Reviewed, UniProtKB/Swiss-Prot P00440 (TYRO_NEUCR)

Names and origin

Protein names

Recommended name:
    Tyrosinase
    EC=1.14.18.1
Alternative name(s):
    Monophenol monooxygenase

Gene names

Name:	T
ORF Names:	90C4.150, NCU00776

Organism

Neurospora crassa [Complete proteome]

Taxonomic identifier

5141 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Sordariomycetidae › Sordariales › Sordariaceae › Neurospora

Protein attributes

Sequence length	685 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.
Catalytic activity	L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O.
Cofactor	Binds 2 copper ions per subunit By similarity.
Sequence similarities	Belongs to the tyrosinase family.
Sequence caution	The sequence AAA33618.1 differs from that shown. Reason: Frameshift at position 596. The sequence AAA33619.1 differs from that shown. Reason: Frameshift at position 596. The sequence EAA35696.2 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Melanin biosynthesis
Ligand	Copper Metal-binding
Molecular function	Monooxygenase Oxidoreductase
PTM	Acetylation Thioether bond
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	melanin biosynthetic process from tyrosine Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	copper ion binding Inferred from electronic annotation. Source: UniProtKB-KW monophenol monooxygenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4 Ref.5
	Chain	2 – 408	407	Tyrosinase		PRO_0000035895
	Propeptide	409 – 685	277	Could be involved in enzyme activation		PRO_0000035896
Sites
	Metal binding	67	1	Copper A By similarity
	Metal binding	97	1	Copper A By similarity
	Metal binding	106	1	Copper A By similarity
	Metal binding	278	1	Copper B By similarity
	Metal binding	282	1	Copper B By similarity
	Metal binding	307	1	Copper B By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylserine
	Cross-link	95 ↔ 97		2'-(S-cysteinyl)-histidine (Cys-His)
Natural variations
	Natural variant	15	1	P → T in strain: Sing, TL and TS.
	Natural variant	30	1	D → E in strain: Sing.
	Natural variant	130	1	V → T in strain: Sing.
	Natural variant	202	1	D → N in strain: TL.
	Natural variant	346 – 347	2	KS → QN in strain: Sing.
	Natural variant	371	1	I → T in strain: Sing.
	Natural variant	424	1	K → N in strain: TS.
	Natural variant	450	1	K → R in strain: TS.
	Natural variant	678	1	G → R in strain: TS.
Experimental info
	Sequence conflict	235	1	N → D Ref.4
	Sequence conflict	235	1	N → D Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P00440-1 [UniParc]. Last modified December 4, 2007. Version 5. Checksum: DF64B764BFF5468A	FASTA	685	75,886
	10 20 30 40 50 60 MSTDIKFAIT GVPTPPSSNG AVPLRRELRD LQQNYPEQFN LYLLGLRDFQ GLDEAKLDSY 70 80 90 100 110 120 YQVAGIHGMP FKPWAGVPSD TDWSQPGSSG FGGYCTHSSI LFITWHRPYL ALYEQALYAS 130 140 150 160 170 180 VQAVAQKFPV EGGLRAKYVA AAKDFRAPYF DWASQPPKGT LAFPESLSSR TIQVVDVDGK 190 200 210 220 230 240 TKSINNPLHR FTFHPVNPSP GDFSAAWSRY PSTVRYPNRL TGASRDERIA PILANELASL 250 260 270 280 290 300 RNNVSLLLLS YKDFDAFSYN RWDPNTNPGD FGSLEDVHNE IHDRTGGNGH MSSLEVSAFD 310 320 330 340 350 360 PLFWLHHVNV DRLWSIWQDL NPNSFMTPRP APYSTFVAQE GESQSKSTPL EPFWDKSAAN 370 380 390 400 410 420 FWTSEQVKDS ITFGYAYPET QKWKYSSVKE YQAAIRKSVT ALYGSNVFAN FVENVADRTP 430 440 450 460 470 480 ALKKPQATGE ESKSTVSAAA AHAVELSGAK KVAEKVHNVF QHAEEKAQKP VVPVKDTKAE 490 500 510 520 530 540 SSTAAGMMIG LSIKRPSKLT ASPGPIPESL KYLAPDGKYT DWIVNVRAQK HGLGQSFRVI 550 560 570 580 590 600 VFLGEFNPDP ETWDDEFNCV GRVSVLGRSA ETQCGKCRKD NANGLIVSGT VPLTSALLQD 610 620 630 640 650 660 IVGGELQSLK PEDVIPHLRA NLKWKVALFN GDEYNLEEVP DLKVSVASTE VTIDEEGLPH 670 680 YSRQYTVYPE ITEGKPCGHG PEDHI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Isolation and characterization of the tyrosinase gene from Neurospora crassa." Kupper U., Niedermann D.M., Travaglini G., Lerch K. J. Biol. Chem. 264:17250-17258(1989) [PubMed: 2529259] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Oak Ridge and TS.
[2]	"What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence." Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U. Nucleic Acids Res. 31:1944-1954(2003) [PubMed: 12655011] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[3]	"The genome sequence of the filamentous fungus Neurospora crassa." 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. Nature 422:859-868(2003) [PubMed: 12712197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
[4]	"Primary structure of tyrosinase from Neurospora crassa. II. Complete amino acid sequence and chemical structure of a tripeptide containing an unusual thioether." Lerch K. J. Biol. Chem. 257:6414-6419(1982) [PubMed: 6210696] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-408. Strain: TL.
[5]	"Comparison of amino acid sequence and thermostability of tyrosinase from three wild type strains of Neurospora crassa." Ruegg C., Ammer D., Lerch K. J. Biol. Chem. 257:6420-6426(1982) [PubMed: 6210697] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-408. Strain: Sing and TS.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M32843 Genomic DNA. Translation: AAA33619.1. Frameshift. M33271 Genomic DNA. Translation: AAA33618.1. Frameshift. BX842680 Genomic DNA. Translation: CAE81941.1. AABX02000002 Genomic DNA. Translation: EAA35696.2. Sequence problems.
PIR	YRNC. A34460.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.14.18.1. 266.
Family and domain databases
InterPro	IPR008922. Di-copper_centre. IPR016216. Monophenol_mOase_fun. IPR002227. Tyrosinase. [Graphical view]
Gene3D	G3DSA:1.10.1280.10. Di-copper_centre. 1 hit.
Pfam	PF00264. Tyrosinase. 1 hit. [Graphical view]
PIRSF	PIRSF000340. MPO_fungal. 1 hit.
PRINTS	PR00092. TYROSINASE.
PROSITE	PS00497. TYROSINASE_1. 1 hit. PS00498. TYROSINASE_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
DrugBank	DB00548. Azelaic Acid.

Entry information

Entry name

TYRO_NEUCR

Accession

Primary (citable) accession number: P00440
Secondary accession number(s): Q6MGJ7, Q7RVL7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	December 4, 2007
Last modified:	January 20, 2009
This is version 71 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)