PCH13_PENRB
ID PCH13_PENRB Reviewed; 398 AA.
AC P9WEW3; Q8NKG0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 25-MAY-2022, entry version 6.
DE RecName: Full=Subtilisin-like serine protease Pen ch 13 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000269|PubMed:11893850, ECO:0000269|PubMed:16436150};
DE AltName: Full=Alkaline serine protease {ECO:0000303|PubMed:11893850};
DE AltName: Allergen=Pen ch 13 {ECO:0000303|PubMed:11893850};
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], PROTEIN SEQUENCE OF 116-125; 137-168 AND
RP 282-291, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND ALLERGEN.
RC STRAIN=ATCC 9179 / BCRC 30568 / CBS 197.46 / NRRL 832 / QM 940;
RX PubMed=11893850; DOI=10.1159/000048165;
RA Chou H., Lai H.Y., Tam M.F., Chou M.Y., Wang S.R., Han S.H., Shen H.D.;
RT "cDNA cloning, biological and immunological characterization of the
RT alkaline serine protease major allergen from Penicillium chrysogenum.";
RL Int. Arch. Allergy Immunol. 127:15-26(2002).
RN [2]
RP PROTEIN SEQUENCE OF 116-125, 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 PROTEIN SEQUENCE OF 116-125, SUBCELLULAR LOCATION, AND ALLERGEN.
RC STRAIN=ATCC 9179 / BCRC 30568 / CBS 197.46 / NRRL 832 / QM 940;
RX PubMed=12602675; DOI=10.1016/s1081-1206(10)62150-3;
RA Chou H., Chang C.Y., Tsai J.J., Tang R.B., Lee S.S., Wang S.R., Peng H.J.,
RA Shen H.D.;
RT "The prevalence of IgE antibody reactivity against the alkaline serine
RT protease major allergen of Penicillium chrysogenum increases with the age
RT of asthmatic patients.";
RL Ann. Allergy Asthma Immunol. 90:248-253(2003).
RN [4]
RP ALLERGEN, IGE-BINDING REGIONS, AND MUTAGENESIS OF HIS-164; PHE-167 AND
RP 318-VAL--TYR-321.
RC STRAIN=ATCC 9179 / BCRC 30568 / CBS 197.46 / NRRL 832 / QM 940;
RX PubMed=15663570; DOI=10.1111/j.1365-2222.2004.02115.x;
RA Lai H.Y., Tam M.F., Chou H., Lee S.S., Tai H.Y., Shen H.D.;
RT "Molecular and structural analysis of immunoglobulin E-binding epitopes of
RT Pen ch 13, an alkaline serine protease major allergen from Penicillium
RT chrysogenum.";
RL Clin. Exp. Allergy 34:1926-1933(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND ALLERGEN.
RC STRAIN=ATCC 9179 / BCRC 30568 / CBS 197.46 / NRRL 832 / QM 940;
RX PubMed=16436150; DOI=10.1111/j.1398-9995.2005.00958.x;
RA Tai H.Y., Tam M.F., Chou H., Peng H.J., Su S.N., Perng D.W., Shen H.D.;
RT "Pen ch 13 allergen induces secretion of mediators and degradation of
RT occludin protein of human lung epithelial cells.";
RL Allergy 61:382-388(2006).
CC -!- FUNCTION: Serine protease (PubMed:11893850, PubMed:16436150).
CC Hydrolyzes casein, gelatin and human collagen type IV, but not elastin
CC in vitro (PubMed:16436150). Hydrolyzes OCLN of the human lung
CC epithelial cells at 202-Gln-|-Ser-203 and Gln-211-|-Ile-212
CC (PubMed:16436150). {ECO:0000269|PubMed:11893850,
CC ECO:0000269|PubMed:16436150}.
CC -!- ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride (PMSF)
CC and diethyl pyrocarbonate (DEPC), but not by benzamidine.
CC {ECO:0000269|PubMed:11893850}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active at neutral to pH 8 with casein as substrate.
