PCH13_PENCH
ID PCH13_PENCH Reviewed; 398 AA.
AC P9WEW4; Q8NKG0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 1.
DT 03-AUG-2022, entry version 8.
DE RecName: Full=Subtilisin-like serine protease EN45_076310 {ECO:0000250|UniProtKB:P9WEW3};
DE EC=3.4.21.- {ECO:0000250|UniProtKB:P9WEW3};
DE AltName: Full=Alkaline serine protease {ECO:0000250|UniProtKB:P9WEW3};
DE Flags: Precursor;
GN ORFNames=EN45_076310;
OS Penicillium chrysogenum (Penicillium notatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=5076;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P2niaD18;
RX PubMed=25059858; DOI=10.1128/genomea.00577-14;
RA Specht T., Dahlmann T.A., Zadra I., Kuernsteiner H., Kueck U.;
RT "Complete sequencing and chromosome-scale genome assembly of the industrial
RT progenitor strain P2niaD18 from the penicillin producer Penicillium
RT chrysogenum.";
RL Genome Announc. 2:E0057714-E0057714(2014).
CC -!- FUNCTION: Serine protease that hydrolyzes casein, gelatin and human
CC collagen type IV, but not elastin in vitro (By similarity). Hydrolyzes
CC OCLN of the human lung epithelial cells at 202-Gln-|-Ser-203 and Gln-
CC 211-|-Ile-212 (By similarity). {ECO:0000250|UniProtKB:P9WEW3}.
CC -!- ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride (PMSF)
CC and diethyl pyrocarbonate (DEPC), but not by benzamidine.
CC {ECO:0000250|UniProtKB:P9WEW3}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P9WEW3}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
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DR EMBL; CM002799; KZN89038.1; -; Genomic_DNA.
DR AlphaFoldDB; P9WEW4; -.
DR SMR; P9WEW4; -.
DR OMA; SAWNDSD; -.
DR Proteomes; UP000076449; Chromosome ii.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 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 3: Inferred from homology;
KW Glycoprotein; Hydrolase; IgE-binding protein; 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:0000250|UniProtKB:P9WEW3, ECO:0000255"
FT /id="PRO_0000451343"
FT CHAIN 116..398
FT /note="Subtilisin-like serine protease EN45_076310"
FT /evidence="ECO:0000250|UniProtKB:P9WEW3"
FT /id="PRO_0000451344"
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:0000250|UniProtKB:P9WEW3"
FT REGION 163..170
FT /note="IgE-binding"
FT /evidence="ECO:0000250|UniProtKB:P9WEW3"
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:0000250|UniProtKB:P9WEW3"
FT REGION 310..318
FT /note="IgE-binding"
FT /evidence="ECO:0000250|UniProtKB:P9WEW3"
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"
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
