ID A0A0A2I076_PENEN Unreviewed; 399 AA.
AC A0A0A2I076;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 22-FEB-2023, entry version 41.
DE RecName: Full=penicillopepsin {ECO:0000256|ARBA:ARBA00013206};
DE EC=3.4.23.20 {ECO:0000256|ARBA:ARBA00013206};
GN ORFNames=PEX2_009280 {ECO:0000313|EMBL:KGO51361.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO51361.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO51361.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO51361.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(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:0000256|ARBA:ARBA00002983}.
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:0000256|ARBA:ARBA00000043};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGO51361.1}.
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DR EMBL; JQFZ01000288; KGO51361.1; -; Genomic_DNA.
DR RefSeq; XP_016594314.1; XM_016738205.1.
DR AlphaFoldDB; A0A0A2I076; -.
DR STRING; 27334.A0A0A2I076; -.
DR GeneID; 27673624; -.
DR HOGENOM; CLU_013253_3_4_1; -.
DR OrthoDB; 615305at2759; -.
DR PhylomeDB; A0A0A2I076; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..399
FT /note="penicillopepsin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009752317"
FT DOMAIN 86..396
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 104
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 288
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 117..122
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 322..355
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 399 AA; 43487 MW; 77778E19B739A160 CRC64;
MMKSFTLLTA SALLGSAAAE VHRLKLNKVP LSEQLNTHNI DAHVHNLGQK YMGIRPEKHQ
DLFHDTSLNP ASGHGVLVDN FLNAQYFSEI TIGTPPQTFK VVLDTGSSNL WVPSSQCSSI
ACFLHSKYDS SSSSTYQKNG TEFEIRYGSG SLSGFVSRDT LQIGDLKVEG QDFAEATNEP
GLAFAFGRFD GILGLGYDTI SVNKMVPPFY HMINQKLVDE PVFAFYLGDT NKDGDDSVAT
FGGIDESHYT GELIKIPLRR KAYWEVELNS IALGNNVAEL DNTGVILDTG TSLIALPSTM
AELLNKEIGA TKGFTGQYSV ECDKRDSLPD LTFTLGGHKF TIGPFDYILE VQGSCISSFM
GMDFPEPVGP LAILGDAFLR RWYSVYDVGN NAVGLAKAK
//