ID CASP7_HUMAN Reviewed; 303 AA. AC P55210; B4DQU7; B5BU45; D3DRB8; Q13364; Q53YD5; Q5SVL0; Q5SVL3; Q96BA0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 229. 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:10497198, ECO:0000269|PubMed:11257230, ECO:0000269|PubMed:11701129, ECO:0000269|PubMed:18723680}; DE AltName: Full=Apoptotic protease Mch-3 {ECO:0000303|PubMed:8521391}; DE AltName: Full=CMH-1 {ECO:0000303|PubMed:8567622}; DE AltName: Full=ICE-like apoptotic protease 3 {ECO:0000303|PubMed:8576161}; DE Short=ICE-LAP3 {ECO:0000303|PubMed:8576161}; 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|HGNC:HGNC:1508}; GN Synonyms=MCH3 {ECO:0000303|PubMed:8521391}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA), AND FUNCTION. RC TISSUE=T-cell; RX PubMed=8521391; RA Fernandes-Alnemri T., Takahashi A., Armstrong R.C., Krebs J., Fritz L.C., RA Tomaselli K.J., Wang L., Yu Z., Croce C.M., Salveson G., Earnshaw W.C., RA Litwack G., Alnemri E.S.; RT "Mch3, a novel human apoptotic cysteine protease highly related to CPP32."; RL Cancer Res. 55:6045-6052(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), FUNCTION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND MUTAGENESIS OF CYS-186. RX PubMed=8576161; DOI=10.1074/jbc.271.3.1621; RA Duan H., Chinnaiyan A.M., Hudson P.L., Wing J.P., He W.-W., Dixit V.M.; RT "ICE-LAP3, a novel mammalian homologue of the Caenorhabditis elegans cell RT death protein Ced-3 is activated during Fas- and tumor necrosis factor- RT induced apoptosis."; RL J. Biol. Chem. 271:1621-1625(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND FUNCTION. RC TISSUE=Spleen; RX PubMed=8567622; DOI=10.1074/jbc.271.4.1825; RA Lippke J.A., Gu Y., Sarnecki C., Caron P.R., Su M.S.-S.; RT "Identification and characterization of CPP32/Mch2 homolog 1, a novel RT cysteine protease similar to CPP32."; RL J. Biol. Chem. 271:1825-1828(1996). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND ALPHA'), AND FUNCTION. RC TISSUE=Fetal lung, and Fetal spleen; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT GLU-4. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA'). RX PubMed=19054851; DOI=10.1038/nmeth.1273; RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B., RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., RA Nomura N.; RT "Human protein factory for converting the transcriptome into an in vitro- RT expressed proteome."; RL Nat. Methods 5:1011-1017(2008). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA), AND VARIANT GLU-4. RC TISSUE=Skin; 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 [11] RP FUNCTION. RX PubMed=8643593; DOI=10.1073/pnas.93.11.5437; RA Pai J.-T., Brown M.S., Goldstein J.L.; RT "Purification and cDNA cloning of a second apoptosis-related cysteine RT protease that cleaves and activates sterol regulatory element binding RT proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 93:5437-5442(1996). RN [12] RP PROTEOLYTIC PROCESSING. RX PubMed=8755496; DOI=10.1073/pnas.93.15.7464; RA Fernandes-Alnemri T., Armstrong R.C., Krebs J.F., Srinivasula S.M., RA Wang L., Bullrich F., Fritz L.C., Trapani J.A., Tomaselli K.J., Litwack G., RA Alnemri E.S.; RT "In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic RT cysteine protease containing two FADD-like domains."; RL Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996). RN [13] RP PROTEOLYTIC CLEAVAGE. RX PubMed=9852092; DOI=10.1074/jbc.273.51.34278; RA Yang X., Stennicke H.R., Wang B., Green D.R., Jaenicke R.U., Srinivasan A., RA Seth P., Salvesen G.S., Froelich C.J.; RT "Granzyme B mimics apical caspases. Description of a unified pathway for RT trans-activation of executioner caspase-3 and -7."; RL J. Biol. Chem. 273:34278-34283(1998). RN [14] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=10497198; DOI=10.1074/jbc.274.40.28379; RA Germain M., Affar E.B., D'Amours D., Dixit V.M., Salvesen G.S., RA Poirier G.G.; RT "Cleavage of automodified poly(ADP-ribose) polymerase during apoptosis. RT Evidence for involvement of caspase-7."; RL J. Biol. Chem. 274:28379-28384(1999). RN [15] RP ACTIVITY REGULATION. RX PubMed=10821855; DOI=10.1074/jbc.275.21.16007; RA Lee D., Long S.A., Adams J.L., Chan G., Vaidya K.S., Francis T.A., RA Kikly K., Winkler J.D., Sung C.