TYRO_ORYLA
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 03-AUG-2022, entry version 107.
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}.
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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.ENSORLP00000013681; -.
DR GeneID; 100049427; -.
DR KEGG; ola:100049427; -.
DR CTD; 7299; -.
DR eggNOG; ENOG502QRET; Eukaryota.
DR InParanoid; P55025; -.
DR OrthoDB; 881347at2759; -.
DR Proteomes; UP000001038; Unplaced.
DR Proteomes; UP000265180; Chromosome 9.
DR Proteomes; UP000265200; Chromosome 9.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
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 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
