ID TYRO_CANLF Reviewed; 530 AA. AC P54834; Q7YRB8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 12-APR-2005, sequence version 2. DT 27-MAR-2024, entry version 129. DE RecName: Full=Tyrosinase; DE EC=1.14.18.1; DE AltName: Full=Monophenol monooxygenase; DE Flags: Precursor; GN Name=TYR; OS Canis lupus familiaris (Dog) (Canis familiaris). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Doberman pinscher; TISSUE=Skin; RA Schmutz S.M., Berryere T.G.; RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-273. RA Tang Q., Williams R.W., Hogan D., Valentine V., Goldowitz D.; RT "Cloning and chromosomal in situ hybridization of the dog tyrosinase exon RT 1."; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: This is a copper-containing oxidase that functions in the CC formation of pigments such as melanins and other polyphenolic compounds CC (By similarity). Catalyzes the initial and rate limiting step in the CC cascade of reactions leading to melanin production from tyrosine (By CC similarity). In addition to hydroxylating tyrosine to DOPA (3,4- CC dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA- CC quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to CC indole-5,6 quinone (By similarity). {ECO:0000250|UniProtKB:P11344}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, CC 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; Xref=Rhea:RHEA:18117, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924, CC ChEBI:CHEBI:58315; EC=1.14.18.1; CC Evidence={ECO:0000250|UniProtKB:P11344}; 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:0000250|UniProtKB:P14679}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68389; CC Evidence={ECO:0000250|UniProtKB:P14679}; CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000250|UniProtKB:Q9ZP19}; CC Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19}; CC -!- SUBUNIT: Forms an OPN3-dependent complex with DCT in response to blue CC light in melanocytes. {ECO:0000250|UniProtKB:P14679}. CC -!- SUBCELLULAR LOCATION: Melanosome membrane CC {ECO:0000250|UniProtKB:P14679}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:P14679}. Melanosome CC {ECO:0000250|UniProtKB:P11344}. Note=Proper trafficking to melanosome CC is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. CC {ECO:0000250|UniProtKB:P11344}. CC -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:P11344}. CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Snowy stardom - Issue 49 of CC August 2004; CC URL="https://web.expasy.org/spotlight/back_issues/049"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY336053; AAQ17535.1; -; mRNA. DR EMBL; U42219; AAA86420.1; -; Genomic_DNA. DR RefSeq; NP_001002941.1; NM_001002941.1. DR AlphaFoldDB; P54834; -. DR SMR; P54834; -. DR STRING; 9615.ENSCAFP00000006504; -. DR GlyCosmos; P54834; 6 sites, No reported glycans. DR PaxDb; 9612-ENSCAFP00000006504; -. DR GeneID; 403405; -. DR KEGG; cfa:403405; -. DR CTD; 7299; -. DR eggNOG; ENOG502QRET; Eukaryota. DR InParanoid; P54834; -. DR OrthoDB; 70287at2759; -. DR Proteomes; UP000002254; Unplaced. DR Proteomes; UP000694429; Unplaced. DR Proteomes; UP000694542; Unplaced. DR Proteomes; UP000805418; Unplaced. 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:tyrosinase activity; IBA:GO_Central. DR GO; GO:0042438; P:melanin biosynthetic process; IBA:GO_Central. DR GO; GO:0043473; P:pigmentation; IBA:GO_Central. DR GO; GO:0009637; P:response to blue light; ISS:UniProtKB. 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 2: Evidence at transcript level; KW Copper; Glycoprotein; Melanin biosynthesis; Membrane; Metal-binding; KW Monooxygenase; Oxidoreductase; Reference proteome; Signal; Transmembrane; KW Transmembrane helix. FT SIGNAL 1..18 FT /evidence="ECO:0000255" FT CHAIN 19..530 FT /note="Tyrosinase" FT /id="PRO_0000035877" FT TOPO_DOM 19..473 FT /note="Lumenal, melanosome" FT /evidence="ECO:0000255" FT TRANSMEM 474..494 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 495..530 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT BINDING 180 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 202 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 211 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 363 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 367 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 390 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT CARBOHYD 86 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 161 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 230 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 337 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 371 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CONFLICT 3 FT /note="L -> V (in Ref. 2; AAA86420)" FT /evidence="ECO:0000305" FT CONFLICT 7 FT /note="C -> R (in Ref. 2; AAA86420)" FT /evidence="ECO:0000305" FT CONFLICT 59 FT /note="I -> V (in Ref. 2; AAA86420)" FT /evidence="ECO:0000305" FT CONFLICT 115 FT /note="K -> R (in Ref. 2; AAA86420)" FT /evidence="ECO:0000305" FT CONFLICT 132 FT /note="N -> D (in Ref. 2; AAA86420)" FT /evidence="ECO:0000305" FT CONFLICT 212 FT /note="R -> T (in Ref. 2; AAA86420)" FT /evidence="ECO:0000305" SQ SEQUENCE 530 AA; 60336 MW; B1C45F6362ACF0E3 CRC64; MLLAALCCLL WSFRTSTGHF PRACASSKSL MEKECCPPWS GDGSPCGQLS GRGACQDIIL SNAPFGPQFP FTGVDDRESW PSVFYNRTCQ CFGNFMGFNC GNCKFGFWGQ NCTEKRLLVR KNIFDLSVPE KNKFLAYLTL AKHTTSPDYV IPTGTYGQMN NGSTPMFNDI NIYDLFVWMH YYVSRDTLLG GSEIWKDIDF AHEAPGFLPW HRLFLLLWEQ EIQKLTGDEN FTIPYWDWRD AKSCDICTDE YMGGRNPANP NLLSPASFFS SWQIVCTRLE EYNSRQALCD GTPEGPLLRN PGNHDKARTP RLPSSADVEF CLSLTQYESD SMDKAANFSF RNTLEGFASP LTGIADASQS SMHNALHIYM NGTMSQVPGS ANDPIFLLHH AFVDSIFEQW LRRHHPLREV YPEANAPIGH NRESYMVPFI PLYRNGDLFI SSRDLGYDYS NLQESERDIF QDYIKPYLEQ ASRIWPWLIG AAVVGCVVTA VLGGLTSLLC RRNRKQLHEE KQPLLMEKED YHSLLYQTHL //