-M., Debouck C., Richardson S., Levy M.A., RA DeWolf W.E. Jr., Keller P.M., Tomaszek T., Head M.S., Ryan M.D., RA Haltiwanger R.C., Liang P.-H., Janson C.A., McDevitt P.J., Johanson K., RA Concha N.O., Chan W., Abdel-Meguid S.S., Badger A.M., Lark M.W., RA Nadeau D.P., Suva L.J., Gowen M., Nuttall M.E.; RT "Potent and selective nonpeptide inhibitors of caspases 3 and 7 inhibit RT apoptosis and maintain cell functionality."; RL J. Biol. Chem. 275:16007-16014(2000). RN [16] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RP AND MUTAGENESIS OF ASP-23; CYS-186; ASP-198 AND ASP-206. RX PubMed=12824163; DOI=10.1074/jbc.m305110200; RA Denault J.B., Salvesen G.S.; RT "Human caspase-7 activity and regulation by its N-terminal peptide."; RL J. Biol. Chem. 278:34042-34050(2003). RN [17] RP INTERACTION WITH BIRC6/BRUCE. RX PubMed=15200957; DOI=10.1016/j.molcel.2004.05.018; RA Bartke T., Pohl C., Pyrowolakis G., Jentsch S.; RT "Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin RT ligase."; RL Mol. Cell 14:801-811(2004). RN [18] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16123041; DOI=10.1074/jbc.m506460200; RA Clarke C.A., Bennett L.N., Clarke P.R.; RT "Cleavage of claspin by caspase-7 during apoptosis inhibits the Chk1 RT pathway."; RL J. Biol. Chem. 280:35337-35345(2005). RN [19] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16374543; DOI=10.1007/s10495-005-3276-y; RA Rodriguez-Hernandez A., Brea-Calvo G., Fernandez-Ayala D.J., Cordero M., RA Navas P., Sanchez-Alcazar J.A.; RT "Nuclear caspase-3 and caspase-7 activation, and poly(ADP-ribose) RT polymerase cleavage are early events in camptothecin-induced apoptosis."; RL Apoptosis 11:131-139(2006). RN [20] RP ACTIVITY REGULATION, INTERACTION WITH XIAP, AND PROTEOLYTIC CLEAVAGE. RX PubMed=16352606; DOI=10.1074/jbc.m507393200; RA Twiddy D., Cohen G.M., Macfarlane M., Cain K.; RT "Caspase-7 is directly activated by the approximately 700-kDa apoptosome RT complex and is released as a stable XIAP-caspase-7 approximately 200-kDa RT complex."; RL J. Biol. Chem. 281:3876-3888(2006). RN [21] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, INTERACTION RP WITH XIAP, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF CYS-186; ASP-192; RP ASP-198 AND ASP-206. RX PubMed=16916640; DOI=10.1016/j.molcel.2006.06.020; RA Denault J.B., Bekes M., Scott F.L., Sexton K.M., Bogyo M., Salvesen G.S.; RT "Engineered hybrid dimers: tracking the activation pathway of caspase-7."; RL Mol. Cell 23:523-533(2006). RN [22] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=17646170; DOI=10.1074/jbc.m705265200; RA Young J.E., Gouw L., Propp S., Sopher B.L., Taylor J., Lin A., Hermel E., RA Logvinova A., Chen S.F., Chen S., Bredesen D.E., Truant R., Ptacek L.J., RA La Spada A.R., Ellerby L.M.; RT "Proteolytic cleavage of ataxin-7 by caspase-7 modulates cellular toxicity RT and transcriptional dysregulation."; RL J. Biol. Chem. 282:30150-30160(2007). RN [23] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18723680; DOI=10.1073/pnas.0707715105; RA Walsh J.G., Cullen S.P., Sheridan C., Luethi A.U., Gerner C., Martin S.J.; RT "Executioner caspase-3 and caspase-7 are functionally distinct proteases."; RL Proc. Natl. Acad. Sci. U.S.A. 105:12815-12819(2008). RN [24] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [25] RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND RP ACTIVITY REGULATION. RX PubMed=19617626; DOI=10.1074/jbc.m109.038174; RA Gafni J., Cong X., Chen S.F., Gibson B.W., Ellerby L.M.; RT "Calpain-1 cleaves and activates caspase-7."; RL J. Biol. Chem. 284:25441-25449(2009). RN [26] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY