ID   PEPA3_PENJA             Reviewed;         394 AA.
AC   Q9HEZ3;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Penicillopepsin-3 {ECO:0000305};
DE            EC=3.4.23.20 {ECO:0000250|UniProtKB:P00798};
DE   AltName: Full=Aspartic protease pepB;
DE   AltName: Full=Propenicillopepsin-JT3 {ECO:0000303|Ref.1};
DE   Flags: Precursor;
GN   Name=pepB {ECO:0000303|Ref.1};
OS   Penicillium janthinellum (Penicillium vitale).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL905;
RA   Kuo K.H.M., Cao Q.-N., Tu G.-C., Lewis P.N., Pai E.F., Hofmann T.;
RT   "A DNA containing the gene for prepropenicillopepsin-JT3, the precursor for
RT   an aspartic proteinase from Penicillium janthinellum.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P00798}.
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:0000250|UniProtKB:P00798};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q12567}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q01972}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01103}.
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DR   EMBL; AF295432; AAG34660.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9HEZ3; -.
DR   SMR; Q9HEZ3; -.
DR   BRENDA; 3.4.23.20; 4621.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   3: Inferred from homology;
KW   Aspartyl protease; Disulfide bond; Hydrolase; Protease; Secreted; Signal;
KW   Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..70
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q12567"
FT                   /id="PRO_0000407056"
FT   CHAIN           71..394
FT                   /note="Penicillopepsin-3"
FT                   /id="PRO_5000058618"
FT   DOMAIN          87..392
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        284
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   DISULFID        320..355
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   394 AA;  41107 MW;  E23FDFFC9B70ED97 CRC64;
     MVSFTQLQLA FLGLSALGAA VPVTGTSEKK TFSLNQVKVA GTKTKNPAEH YANALRKYGA
     EVPSHVLAAA AATGSVTTSP TEFDSEYLTP IDVGGTTMNL DIDTGSSDLW VFSKELPSSE
     TSGHAVYSPS SQSQLLNGYS WSISYGDGSS ASGNVYLDYV TVGGVTASSQ AVEAAETISS
     EFQQDPSDGL MGLAFSSINT VQPESQSTFF DNVQSNLASP VFCADLKYEA PGVYDFGFID
     SSKHTGSVTY TPVDNSQGFW GFTASGYAVG SGSTVSTSIS GIADTGTTLL LLPSSIVKKY
     YAQVKGSSNS ATYGGYVFPC SATLPKFTVV INGYKAVIAA QYLNYSPVET GSSTCFGGIQ
     SDTGIGFSIF GDIFLKSQYV VFDASGPRLG FAPQ