ID   PLNC_PENCI              Reviewed;         351 AA.
AC   P47189;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Penicillolysin;
DE            EC=3.4.24.39;
DE   AltName: Full=Deuterolysin;
DE   Flags: Precursor;
GN   Name=plnC;
OS   Penicillium citrinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5077;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=NBRC 6026 / FAT 1131;
RX   PubMed=8049277; DOI=10.1016/0167-4781(94)90209-7;
RA   Matsumoto K., Yamaguchi M., Ichishima E.;
RT   "Molecular cloning and nucleotide sequence of the complementary DNA for
RT   penicillolysin gene, plnC, and 18 kDa metalloendopeptidase gene from
RT   Penicillium citrinum.";
RL   Biochim. Biophys. Acta 1218:469-472(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of bonds with hydrophobic residues in
CC         P1'. Also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.;
CC         EC=3.4.24.39;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR   EMBL; D25535; BAA05018.1; -; mRNA.
DR   PIR; S47635; S47635.
DR   AlphaFoldDB; P47189; -.
DR   SMR; P47189; -.
DR   MEROPS; M35.001; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR001384; Peptidase_M35.
DR   Pfam; PF02102; Peptidase_M35; 1.
DR   PRINTS; PR00768; DEUTEROLYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease; Signal;
KW   Zinc; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..174
FT                   /id="PRO_0000029234"
FT   CHAIN           175..351
FT                   /note="Penicillolysin"
FT                   /id="PRO_0000029235"
FT   ACT_SITE        303
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         302
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         306
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         317
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   CARBOHYD        52
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   351 AA;  37387 MW;  5FA83F285F2E2F16 CRC64;
     MRFTTLSTAF LALAQNVYAF PIESDLSALD VTLSQVSDTR IKAVVKNTGA ENVTFVHLNF
     FRDSAPVKKV SVYRENNEVV FDGIKRRFQL QGLASESLTT LEAGEVLEDE FDIATTTDLS
     SGGAITLRSN GLVPVVKDGA VTGYLPYSSN DLKLNIDGAK ASTVTKALKP LDRRTKETCS
     NASRKSALEK ALSNTVKLAN AAATAARSGS ASKFSEYFKT TSSSTRSVVA ARLEAVAKEA
     QSASSGSTTY YCSDTLGYCE TNVLAYTLPA RNIIANCDIY YSYLPALAGT CHQQDQATTT
     LHEFTHAPGV YSPGTDDLGY GYSAATSLSS SQAVLNADSY ALYANAINLG C