ID   CLIT2_CLINE             Reviewed;         152 AA.
AC   Q3Y9I4;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Clitocypin-2;
DE   AltName: Full=Cysteine protease inhibitor clt2;
GN   Name=clt2;
OS   Clitocybe nebularis (Clouded agaric) (Lepista nebularis).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomataceae; Clitocybe.
OX   NCBI_TaxID=117024;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Kras2004;
RX   PubMed=17132101; DOI=10.1515/bc.2006.194;
RA   Sabotic J., Gaser D., Rogelj B., Gruden K., Strukelj B., Brzin J.;
RT   "Heterogeneity in the cysteine protease inhibitor clitocypin gene family.";
RL   Biol. Chem. 387:1559-1566(2006).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), AND MUTAGENESIS OF GLY-24 AND
RP   ASN-70.
RX   PubMed=19846555; DOI=10.1074/jbc.m109.043331;
RA   Renko M., Sabotic J., Mihelic M., Brzin J., Kos J., Turk D.;
RT   "Versatile loops in mycocypins inhibit three protease families.";
RL   J. Biol. Chem. 285:308-316(2010).
CC   -!- FUNCTION: Binds and inhibits cysteine proteinases. Inhibits most
CC       strongly papain and cathepsin L, more weakly bromelain and cathepsin B
CC       while it is completely ineffective against cathepsin H.
CC       {ECO:0000250|UniProtKB:Q9P4A2}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9P4A2}.
CC   -!- SUBCELLULAR LOCATION: Note=Not secreted.
CC       {ECO:0000250|UniProtKB:Q9P4A2}.
CC   -!- TISSUE SPECIFICITY: Expressed in all analyzed tissues, but expression
CC       was higher in the pileus and in the lower part of the stipe.
CC       {ECO:0000269|PubMed:17132101}.
CC   -!- SIMILARITY: Belongs to the protease inhibitor I48 family.
CC       {ECO:0000305}.
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DR   EMBL; DQ150590; AAZ78483.1; -; Genomic_DNA.
DR   PDB; 3H6R; X-ray; 1.95 A; A/B=1-152.
DR   PDBsum; 3H6R; -.
DR   AlphaFoldDB; Q3Y9I4; -.
DR   SMR; Q3Y9I4; -.
DR   MEROPS; I48.001; -.
DR   EvolutionaryTrace; Q3Y9I4; -.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   InterPro; IPR019508; Prot_inh_I48_clitocypin.
DR   Pfam; PF10467; Inhibitor_I48; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Protease inhibitor; Thiol protease inhibitor.
FT   CHAIN           1..152
FT                   /note="Clitocypin-2"
FT                   /id="PRO_0000397840"
FT   MUTAGEN         24
FT                   /note="G->A: 20-fold lower inhibition."
FT                   /evidence="ECO:0000269|PubMed:19846555"
FT   MUTAGEN         70
FT                   /note="N->K: No inhibition of asparaginyl endopeptidase."
FT                   /evidence="ECO:0000269|PubMed:19846555"
FT   STRAND          6..19
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          38..42
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   TURN            44..46
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          52..56
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          62..69
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          76..78
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          89..92
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          96..100
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          105..111
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          119..126
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          129..136
FT                   /evidence="ECO:0007829|PDB:3H6R"
FT   STRAND          145..151
FT                   /evidence="ECO:0007829|PDB:3H6R"
SQ   SEQUENCE   152 AA;  16953 MW;  094163919603738A CRC64;
     MASLEDGIYR LRAVTTHNPD PGVGGEYATV EGARRPVKAE PNTPPFFEQQ IWQVTRNADG
     QYTIKYQGLN TPFEYGFSYD ELEPNAPVIA GDPKEYILQL VPSTADVYII RAPIQRIGVD
     VEVGVQGNTL VYKFFPVDGS GGDRPAWRFT RE