MCP1A_MACPC
ID MCP1A_MACPC Reviewed; 169 AA.
AC B9V973;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 20.
DE RecName: Full=Macrocypin-1a;
OS Macrolepiota procera (Parasol mushroom).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricaceae; Macrolepiota.
OX NCBI_TaxID=56183;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN
RP SEQUENCE OF 2-46, AND FUNCTION.
RC TISSUE=Fruiting body;
RX PubMed=19678836; DOI=10.1111/j.1742-4658.2009.07138.x;
RA Sabotic J., Popovic T., Puizdar V., Brzin J.;
RT "Macrocypins, a family of cysteine protease inhibitors from the
RT basidiomycete Macrolepiota procera.";
RL FEBS J. 276:4334-4345(2009).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS), AND MUTAGENESIS OF GLY-25.
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: Inhibits papain and cysteine cathepsin endopeptidases, and
CC also inhibits cathepsins B and H, which exhibit both exopeptidase and
CC endopeptidase activities. {ECO:0000269|PubMed:19678836}.
CC -!- SIMILARITY: Belongs to the protease inhibitor I85 family.
CC {ECO:0000305}.
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DR EMBL; FJ495239; ACL99723.1; -; mRNA.
DR EMBL; FJ495240; ACL99724.1; -; Genomic_DNA.
DR PDB; 3H6Q; X-ray; 1.64 A; A=1-169.
DR PDBsum; 3H6Q; -.
DR AlphaFoldDB; B9V973; -.
DR SMR; B9V973; -.
DR MEROPS; I85.001; -.
DR GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Protease inhibitor;
KW Thiol protease inhibitor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:19678836"
FT CHAIN 2..169
FT /note="Macrocypin-1a"
FT /id="PRO_0000397842"
FT MUTAGEN 25
FT /note="G->A: 20-fold lower inhibition."
FT /evidence="ECO:0000269|PubMed:19846555"
FT CONFLICT 3
FT /note="F -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 7
FT /note="F -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="L -> R (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="A -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 18
FT /note="H -> P (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 21..22
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="G -> P (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 6..13
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:3H6Q"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:3H6Q"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 131..140
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 143..151
FT /evidence="ECO:0007829|PDB:3H6Q"
FT STRAND 161..167
FT /evidence="ECO:0007829|PDB:3H6Q"
SQ SEQUENCE 169 AA; 19194 MW; F6500168477E4957 CRC64;
MGFEDGFYTI LHLAEGQHPN SKIPGGMYAS SKDGKDVPVT AEPLGPQSKI RWWIARDPQA
GDDMYTITEF RIDNSIPGQW SRSPVETEVP VYLYDRIKAE ETGYTCAWRI QPADHGADGV
YHIVGNVRIG STDWADLREE YGEPQVYMKP VPVIPNVYIP RWFILGYEE