ID CASP7_MOUSE Reviewed; 303 AA. AC P97864; O08669; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 02-SEP-2026, entry version 207. DE RecName: Full=Caspase-7 {ECO:0000303|PubMed:9070923}; DE Short=CASP-7 {ECO:0000303|PubMed:9070923}; DE EC=3.4.22.60 {ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:35705808}; DE AltName: Full=Apoptotic protease Mch-3; DE AltName: Full=Cysteine protease LICE2; DE Contains: DE RecName: Full=Caspase-7 subunit p20; DE Contains: DE RecName: Full=Caspase-7 subunit p11; DE Flags: Precursor; GN Name=Casp7 {ECO:0000303|PubMed:9070923, ECO:0000312|MGI:MGI:109383}; GN Synonyms=Lice2, Mch3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Skeletal muscle; RX PubMed=9070923; DOI=10.1006/geno.1996.4548; RA Juan T.S.-C., McNiece I.K., Argento J.M., Jenkins N.A., Gilbert D.J., RA Copeland N.G., Fletcher F.A.; RT "Identification and mapping of Casp7, a cysteine protease resembling CPP32 RT beta, interleukin-1 beta converting enzyme, and CED-3."; RL Genomics 40:86-93(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=9125129; DOI=10.1006/bbrc.1997.6234; RA Mukasa T., Khoroku Y., Tsukahara T., Momoi M.Y., Kimura I., Momoi T.; RT "Wortmannin enhances CPP32-like activity during neuronal differentiation of RT P19 embryonal carcinoma cells induced by retinoic acid."; RL Biochem. Biophys. Res. Commun. 232:192-197(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=C3H/An; RX 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). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [6] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=16469926; DOI=10.1126/science.1115035; RA Lakhani S.A., Masud A., Kuida K., Porter G.A. Jr., Booth C.J., Mehal W.Z., RA Inayat I., Flavell R.A.; RT "Caspases 3 and 7: key mediators of mitochondrial events of apoptosis."; RL Science 311:847-851(2006). RN [7] RP ACTIVITY REGULATION, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ASP-23 AND RP ASP-198. RX PubMed=18667412; DOI=10.1074/mcp.m800132-mcp200; RA Lamkanfi M., Kanneganti T.D., Van Damme P., Vanden Berghe T., RA Vanoverberghe I., Vandekerckhove J., Vandenabeele P., Gevaert K., Nunez G.; RT "Targeted peptidecentric proteomics reveals caspase-7 as a substrate of the RT caspase-1 inflammasomes."; RL Mol. Cell. Proteomics 7:2350-2363(2008). RN [8] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=19168786; DOI=10.1182/blood-2008-09-178038; RA Lamkanfi M., Moreira L.O., Makena P., Spierings D.C., Boyd K., Murray P.J., RA Green D.R., Kanneganti T.D.; RT "Caspase-7 deficiency protects from endotoxin-induced lymphocyte apoptosis RT and improves survival."; RL Blood 113:2742-2745(2009). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Heart, Kidney, Liver, Lung, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [10] RP FUNCTION. RX PubMed=22464733; DOI=10.1016/j.molcel.2012.02.016; RA Erener S., Petrilli V., Kassner I., Minotti R., Castillo R., Santoro R., RA Hassa P.O., Tschopp J., Hottiger M.O.; RT "Inflammasome-activated caspase 7 cleaves PARP1 to enhance the expression RT of a subset of NF-kappaB target genes."; RL Mol. Cell 46:200-211(2012). RN [11] RP FUNCTION, AND PROTEOLYTIC CLEAVAGE. RX PubMed=22807671; DOI=10.1371/journal.ppat.1002628; RA Cassidy S.K., Hagar J.A., Kanneganti T.D., Franchi L., Nunez G., RA O'Riordan M.X.; RT "Membrane damage during Listeria monocytogenes infection triggers a RT caspase-7 dependent cytoprotective response."; RL PLoS Pathog. 