PENC1_PENCI
ID PENC1_PENCI Reviewed; 397 AA.
AC Q9Y749;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Subtilisin-like serine protease Pen c 1 {ECO:0000305};
DE EC=3.4.21.- {ECO:0000269|PubMed:10103041, ECO:0000269|PubMed:7763554};
DE AltName: Full=Alkaline serine protease {ECO:0000303|PubMed:9117886};
DE AltName: Allergen=Pen c 1 {ECO:0000303|PubMed:10103041};
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:AAD25926.1};
RN [1] {ECO:0000312|EMBL:AAD25926.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 116-131 AND 296-311,
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP AND ALLERGEN.
RC STRAIN=52-5 {ECO:0000303|PubMed:10103041, ECO:0000312|EMBL:AAD25926.1};
RC TISSUE=Mycelium {ECO:0000303|PubMed:10103041};
RX PubMed=10103041; DOI=10.1046/j.1432-1327.1999.00242.x;
RA Su N.Y., Yu C.J., Shen H.D., Pan F.M., Chow L.P.;
RT "Pen c 1, a novel enzymic allergen protein from Penicillium citrinum.
RT Purification, characterization, cloning and expression.";
RL Eur. J. Biochem. 261:115-123(1999).
RN [2]
RP ERRATUM OF PUBMED:10103041.
RA Su N.Y., Yu C.J., Shen H.D., Pan F.M., Chow L.P.;
RL Eur. J. Biochem. 261:821-821(1999).
RN [3]
RP PROTEIN SEQUENCE OF 116-159 AND 292-311, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND CIRCULAR DICHROISM
RP ANALYSIS.
RX PubMed=7763554; DOI=10.1016/0031-9422(93)85144-g;
RA Yamamoto N., Matsumoto K., Yamagata Y., Hirano K., Ichishima E.;
RT "A heat-labile serine proteinase from Penicillium citrinum.";
RL Phytochemistry 32:1393-1397(1993).
RN [4]
RP PROTEIN SEQUENCE OF 116-128.
RC STRAIN=52-5 {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).
RN [5]
RP PROTEIN SEQUENCE OF 116-124, AND ALLERGEN.
RC STRAIN=52-5 {ECO:0000303|PubMed:9117886};
RX PubMed=9117886; DOI=10.1111/j.1365-2222.1997.tb00676.x;
RA Shen H.D., Lin W.L., Liaw S.F., Tam M.F., Han S.H.;
RT "Characterization of the 33-kilodalton major allergen of Penicillium
RT citrinum by using MoAbs and N-terminal amino acid sequencing.";
RL Clin. Exp. Allergy 27:79-86(1997).
CC -!- FUNCTION: Serine protease (PubMed:10103041, PubMed:7763554). Hydrolyzes
CC azocasein (PubMed:10103041). Cleaves peptide bonds of the oxidized
CC insulin B chain preferably at 15-Leu-|-Tyr-16, but also at 4-Gln-|-His-
CC 5 and 24-Phe-|-Phe-25, and to a lesser extent at 5-His-|-Leu-6 and 25-
CC Phe-|-Tyr-26. Hydrolyzes amide bonds between amino acids and 7-amino-4-
CC methylcoumarin (AMC) in vitro (PubMed:7763554).
CC {ECO:0000269|PubMed:10103041, ECO:0000269|PubMed:7763554}.
CC -!- ACTIVITY REGULATION: Inhibited by 0.1 mM diisopropyl fluorophosphate
CC (DFP), phenylmethanesulfonyl fluoride (PMSF), chymostatin and
CC elastatinal. Not inhibited by N-alpha-p-tosyl-L-lysine
CC chloromethylketone (TLCK), N-tosyl-L-phenylalanyl chloromethyl ketone
CC (TPCK) or N-carbobenzoxy-L-phenylalanine chloromethylketone (ZPCK).
