Search by BoMiProt ID - Bomi3532


Primary Information

BoMiProt ID Bomi3532
Protein Name 5,6-dihydroxyindole-2-carboxylic acid oxidase/Tyrosinase-related protein 1/TRP-1
Organism Bos taurus
Uniprot IdQ8WN57
Milk FractionWhey
Ref Sequence Id NP_776905.2
Aminoacid Length 537
Molecular Weight 60617
Fasta Sequence https://www.uniprot.org/uniprot/Q8WN57.fasta
Gene Name TYRP1
Gene Id 282105
Protein Existence Status reviewed

Secondary Information

Protein Function At low concentration, DHICA acts as a cofactor for their tyrosine hydroxylase activities, whereas at higher concentrations, it inhibits tyrosine hydroxylation.
Biochemical Properties Tyrosinase and tyrosinase-related protein 1 (TRP-1) share a significant level of homology in several regions including the catalytic domain and the potential N-glycosylation sites.
PTMs N-linked Glycosylation at Asn
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
>sp|Q8WN57|TYRP1_BOVIN 5,6-dihydroxyindole-2-carboxylic acid oxidase OS=Bos taurus OX=9913 GN=TYRP1 PE=2 SV=2 MKSPTLLSLGYMFLVLLFFQQAWAQFPRECATIEALRNGVCCPDLSPLSGPGSDRCGLSS GRGRCEVVIADSRPHSHHYPHDGRDDREGWPTRSFN*96RTCHCNGN*104FSGHNCGTCRPGWGGA ACDQRVLTVRRNLLDLSTEEKNRFVRALDMAKRTTHPQFVIATRRSEEILGPDGNTPQFE N*181ISIYNYFVWTHYYSVKKTFLGAGQESFGEVDFSHEGPAFLTWHRYHLLQLERDMQEMLQ DPSFSLPYWNFATGKNTCDICTDDLMGSRSNFDSTLISPNSVFSQWRVVCESLEDYDTLG TLCN*304STEGGPIKRNPAGNVARPMVQRLPKPQDVAQCLEVGSYDTPPFYSN*350STNSFRNTVE GYSHPTGRYDPAVRSLHNLAHLFLN*385GTGGQTHLSPNDPIFVLLHTFTDAVFDEWLRRYNA DISTYPLENAPIGHNRQYNMVPFWPPVTNIEMFVTAPDNLGYTYEVQWPSRSFSISEIVT IAVVAALSLVAVIFAGASCLIRARSNMDEANQPLLTDQYQHYIEEYEKIHNPNQSVV
Predicted Disorder Regions 78-83, 360-369, 526-537
DisProt Annotation
TM Helix Prediction 2TMHs; (7-25), (479-501)
Significance of PTMs It has been clearly established that N-glycosylation is essential for the correct folding of tyrosinase related protein 1.
Additional Comments In mouse melanocytes, DHICA is formed by the dopachrome tautomerase-catalysed tautomerization of dopachrome, and its incorporation into melanin is accounted for by oxidation to the corresponding and unstable quinone by tyrp1.
Bibliography 1.Olivares C, Jiménez-Cervantes C, Lozano JA, Solano F, García-Borrón JC. The 5,6-dihydroxyindole-2-carboxylic acid (DHICA) oxidase activity of human tyrosinase. Biochem J. 2001 Feb 15;354(Pt 1):131-9. doi: 10.1042/0264-6021:3540131. PMID: 11171088; PMCID: PMC1221637. 2. Wilczek, A. and Mishima, Y. (1995) Inhibitory effects of melanin monomers, dihydroxyindole-2-carboxylic acid (DHICA) and dihydroxyindole (DHI) on mammalian tyrosinase, with a special reference to the role of DHICA/DHI ratio in melanogenesis. Pigment Cell Res. 8, 105–112. 3.Branza-Nichita, Norica; Petrescu, Andrei J.; Negroiu, Gabriela; Dwek,Raymond A.; Petrescu, Stefana M. (2000). N Glycosylation Processing and Glycoprotein Folding−Lessons from the Tyrosinase-Related Proteins. Chemical Reviews, 100(12), 4697–4712. doi:10.1021/cr990291y.