TYRO_CANLF
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 03-AUG-2022, entry version 121.
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 -!- 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";
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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; 9612.ENSCAFP00000006504; -.
DR PaxDb; P54834; -.
DR GeneID; 403405; -.
DR KEGG; cfa:403405; -.
DR CTD; 7299; -.
DR eggNOG; ENOG502QRET; Eukaryota.
DR InParanoid; P54834; -.
DR OrthoDB; 881347at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; IEA:UniProtKB-EC.
DR GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009637; P:response to blue light; ISS:UniProtKB.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
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..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
