CLIT5_CLINE
ID CLIT5_CLINE Reviewed; 152 AA.
AC Q3Y9I6;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 32.
DE RecName: Full=Clitocypin-5;
DE AltName: Full=Cysteine protease inhibitor clt5;
GN Name=clt5;
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 [MRNA].
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 PROTEIN SEQUENCE OF 2-9, FUNCTION, SUBUNIT, AND MASS SPECTROMETRY.
RX PubMed=17223361; DOI=10.1016/j.pep.2006.11.015;
RA Sabotic J., Galesa K., Popovic T., Leonardi A., Brzin J.;
RT "Comparison of natural and recombinant clitocypins, the fungal cysteine
RT protease inhibitors.";
RL Protein Expr. Purif. 53:104-111(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF COMPLEX WITH CATHEPSIN L2.
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:0000269|PubMed:17223361}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17223361}.
CC -!- SUBCELLULAR LOCATION: Note=Not secreted.
CC {ECO:0000250|UniProtKB:Q9P4A2}.
CC -!- MASS SPECTROMETRY: Mass=16701; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:17223361};
CC -!- SIMILARITY: Belongs to the protease inhibitor I48 family.
CC {ECO:0000305}.
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DR EMBL; DQ150588; AAZ78481.1; -; mRNA.
DR PDB; 3H6S; X-ray; 2.22 A; E/F/G/H=1-152.
DR PDBsum; 3H6S; -.
DR AlphaFoldDB; Q3Y9I6; -.
DR SMR; Q3Y9I6; -.
DR MEROPS; I48.001; -.
DR EvolutionaryTrace; Q3Y9I6; -.
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; Direct protein sequencing; Protease inhibitor;
KW Thiol protease inhibitor.
FT CHAIN 1..152
FT /note="Clitocypin-5"
FT /id="PRO_0000397841"
FT STRAND 6..17
FT /evidence="ECO:0007829|PDB:3H6S"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:3H6S"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:3H6S"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:3H6S"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3H6S"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:3H6S"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:3H6S"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3H6S"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3H6S"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:3H6S"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:3H6S"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3H6S"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:3H6S"
FT STRAND 129..136
FT /evidence="ECO:0007829|PDB:3H6S"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3H6S"
SQ SEQUENCE 152 AA; 16833 MW; 7F6A917E9AF6A479 CRC64;
MASLEDGTYR LRAVTTSNPD PGVGGEYATV EGARQPVKAE PSTPPFFERQ IWQVTRNSDG
QSTIKYQGLN APFEYGFSYD QLEQNAPVIA GDPKEYILQL VPSTTDVYII RAPIQRVGVD
VEVGVQGNNL VYKFFPVDGS GGDRPAWRFT RE
