ID CASP1_MOUSE Reviewed; 402 AA. AC P29452; DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot. DT 01-APR-1993, sequence version 1. DT 16-DEC-2008, entry version 90. DE RecName: Full=Caspase-1; DE Short=CASP-1; DE EC=3.4.22.36; DE AltName: Full=Interleukin-1 beta convertase; DE Short=IL-1BC; DE AltName: Full=Interleukin-1 beta-converting enzyme; DE Short=IL-1 beta-converting enzyme; DE Short=ICE; DE AltName: Full=p45; DE Contains: DE RecName: Full=Caspase-1 subunit p20; DE Contains: DE RecName: Full=Caspase-1 subunit p10; DE Flags: Precursor; GN Name=Casp1; Synonyms=Il1bc; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=93056487; PubMed=1431103; RA Nett-Fiordalisi M.A., Cerretti D.P., Berson D.R., Gilbert D.J., RA Jenkins N.A., Copeland N.G., Black R.A., Chaplin D.D.; RT "Molecular cloning of the murine IL-1 beta converting enzyme cDNA."; RL J. Immunol. 149:3254-3259(1992). RN [2] RP NUCLEOTIDE SEQUENCE. RX MEDLINE=93189587; PubMed=8446594; RA Molineaux S.M., Casano F.J., Rolando A.M., Peterson E.P., Limjuco G., RA Chin J., Griffin P.R., Calaycay J.R., Ding G.J.-F., Yamin T.-T., RA Palyha O.C., Luell S., Fletcher D., Miller D.K., Howard A.D., RA Thornberry N.A., Kostura M.J.; RT "Interleukin 1 beta (IL-1 beta) processing in murine macrophages RT requires a structurally conserved homologue of human IL-1 beta RT converting enzyme."; RL Proc. Natl. Acad. Sci. U.S.A. 90:1809-1813(1993). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129; RX MEDLINE=94307735; PubMed=8034321; DOI=10.1006/geno.1994.1203; RA Casano F.J., Rolando A.M., Mudgett J.S., Molineaux S.M.; RT "The structure and complete nucleotide sequence of the murine gene RT encoding interleukin-1 beta converting enzyme (ICE)."; RL Genomics 20:474-481(1994). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Mammary gland; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP CHARACTERIZATION. RC STRAIN=C3H/An; RX MEDLINE=97190206; PubMed=9038361; DOI=10.1016/S0014-5793(97)00026-4; RA van de Craen M., Vandenabeele P., Declercq W., van den Brande I., RA van Loo G., Molemans F., Schotte P., van Criekinge W., Beyaert R., RA Fiers W.; RT "Characterization of seven murine caspase family members."; RL FEBS Lett. 403:61-69(1997). CC -!- FUNCTION: Thiol protease that cleaves IL-1 beta between an Asp and CC an Ala, releasing the mature cytokine which is involved in a CC variety of inflammatory processes. Important for defense against CC pathogens. Cleaves and activates sterol regulatory element binding CC proteins (SREBPs). Can also promote apoptosis. CC -!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at CC position P1 and has a preferred cleavage sequence of Tyr-Val-Ala- CC Asp-|-. CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel CC arranged heterodimers, each one formed by a 20 kDa (p20) and a 10 CC kDa (p10) subunit. The p20 subunit can also form a heterodimer CC with the epsilon isoform which then has an inhibitory effect. May CC be a component of the inflammasome, a protein complex which also CC includes PYCARD, CARD8 and NALP2 and whose function would be the CC activation of proinflammatory caspases. Interacts with INCA (By CC similarity). CC -!