TYRP_ASPTN
ID TYRP_ASPTN Reviewed; 356 AA.
AC Q0CRX0;
DT 11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Tyrosinase P {ECO:0000303|PubMed:27133313};
DE EC=1.14.18.- {ECO:0000269|PubMed:27133313};
DE AltName: Full=Melanin biosynthesis protein B {ECO:0000303|PubMed:28791090};
DE Flags: Precursor;
GN Name=tyrP {ECO:0000303|PubMed:27133313};
GN Synonyms=melB {ECO:0000303|PubMed:28791090}; ORFNames=ATEG_03564;
OS Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=341663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIH 2624 / FGSC A1156;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA Nierman W.C., Milne T., Madden K.;
RT "Annotation of the Aspergillus terreus NIH2624 genome.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=28791090; DOI=10.1039/c5sc01058f;
RA Guo C.J., Sun W.W., Bruno K.S., Oakley B.R., Keller N.P., Wang C.C.C.;
RT "Spatial regulation of a common precursor from two distinct genes generates
RT metabolite diversity.";
RL Chem. Sci. 6:5913-5921(2015).
RN [3]
RP INDUCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, GLYCOSYLATION,
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND PATHWAY.
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 [4]
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:28791090,
CC PubMed:27133313, PubMed:29270299). The nonribosomal peptide synthase
CC melA converts 4-hydroxyphenylpyruvate (4-HPPA) to aspulvinone E
CC (PubMed:27133313, PubMed:29270299). The tyrosinase tyrP then performs
CC hydroxylations of both aromatic moieties of aspulvinone E
CC (PubMed:27133313). The product of tyrP is highly unstable, and, due to
CC the high reactivity of methides and ortho-diquinones, the polymeric
CC Asp-melanin forms spontaneously (PubMed:27133313).
CC {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:28791090,
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 -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:28791090}.
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: Impairs the production of Asp-melanin
CC (PubMed:28791090). Results in yellow fluorescent conidia and
CC accumulates aspulvinone E in conidia (PubMed:27133313).
CC {ECO:0000269|PubMed:27133313, ECO:0000269|PubMed:28791090}.
CC -!- SIMILARITY: Belongs to the tyrosinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAU36838.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH476597; EAU36838.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001212742.1; XM_001212742.1.
DR AlphaFoldDB; Q0CRX0; -.
DR SMR; Q0CRX0; -.
DR EnsemblFungi; EAU36838; EAU36838; ATEG_03564.
DR GeneID; 4317933; -.
DR HOGENOM; CLU_035914_0_2_1; -.
DR OrthoDB; 518234at2759; -.
DR Proteomes; UP000007963; Unassembled WGS sequence.
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; Reference proteome; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..356
FT /note="Tyrosinase P"
FT /evidence="ECO:0000255"
FT /id="PRO_0000448623"
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
