TYRO_NEUCR
ID TYRO_NEUCR Reviewed; 685 AA.
AC P00440; Q6MGJ7; Q7RVL7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 5.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Tyrosinase;
DE EC=1.14.18.1;
DE AltName: Full=Monophenol monooxygenase;
DE Flags: Precursor;
GN Name=T; ORFNames=90C4.150, NCU00776;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oak Ridge, and TS;
RX PubMed=2529259; DOI=10.1016/s0021-9258(18)71485-3;
RA Kupper U., Niedermann D.M., Travaglini G., Lerch K.;
RT "Isolation and characterization of the tyrosinase gene from Neurospora
RT crassa.";
RL J. Biol. Chem. 264:17250-17258(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
RN [4]
RP PROTEIN SEQUENCE OF 2-408, AND ACETYLATION AT SER-2.
RC STRAIN=TL;
RX PubMed=6210696; DOI=10.1016/s0021-9258(20)65157-2;
RA Lerch K.;
RT "Primary structure of tyrosinase from Neurospora crassa. II. Complete amino
RT acid sequence and chemical structure of a tripeptide containing an unusual
RT thioether.";
RL J. Biol. Chem. 257:6414-6419(1982).
RN [5]
RP PROTEIN SEQUENCE OF 2-408.
RC STRAIN=Sing, and TS;
RX PubMed=6210697; DOI=10.1016/s0021-9258(20)65158-4;
RA Ruegg C., Ammer D., Lerch K.;
RT "Comparison of amino acid sequence and thermostability of tyrosinase from
RT three wild type strains of Neurospora crassa.";
RL J. Biol. Chem. 257:6420-6426(1982).
CC -!- FUNCTION: This is a copper-containing oxidase that functions in the
CC formation of pigments such as melanins and other polyphenolic
CC compounds.
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 -!- 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 -!- 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 -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA33618.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA33619.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=EAA35696.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M32843; AAA33619.1; ALT_FRAME; Genomic_DNA.
DR EMBL; M33271; AAA33618.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BX842680; CAE81941.1; -; Genomic_DNA.
DR EMBL; CM002236; EAA35696.3; ALT_SEQ; Genomic_DNA.
DR PIR; A34460; YRNC.
DR RefSeq; XP_964932.3; XM_959839.3.
DR AlphaFoldDB; P00440; -.
DR SMR; P00440; -.
DR STRING; 5141.EFNCRP00000000584; -.
DR iPTMnet; P00440; -.
DR EnsemblFungi; EAA35696; EAA35696; NCU00776.
DR GeneID; 3881081; -.
DR KEGG; ncr:NCU00776; -.
DR HOGENOM; CLU_013691_3_1_1; -.
DR InParanoid; P00440; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
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 Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR016216; Monophenol_mOase_fun.
DR InterPro; IPR041640; Tyosinase_C.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF18132; Tyosinase_C; 1.
DR Pfam; PF00264; Tyrosinase; 1.
DR PIRSF; PIRSF000340; MPO_fungal; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS00497; TYROSINASE_1; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Copper; Direct protein sequencing; Melanin biosynthesis;
KW Metal-binding; Monooxygenase; Oxidoreductase; Reference proteome;
KW Thioether bond.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:6210696,
FT ECO:0000269|PubMed:6210697"
FT CHAIN 2..408
FT /note="Tyrosinase"
FT /id="PRO_0000035895"
FT PROPEP 409..685
FT /note="Could be involved in enzyme activation"
FT /id="PRO_0000035896"
FT BINDING 67
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 97
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 106
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 278
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 282
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 307
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:6210696"
FT CROSSLNK 95..97
FT /note="2'-(S-cysteinyl)-histidine (Cys-His)"
FT VARIANT 15
FT /note="P -> T (in strain: Sing, TL and TS)"
FT VARIANT 30
FT /note="D -> E (in strain: Sing)"
FT VARIANT 130
FT /note="V -> T (in strain: Sing)"
FT VARIANT 202
FT /note="D -> N (in strain: TL)"
FT VARIANT 346..347
FT /note="KS -> QN (in strain: Sing)"
FT VARIANT 371
FT /note="I -> T (in strain: Sing)"
FT VARIANT 424
FT /note="K -> N (in strain: TS)"
FT VARIANT 450
FT /note="K -> R (in strain: TS)"
FT VARIANT 678
FT /note="G -> R (in strain: TS)"
FT CONFLICT 235
FT /note="N -> D (in Ref. 4; AA sequence and 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ 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
