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Database: UniProt
Entry: P55024
LinkDB: P55024
Original site: P55024 
ID   TYRO_CHICK              Reviewed;         529 AA.
AC   P55024;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   10-APR-2019, entry version 127.
DE   RecName: Full=Tyrosinase;
DE            EC=1.14.18.1;
DE   AltName: Full=Monophenol monooxygenase;
DE   Flags: Precursor;
GN   Name=TYR;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
OC   Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=White leghorn;
RX   PubMed=1494538; DOI=10.1111/j.1600-0749.1992.tb00454.x;
RA   Mochii M., Iio A., Yamamoto H., Takeuchi T., Eguchi G.;
RT   "Isolation and characterization of a chicken tyrosinase cDNA.";
RL   Pigment Cell Res. 5:162-167(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-273.
RX   PubMed=8647445; DOI=10.1016/0378-1119(95)00784-9;
RA   Ferguson C.A., Kidson S.H.;
RT   "Characteristic sequences in the promoter region of the chicken
RT   tyrosinase-encoding gene.";
RL   Gene 169:191-195(1996).
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; D88349; BAA13590.1; -; mRNA.
DR   EMBL; L46805; AAB08441.1; -; Genomic_DNA.
DR   PIR; PC4153; PC4153.
DR   RefSeq; NP_989491.1; NM_204160.1.
DR   UniGene; Gga.928; -.
DR   ProteinModelPortal; P55024; -.
DR   SMR; P55024; -.
DR   STRING; 9031.ENSGALP00000027812; -.
DR   PaxDb; P55024; -.
DR   PRIDE; P55024; -.
DR   GeneID; 373971; -.
DR   KEGG; gga:373971; -.
DR   CTD; 7299; -.
DR   eggNOG; ENOG410IEZU; Eukaryota.
DR   eggNOG; ENOG410Y42I; LUCA.
DR   HOGENOM; HOG000118376; -.
DR   HOVERGEN; HBG003553; -.
DR   InParanoid; P55024; -.
DR   KO; K00505; -.
DR   OrthoDB; 881347at2759; -.
DR   PhylomeDB; P55024; -.
DR   TreeFam; TF315865; -.
DR   Reactome; R-GGA-5662702; Melanin biosynthesis.
DR   PRO; PR:P55024; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:Ensembl.
DR   GO; GO:0042470; C:melanosome; ISS:UniProtKB.
DR   GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0005507; F:copper ion binding; IEA:Ensembl.
DR   GO; GO:0004503; F:monophenol monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR   GO; GO:0042438; P:melanin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0043473; P:pigmentation; IBA:GO_Central.
DR   GO; GO:0009411; P:response to UV; IBA:GO_Central.
DR   GO; GO:0033280; P:response to vitamin D; IBA:GO_Central.
DR   GO; GO:0048538; P:thymus development; IEA:Ensembl.
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.
DR   PROSITE; PS00498; TYROSINASE_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Copper; Glycoprotein; Melanin biosynthesis;
KW   Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    529       Tyrosinase.
FT                                /FTId=PRO_0000035881.
FT   TOPO_DOM     19    476       Lumenal, melanosome. {ECO:0000255}.
FT   TRANSMEM    477    497       Helical. {ECO:0000255}.
FT   TOPO_DOM    498    529       Cytoplasmic. {ECO:0000255}.
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   METAL       363    363       Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       367    367       Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       390    390       Copper B. {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   CARBOHYD    290    290       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    337    337       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    356    356       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    371    371       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
SQ   SEQUENCE   529 AA;  60357 MW;  74B464A52C3EFBF5 CRC64;
     MFLFAMGLLL VILQPSTGQF PRVCANTQSL LRKECCPPWD GDGTPCGERS NRGTCQRILL
     SQAPLGPQFP FSGVDDREDW PSVFYNRTCR CRGNFMGFNC GECKFGFSGQ NCTERRLRTR
     RNIFQLTISE KDKFLAYLNL AKNIPSKDYV IATGTYAQMN NGSNPMFRNI NVYDLFVWMH
     YYASRDTLLG GSNVWRDIDF AHEAPGFLPW HRAFLLLWER EIQKITGDEN FTIPYWDWRD
     AEDCVICTDE YMGGQHPTNP NLLSPASFFS SWQVICTQSE EYNSQQALCN ATSEGPILRN
     PGNNDKSRTP RLPSSSEVEF CLTLTQYESG SMDKMANYSF RNTLEGFADP HTAISNISQS
     GLHNALHIYM NGSMSQVQGS ANDPIFILHH AFVDSIFERW LRRHRPMLEV YPAANAPIGH
     NRENYMVPFI PLYRNGEFFI SSRELGYDYE YLQEPALGSF QDFLIPYLKQ AHQIWPWLVG
     AAVIGGIITA VLSGLILACR KKRKGTSPEI QPLLTESEDY NNVSYQSHF
//
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