CASP1_SPOFR
ID CASP1_SPOFR Reviewed; 299 AA.
AC P89116;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Caspase-1;
DE EC=3.4.22.-;
DE Contains:
DE RecName: Full=Caspase-1 subunit p19/18;
DE Contains:
DE RecName: Full=Caspase-1 subunit p12;
DE Flags: Precursor;
OS Spodoptera frugiperda (Fall armyworm).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Noctuoidea;
OC Noctuidae; Amphipyrinae; Spodoptera.
OX NCBI_TaxID=7108;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8999805; DOI=10.1074/jbc.272.3.1421;
RA Ahmad M., Srinivasula S.M., Wang L., Litwack G., Fernandes-Alnemri T.,
RA Alnemri E.S.;
RT "Spodoptera frugiperda caspase-1, a novel insect death protease that
RT cleaves the nuclear immunophilin FKBP46, is the target of the baculovirus
RT antiapoptotic protein p35.";
RL J. Biol. Chem. 272:1421-1424(1997).
CC -!- FUNCTION: Involved in the activation cascade of caspases responsible
CC for apoptosis execution (By similarity). Inhibited by the baculovirus
CC anti-apoptotic protein p35. Cleaves p35 and nuclear immunophilin
CC FKBP46. {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 19/18 kDa (p19/18) and a 12 kDa
CC (p12) subunit.
CC -!- PTM: The two subunits are derived from the precursor sequence by an
CC autocatalytic mechanism.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR EMBL; U81510; AAC47442.1; -; mRNA.
DR PDB; 1M72; X-ray; 2.30 A; A/B/C=29-299.
DR PDB; 2NN3; X-ray; 3.00 A; C/D=1-299.
DR PDBsum; 1M72; -.
DR PDBsum; 2NN3; -.
DR AlphaFoldDB; P89116; -.
DR SMR; P89116; -.
DR MEROPS; C14.015; -.
DR BRENDA; 3.4.22.36; 5836.
DR EvolutionaryTrace; P89116; -.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:UniProt.
DR CDD; cd00032; CASc; 1.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR002398; Pept_C14.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Direct protein sequencing; Hydrolase; Protease;
KW Thiol protease; Zymogen.
FT PROPEP 1..28
FT /id="PRO_0000004658"
FT CHAIN 29..184
FT /note="Caspase-1 subunit p19/18"
FT /id="PRO_0000004659"
FT PROPEP 185..195
FT /evidence="ECO:0000255"
FT /id="PRO_0000004660"
FT CHAIN 196..299
FT /note="Caspase-1 subunit p12"
FT /id="PRO_0000004661"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 136
FT /evidence="ECO:0000250"
FT ACT_SITE 178
FT /evidence="ECO:0000250"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:1M72"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:1M72"
FT HELIX 108..119
FT /evidence="ECO:0007829|PDB:1M72"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2NN3"
FT STRAND 126..135
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:1M72"
FT HELIX 153..156
FT /evidence="ECO:0007829|PDB:1M72"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:1M72"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:1M72"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:1M72"
FT HELIX 231..243
FT /evidence="ECO:0007829|PDB:1M72"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:1M72"
FT HELIX 249..263
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:2NN3"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 282..285
FT /evidence="ECO:0007829|PDB:1M72"
FT STRAND 288..290
FT /evidence="ECO:0007829|PDB:1M72"
SQ SEQUENCE 299 AA; 33527 MW; 99F4FED09B04EEDE CRC64;
MLDGKQDNGN VDSVDIKQRT NGGGDEGDAL GSNSSSQPNR VARMPVDRNA PYYNMNHKHR
GMAIIFNHEH FDIHSLKSRT GTNVDSDNLS KVLKTLGFKV TVFPNLKSEE INKFIQQTAE
MDHSDADCLL VAVLTHGELG MLYAKDTHYK PDNLWYYFTA DKCPTLAGKP KLFFIQACQG
DRLDGGITLS RTETDGSPST SYRIPVHADF LIAFSTVPGY FSWRNTTRGS WFMQALCEEL
RYAGTERDIL TLLTFVCQKV ALDFESNAPD SAMMHQQKQV PCITSMLTRL LVFGKKQSH
