ID TYRO_ORYLA Reviewed; 540 AA. AC P55025; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 24-JAN-2024, entry version 110. DE RecName: Full=Tyrosinase; DE EC=1.14.18.1; DE AltName: Full=Monophenol monooxygenase; DE Flags: Precursor; GN Name=tyr; Synonyms=tyro; OS Oryzias latipes (Japanese rice fish) (Japanese killifish). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata; OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae; OC Oryzias. OX NCBI_TaxID=8090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Eye; RX PubMed=7821799; DOI=10.1016/0378-1119(94)90445-6; RA Inagaki H., Bessho Y., Koga A., Hori H.; RT "Expression of the tyrosinase-encoding gene in a colorless melanophore RT mutant of the medaka fish, Oryzias latipes."; RL Gene 150:319-324(1994). RN [2] RP NUCLEOTIDE SEQUENCE. RA Inagaki H., Koga A., Bessho Y., Hori H.; RT "The tyrosinase gene from medaka: transgenic expression rescued albino RT mutation."; RL Submitted (JAN-1998) 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 CC compounds. 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 -!- 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 -!- 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 -!- SUBCELLULAR LOCATION: Melanosome membrane; Single-pass type I membrane CC protein. CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}. 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; D29687; BAA06156.1; -; mRNA. DR EMBL; D29686; BAA06155.1; -; mRNA. DR EMBL; AB010101; BAA31348.1; -; Genomic_DNA. DR RefSeq; NP_001098272.1; NM_001104802.1. DR AlphaFoldDB; P55025; -. DR SMR; P55025; -. DR STRING; 8090.ENSORLP00000041517; -. DR GlyCosmos; P55025; 5 sites, No reported glycans. DR GeneID; 100049427; -. DR KEGG; ola:100049427; -. DR CTD; 7299; -. DR eggNOG; ENOG502QRET; Eukaryota. DR InParanoid; P55025; -. DR OrthoDB; 70287at2759; -. DR Proteomes; UP000001038; Unplaced. DR Proteomes; UP000265180; Chromosome 9. DR Proteomes; UP000265200; Chromosome 9. 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 CDD; cd00055; EGF_Lam; 1. 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; IPR002049; LE_dom. 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..19 FT /evidence="ECO:0000255" FT CHAIN 20..540 FT /note="Tyrosinase" FT /id="PRO_0000035883" FT TOPO_DOM 20..480 FT /note="Lumenal, melanosome" FT /evidence="ECO:0000255" FT TRANSMEM 481..501 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 502..540 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 511..540 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 521..540 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 182 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 205 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 214 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="A" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 366 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 370 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT BINDING 393 FT /ligand="Cu cation" FT /ligand_id="ChEBI:CHEBI:23378" FT /ligand_label="B" FT /evidence="ECO:0000250|UniProtKB:Q9ZP19" FT CARBOHYD 87 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 233 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 293 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 340 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 374 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 540 AA; 61254 MW; 7ADEA02C3870CAE4 CRC64; MKSLFLSAVL LQFFETCWSQ FPRPCANSEG LRTKECCPVW SGDGSPCGAL SGRGFCADVS VSDEPNGPQY PHSGIDDRER WPLAFFNRTC RCAGNYGGFN CGECRFGYWG SNCAEYRESV RRNIMSMSTT EQQKFISYLN LAKNTINPDY VITTGTRAEM GENGESPMFS DINTYDLFVW IHYYVSRDTF LGGPGNVWRD IDFAHESAAF LPWHRVYLLH WEQEIRKITG DFNFTIPYWD WRDAQSCEVC TDNLMGGRNA LNPNLISPAS VFSSWKVICT QQEEYNNQEA LCNATAEGPL LRNPGNHDPN RVPRIPTTAD VEFTISLPEY ETGSMDRFAN NSFRNVLEGF ASPETGMAVQ GQSTMHNALH VFMNGSMSSV QGSANDPIFL LHHAFIDSIF ERWLRTHQPP RSIYPRTNAP IGHNDGYYMV PFLPLYRNGD YLLSNKALGY EYAYLLDPGQ RFVQEFLTPY LQQAQQIWQW LLGAGILGAL IATIVAAVIV FARRKRRRNQ KRKRAPSFGE RQPLLQSSSE EGSSSYQTTL //