PEPA_PENRO
ID PEPA_PENRO Reviewed; 397 AA.
AC Q01972;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Penicillopepsin-1 {ECO:0000305};
DE EC=3.4.23.20 {ECO:0000269|PubMed:4790849};
DE AltName: Full=Acid protease {ECO:0000303|PubMed:4790849};
DE AltName: Full=Aspartic protease aspA {ECO:0000303|PubMed:9413440};
DE Flags: Precursor;
GN Name=aspA {ECO:0000303|PubMed:9413440};
OS Penicillium roqueforti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=5082;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, AND
RP INDUCTION.
RC STRAIN=P2;
RX PubMed=9413440; DOI=10.1007/s004380050601;
RA Gente S., Durand-Poussereau N., Fevre M.;
RT "Controls of the expression of aspA, the aspartyl protease gene from
RT Penicillium roqueforti.";
RL Mol. Gen. Genet. 256:557-565(1997).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=431;
RX PubMed=4790849;
RA Zevaco C., Hermier J., Gripon J.C.;
RT "Proteolytic system in Penicillium roqueforti. 2. Purification and
RT properties of acid protease.";
RL Biochimie 55:1353-1360(1973).
CC -!- FUNCTION: Secreted aspartic endopeptidase that allows assimilation of
CC proteinaceous substrates. The scissile peptide bond is attacked by a
CC nucleophilic water molecule activated by two aspartic residues in the
CC active site. Shows a broad primary substrate specificity. Favors
CC hydrophobic residues at the P1 and P1' positions, but can also activate
CC trypsinogen and hydrolyze the B chain of insulin between positions
CC 'Gly-20' and 'Glu-21'. {ECO:0000269|PubMed:4790849,
CC ECO:0000269|PubMed:9413440}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity similar to that
CC of pepsin A, preferring hydrophobic residues at P1 and P1', but also
CC cleaving 20-Gly-|-Glu-21 in the B chain of insulin. Clots milk, and
CC activates trypsinogen.; EC=3.4.23.20;
CC Evidence={ECO:0000269|PubMed:4790849};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 3.5. {ECO:0000269|PubMed:4790849};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:4790849};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q12567}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9413440}.
CC -!- INDUCTION: Repressed by alkaline pH and in presence of ammonia.
CC {ECO:0000269|PubMed:9413440}.
CC -!- MISCELLANEOUS: Used in the production of blue cheese. During the
CC fermentation process, aspartic protease hydrolyzes casein which leads
CC to clotting of the milk. {ECO:0000305|PubMed:4790849}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01103}.
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DR EMBL; X85984; CAA59972.1; -; Genomic_DNA.
DR PIR; S52783; S52783.
DR AlphaFoldDB; Q01972; -.
DR SMR; Q01972; -.
DR MEROPS; A01.026; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0060359; P:response to ammonium ion; IDA:UniProtKB.
DR GO; GO:0009268; P:response to pH; IDA:UniProtKB.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Secreted; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..71
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:9413440"
FT /id="PRO_0000407057"
FT CHAIN 72..397
FT /note="Penicillopepsin-1"
FT /id="PRO_0000407058"
FT DOMAIN 87..394
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 285
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT CARBOHYD 311
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 322..357
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 397 AA; 41112 MW; 78993028B8A94EFE CRC64;
MVVFSQVTVA LTCFSAIASA AAVRQEPPQG FTVNQVQKAV PGTRTVNLPG LYANALVKYG
ATVPATVHAA AVSGSAITTP EADDVEYLTP VTIGSSTLNL DFDTGSADLW VFSSELTSSQ
QSGHDVYNVG SLGTKLSGAS WSISYGDGSS ASGDVYKDTV TVGGVKATGQ AVEAAKKISS
QFLQDKNNDG LLGMAFSSIN TVSPTPQKTF FDTVKSSLGE PLFAVTLQGT GRPWHLRFGY
IDSDKYTGTL AYADVDDSDG FWSFTADSYK IGTGAAGKSI TGIADTGTTL LLLDSSIVTG
LLQEGYPGSQ NSSSAGGYIF PCSATLPDFT VTINGYDAVV PGKYINFAPV STGSSSCYGG
IQSNSGIGFS IFGDIFLKSQ YVVFDSEGPR LGFAAQA
