
Note: Contains bound zinc ions after heterologous expression in insect cells.
Pathway
Pigment biosynthesis; melanin biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 182 | Zn2+ A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 205 | Zn2+ A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 214 | Zn2+ A (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 367 | Zn2+ B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 371 | Zn2+ B (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 394 | Zn2+ B (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | melanosome | |
Cellular Component | melanosome membrane | |
Molecular Function | metal ion binding | |
Molecular Function | monooxygenase activity | |
Biological Process | melanin biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name5,6-dihydroxyindole-2-carboxylic acid oxidase
- EC number
- Short namesDHICA oxidase
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Cyprinidae > Cyprininae > Carassius
Accessions
- Primary accessionP55028
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Melanosome membrane ; Single-pass type I membrane protein
Note: Located to mature stage III and IV melanosomes and apposed endosomal tubular membranes. Transported to pigmented melanosomes by the BLOC-1 complex. 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 | 22-470 | Lumenal, melanosome | ||||
Sequence: QFPRACVTPEGLRSAQCCPSPSALESDPCGALAGPGRCVDVRMRAHGPQYPYEGATTRALARASSRACRCNGNFGGFDCGGCAHGFTGDACEQRVPVVRRNVMQLSADEKRFFVNALDQAKRAPHPDTVIATRRYSEILGPDNSTTQFENISIYNLFVWTHYYSVSKTFLGAGQDSFGGVDFSHEGPGFLTWHRYHLLQLERDMQVMLGDPSFALPYWDFAIGGSECDICTDELMGARSSSDSSSISSNSIFSRWRVICESVEEYDTLGTICNSSESSPIRRNPAGNTARPMVQRLPEPQDVEACLELTAFDSPPFYSTSSDSFRNSIEGYSAPQGNYDPVVRSLHNLAHLFLNGTGGQTHLSPNDPIFVLLHTFTDAVFDEWLRRHASDASIYPLENTPIGHNREFNMVPFWPPVTNAEMFVTAAENLGYSYEAEWPARPLTPTQIVT | ||||||
Transmembrane | 471-491 | Helical | ||||
Sequence: VAVVAALLLVAIIFAASTCVV | ||||||
Topological domain | 492-522 | Cytoplasmic | ||||
Sequence: HLRGNRTEGRQPLLGDQYQRYEDHNKTQSVV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MLRTSCGGMLLLVHALGLVRA | ||||||
Chain | PRO_0000035887 | 22-522 | 5,6-dihydroxyindole-2-carboxylic acid oxidase | |||
Sequence: QFPRACVTPEGLRSAQCCPSPSALESDPCGALAGPGRCVDVRMRAHGPQYPYEGATTRALARASSRACRCNGNFGGFDCGGCAHGFTGDACEQRVPVVRRNVMQLSADEKRFFVNALDQAKRAPHPDTVIATRRYSEILGPDNSTTQFENISIYNLFVWTHYYSVSKTFLGAGQDSFGGVDFSHEGPGFLTWHRYHLLQLERDMQVMLGDPSFALPYWDFAIGGSECDICTDELMGARSSSDSSSISSNSIFSRWRVICESVEEYDTLGTICNSSESSPIRRNPAGNTARPMVQRLPEPQDVEACLELTAFDSPPFYSTSSDSFRNSIEGYSAPQGNYDPVVRSLHNLAHLFLNGTGGQTHLSPNDPIFVLLHTFTDAVFDEWLRRHASDASIYPLENTPIGHNREFNMVPFWPPVTNAEMFVTAAENLGYSYEAEWPARPLTPTQIVTVAVVAALLLVAIIFAASTCVVHLRGNRTEGRQPLLGDQYQRYEDHNKTQSVV | ||||||
Disulfide bond | 27↔38 | |||||
Sequence: CVTPEGLRSAQC | ||||||
Disulfide bond | 39↔59 | |||||
Sequence: CPSPSALESDPCGALAGPGRC | ||||||
Disulfide bond | 50↔89 | |||||
Sequence: CGALAGPGRCVDVRMRAHGPQYPYEGATTRALARASSRAC | ||||||
Disulfide bond | 91↔100 | |||||
Sequence: CNGNFGGFDC | ||||||
Disulfide bond | 103↔112 | |||||
Sequence: CAHGFTGDAC | ||||||
Glycosylation | 164 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 171 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 248↔251 | |||||
Sequence: CDIC | ||||||
Disulfide bond | 280↔293 | |||||
Sequence: CESVEEYDTLGTIC | ||||||
Glycosylation | 294 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 375 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
PTM databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length522
- Mass (Da)57,519
- Last updated1996-10-01 v1
- ChecksumD12410BF828C1D31
Keywords
- Technical term