8:e1002628-e1002628(2012). RN [12] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=25231987; DOI=10.1074/jbc.m114.583419; RA Suzuki J., Imanishi E., Nagata S.; RT "Exposure of phosphatidylserine by Xk-related protein family members during RT apoptosis."; RL J. Biol. Chem. 289:30257-30267(2014). RN [13] RP FUNCTION. RX PubMed=30878284; DOI=10.1016/j.molcel.2019.02.013; RA Ning X., Wang Y., Jing M., Sha M., Lv M., Gao P., Zhang R., Huang X., RA Feng J.M., Jiang Z.; RT "Apoptotic caspases suppress type i interferon production via the cleavage RT of cGAS, MAVS, and IRF3."; RL Mol. Cell 74:19-31(2019). RN [14] RP PROTEOLYTIC CLEAVAGE. RX PubMed=31251782; DOI=10.1371/journal.ppat.1007886; RA Goncalves A.V., Margolis S.R., Quirino G.F.S., Mascarenhas D.P.A., RA Rauch I., Nichols R.D., Ansaldo E., Fontana M.F., Vance R.E., Zamboni D.S.; RT "Gasdermin-D and Caspase-7 are the key Caspase-1/8 substrates downstream of RT the NAIP5/NLRC4 inflammasome required for restriction of Legionella RT pneumophila."; RL PLoS Pathog. 15:e1007886-e1007886(2019). RN [15] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RP AND PROTEOLYTIC CLEAVAGE. RX PubMed=35705808; DOI=10.1038/s41586-022-04825-8; RA Nozaki K., Maltez V.I., Rayamajhi M., Tubbs A.L., Mitchell J.E., RA Lacey C.A., Harvest C.K., Li L., Nash W.T., Larson H.N., McGlaughon B.D., RA Moorman N.J., Brown M.G., Whitmire J.K., Miao E.A.; RT "Caspase-7 activates ASM to repair gasdermin and perforin pores."; RL Nature 0:0-0(2022). CC -!- FUNCTION: Thiol protease involved in different programmed cell death CC processes, such as apoptosis, pyroptosis or granzyme-mediated CC programmed cell death, by proteolytically cleaving target proteins CC (PubMed:16469926, PubMed:19168786). Has a marked preference for Asp- CC Glu-Val-Asp (DEVD) consensus sequences, with some plasticity for CC alternate non-canonical sequences (PubMed:25231987). Its involvement in CC the different programmed cell death processes is probably determined by CC upstream proteases that activate CASP7 (PubMed:18667412, CC PubMed:35705808). Acts as an effector caspase involved in the execution CC phase of apoptosis: following cleavage and activation by initiator CC caspases (CASP8 and/or CASP9), mediates execution of apoptosis by CC catalyzing cleavage of proteins, such as CLSPN, PARP1, PTGES3 and YY1 CC (PubMed:16469926). Compared to CASP3, acts as a minor executioner CC caspase and cleaves a limited set of target proteins (PubMed:16469926). CC Acts as a key regulator of the inflammatory response in response to CC bacterial infection by catalyzing cleavage and activation of the CC sphingomyelin phosphodiesterase SMPD1 in the extracellular milieu, CC thereby promoting membrane repair (PubMed:35705808). Regulates CC pyroptosis in intestinal epithelial cells: cleaved and activated by CC CASP1 in response to S.typhimurium infection, promoting its secretion CC to the extracellular milieu, where it catalyzes activation of SMPD1, CC generating ceramides that repair membranes and counteract the action of CC gasdermin-D (GSDMD) pores (PubMed:22807671, PubMed:35705808). Regulates CC granzyme-mediated programmed cell death in hepatocytes: cleaved and CC activated by granzyme B (GZMB) in response to bacterial infection, CC promoting its secretion to the extracellular milieu, where it catalyzes CC activation of SMPD1, generating ceramides that repair membranes and CC counteract the action of perforin (PRF1) pores (PubMed:35705808). CC Following cleavage by CASP1 in response to inflammasome activation, CC catalyzes