PCH18_PENRB
ID PCH18_PENRB Reviewed; 494 AA.
AC P9WEW5; Q9HF04;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 03-AUG-2022, entry version 7.
DE RecName: Full=Subtilisin-like serine protease Pen ch 18 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000250|UniProtKB:Q9Y749};
DE AltName: Full=Vacuolar serine protease {ECO:0000303|PubMed:10231324, ECO:0000303|PubMed:14510716, ECO:0000303|PubMed:18760997};
DE AltName: Allergen=Pen ch 18 {ECO:0000303|PubMed:14510716, ECO:0000303|PubMed:18760997};
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]
RP NUCLEOTIDE SEQUENCE [MRNA], ALLERGEN, AND REGION.
RC STRAIN=ATCC 9179 / BCRC 30568 / CBS 197.46 / NRRL 832 / QM 940;
RX PubMed=14510716; DOI=10.1034/j.1398-9995.2003.00107.x;
RA Shen H.D., Chou H., Tam M.F., Chang C.Y., Lai H.Y., Wang S.R.;
RT "Molecular and immunological characterization of Pen ch 18, the vacuolar
RT serine protease major allergen of Penicillium chrysogenum.";
RL Allergy 58:993-1002(2003).
RN [2]
RP PROTEIN SEQUENCE OF 137-156 AND 168-182, AND ALLERGEN.
RC STRAIN=ATCC 9179 / BCRC 30568 / CBS 197.46 / NRRL 832 / QM 940;
RX PubMed=10231324; DOI=10.1046/j.1365-2222.1999.00509.x;
RA Shen H.D., Lin W.L., Tam M.F., Wang S.R., Tzean S.S., Huang M.H., Han S.H.;
RT "Characterization of allergens from Penicillium oxalicum and P. notatum by
RT immunoblotting and N-terminal amino acid sequence analysis.";
RL Clin. Exp. Allergy 29:642-651(1999).
RN [3]
RP 3D-STRUCTURE MODELING, ALLERGEN, AND MUTAGENESIS OF LYS-225; LYS-226 AND
RP PHE-227.
RX PubMed=18760997; DOI=10.1016/j.bbrc.2008.08.097;
RA Cheng T.T., Tam M.F., Chou H., Tai H.Y., Shen H.D.;
RT "Lys89, Lys90, and Phe91 are critical core amino acid residues of the Pen
RT ch 18 major fungal allergen recognized by human IgE antibodies.";
RL Biochem. Biophys. Res. Commun. 375:671-674(2008).
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 (PubMed:10231324, PubMed:14510716,
CC PubMed:18760997). Binds to IgE in 24% of the 41 patients tested
CC (PubMed:14510716). {ECO:0000269|PubMed:10231324,
CC ECO:0000269|PubMed:14510716, ECO:0000269|PubMed:18760997}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; AF263454; AAG44693.2; -; mRNA.
DR AlphaFoldDB; P9WEW5; -.
DR SMR; P9WEW5; -.
DR EnsemblFungi; KZN89274; KZN89274; EN45_078720.
DR OMA; SNYGKCN; -.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:10231324"
FT /id="PRO_0000446668"
FT CHAIN 137..453
FT /note="Subtilisin-like serine protease Pen ch 18"
FT /evidence="ECO:0000305|PubMed:10231324"
FT /id="PRO_5004327177"
FT PROPEP 454..494
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000446669"
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:0000250|UniProtKB:Q9P8G3"
FT REGION 209..231
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:14510716"
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"
FT MUTAGEN 225
FT /note="K->A: Significantly reduced IgE-binding."
FT /evidence="ECO:0000269|PubMed:18760997"
FT MUTAGEN 226
FT /note="K->A: Significantly reduced IgE-binding."
FT /evidence="ECO:0000269|PubMed:18760997"
FT MUTAGEN 227
FT /note="F->A: Significantly reduced IgE-binding."
FT /evidence="ECO:0000269|PubMed:18760997"
SQ SEQUENCE 494 AA; 52309 MW; 5F6A37AF0DAEA894 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 TVEDRIGGII DSAEKAFHKE
LGAIYSEIKD AVSA