- INTERACTION: CC P18011:ipaB (xeno); NbExp=3; IntAct=EBI-489700, EBI-490239; CC Q56134:sipB (xeno); NbExp=2; IntAct=EBI-489700, EBI-489689; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- TISSUE SPECIFICITY: High level expression seen in spleen and lung, CC low level expression seen in brain, heart, liver, kidney, testis CC and skeletal muscle. CC -!- PTM: The two subunits are derived from the precursor sequence by a CC autocatalytic mechanism. CC -!- SIMILARITY: Belongs to the peptidase C14A family. CC -!- SIMILARITY: Contains 1 CARD domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L03799; AAA39306.1; -; mRNA. DR EMBL; L28095; AAA20209.1; -; mRNA. DR EMBL; U04269; AAA56992.1; -; Genomic_DNA. DR EMBL; BC008152; AAH08152.1; -; mRNA. DR PIR; A46495; A46495. DR RefSeq; NP_033937.2; -. DR RefSeq; XP_001471691.1; -. DR UniGene; Mm.1051; -. DR HSSP; P29466; 1ICE. DR SMR; P29452; 315-402. DR IntAct; P29452; 2. DR MEROPS; C14.001; -. DR PhosphoSite; P29452; -. DR PRIDE; P29452; -. DR Ensembl; ENSMUSG00000025888; Mus musculus. DR GeneID; 100044207; -. DR GeneID; 12362; -. DR KEGG; mmu:100044207; -. DR KEGG; mmu:12362; -. DR MGI; MGI:96544; Casp1. DR HOGENOM; P29452; -. DR HOVERGEN; P29452; -. DR NextBio; 457711; -. DR ArrayExpress; P29452; -. DR CleanEx; MM_CASP1; -. DR GermOnline; ENSMUSG00000025888; Mus musculus. DR GO; GO:0005737; C:cytoplasm; TAS:MGI. DR GO; GO:0005576; C:extracellular region; IDA:MGI. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006917; P:induction of apoptosis; IDA:MGI. DR GO; GO:0050717; P:positive regulation of interleukin-1 alpha ...; IMP:MGI. DR GO; GO:0050718; P:positive regulation of interleukin-1 beta s...; IMP:MGI. DR GO; GO:0016485; P:protein processing; IDA:MGI. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR GO; GO:0033198; P:response to ATP; IMP:MGI. DR GO; GO:0001666; P:response to hypoxia; IMP:MGI. DR InterPro; IPR001315; CARD. DR InterPro; IPR017350; Caspase_IL-1_beta. DR InterPro; IPR011029; DEATH_like. DR InterPro; IPR011600; Pept_C14_cat. DR InterPro; IPR001309; Pept_C14_ICE_p20. DR InterPro; IPR016129; Pept_C14_ICE_p20_AS. DR InterPro; IPR002138; Pept_C14_p10. DR InterPro; IPR002398; Pept_C14_p45. DR InterPro; IPR015917; Pept_C14_p45_core. DR Gene3D; G3DSA:1.10.533.10; DEATH_like; 1. DR PANTHER; PTHR10454; Pept_C14_p45; 1. DR Pfam; PF00619; CARD; 1. DR Pfam; PF00656; Peptidase_C14; 1. DR PIRSF; PIRSF038001; Caspase_ICE; 1. DR PRINTS; PR00376; IL1BCENZYME. DR SMART; SM00114; CARD; 1. DR SMART; SM00115; CASc; 1. DR PROSITE; PS50209; CARD; 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 Apoptosis; Cytoplasm; Hydrolase; Protease; Thiol protease; Zymogen. FT PROPEP 1 ?118 Potential. FT /FTId=PRO_0000004525. FT CHAIN ?119 296 Caspase-1 subunit p20. FT /FTId=PRO_0000004526. FT PROPEP 297 314 Potential. FT /FTId=PRO_0000004527. FT CHAIN 315 402 Caspase-1 subunit p10. FT /FTId=PRO_0000004528. FT DOMAIN 1 91 CARD. FT ACT_SITE 236 236 By similarity. FT ACT_SITE 284 284 By similarity. FT CONFLICT 3 6 DKIL -> V (in Ref. 3). SQ SEQUENCE 402 AA; 45640 MW; 3BEBCEFA67C69B03 CRC64; MADKILRAKR KQFINSVSIG TINGLLDELL EKRVLNQEEM DKIKLANITA MDKARDLCDH VSKKGPQASQ IFITYICNED CYLAGILELQ SAPSAETFVA TEDSKGGHPS SSETKEEQNK EDGTFPGLTG TLKFCPLEKA QKLWKENPSE IYPIMNTTTR TRLALIICNT EFQHLSPRVG AQVDLREMKL LLEDLGYTVK VKENLTALEM VKEVKEFAAC PEHKTSDSTF LVFMSHGIQE GICGTTYSNE VSDILKVDTI FQMMNTLKCP SLKDKPKVII IQACRGEKQG VVLLKDSVRD SEEDFLTDAI FEDDGIKKAH IEKDFIAFCS STPDNVSWRH PVRGSLFIES LIKHMKEYAW SCDLEDIFRK VRFSFEQPEF RLQMPTADRV TLTKRFYLFP GH //