processing and inactivation of PARP1, alleviating the CC transcription repressor activity of PARP1 (PubMed:22464733). Acts as an CC inhibitor of type I interferon production during virus-induced CC apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and CC MAVS, thereby preventing cytokine overproduction (PubMed:30878284). CC Cleaves and activates sterol regulatory element binding proteins CC (SREBPs) (By similarity). Cleaves phospholipid scramblase proteins CC XKR4, XKR8 and XKR9 (PubMed:25231987). Cleaves BIRC6 following CC inhibition of BIRC6-caspase binding by DIABLO/SMAC (By similarity). CC {ECO:0000250|UniProtKB:P55210, ECO:0000269|PubMed:16469926, CC ECO:0000269|PubMed:18667412, ECO:0000269|PubMed:19168786, CC ECO:0000269|PubMed:22464733, ECO:0000269|PubMed:22807671, CC ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:30878284, CC ECO:0000269|PubMed:35705808}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Strict requirement for an Asp residue at position P1 and has a CC preferred cleavage sequence of Asp-Glu-Val-Asp-|-.; EC=3.4.22.60; CC Evidence={ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:35705808}; CC -!- ACTIVITY REGULATION: During activation, the N-terminal disordered CC prodomain is removed by cleavage (PubMed:18667412). Concomitantly, CC double cleavage gives rise to a large Caspase-7 subunit p20 and a small CC Caspase-7 subunit p11 (PubMed:18667412). The two large and two small CC subunits then assemble to form the active CASP7 complex CC (PubMed:18667412). Can be cleaved and activated by different caspases, CC depending on the context (PubMed:18667412, PubMed:35705808). Cleaved CC and activated by initiator caspases (CASP8 and/or CASP9), leading to CC execution phase of apoptosis (By similarity). Cleavage and maturation CC by GZMB regulates granzyme-mediated programmed cell death CC (PubMed:35705808). Cleavage and maturation by CASP1 regulates CC pyroptosis (PubMed:18667412, PubMed:35705808). Inhibited by XIAP, which CC directly binds to the active site pocket and obstructs substrate entry CC (By similarity). Phosphorylation at Ser-30 and Ser-239 by PAK2 inhibits CC its activity (By similarity). Inhibited by BIRC6; following inhibition CC of BIRC6-caspase binding by DIABLO/SMAC, BIRC6 is subjected to caspase CC cleavage, leading to an increase in active caspases (By similarity). CC {ECO:0000250|UniProtKB:P42574, ECO:0000250|UniProtKB:P55210, CC ECO:0000269|PubMed:18667412, ECO:0000269|PubMed:35705808}. CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged CC heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11) CC subunit (By similarity). Interacts with XIAP (via its second BIR CC domain); inhibiting CASP7 activity (By similarity). Interacts with CC BIRC6/bruce. Interacts with ATXN3 (short isoform 1) (By similarity). CC Interacts with HSPA5 (By similarity). {ECO:0000250|UniProtKB:P55210}. CC -!- INTERACTION: CC P97864; P11103: Parp1; NbExp=3; IntAct=EBI-5307197, EBI-642213; CC P97864; P62270: Rps18; NbExp=4; IntAct=EBI-5307197, EBI-352460; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:P55210}. Nucleus {ECO:0000250|UniProtKB:P55210}. CC Secreted, extracellular space {ECO:0000269|PubMed:35705808}. CC Note=Following cleavage and activation by CASP1 or granzyme B (GZMB), CC secreted into the extracellular milieu by passing through the CC gasdermin-D (GSDMD) pores or perforin (PRF1) pore, respectively. CC {ECO:0000269|PubMed:35705808}. CC -!