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Database: UniProt
Entry: Q8MIU0
LinkDB: Q8MIU0
Original site: Q8MIU0 
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   16-JAN-2019, entry version 91.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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.,
RA   Schmidtz B.H., 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
CC       the formation of pigments such as melanins and other polyphenolic
CC       compounds. Catalyzes the initial and rate limiting step in the
CC       cascade of reactions leading to melanin production from tyrosine.
CC       In addition to hydroxylating tyrosine to DOPA (3,4-
CC       dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to
CC       DOPA-quinone, and possibly the oxidation of DHI (5,6-
CC       dihydroxyindole) to indole-5,6 quinone.
CC       {ECO:0000250|UniProtKB:P11344}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone;
CC         Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57504, 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;
CC         Xref=Rhea:RHEA:18117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:57924, 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.
CC       {ECO:0000250|UniProtKB:Q9ZP19};
CC   -!- SUBCELLULAR LOCATION: Melanosome membrane
CC       {ECO:0000250|UniProtKB:P14679}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P14679}. Melanosome
CC       {ECO:0000250|UniProtKB:P11344}. Note=Proper trafficking to
CC       melanosome 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
CC       in 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
CC       49 of August 2004;
CC       URL="https://web.expasy.org/spotlight/back_issues/049";
DR   EMBL; AY046527; AAL02331.2; -; mRNA.
DR   EMBL; AF445639; AAL38168.1; -; mRNA.
DR   RefSeq; NP_851344.1; NM_181001.3.
DR   UniGene; Bt.9028; -.
DR   STRING; 9913.ENSBTAP00000015679; -.
DR   PaxDb; Q8MIU0; -.
DR   PRIDE; Q8MIU0; -.
DR   GeneID; 280951; -.
DR   KEGG; bta:280951; -.
DR   CTD; 7299; -.
DR   eggNOG; ENOG410IEZU; Eukaryota.
DR   eggNOG; ENOG410Y42I; LUCA.
DR   HOGENOM; HOG000118376; -.
DR   HOVERGEN; HBG003553; -.
DR   InParanoid; Q8MIU0; -.
DR   KO; K00505; -.
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:0004503; F:monophenol monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0042438; P:melanin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0043473; P:pigmentation; IBA:GO_Central.
DR   GO; GO:0009411; P:response to UV; IBA:GO_Central.
DR   GO; GO:0033280; P:response to vitamin D; IBA:GO_Central.
DR   Gene3D; 1.10.1280.10; -; 1.
DR   InterPro; IPR002227; Tyrosinase_Cu-bd.
DR   InterPro; IPR008922; Unchr_di-copper_centre.
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; Complete proteome; Copper; Glycoprotein;
KW   Melanin biosynthesis; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     17       {ECO:0000255}.
FT   CHAIN        18    530       Tyrosinase.
FT                                /FTId=PRO_0000035876.
FT   TOPO_DOM     19    473       Lumenal, melanosome. {ECO:0000255}.
FT   TRANSMEM    474    494       Helical. {ECO:0000255}.
FT   TOPO_DOM    495    530       Cytoplasmic. {ECO:0000255}.
FT   METAL       180    180       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       202    202       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       211    211       Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       363    363       Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       367    367       Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   METAL       390    390       Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
FT   CARBOHYD     86     86       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    230    230       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    290    290       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    337    337       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    371    371       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CONFLICT    172    172       V -> A (in Ref. 2; AAL38168).
FT                                {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
//
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