PEN18_PENRB
ID PEN18_PENRB Reviewed; 494 AA.
AC Q9P8G3;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Subtilisin-like serine protease Pen ch 18.0101 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000250|UniProtKB:Q9Y749};
DE AltName: Full=Allergen Pen n 18 {ECO:0000303|PubMed:11964171, ECO:0000312|EMBL:AAF71379.1};
DE AltName: Full=Vacuolar serine protease {ECO:0000303|PubMed:11964171};
DE AltName: Allergen=Pen ch 18.0101 {ECO:0000305};
DE Flags: Precursor;
OS Penicillium rubens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=1108849;
RN [1] {ECO:0000312|EMBL:AAF71379.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 137-143; 144-151; 175-179;
RP 180-184; 201-205; 242-246; 262-266; 358-362; 401-405; 411-415 AND 421-425,
RP IDENTIFICATION BY MASS SPECTROMETRY, 3D-STRUCTURE MODELING, ALLERGEN, AND
RP REGION.
RC STRAIN=ATCC 9179 / BCRC 30568 / CBS 197.46 / NRRL 832 / QM 940
RC {ECO:0000303|PubMed:11964171};
RC TISSUE=Mycelium {ECO:0000303|PubMed:11964171};
RX PubMed=11964171; DOI=10.1042/bj3630707;
RA Yu C.J., Chen Y.M., Su S.N., Forouhar F., Lee S.H., Chow L.P.;
RT "Molecular and immunological characterization and IgE epitope mapping of
RT Pen n 18, a major allergen of Penicillium notatum.";
RL Biochem. J. 363:707-715(2002).
CC -!- FUNCTION: Serine protease. {ECO:0000250|UniProtKB:Q9Y749}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients with bronchial asthma. {ECO:0000269|PubMed:11964171}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255,
CC ECO:0000305}.
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DR EMBL; AF264027; AAF71379.1; -; mRNA.
DR AlphaFoldDB; Q9P8G3; -.
DR SMR; Q9P8G3; -.
DR Allergome; 3407; Pen ch 18.0101.
DR Allergome; 525; Pen ch 18.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR CDD; cd04077; Peptidases_S8_PCSK9_ProteinaseK_like; 1.
DR Gene3D; 3.30.70.80; -; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR034193; PCSK9_ProteinaseK-like.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR010259; S8pro/Inhibitor_I9.
DR InterPro; IPR037045; S8pro/Inhibitor_I9_sf.
DR Pfam; PF05922; Inhibitor_I9; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Glycoprotein; Hydrolase;
KW IgE-binding protein; Protease; Serine protease; Signal; Zymogen.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..136
FT /note="Removed in mature form"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:11964171"
FT /id="PRO_0000446670"
FT CHAIN 137..453
FT /note="Subtilisin-like serine protease Pen ch 18.0101"
FT /evidence="ECO:0000305, ECO:0000305|PubMed:11964171"
FT /id="PRO_5004330871"
FT PROPEP 454..494
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000446671"
FT DOMAIN 43..136
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 146..448
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 180..198
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:11964171"
FT REGION 209..231
FT /note="IgE-binding"
FT /evidence="ECO:0000250|UniProtKB:P9WEW5"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 376
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT SITE 311
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q5JIZ5"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 280
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 443
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 494 AA; 52393 MW; 407A394FE3AEA894 CRC64;
MKGFLSLTLL PLLVAASPVA VNSIHNDAAP ILSSMTSKDI PDSYIVVFKK HVDPSSASAH
QSWLQEVHTA HTGRMELKKR SLFGFDFEAF MGLKHTFHIA GSLLGYAGHF HEDVIEQIRR
HPDVDYIEKD SEVRTMSEGS VEKNAPWGLA RISHRESLSF GNFNKYLYAE EGGEGVDAYV
IDTGANVKHV DFEGRANWGK TIPQGDADED GNGHGTHCSG TIAGKKFGVA KKANVYAVKV
LRSNGSGTMS DVVKGVEWAA EAHIKKSKKG DKKFKGSVAN MSLGGGSSRT LDLAVNAAVD
AGIHFAVAAG NDNADACNYS PAAAEKAITV GASTLADERA YFSNYGKCTD IFAPGLNILS
TWVGSDHATN TISGTSMASP HIAGLLAYYV SLAPAKDSAY AVADVTPKQL KAALISVATE
GTLTDIPSDT PNLLAWNGGG SANYTKILAD GGYKAHNAET TVEDRIGIII DSAEKAFHKE
LGAIYSEIKD AVSV
