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Database: UniProt
Entry: P54834
LinkDB: P54834
Original site: P54834 
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   10-APR-2019, entry version 109.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   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
RT   exon 1.";
RL   Submitted (FEB-1996) 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   -!- 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; AY336053; AAQ17535.1; -; mRNA.
DR   EMBL; U42219; AAA86420.1; -; Genomic_DNA.
DR   RefSeq; NP_001002941.1; NM_001002941.1.
DR   UniGene; Cfa.104; -.
DR   ProteinModelPortal; P54834; -.
DR   SMR; P54834; -.
DR   STRING; 9612.ENSCAFP00000006504; -.
DR   PaxDb; P54834; -.
DR   GeneID; 403405; -.
DR   KEGG; cfa:403405; -.
DR   CTD; 7299; -.
DR   eggNOG; ENOG410IEZU; Eukaryota.
DR   eggNOG; ENOG410Y42I; LUCA.
DR   HOGENOM; HOG000118376; -.
DR   HOVERGEN; HBG003553; -.
DR   InParanoid; P54834; -.
DR   KO; K00505; -.
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:monophenol monooxygenase 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   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   Complete proteome; Copper; Glycoprotein; Melanin biosynthesis;
KW   Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     18       {ECO:0000255}.
FT   CHAIN        19    530       Tyrosinase.
FT                                /FTId=PRO_0000035877.
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    111    111       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    161    161       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    230    230       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      3      3       L -> V (in Ref. 2; AAA86420).
FT                                {ECO:0000305}.
FT   CONFLICT      7      7       C -> R (in Ref. 2; AAA86420).
FT                                {ECO:0000305}.
FT   CONFLICT     59     59       I -> V (in Ref. 2; AAA86420).
FT                                {ECO:0000305}.
FT   CONFLICT    115    115       K -> R (in Ref. 2; AAA86420).
FT                                {ECO:0000305}.
FT   CONFLICT    132    132       N -> D (in Ref. 2; AAA86420).
FT                                {ECO:0000305}.
FT   CONFLICT    212    212       R -> T (in Ref. 2; AAA86420).
FT                                {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
//
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