- TISSUE SPECIFICITY: Highly expressed in heart, lung, liver and kidney. CC Low levels in spleen, skeletal muscle and testis. No expression in the CC brain. {ECO:0000269|PubMed:9070923}. CC -!- DOMAIN: The exosite polybasic region mediates non-specific RNA-binding, CC acting as a bridge for RNA-binding target proteins, such as PARP1. The CC exosite is also required for interaction with non-RNA-binding proteins, CC such as Hsp90 co-chaperone PTGES3. {ECO:0000250|UniProtKB:P55210}. CC -!- PTM: Cleavage by different proteases, such as granzyme B (GZMB), CC caspase-1 (CASP1), caspase-8 (CASP8) or caspase-9 (CASP9) generate the CC two active subunits (PubMed:18667412, PubMed:22807671, PubMed:31251782, CC PubMed:35705808). Its involvement in different programmed cell death CC processes is probably specified by the protease that activates CASP7 CC (PubMed:35705808). Cleaved and activated by initiator caspases (CASP8 CC and/or CASP9), leading to execution phase of apoptosis (By similarity). CC Cleavage and maturation by GZMB regulates granzyme-mediated programmed CC cell death (PubMed:35705808). Cleaved and activated by CASP1 in CC response to bacterial infection (PubMed:18667412, PubMed:31251782, CC PubMed:35705808). Propeptide domains can also be cleaved efficiently by CC CASP3 (By similarity). Active heterodimers between the small subunit of CC caspase-7 and the large subunit of CASP3, and vice versa, also occur CC (By similarity). Also cleaved at the N-terminus at alternative sites by CC CAPN1, leading to its activation (By similarity). CC {ECO:0000250|UniProtKB:P55210, ECO:0000269|PubMed:18667412, CC ECO:0000269|PubMed:22807671, ECO:0000269|PubMed:31251782, CC ECO:0000269|PubMed:35705808}. CC -!- PTM: Phosphorylation at Ser-30 and Ser-239 by PAK2 inhibits its CC activity (By similarity). Phosphorylation at Ser-30 prevents cleavage CC and activation by initiator caspase CASP9, while phosphorylation at CC Ser-239 prevents thiol protease activity by preventing substrate- CC binding (By similarity). {ECO:0000250|UniProtKB:P55210}. CC -!- PTM: Ubiquitinated by BIRC6; this activity is inhibited by DIABLO/SMAC. CC {ECO:0000250|UniProtKB:P42574}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype; on the 129/Svj background, CC mice are healthy (PubMed:16469926). Mice display impaired CC lipopolysaccharide (LPS)-induced lymphocyte apoptosis and are markedly CC protected from LPS-induced lethality (PubMed:19168786). Mice lacking CC Casp3 and Casp7 on the C57BL/6J background die immediately after birth CC because of defective heart development (PubMed:16469926). CC {ECO:0000269|PubMed:16469926, ECO:0000269|PubMed:19168786}. CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC53068.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Delayed - Issue 252 of CC November 2022; CC URL="https://www.proteinspotlight.org/back_issues/252/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U67321; AAC53068.1; ALT_INIT; mRNA. DR EMBL; D86353; BAA19730.1; -; mRNA. DR EMBL; Y13088; CAA73530.1; -; mRNA. DR EMBL; BC005428; AAH05428.1; -; mRNA. DR CCDS; CCDS29915.1; -. DR RefSeq; NP_031637.1; NM_007611.3. DR AlphaFoldDB; P97864; -. DR SMR; P97864; -. DR BioGRID; 198499; 7. DR ComplexPortal; CPX-3947; Caspase-7 complex. DR FunCoup; P97864; 1465. DR IntAct; P97864; 10. DR STRING; 10090.ENSMUSP00000026062; -. DR ChEMBL; CHEMBL6066205; -. DR MEROPS; C14.004; -. DR iPTMnet; P97864; -. DR PhosphoSitePlus; P97864; -. DR jPOST; P97864; -. DR PaxDb; 10090-ENSMUSP00000026062; -. DR PeptideAtlas; P97864; -. DR ProteomicsDB; 