TYRP_ASPTE
ID TYRP_ASPTE Reviewed; 356 AA.
AC A0A336U966;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Tyrosinase P {ECO:0000303|PubMed:27133313};
DE EC=1.14.18.- {ECO:0000269|PubMed:27133313};
DE Flags: Precursor;
GN Name=tyrP;
OS Aspergillus terreus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=33178;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, DISRUPTION PHENOTYPE,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=SBUG844;
RX PubMed=27133313; DOI=10.1016/j.chembiol.2016.03.014;
RA Geib E., Gressler M., Viediernikova I., Hillmann F., Jacobsen I.D.,
RA Nietzsche S., Hertweck C., Brock M.;
RT "A non-canonical melanin biosynthesis pathway protects Aspergillus terreus
RT conidia from environmental stress.";
RL Cell Chem. Biol. 23:587-597(2016).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29270299; DOI=10.1186/s40694-017-0042-1;
RA Geib E., Brock M.;
RT "ATNT: an enhanced system for expression of polycistronic secondary
RT metabolite gene clusters in Aspergillus niger.";
RL Fungal Biol. Biotechnol. 4:13-13(2017).
CC -!- FUNCTION: Tyrosinase; part of the gene cluster that mediates the
CC biosynthesis of Asp-melanin, a pigment that confers resistance against
CC UV light and hampers phagocytosis by soil amoeba (PubMed:27133313,
CC PubMed:29270299). The nonribosomal peptide synthase melA converts 4-
CC hydroxyphenylpyruvate (4-HPPA) to aspulvinone E (PubMed:27133313,
CC PubMed:29270299). The tyrosinase tyrP then performs hydroxylations of
CC both aromatic moieties of aspulvinone E (PubMed:27133313). The product
CC of tyrP is highly unstable, and, due to the high reactivity of methides
CC and ortho-diquinones, the polymeric Asp-melanin forms spontaneously
CC (PubMed:27133313). {ECO:0000269|PubMed:27133313,
CC ECO:0000269|PubMed:29270299}.
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 -!- ACTIVITY REGULATION: Activity is inhibited by the presence of
CC dithiothreitol (DTT). {ECO:0000269|PubMed:27133313}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5-7. {ECO:0000269|PubMed:27133313};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:29270299}. Golgi
CC apparatus lumen {ECO:0000269|PubMed:27133313,
CC ECO:0000269|PubMed:29270299}. Note=The oxidizing environment of Golgi
CC or endoplasmic reticulum (ER) is required for tyrP to be active.
CC {ECO:0000269|PubMed:29270299}.
CC -!- INDUCTION: Expression is induced during conidiation.
CC {ECO:0000269|PubMed:27133313}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:27133313}.
CC -!- DISRUPTION PHENOTYPE: Results in yellow fluorescent conidia and
CC accumulates aspulvinone E in conidia. {ECO:0000269|PubMed:27133313}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
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DR EMBL; KU530118; AND66116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A336U966; -.
DR SMR; A0A336U966; -.
DR VEuPathDB; FungiDB:ATEG_03564; -.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005796; C:Golgi lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1280.10; -; 1.
DR InterPro; IPR008922; Di-copper_centre_dom_sf.
DR InterPro; IPR002227; Tyrosinase_Cu-bd.
DR Pfam; PF00264; Tyrosinase; 1.
DR PRINTS; PR00092; TYROSINASE.
DR SUPFAM; SSF48056; SSF48056; 1.
DR PROSITE; PS00498; TYROSINASE_2; 1.
PE 1: Evidence at protein level;
KW Copper; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Metal-binding; Oxidoreductase; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..356
FT /note="Tyrosinase P"
FT /evidence="ECO:0000255"
FT /id="PRO_0000448624"
FT BINDING 87
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 96
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 203
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 263
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT BINDING 286
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="B"
FT /evidence="ECO:0000250|UniProtKB:Q9ZP19"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 356 AA; 40470 MW; 8B6D196601BF66CD CRC64;
MGFYRNLVLV AASCTQALGL CPAPRCDSPD IRHEWGELSR EDRLSYISAV QCMKDRPPEL
SVEEVPAVRS RYDDFTAVHI NYTLQIHNSG IFLPWHRHFI WLWEKALREE CGFTGTLPYW
DWVMWPNLAA SPLFDGTETS LSGDGEFNAT EQPTELNPEP GLTITIPRGA GGGCVRTGPF
KDWVINMGPF AFNESYEPAL PDHAFDYNPR CLVRSLNDWV IQTYNNQTVV DTLLDSPDIV
EFQNIMGGFP NPPIPIGPHA MGHRSLGPDM LDFFASPQDP AFWQHHGMVD RLWTVWQDAD
EPWRRFALNG SSTTWYKDDT PEVTLQTTVE FGILDEPRPL YELMSPTAGP YCYTYT