CC {ECO:0000269|PubMed:11893850};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11893850,
CC ECO:0000269|PubMed:12602675, ECO:0000269|PubMed:16436150}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients suffering from bronchial asthma (PubMed:10231324,
CC PubMed:11893850, PubMed:12602675, PubMed:15663570). Binds to IgE in 17%
CC of the 212 asthmatic patients of different age (3 to 94 years old). The
CC binding frequency and intensity to IgE increases significantly with
CC age. Binds also to IgG and IgG4 (PubMed:12602675). Induces histamine
CC release from basophils of asthmatic patients (PubMed:11893850). May
CC contribute to asthma by damaging the barrier formed by the airway
CC epithelium by cleaving the tight junction protein OCLN and stimulating
CC the release of mediators, such as PGE2, CXCL8 and TGFB1, in human
CC respiratory epithelial cells (PubMed:16436150).
CC {ECO:0000269|PubMed:10231324, ECO:0000269|PubMed:11893850,
CC ECO:0000269|PubMed:12602675, ECO:0000269|PubMed:15663570,
CC ECO:0000269|PubMed:16436150}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255,
CC ECO:0000305}.
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DR EMBL; AF321100; AAM33821.1; -; mRNA.
DR AlphaFoldDB; P9WEW3; -.
DR SMR; P9WEW3; -.
DR EnsemblFungi; KZN89038; KZN89038; EN45_076310.
DR OMA; SAWNDSD; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA: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;
KW IgE-binding protein; Protease; 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:10231324,
FT ECO:0000305|PubMed:11893850, ECO:0000305|PubMed:12602675"
FT /id="PRO_0000446677"
FT CHAIN 116..398
FT /note="Subtilisin-like serine protease Pen ch 13"
FT /evidence="ECO:0000305|PubMed:10231324,
FT ECO:0000305|PubMed:11893850, ECO:0000305|PubMed:12602675"
FT /id="PRO_5004312984"
FT DOMAIN 35..113
FT /note="Inhibitor I9"
FT /evidence="ECO:0000255"
FT DOMAIN 125..398
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 124..134
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:15663570"
FT REGION 163..170
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:15663570"
FT REGION 175..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..245
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:15663570"
FT REGION 310..318
FT /note="IgE-binding"
FT /evidence="ECO:0000269|PubMed:15663570"
FT COMPBIAS 176..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 MUTAGEN 164
FT /note="H->M: Reduced IgE-binding. Significantly reduced
FT IgE-binding; when associated with M-167."
FT /evidence="ECO:0000269|PubMed:15663570"
FT MUTAGEN 167
FT /note="F->M: Reduced IgE-binding. Significantly reduced
FT IgE-binding; when associated with M-164."
FT /evidence="ECO:0000269|PubMed:15663570"
FT MUTAGEN 318..321
FT /note="VDLY->AAL: Reduced IgE-binding."
FT /evidence="ECO:0000269|PubMed:15663570"
SQ SEQUENCE 398 AA; 40362 MW; 8E85FE9E942080D3 CRC64;
MGFLKLLSTS LATLAVVNAG KLLTANDGDE VVPSSYIVVM NDGVSTAQFE THRNWAANVH
ARTRSLKGGE SGPGKHFDIN GMKGYSASFD DRTVKDIASD PTVKYVEPDM VVNATANVVQ
RNAPSWGLSR ISSKKSGATD YVYDSTAGEG IVIYGVDTGI DIGHADFGGR AEWGTNTADN
DDTDGNGHGT HTASTAAGSK FGVAKKASVV AVKVLGADGS GTNSQVIAGM DWAVKDSKSR
GATGKSVMNM SLGGAYSRAM NDAAANVVRS GVFLSVAAGN EAQDASNSSP ASAPNVCTIA
ASTNSDGSAS FTNFGSVVDL YAPGKDITAA YPGGGSKTLS GTSMAAPHVA GAAAYLMALE
GVTSDKACAR IVELAISSIS SAPSGTTSKL LYNGINAQ
