9.B.423.1.1 Tyrosinase, Tyr or TYR, of 529 aas and 2 TMSs, one signal sequence at the N-terminus, and one very hydrophobic TMS at the C-terminus. It is a copper-containing oxidase that functions in the formation of
pigments such as melanins and other polyphenolic compounds (Olivares and Solano 2009). This enzyme, for which the 3-d structure is known, catalyzes
the initial and rate limiting step in the cascade of reactions leading
to melanin production from tyrosine (Lai et al. 2018). In addition to hydroxylating tyrosine to DOPA
(3,4-dihydroxyphenylalanine), TYR also catalyzes the oxidation of DOPA to
DOPA-quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to
indole-5,6 quinone ((Hutchinson et al. 2019). It forms a trimeric complex with TYRP1 (TC# 9.B.423.1.2) and TYRP2 (TC# 9.B.423.1.3) (Lavinda et al. 2021).
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Accession Number: | P14679 |
Protein Name: | Tyrosinase |
Length: | 529 |
Molecular Weight: | 60393.00 |
Species: | Homo sapiens (Human) [9606] |
Number of TMSs: | 1 |
Location1 / Topology2 / Orientation3: |
Melanosome membrane1 / Single-pass type I membrane protein2 |
Substrate |
tyrosine |
---|
1: MLLAVLYCLL WSFQTSAGHF PRACVSSKNL MEKECCPPWS GDRSPCGQLS GRGSCQNILL
61: SNAPLGPQFP FTGVDDRESW PSVFYNRTCQ CSGNFMGFNC GNCKFGFWGP NCTERRLLVR
121: RNIFDLSAPE KDKFFAYLTL AKHTISSDYV IPIGTYGQMK NGSTPMFNDI NIYDLFVWMH
181: YYVSMDALLG GSEIWRDIDF AHEAPAFLPW HRLFLLRWEQ EIQKLTGDEN FTIPYWDWRD
241: AEKCDICTDE YMGGQHPTNP NLLSPASFFS SWQIVCSRLE EYNSHQSLCN GTPEGPLRRN
301: PGNHDKSRTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFASP LTGIADASQS
361: SMHNALHIYM NGTMSQVQGS ANDPIFLLHH AFVDSIFEQW LRRHRPLQEV YPEANAPIGH
421: NRESYMVPFI PLYRNGDFFI SSKDLGYDYS YLQDSDPDSF QDYIKSYLEQ ASRIWSWLLG
481: AAMVGAVLTA LLAGLVSLLC RHKRKQLPEE KQPLLMEKED YHSLYQSHL