ID A0A0D9S0Q1_CHLSB Unreviewed; 401 AA.
AC A0A0D9S0Q1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Tyrosinase {ECO:0000256|ARBA:ARBA00039304};
DE EC=1.14.18.1 {ECO:0000256|ARBA:ARBA00011906};
DE AltName: Full=Monophenol monooxygenase {ECO:0000256|ARBA:ARBA00042251};
GN Name=TYR {ECO:0000313|Ensembl:ENSCSAP00000014440.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000014440.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000014440.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000014440.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 5,6-dihydroxyindole-2-carboxylate + O2 = 2 H2O + 2
CC indole-5,6-quinone-2-carboxylate; Xref=Rhea:RHEA:68388,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16875,
CC ChEBI:CHEBI:177869; Evidence={ECO:0000256|ARBA:ARBA00036464};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68389;
CC Evidence={ECO:0000256|ARBA:ARBA00036464};
CC -!- COFACTOR:
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000256|ARBA:ARBA00001973};
CC -!- SUBUNIT: Forms an OPN3-dependent complex with DCT in response to blue
CC light in melanocytes. {ECO:0000256|ARBA:ARBA00038813}.
CC -!- SUBCELLULAR LOCATION: Melanosome membrane
CC {ECO:0000256|ARBA:ARBA00004573}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004573}.
CC -!- SIMILARITY: Belongs to the tyrosinase family.
CC {ECO:0000256|ARBA:ARBA00009928}.
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DR EMBL; AQIB01098638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01098639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01098640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01098641; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01098642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A0D9S0Q1; -.
DR STRING; 60711.ENSCSAP00000014440; -.
DR Ensembl; ENSCSAT00000001641.1; ENSCSAP00000014440.1; ENSCSAG00000003613.1.
DR eggNOG; ENOG502QRET; Eukaryota.
DR GeneTree; ENSGT00940000155336; -.
DR OMA; CSQLEEY; -.
DR Proteomes; UP000029965; Chromosome 1.
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:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0004503; F:tyrosinase activity; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0043473; P:pigmentation; IEA:Ensembl.
DR GO; GO:0009637; P:response to blue light; IEA:Ensembl.
DR GO; GO:0048538; P:thymus development; IEA:Ensembl.
DR Gene3D; 1.10.1280.10; Di-copper center containing domain from catechol oxidase; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR PANTHER; PTHR11474:SF124; TYROSINASE; 1.
DR PANTHER; PTHR11474; TYROSINASE FAMILY MEMBER; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; Di-copper centre-containing domain; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Melanin biosynthesis {ECO:0000256|ARBA:ARBA00023101};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..401
FT /note="Tyrosinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002346206"
FT DOMAIN 202..219
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00497"
FT DOMAIN 383..394
FT /note="Tyrosinase copper-binding"
FT /evidence="ECO:0000259|PROSITE:PS00498"
FT REGION 290..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 401 AA; 45277 MW; 930A416613DB0702 CRC64;
MILAVLYCLL WSFQTSAGHF PRACVSSKNL MEKECCPPWS GDGSPCGQLS GRGSCQNILL
SNAPLGPQFP FTGVDDRESW PSIFYNRTCQ CSGNFTGFDC GNCKFGFWGP NCTDRRLLVR
RNIFDLSAPE KDKFFAYLTL AKHTISSDYV IPIGTYGQMK NGSTPMFSDI NIYDLFVWIH
YYVSMDALLG GSEIWRDIDF AHEAPAFLPW HRLFLLRWEQ EIQKLTGDEN FTIPYWDWRD
AEKCDICTDE YMGGQHPANP NLLSPASFFS SWQIICSRLE EYNSHQSLCN GMPEGPLRRN
PGNHDKSRTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFASP LTGIADASQS
SMHNALHIYM NGTMSQVQGS ANDPIFLLHH AFVDRVCAHW I
//
