ID   PEPA_TALSN              Reviewed;         387 AA.
AC   B8MF81;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Penicillopepsin-1 {ECO:0000305};
DE            EC=3.4.23.20 {ECO:0000250|UniProtKB:P00798};
DE   AltName: Full=Aspartic protease pepA;
DE   Flags: Precursor;
GN   Name=pepA; ORFNames=TSTA_012870;
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX   PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA   Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT   "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT   (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT   (ATCC10500).";
RL   Genome Announc. 3:E0155914-E0155914(2015).
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; EQ962656; EED16180.1; -; Genomic_DNA.
DR   RefSeq; XP_002483414.1; XM_002483369.1.
DR   AlphaFoldDB; B8MF81; -.
DR   SMR; B8MF81; -.
DR   STRING; 441959.B8MF81; -.
DR   EnsemblFungi; EED16180; EED16180; TSTA_012870.
DR   GeneID; 8108163; -.
DR   VEuPathDB; FungiDB:TSTA_012870; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_0_0_1; -.
DR   InParanoid; B8MF81; -.
DR   OMA; YGSGNAK; -.
DR   OrthoDB; 1619495at2759; -.
DR   PhylomeDB; B8MF81; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
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; Glycoprotein; Hydrolase; Protease;
KW   Reference proteome; Secreted; Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..66
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000250|UniProtKB:Q12567"
FT                   /id="PRO_0000407061"
FT   CHAIN           67..387
FT                   /note="Penicillopepsin-1"
FT                   /id="PRO_0000407062"
FT   DOMAIN          85..384
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        279
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   CARBOHYD        304
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        315..347
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   387 AA;  39923 MW;  52949806E4AEE95D CRC64;
     MVNSKTVVSA LALSALAAAA PAPSSTTSFS INQVAVKKPA IHPAVKYAKA LAKYHAEIPS
     NVASAAASAQ SGSATNKPTA DDEEYVTPIT AGSSTLHLDF DTGSADLWTY SASTRGVGSH
     STYDTSTGKK VSGASWQISY GDGSSASGVV YKDKVVVGGV TASSQAVEVA TQVSSEFSQD
     TSNDGLLGLA FSSINTVSPT PQKTFYDNVK SSLAKPVFAV TLKHQAPGTY DFGFIDKSKY
     KGSLAYTNVD NSQGFWQFTA DGYSIGGSGG GSSFSAIADT GTTLVLLDDS IVDEYYSQVQ
     GAQNDSSQGG YVFDCSADLP DFGVQIGDYT AVIPGKYINY ASTGSTCFGG IQSNSGIGFS
     ILGDVFLKSQ YVVFDGDNLQ LGFAAQA