TYRO_BOVIN
ID TYRO_BOVIN Reviewed; 530 AA.
AC Q8MIU0; Q8WN56;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Tyrosinase;
DE EC=1.14.18.1;
DE AltName: Full=Monophenol monooxygenase;
DE Flags: Precursor;
GN Name=TYR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN ALBINISM.
RC STRAIN=White Galloway;
RX PubMed=14727143; DOI=10.1007/s00335-002-2249-5;
RA Schmutz S.M., Berryere T.G., Ciobanu D.C., Mileham A.J., Schmidtz B.H.,
RA Fredholm M.;
RT "A form of albinism in cattle is caused by a tyrosinase frameshift
RT mutation.";
RL Mamm. Genome 15:62-67(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skin;
RA Guibert S., Julien R., Oulmouden A.;
RT "Transcriptional regulation of bovine TYR gene.";
RL Submitted (NOV-2001) 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 -!- DISEASE: Note=Defects in TYR are the cause of a form of albinism in
CC Braunvieh calf. {ECO:0000269|PubMed:14727143}.
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; AY046527; AAL02331.2; -; mRNA.
DR EMBL; AF445639; AAL38168.1; -; mRNA.
DR RefSeq; NP_851344.1; NM_181001.3.
DR STRING; 9913.ENSBTAP00000015679; -.
DR PaxDb; Q8MIU0; -.
DR GeneID; 280951; -.
DR KEGG; bta:280951; -.
DR CTD; 7299; -.
DR eggNOG; ENOG502QRET; Eukaryota.
DR InParanoid; Q8MIU0; -.
DR OrthoDB; 881347at2759; -.
DR SABIO-RK; Q8MIU0; -.
DR Proteomes; UP000009136; 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:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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 Albinism; Copper; Glycoprotein; Melanin biosynthesis; Membrane;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..530
FT /note="Tyrosinase"
FT /id="PRO_0000035876"
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 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
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 172
FT /note="V -> A (in Ref. 2; AAL38168)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 530 AA; 60304 MW; 1C0CEF3D8CB1356C CRC64;
MLLAALYCLL WSFRTSAGHF PRACASSKSL TEKECCPPWA GDGSPCGRLS GRGSCQDVIL
STAPLGPQFP FTGVDDRESW PSIFYNRTCQ CFSNFMGFNC GSCKFGFRGP RCTERRLLVR
RNIFDLSVPE KNKFLAYLTL AKHTTSPDYV IPTGTYGQMN HGTTPLFNDV SVYDLFVWMH
YYVSRDTLLG DSEVWRDIDF AHEAPGFLPW HRLFLLLWEQ EIQKLTGDEN FTIPYWDWRD
AENCDVCTDE YMGGRNPANP NLLSPASFFS SWQIVCSRLE EYNSRQALCN GTSEGPLLRN
PGNHDKARTP RLPSSADVEF CLSLTQYESG SMDKAANFSF RNTLEGFADP VTGIADASQS
SMHNALHIYM NGTMSQVPGS ANDPIFLLHH AFVDSIFEQW LRKYHPLQDV YPEANAPIGH
NRESYMVPFI PLYRNGDFFI SSKDXGYDYS YLQDSEPDIF QDYIKPYLEQ AQRIWPWLIG
AAVVGSVLTA VLGGLTSLLC RRKRNQLPEE KQPLLMEKED YHNLMYQSHL
