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Tyrosinase (EC 1.14.18.1) (Monophenol monooxygenase)

 TYRO_NEUCR              Reviewed;         685 AA.
P00440; Q6MGJ7; Q7RVL7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
04-DEC-2007, sequence version 5.
23-MAY-2018, entry version 118.
RecName: Full=Tyrosinase;
EC=1.14.18.1;
AltName: Full=Monophenol monooxygenase;
Flags: Precursor;
Name=T; ORFNames=90C4.150, NCU00776;
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
1257 / FGSC 987).
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
Neurospora.
NCBI_TaxID=367110;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Oak Ridge, and TS;
PubMed=2529259;
Kupper U., Niedermann D.M., Travaglini G., Lerch K.;
"Isolation and characterization of the tyrosinase gene from Neurospora
crassa.";
J. Biol. Chem. 264:17250-17258(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12655011; DOI=10.1093/nar/gkg293;
Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V.,
Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J.,
Schulte U.;
"What's in the genome of a filamentous fungus? Analysis of the
Neurospora genome sequence.";
Nucleic Acids Res. 31:1944-1954(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
PubMed=12712197; DOI=10.1038/nature01554;
Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S.,
Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
"The genome sequence of the filamentous fungus Neurospora crassa.";
Nature 422:859-868(2003).
[4]
PROTEIN SEQUENCE OF 2-408, AND ACETYLATION AT SER-2.
STRAIN=TL;
PubMed=6210696;
Lerch K.;
"Primary structure of tyrosinase from Neurospora crassa. II. Complete
amino acid sequence and chemical structure of a tripeptide containing
an unusual thioether.";
J. Biol. Chem. 257:6414-6419(1982).
[5]
PROTEIN SEQUENCE OF 2-408.
STRAIN=Sing, and TS;
PubMed=6210697;
Ruegg C., Ammer D., Lerch K.;
"Comparison of amino acid sequence and thermostability of tyrosinase
from three wild type strains of Neurospora crassa.";
J. Biol. Chem. 257:6420-6426(1982).
-!- FUNCTION: This is a copper-containing oxidase that functions in
the formation of pigments such as melanins and other polyphenolic
compounds.
-!- CATALYTIC ACTIVITY: 2 L-dopa + O(2) = 2 dopaquinone + 2 H(2)O.
-!- CATALYTIC ACTIVITY: L-tyrosine + O(2) = dopaquinone + H(2)O.
-!- COFACTOR:
Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
Evidence={ECO:0000250|UniProtKB:Q9ZP19};
Note=Binds 2 copper ions per subunit.
{ECO:0000250|UniProtKB:Q9ZP19};
-!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA33618.1; Type=Frameshift; Positions=596; Evidence={ECO:0000305};
Sequence=AAA33619.1; Type=Frameshift; Positions=596; Evidence={ECO:0000305};
Sequence=EAA35696.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M32843; AAA33619.1; ALT_FRAME; Genomic_DNA.
EMBL; M33271; AAA33618.1; ALT_FRAME; Genomic_DNA.
EMBL; BX842680; CAE81941.1; -; Genomic_DNA.
EMBL; CM002236; EAA35696.3; ALT_SEQ; Genomic_DNA.
PIR; A34460; YRNC.
RefSeq; XP_964932.3; XM_959839.3.
ProteinModelPortal; P00440; -.
SMR; P00440; -.
iPTMnet; P00440; -.
PRIDE; P00440; -.
EnsemblFungi; EAA35696; EAA35696; NCU00776.
GeneID; 3881081; -.
KEGG; ncr:NCU00776; -.
EuPathDB; FungiDB:NCU00776; -.
InParanoid; P00440; -.
KO; K00505; -.
OrthoDB; EOG092C1Z2C; -.
Proteomes; UP000001805; Chromosome 1, Linkage Group I.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004503; F:monophenol monooxygenase activity; IEA:UniProtKB-EC.
GO; GO:0042438; P:melanin biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 1.10.1280.10; -; 1.
InterPro; IPR016216; Monophenol_mOase_fun.
InterPro; IPR002227; Tyrosinase_Cu-bd.
InterPro; IPR008922; Unchr_di-copper_centre.
Pfam; PF00264; Tyrosinase; 1.
PIRSF; PIRSF000340; MPO_fungal; 1.
PRINTS; PR00092; TYROSINASE.
SUPFAM; SSF48056; SSF48056; 1.
PROSITE; PS00497; TYROSINASE_1; 1.
PROSITE; PS00498; TYROSINASE_2; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Copper; Direct protein sequencing;
Melanin biosynthesis; Metal-binding; Monooxygenase; Oxidoreductase;
Reference proteome; Thioether bond.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6210696,
ECO:0000269|PubMed:6210697}.
CHAIN 2 408 Tyrosinase.
/FTId=PRO_0000035895.
PROPEP 409 685 Could be involved in enzyme activation.
/FTId=PRO_0000035896.
METAL 67 67 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 97 97 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 106 106 Copper A. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 278 278 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 282 282 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
METAL 307 307 Copper B. {ECO:0000250|UniProtKB:Q9ZP19}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:6210696}.
CROSSLNK 95 97 2'-(S-cysteinyl)-histidine (Cys-His).
VARIANT 15 15 P -> T (in strain: Sing, TL and TS).
VARIANT 30 30 D -> E (in strain: Sing).
VARIANT 130 130 V -> T (in strain: Sing).
VARIANT 202 202 D -> N (in strain: TL).
VARIANT 346 347 KS -> QN (in strain: Sing).
VARIANT 371 371 I -> T (in strain: Sing).
VARIANT 424 424 K -> N (in strain: TS).
VARIANT 450 450 K -> R (in strain: TS).
VARIANT 678 678 G -> R (in strain: TS).
CONFLICT 235 235 N -> D (in Ref. 4; AA sequence and 5; AA
sequence). {ECO:0000305}.
SEQUENCE 685 AA; 75886 MW; DF64B764BFF5468A CRC64;
MSTDIKFAIT GVPTPPSSNG AVPLRRELRD LQQNYPEQFN LYLLGLRDFQ GLDEAKLDSY
YQVAGIHGMP FKPWAGVPSD TDWSQPGSSG FGGYCTHSSI LFITWHRPYL ALYEQALYAS
VQAVAQKFPV EGGLRAKYVA AAKDFRAPYF DWASQPPKGT LAFPESLSSR TIQVVDVDGK
TKSINNPLHR FTFHPVNPSP GDFSAAWSRY PSTVRYPNRL TGASRDERIA PILANELASL
RNNVSLLLLS YKDFDAFSYN RWDPNTNPGD FGSLEDVHNE IHDRTGGNGH MSSLEVSAFD
PLFWLHHVNV DRLWSIWQDL NPNSFMTPRP APYSTFVAQE GESQSKSTPL EPFWDKSAAN
FWTSEQVKDS ITFGYAYPET QKWKYSSVKE YQAAIRKSVT ALYGSNVFAN FVENVADRTP
ALKKPQATGE ESKSTVSAAA AHAVELSGAK KVAEKVHNVF QHAEEKAQKP VVPVKDTKAE
SSTAAGMMIG LSIKRPSKLT ASPGPIPESL KYLAPDGKYT DWIVNVRAQK HGLGQSFRVI
VFLGEFNPDP ETWDDEFNCV GRVSVLGRSA ETQCGKCRKD NANGLIVSGT VPLTSALLQD
IVGGELQSLK PEDVIPHLRA NLKWKVALFN GDEYNLEEVP DLKVSVASTE VTIDEEGLPH
YSRQYTVYPE ITEGKPCGHG PEDHI


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