ID   PENC2_PENCI             Reviewed;         457 AA.
AC   Q9Y755;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Subtilisin-like serine protease Pen c 2 {ECO:0000305};
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:Q9Y749, ECO:0000312|EMBL:AAD25995.1};
DE   AltName: Full=Vacuolar serine protease Pen c 2 {ECO:0000303|PubMed:10377244};
DE   AltName: Allergen=Pen c 2 {ECO:0000303|PubMed:10377244};
DE   Flags: Precursor;
OS   Penicillium citrinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5077 {ECO:0000312|EMBL:AAD25995.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 137-149, AND ALLERGEN.
RC   STRAIN=52-5 {ECO:0000303|PubMed:10377244};
RC   TISSUE=Mycelium {ECO:0000303|PubMed:10377244};
RX   PubMed=10377244; DOI=10.1042/bj3410051;
RA   Chow L.P., Su N.Y., Yu C.J., Chiang B.L., Shen H.D.;
RT   "Identification and expression of Pen c 2, a novel allergen from
RT   Penicillium citrinum.";
RL   Biochem. J. 341:51-59(1999).
CC   -!- FUNCTION: Serine protease. {ECO:0000250|UniProtKB:Q9Y749}.
CC   -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC       {ECO:0000269|PubMed:10377244}.
CC   -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255,
CC       ECO:0000305}.
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DR   EMBL; AF098517; AAD25995.1; -; mRNA.
DR   AlphaFoldDB; Q9Y755; -.
DR   SMR; Q9Y755; -.
DR   Allergome; 521; Pen c 2.
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; Protease;
KW   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:10377244"
FT                   /id="PRO_0000446633"
FT   CHAIN           137..457
FT                   /note="Subtilisin-like serine protease Pen c 2"
FT                   /evidence="ECO:0000305|PubMed:10377244"
FT                   /id="PRO_5004338782"
FT   DOMAIN          43..134
FT                   /note="Inhibitor I9"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          146..457
FT                   /note="Peptidase S8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
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        380
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT   SITE            315
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        284
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        447
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   457 AA;  48175 MW;  B26C3D5453AB8D06 CRC64;
     MKGFLGLALL PLLTAASPVS VESIHNGAAP IISSMNSQEI PDSYIVVFKK HVDTSAAAAH
     HSWVQDIHSA VNGRMELKKR GLFGFDTDAF LGVKHSFHVA GSLMGYAGHF HEDVIEQVRR
     HPDVDYIEKD SEVHHFDSPS VEKNAPWGLA RISHRDSLSF GTFNKYLYAE DGGEGVDAYV
     IDTGTNTDHV DFEGRASWGK TIPQGDEDVD GNGHGTHCSG TIAGKKYGVA KKANVYAVKV
     LRSNGSGTMS DVVKGVEWAA EAHIKKSKAA KDGKAKGFKG SVANMSLGGG SSRTLDLAVN
     AAVDAGMHFA VAAGNDNADA CNYSPAAAEK AVTVGASTLA DERAYFSNYG KCTDIFAPGL
     NILSTWIGSK YAVNTISGTS MASPHIAGLL AYYVSLQPSD DSAFAVEKIT PKKLKEALIT
     VATSGALTDI PSDTPNLLAW NGGGSSNYTD IVAQGGY