265536; -. DR Pumba; P97864; -. DR Antibodypedia; 18528; 1104 antibodies from 50 providers. DR DNASU; 12369; -. DR Ensembl; ENSMUST00000026062.10; ENSMUSP00000026062.10; ENSMUSG00000025076.13. DR GeneID; 12369; -. DR KEGG; mmu:12369; -. DR UCSC; uc008hyw.1; mouse. DR AGR; MGI:109383; -. DR CTD; 840; -. DR MGI; MGI:109383; Casp7. DR VEuPathDB; HostDB:ENSMUSG00000025076; -. DR eggNOG; KOG3573; Eukaryota. DR GeneTree; ENSGT00940000153232; -. DR HOGENOM; CLU_036904_2_0_1; -. DR InParanoid; P97864; -. DR OMA; ENTGMNV; -. DR OrthoDB; 6116485at2759; -. DR PhylomeDB; P97864; -. DR BRENDA; 3.4.22.60; 3474. DR Reactome; R-MMU-111459; Activation of caspases through apoptosome-mediated cleavage. DR Reactome; R-MMU-111463; SMAC (DIABLO) binds to IAPs. DR Reactome; R-MMU-111464; SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes. DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins. DR Reactome; R-MMU-111469; SMAC, XIAP-regulated apoptotic response. DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins. DR BioGRID-ORCS; 12369; 4 hits in 78 CRISPR screens. DR PRO; PR:P97864; -. DR Proteomes; UP000000589; Chromosome 19. DR RNAct; P97864; protein. DR Bgee; ENSMUSG00000025076; Expressed in intestinal villus and 219 other cell types or tissues. DR ExpressionAtlas; P97864; baseline and differential. DR GO; GO:0008303; C:caspase complex; ISO:GO_Central. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB. DR GO; GO:0001650; C:fibrillar center; ISO:GO_Central. DR GO; GO:0005654; C:nucleoplasm; ISO:GO_Central. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISO:GO_Central. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:UniProtKB. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB. DR GO; GO:0008234; F:cysteine-type peptidase activity; ISO:GO_Central. DR GO; GO:0008233; F:peptidase activity; ISO:GO_Central. DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IGI:MGI. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:GO_Central. DR GO; GO:0072734; P:cellular response to staurosporine; ISO:GO_Central. DR GO; GO:0046513; P:ceramide biosynthetic process; ISO:GO_Central. DR GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB. DR GO; GO:0097194; P:execution phase of apoptosis; IGI:MGI. DR GO; GO:0007507; P:heart development; IGI:MGI. DR GO; GO:0070227; P:lymphocyte apoptotic process; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:GO_Central. DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI. DR GO; GO:0001778; P:plasma membrane repair; ISO:GO_Central. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:GO_Central. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISO:GO_Central. DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IBA:GO_Central. DR GO; GO:1905686; P:positive regulation of plasma membrane repair; IDA:UniProtKB. DR GO; GO:0030163; P:protein catabolic process; ISO:GO_Central. DR GO; GO:0051604; P:protein maturation; IDA:UniProt. DR GO; GO:0070212; P:protein poly-ADP-ribosylation; ISO:GO_Central. DR GO; GO:0016485; P:protein processing; IDA:MGI. DR GO; GO:0006508; P:proteolysis; ISO:GO_Central. DR GO; GO:0070269; P:pyroptotic inflammatory response; ISO:GO_Central. