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Database: UniProt
Entry: Q08410
LinkDB: Q08410
Original site: Q08410 
ID   TYRO_COTJA              Reviewed;         273 AA.
AC   Q08410; Q54AH4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   05-DEC-2018, entry version 83.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1;
DE   AltName: Full=Monophenol monooxygenase;
DE   Flags: Precursor; Fragment;
GN   Name=TYR;
OS   Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Perdicinae; Coturnix.
OX   NCBI_TaxID=93934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1292011; DOI=10.1111/j.1600-0749.1992.tb00551.x;
RA   Yamamoto H., Kudo T., Masuko N., Miura H., Sato S., Tanaka M.,
RA   Tanaka S., Takeuchi S., Shibahara S., Takeuchi T.;
RT   "Phylogeny of regulatory regions of vertebrate tyrosinase genes.";
RL   Pigment Cell Res. 5:284-294(1992).
CC   -!- FUNCTION: This is a copper-containing oxidase that functions in
CC       the formation of pigments such as melanins and other polyphenolic
CC       compounds. Catalyzes the initial and rate limiting step in the
CC       cascade of reactions leading to melanin production from tyrosine.
CC       In addition to hydroxylating tyrosine to DOPA (3,4-
CC       dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to
CC       DOPA-quinone, and possibly the oxidation of DHI (5,6-
CC       dihydroxyindole) to indole-5,6 quinone.
CC       {ECO:0000250|UniProtKB:P11344}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone;
CC         Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1;
CC         Evidence={ECO:0000250|UniProtKB:P11344};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosine + O2 = H2O + L-dopaquinone;
CC         Xref=Rhea:RHEA:18117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57924, ChEBI:CHEBI:58315; EC=1.14.18.1;
CC         Evidence={ECO:0000250|UniProtKB:P11344};
CC   -!- COFACTOR:
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC         Evidence={ECO:0000250|UniProtKB:Q9ZP19};
CC       Note=Binds 2 copper ions per subunit.
CC       {ECO:0000250|UniProtKB:Q9ZP19};
CC   -!- SUBCELLULAR LOCATION: Melanosome membrane
CC       {ECO:0000250|UniProtKB:P14679}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P14679}. Melanosome
CC       {ECO:0000250|UniProtKB:P11344}. Note=Proper trafficking to
CC       melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38.
CC       {ECO:0000250|UniProtKB:P11344}.
CC   -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
DR   EMBL; AB024279; BAB21535.1; -; Genomic_DNA.
DR   EMBL; S56788; AAB25510.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q08410; -.
DR   SMR; Q08410; -.
DR   HOVERGEN; HBG003553; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR   GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004503; F:monophenol monooxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1280.10; -; 1.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   InterPro; IPR008922; Unchr_di-copper_centre.
DR   Pfam; PF00264; Tyrosinase; 1.
DR   PRINTS; PR00092; TYROSINASE.
DR   SUPFAM; SSF48056; SSF48056; 1.
DR   PROSITE; PS00497; TYROSINASE_1; 1.
PE   3: Inferred from homology;
KW   Copper; Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding;
KW   Monooxygenase; Oxidoreductase; Signal; Transmembrane.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19   >273       Tyrosinase.
FT                                /FTId=PRO_0000035882.
FT   METAL       180    180       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       202    202       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       211    211       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   CARBOHYD     86     86       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    111    111       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    161    161       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    230    230       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   NON_TER     273    273
SQ   SEQUENCE   273 AA;  31500 MW;  0EA3DE55BE11EA1A CRC64;
     MLLFTMGLLL AILQPSTGQF PRVCANTQSL LRKECCPPWE GDGSPCGERS NRGTCQRILL
     SQAPLGPQFP FSGVDDREDW PSVFYNRTCR CRGNFMGFNC GECKFGFSGQ NCTERRLRTR
     RNIFQLTIRE KDKFLAYLNL AKNIPSKDYV IATGTYAQMN NGSNPMFRNI NVYDLFVWMH
     YYASRDTLLG GSNVWRDIDF AHEAPGFLPW HRAFLLLWER EIQKITGDEN FTIPYWDWRD
     AEDCVICTDE YMGGQHPTNP NLLSPASFFS SWQ
//
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