CC {ECO:0000269|PubMed:7763554}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.14 mM for t-butyloxycarbonyl-Val-Leu-Lys-4-methylcoumaryl-7-
CC amide (Boc-VLK-MCA) (at pH 7.0) {ECO:0000269|PubMed:7763554};
CC KM=0.11 mM for t-butyloxycarbonyl-Leu-Ser-Thr-Arg-4-methylcoumaryl-7-
CC amide ((Boc-LSTR-MCA) (at pH 7.0) {ECO:0000269|PubMed:7763554};
CC KM=0.13 mM for succinyl-Leu-Leu-Val-Tyr-4-methylcoumaryl-7-amide
CC (Suc-LLVY-MCA) (at pH 7.0) {ECO:0000269|PubMed:7763554};
CC pH dependence:
CC Active at pH 7 (up to 40 degrees Celsius for 30 min) and at pH 11 (up
CC to 25 degrees Celsius). {ECO:0000269|PubMed:7763554};
CC Temperature dependence:
CC Protease activity is retained up to 40 degrees Celsius for 30 min,
CC but completely inactivated at 50 degrees Celsius (at pH 7). Activity
CC is retained up to 25 degrees Celsius, and completely inactivated at
CC 40 degrees Celsius (at pH 11). {ECO:0000269|PubMed:7763554};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255,
CC ECO:0000269|PubMed:10103041}.
CC -!- DEVELOPMENTAL STAGE: Expression is induced in mycelia after 24 hours of
CC growth. Maximal expression is reached at about 42 hours and expression
CC is slightly decayed after 48 hours. {ECO:0000269|PubMed:10103041}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE.
CC {ECO:0000269|PubMed:10103041, ECO:0000269|PubMed:9117886}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255,
CC ECO:0000305}.
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DR EMBL; AF084546; AAD25926.1; -; mRNA.
DR AlphaFoldDB; Q9Y749; -.
DR SMR; Q9Y749; -.
DR Allergome; 517; Pen c 1.
DR MEROPS; S08.025; -.
DR BRENDA; 3.4.21.63; 4608.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
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; Hydrolase; Protease; Secreted;
KW 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:10103041,
FT ECO:0000305|PubMed:10377244, ECO:0000305|PubMed:7763554,
FT ECO:0000305|PubMed:9117886"
FT /id="PRO_0000446632"
FT CHAIN 116..397
FT /note="Subtilisin-like serine protease Pen c 1"
FT /evidence="ECO:0000305|PubMed:10103041,
FT ECO:0000305|PubMed:10377244, ECO:0000305|PubMed:7763554,
FT ECO:0000305|PubMed:9117886"
FT /id="PRO_5004337123"
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 113
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:10103041"
FT SITE 249
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:10103041"
FT SITE 280
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:Q5JIZ5"
FT SITE 284
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:10103041"
FT CONFLICT 136
FT /note="T -> P (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="C -> S (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="T -> I (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 397 AA; 40384 MW; 2E4056A735C0EF24 CRC64;
MGFLKVLATS LATLAVVDAG TLLTASNTDA VIPSSYIVVM NDDVSTAEFN THREWATNVH
ARLSRRKNGE TGPGKHFEIN GLKGYTASFD ESTAKDIAND PAVKYIEPDM IVNATANVVQ
SNVPSWGLAR ISSKRTGTTS YTYDSTAGEG VVFYGVDTGI DISHSDFGGR AKWGTNVVDN
DNTDGNGHGT HTASTAAGSK YGVAKKATLV AVKVLGADGS GTNSGVISGM DWAVKDAKSR
GANGKYVMNM SLGGEFSKAV NDAAANVVKS GIFLSVAAGN EAENASNSSP ASAAEVCTIA
ASTSTDGSAS FTNFGSVVDL YAPGQSITAA YPGGGSKTLS GTSMAAPHVA GVAAYLMALE
GVSAGNACAR IVQLATSSIS RAPSGTTSKL LYNGINV