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:GO_Central. DR GO; GO:0009411; P:response to UV; IGI:MGI. DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl. DR CDD; cd00032; CASc; 1. DR FunFam; 3.30.70.1470:FF:000002; Caspase-3; 1. DR FunFam; 3.40.50.1460:FF:000001; Caspase-3 preproprotein; 1. DR Gene3D; 3.40.50.1460; -; 1. DR Gene3D; 3.30.70.1470; Caspase-like; 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; IPR011600; Pept_C14_caspase. DR InterPro; IPR002138; Pept_C14_p10. DR InterPro; IPR001309; Pept_C14_p20. DR InterPro; IPR015917; Pept_C14A. DR PANTHER; PTHR10454; CASPASE; 1. DR PANTHER; PTHR10454:SF31; CASPASE-7; 1. DR Pfam; PF00656; Peptidase_C14; 1. DR PIRSF; PIRSF038001; Caspase_ICE; 1. DR PRINTS; PR00376; IL1BCENZYME. DR SMART; SM00115; CASc; 1. DR SUPFAM; SSF52129; Caspase-like; 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 Acetylation; Allosteric enzyme; Apoptosis; Cytoplasm; Hydrolase; Nucleus; KW Phosphoprotein; Protease; Reference proteome; RNA-binding; Secreted; KW Thiol protease; Ubl conjugation; Zymogen. FT PROPEP 1..23 FT /evidence="ECO:0000305|PubMed:18667412" FT /id="PRO_0000004624" FT CHAIN 24..198 FT /note="Caspase-7 subunit p20" FT /evidence="ECO:0000305|PubMed:18667412" FT /id="PRO_0000004625" FT PROPEP 199..206 FT /evidence="ECO:0000305|PubMed:18667412" FT /id="PRO_0000004626" FT CHAIN 207..303 FT /note="Caspase-7 subunit p11" FT /evidence="ECO:0000250|UniProtKB:P55210" FT /id="PRO_0000004627" FT REGION 1..26 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 38..41 FT /note="Exosite" FT /evidence="ECO:0000250|UniProtKB:P55210" FT REGION 76..87 FT /note="Loop L1" FT /evidence="ECO:0000250|UniProtKB:P55210" FT REGION 187..196 FT /note="Loop L2" FT /evidence="ECO:0000250|UniProtKB:P55210" FT REGION 226..238 FT /note="Loop L3" FT /evidence="ECO:0000250|UniProtKB:P55210" FT REGION 274..288 FT /note="Loop L4" FT /evidence="ECO:0000250|UniProtKB:P55210" FT COMPBIAS 10..26 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 144 FT /evidence="ECO:0000250|UniProtKB:P29466" FT ACT_SITE 186 FT /evidence="ECO:0000250|UniProtKB:P55210" FT SITE 36..37 FT /note="Cleavage; by CAPN1" FT /evidence="ECO:0000250|UniProtKB:P55210" FT SITE 45..46 FT /note="Cleavage; by CAPN1" FT /evidence="ECO:0000250|UniProtKB:P55210" FT SITE 47..48 FT /note="Cleavage; by CAPN1" FT /evidence="ECO:0000250|UniProtKB:P55210" FT SITE 187 FT /note="Involved in allosteric regulation" FT /evidence="ECO:0000250|UniProtKB:P55210" FT SITE 223 FT /note="Involved in allosteric regulation" FT /evidence="ECO:0000250|UniProtKB:P55210" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:17242355" FT MOD_RES 30 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55210" FT MOD_RES 173 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P55210" FT MOD_RES 239 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P55210" FT MUTAGEN 23 FT /note="D->A: Abolished cleavage and activation; when FT associated with A-198." FT /evidence="ECO:0000269|PubMed:18667412" FT MUTAGEN 198 FT /note="D->A: Abolished cleavage and activation; when FT associated with A-23." FT /evidence="ECO:0000269|PubMed:18667412" FT CONFLICT 10..11 FT /note="EL -> DW (in Ref. 2; BAA19730)" FT /evidence="ECO:0000305" FT CONFLICT 45 FT /note="A -> T (in Ref. 2; BAA19730)" FT /evidence="ECO:0000305" FT CONFLICT 48..49 FT /note="VR -> RQ (in Ref. 2; BAA19730)" FT /evidence="ECO:0000305" SQ SEQUENCE 303 AA; 34061 MW; 747787B5BDE5F744 CRC64; MTDDQDCAAE LEKVDSSSED GVDAKPDRSS IISSILLKKK RNASAGPVRT GRDRVPTYLY RMDFQKMGKC IIINNKNFDK ATGMDVRNGT DKDAGALFKC FQNLGFEVTV HNDCSCAKMQ DLLRKASEED HSNSACFACV LLSHGEEDLI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL FFIQACRGTE LDDGIQADSG PINDIDANPR NKIPVEADFL FAYSTVPGYY SWRNPGKGSW FVQALCSILN EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP RFNEKKQIPC MVSMLTKELY FSR //