ID   PEN13_PENRB             Reviewed;         397 AA.
AC   Q9URR2;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 110.
DE   RecName: Full=Subtilisin-like serine protease Pen ch 13.0101 {ECO:0000305};
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:Q9Y749};
DE   AltName: Full=Alkaline serine protease {ECO:0000303|PubMed:10694469};
DE   AltName: Full=Allergen Pen n 13 {ECO:0000303|PubMed:10694469};
DE   AltName: Allergen=Pen ch 13.0101 {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:AAF23726.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 116-128, AND ALLERGEN.
RC   STRAIN=ATCC 9179 / BCRC 30568 / CBS 197.46 / NRRL 832 / QM 940
RC   {ECO:0000303|PubMed:10694469, ECO:0000312|EMBL:AAF23726.1};
RC   TISSUE=Mycelium {ECO:0000303|PubMed:10694469};
RX   PubMed=10694469; DOI=10.1006/bbrc.2000.2253;
RA   Chow L.P., Chiou S.H., Hsiao M.C., Yu C.J., Chiang B.L.;
RT   "Characterization of Pen n 13, a major allergen from the mold Penicillium
RT   notatum.";
RL   Biochem. Biophys. Res. Commun. 269:14-20(2000).
CC   -!- FUNCTION: Serine protease. {ECO:0000250|UniProtKB:Q9Y749}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9Y749,
CC       ECO:0000255}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC       Penicillium-sensitive patients. {ECO:0000269|PubMed:10694469}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255,
CC       ECO:0000305}.
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DR   EMBL; AF193420; AAF23726.1; -; mRNA.
DR   PIR; JC7208; JC7208.
DR   AlphaFoldDB; Q9URR2; -.
DR   SMR; Q9URR2; -.
DR   Allergome; 3406; Pen ch 13.0101.
DR   Allergome; 524; Pen ch 13.
DR   MEROPS; S08.025; -.
DR   GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
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; 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; PS00138; SUBTILASE_SER; 1.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Glycoprotein; Hydrolase; Protease;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..115
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255, ECO:0000305|PubMed:10694469"
FT                   /id="PRO_0000446678"
FT   CHAIN           116..397
FT                   /note="Subtilisin-like serine protease Pen ch 13.0101"
FT                   /evidence="ECO:0000305|PubMed:10694469"
FT                   /id="PRO_5004335276"
FT   DOMAIN          35..113
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          125..397
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        157
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        188
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        343
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   SITE            280
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q5JIZ5"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   397 AA;  40326 MW;  2235A5AF5EBCDFE8 CRC64;
     MGFLKVLATS LATLAVVDAG TLLTASNTDA VIPSSYIVVM NDDVSTAEFS THREWATNVH
     ARLSRRKNGE TGPGKHFEIN GLKGYTASFD ENTAKDIAND PAVKYIEPDM IVNATANVVQ
     SNVPSWGLAR ISSKRTGTTS YTYDSTAGEG VVFYGVDTGI DISHSDFGGR AKWGTNVVDN
     DNTDGNGHGT HTASTAAGSK YGVAKKATLV AVKVLGADGS GTNSGVISGM DWAVKDAKSR
     GANGKYVMNT SLGGEFSKAV NDAAANVVKS GIFLSVAAGN EAENASNSSP ASAAEACTIA
     ASTSTDGSAS FTNFGSVVDL YAPGQSITAA YPGGGSKTLS GTSMAAPHVA GVAAYLMALE
     GVSAGNACAR IVQLATSSIS RAPSGTTSKL LYNGINV