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P00440

- TYRO_NEUCR

UniProt

P00440 - TYRO_NEUCR

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Protein
Tyrosinase
Gene
T, 90C4.150, NCU00776
Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds.

Catalytic activityi

2 L-dopa + O2 = 2 dopaquinone + 2 H2O.
L-tyrosine + O2 = dopaquinone + H2O.

Cofactori

Binds 2 copper ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi67 – 671Copper A By similarity
Metal bindingi97 – 971Copper A By similarity
Metal bindingi106 – 1061Copper A By similarity
Metal bindingi278 – 2781Copper B By similarity
Metal bindingi282 – 2821Copper B By similarity
Metal bindingi307 – 3071Copper B By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. monophenol monooxygenase activity Source: UniProtKB-EC

GO - Biological processi

  1. melanin biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Monooxygenase, Oxidoreductase

Keywords - Biological processi

Melanin biosynthesis

Keywords - Ligandi

Copper, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosinase (EC:1.14.18.1)
Alternative name(s):
Monophenol monooxygenase
Gene namesi
Name:T
ORF Names:90C4.150, NCU00776
OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic identifieri367110 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
ProteomesiUP000001805: Chromosome 1, Linkage Group I

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 408407Tyrosinase
PRO_0000035895Add
BLAST
Propeptidei409 – 685277Could be involved in enzyme activation
PRO_0000035896Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine
Cross-linki95 ↔ 972'-(S-cysteinyl)-histidine (Cys-His)

Keywords - PTMi

Acetylation, Thioether bond

Interactioni

Protein-protein interaction databases

STRINGi5141.NCU00776.1.

Structurei

3D structure databases

ProteinModelPortaliP00440.

Family & Domainsi

Sequence similaritiesi

Belongs to the tyrosinase family.

Phylogenomic databases

eggNOGiNOG68512.
KOiK00505.
OrthoDBiEOG79PJXV.

Family and domain databases

Gene3Di1.10.1280.10. 1 hit.
InterProiIPR016216. Monophenol_mOase_fun.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view]
PfamiPF00264. Tyrosinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000340. MPO_fungal. 1 hit.
PRINTSiPR00092. TYROSINASE.
SUPFAMiSSF48056. SSF48056. 1 hit.
PROSITEiPS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00440-1 [UniParc]FASTAAdd to Basket

« Hide

MSTDIKFAIT GVPTPPSSNG AVPLRRELRD LQQNYPEQFN LYLLGLRDFQ    50
GLDEAKLDSY YQVAGIHGMP FKPWAGVPSD TDWSQPGSSG FGGYCTHSSI 100
LFITWHRPYL ALYEQALYAS VQAVAQKFPV EGGLRAKYVA AAKDFRAPYF 150
DWASQPPKGT LAFPESLSSR TIQVVDVDGK TKSINNPLHR FTFHPVNPSP 200
GDFSAAWSRY PSTVRYPNRL TGASRDERIA PILANELASL RNNVSLLLLS 250
YKDFDAFSYN RWDPNTNPGD FGSLEDVHNE IHDRTGGNGH MSSLEVSAFD 300
PLFWLHHVNV DRLWSIWQDL NPNSFMTPRP APYSTFVAQE GESQSKSTPL 350
EPFWDKSAAN FWTSEQVKDS ITFGYAYPET QKWKYSSVKE YQAAIRKSVT 400
ALYGSNVFAN FVENVADRTP ALKKPQATGE ESKSTVSAAA AHAVELSGAK 450
KVAEKVHNVF QHAEEKAQKP VVPVKDTKAE SSTAAGMMIG LSIKRPSKLT 500
ASPGPIPESL KYLAPDGKYT DWIVNVRAQK HGLGQSFRVI VFLGEFNPDP 550
ETWDDEFNCV GRVSVLGRSA ETQCGKCRKD NANGLIVSGT VPLTSALLQD 600
IVGGELQSLK PEDVIPHLRA NLKWKVALFN GDEYNLEEVP DLKVSVASTE 650
VTIDEEGLPH YSRQYTVYPE ITEGKPCGHG PEDHI 685
Length:685
Mass (Da):75,886
Last modified:December 4, 2007 - v5
Checksum:iDF64B764BFF5468A
GO

Sequence cautioni

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 EAA35696.3 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151P → T in strain: Sing, TL and TS.
Natural varianti30 – 301D → E in strain: Sing.
Natural varianti130 – 1301V → T in strain: Sing.
Natural varianti202 – 2021D → N in strain: TL.
Natural varianti346 – 3472KS → QN in strain: Sing.
Natural varianti371 – 3711I → T in strain: Sing.
Natural varianti424 – 4241K → N in strain: TS.
Natural varianti450 – 4501K → R in strain: TS.
Natural varianti678 – 6781G → R in strain: TS.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2351N → D AA sequence 1 Publication
Sequence conflicti235 – 2351N → D AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M32843 Genomic DNA. Translation: AAA33619.1. Frameshift.
M33271 Genomic DNA. Translation: AAA33618.1. Frameshift.
BX842680 Genomic DNA. Translation: CAE81941.1.
CM002236 Genomic DNA. Translation: EAA35696.3. Sequence problems.
PIRiA34460. YRNC.
RefSeqiXP_964932.2. XM_959839.2.

Genome annotation databases

EnsemblFungiiEFNCRT00000000584; EFNCRP00000000584; EFNCRG00000000584.
GeneIDi3881081.
KEGGincr:NCU00776.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M32843 Genomic DNA. Translation: AAA33619.1 . Frameshift.
M33271 Genomic DNA. Translation: AAA33618.1 . Frameshift.
BX842680 Genomic DNA. Translation: CAE81941.1 .
CM002236 Genomic DNA. Translation: EAA35696.3 . Sequence problems.
PIRi A34460. YRNC.
RefSeqi XP_964932.2. XM_959839.2.

3D structure databases

ProteinModelPortali P00440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5141.NCU00776.1.

Chemistry

DrugBanki DB00548. Azelaic Acid.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii EFNCRT00000000584 ; EFNCRP00000000584 ; EFNCRG00000000584 .
GeneIDi 3881081.
KEGGi ncr:NCU00776.

Phylogenomic databases

eggNOGi NOG68512.
KOi K00505.
OrthoDBi EOG79PJXV.

Family and domain databases

Gene3Di 1.10.1280.10. 1 hit.
InterProi IPR016216. Monophenol_mOase_fun.
IPR002227. Tyrosinase_Cu-bd.
IPR008922. Unchr_di-copper_centre.
[Graphical view ]
Pfami PF00264. Tyrosinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000340. MPO_fungal. 1 hit.
PRINTSi PR00092. TYROSINASE.
SUPFAMi SSF48056. SSF48056. 1 hit.
PROSITEi PS00497. TYROSINASE_1. 1 hit.
PS00498. TYROSINASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-408.
    Strain: Sing and TS.

Entry informationi

Entry nameiTYRO_NEUCR
AccessioniPrimary (citable) accession number: P00440
Secondary accession number(s): Q6MGJ7, Q7RVL7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 4, 2007
Last modified: June 11, 2014
This is version 100 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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