RP REGULATION, AND MUTAGENESIS OF ARG-187; TYR-223; TYR-229 AND CYS-290. RX PubMed=19581639; DOI=10.1074/jbc.m109.001826; RA Hardy J.A., Wells J.A.; RT "Dissecting an allosteric switch in caspase-7 using chemical and mutational RT probes."; RL J. Biol. Chem. 284:26063-26069(2009). RN [27] RP FUNCTION. RX PubMed=20159985; DOI=10.1074/jbc.m109.068221; RA Majerciak V., Kruhlak M., Dagur P.K., McCoy J.P. Jr., Zheng Z.M.; RT "Caspase-7 cleavage of Kaposi sarcoma-associated herpesvirus ORF57 confers RT a cellular function against viral lytic gene expression."; RL J. Biol. Chem. 285:11297-11307(2010). RN [28] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=20566630; DOI=10.1074/jbc.m110.126573; RA Nakatsumi H., Yonehara S.; RT "Identification of functional regions defining different activity in RT caspase-3 and caspase-7 within cells."; RL J. Biol. Chem. 285:25418-25425(2010). RN [29] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [30] RP FUNCTION. RX PubMed=21157428; DOI=10.1038/emboj.2010.326; RA Edelmann B., Bertsch U., Tchikov V., Winoto-Morbach S., Perrotta C., RA Jakob M., Adam-Klages S., Kabelitz D., Schuetze S.; RT "Caspase-8 and caspase-7 sequentially mediate proteolytic activation of RT acid sphingomyelinase in TNF-R1 receptosomes."; RL EMBO J. 30:379-394(2011). RN [31] RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT RP SER-30; THR-173 AND SER-239, AND MUTAGENESIS OF SER-30; THR-173 AND RP SER-239. RX PubMed=21555521; DOI=10.1074/jbc.m111.236596; RA Li X., Wen W., Liu K., Zhu F., Malakhova M., Peng C., Li T., Kim H.G., RA Ma W., Cho Y.Y., Bode A.M., Dong Z., Dong Z.; RT "Phosphorylation of caspase-7 by p21-activated protein kinase (PAK) 2 RT inhibits chemotherapeutic drug-induced apoptosis of breast cancer cell RT lines."; RL J. Biol. Chem. 286:22291-22299(2011). RN [32] 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 [33] RP FUNCTION. RX PubMed=22184066; DOI=10.1128/mcb.06466-11; RA Riman S., Rizkallah R., Kassardjian A., Alexander K.E., Luescher B., RA Hurt M.M.; RT "Phosphorylation of the transcription factor YY1 by CK2alpha prevents RT cleavage by caspase 7 during apoptosis."; RL Mol. Cell. Biol. 32:797-807(2012). RN [34] RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND MUTAGENESIS OF ASP-23; RP 38-LYS--LYS-41; 39-LYS-LYS-40 AND LYS-39. RX PubMed=22451931; DOI=10.1073/pnas.1200934109; RA Boucher D., Blais V., Denault J.B.; RT "Caspase-7 uses an exosite to promote poly(ADP ribose) polymerase 1 RT proteolysis."; RL Proc. Natl. Acad. Sci. U.S.A. 109:5669-5674(2012). RN [35] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [36] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [37] RP INTERACTION WITH HSPA5. RX PubMed=26045166; DOI=10.1158/0008-5472.can-14-3751; RA Kang J.M., Park S., Kim S.J., Kim H., Lee B., Kim J., Park J., Kim S.T., RA Yang H.K., Kim W.H., Kim S.J.; RT "KIAA1324 Suppresses Gastric Cancer Progression by Inhibiting the RT Oncoprotein GRP78."; RL Cancer Res. 75:3087-3097(2015). RN [38] RP FUNCTION, AND MUTAGENESIS OF 38-LYS--LYS-41. RX PubMed=28863261; DOI=10.1021/acs.biochem.7b00298; RA Martini C., Bedard M., Lavigne P., Denault J.B.; RT "Characterization of Hsp90 co-chaperone p23 cleavage by caspase-7 uncovers RT a peptidase-substrate interaction involving intrinsically disordered RT regions."; RL Biochemistry 56:5099-5111(2017). RN [39] RP INTERACTION WITH ATXN3. RX PubMed=30455355; DOI=10.1074/jbc.ra118.005801; RA Weishaeupl D., Schneider J., Peixoto Pinheiro B., Ruess C., Dold S.M., RA von Zweydorf F., Gloeckner C.J., Schmidt J., Riess O., Schmidt T.; RT "Physiological and pathophysiological characteristics of ataxin-3 RT isoforms."; RL J. Biol. Chem. 294:644-661(2019). RN [40] RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, RNA-BINDING, AND MUTAGENESIS OF RP 38-LYS--LYS-41 AND 39-LYS-LYS-40. RX PubMed=31586028; DOI=10.1073/pnas.1909283116; RA Desroches A., Denault J.B.; RT "Caspase-7 uses RNA to enhance proteolysis of poly(ADP-ribose) polymerase 1 RT and other RNA-binding proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 116:21521-21528(2019). RN [41] RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, RNA-BINDING, AND MUTAGENESIS OF RP ASP-23 AND 39-LYS-LYS-40. RX PubMed=34156061; DOI=10.1042/bcj20210366; RA Desroches A., Denault J.B.; RT "Characterization of caspase-7 interaction with RNA."; RL Biochem. J. 478:2681-2696(2021). RN [42] RP FUNCTION, PROTEOLYTIC CLEAVAGE, AND ADP-RIBOXANATION AT ARG-233 (MICROBIAL RP INFECTION). RX PubMed=35338844; DOI=10.1016/j.molcel.2022.03.010; RA Peng T., Tao X., Xia Z., Hu S., Xue J., Zhu Q., Pan X., Zhang Q., Li S.; RT "Pathogen hijacks programmed cell death signaling by arginine ADPR- RT deacylization of caspases."; RL Mol. Cell 82:1806-1820(2022). RN [43] {ECO:0007744|PDB:1I51} RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 51-198 AND 199-303 IN COMPLEX RP WITH XIAP, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND RP INTERACTION WITH XIAP. RX PubMed=11257230; DOI=10.1016/s0092-8674(01)00272-0; RA Chai J., Shiozaki E., Srinivasula S.M., Wu Q., Datta P., Alnemri E.S., RA Shi Y., Dataa P.; RT "Structural basis of caspase-7 inhibition by XIAP."; RL Cell 104:769-780(2001). RN [44] {ECO:0007744|PDB:1I4O} RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 24-303 IN COMPLEX WITH XIAP, RP FUNCTION, ACTIVITY REGULATION, AND INTERACTION WITH XIAP. RX PubMed=11257231; DOI=10.1016/s0092-8674(02)02075-5; RA Huang Y., Park Y.C., Rich R.L., Segal D., Myszka D.G., Wu H.; RT "Structural basis of caspase inhibition by XIAP: differential roles of the RT linker versus the BIR domain."; RL Cell 104:781-790(2001). RN [45] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 51-303, FUNCTION, CATALYTIC RP ACTIVITY, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF CYS-186. RX PubMed=11701129; DOI=10.1016/s0092-8674(01)00544-x; RA Chai J., Wu Q., Shiozaki E., Srinivasula S.M., Alnemri E.S., Shi Y.; RT "Crystal structure of a procaspase-7 zymogen: mechanisms of activation and RT substrate binding."; RL Cell 107:399-407(2001). RN [46] {ECO:0007744|PDB:1GQF} RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 47-303, SUBUNIT, AND MUTAGENESIS RP OF CYS-186. RX PubMed=11752425; DOI=10.1073/pnas.221580098; RA Riedl S.J., Fuentes-Prior P., Renatus M., Kairies N., Krapp S., Huber R., RA Salvesen G.S., Bode W.; RT "Structural basis for the activation of human procaspase-7."; RL Proc. Natl. Acad. Sci. U.S.A. 98:14790-14795(2001). RN [47] {ECO:0007744|PDB:1SHJ, ECO:0007744|PDB:1SHL} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 50-303 IN COMPLEX WITH DICA AND RP FICA ALLOSTERIC INHIBITORS, FUNCTION, ACTIVITY REGULATION, AND ACTIVE RP SITES. RX PubMed=15314233; DOI=10.1073/pnas.0404781101; RA Hardy J.A., Lam J., Nguyen J.T., O'Brien T., Wells J.A.; RT "Discovery of an allosteric site in the caspases."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12461-12466(2004). RN [48] {ECO:0007744|PDB:2QL5, ECO:0007744|PDB:2QL7, ECO:0007744|PDB:2QL9, ECO:0007744|PDB:2QLB, ECO:0007744|PDB:2QLF, ECO:0007744|PDB:2QLJ} RP X-RAY CRYSTALLOGRAPHY (2.14 ANGSTROMS) OF 24-196 AND 207-303, FUNCTION, AND RP CATALYTIC ACTIVITY. RX PubMed=17697120; DOI=10.1111/j.1742-4658.2007.05994.x; RA Agniswamy J., Fang B., Weber I.T.; RT "Plasticity of S2-S4 specificity pockets of executioner caspase-7 revealed RT by structural and kinetic analysis."; RL FEBS J. 274:4752-4765(2007). RN [49] {ECO:0007744|PDB:4HQ0, ECO:0007744|PDB:4HQR} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 47-303 OF MUTANT IV IN COMPLEX RP WITH AC-DEVD-CHO INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS RP OF 195-ILE--ASP-204; 195-ILE--ASP-206 AND 195-ILE--GLY-200. RX PubMed=23897474; DOI=10.1107/s0907444913010196; RA Kang H.J., Lee Y.M., Bae K.H., Kim S.J., Chung S.J.; RT "Structural asymmetry of procaspase-7 bound to a specific inhibitor."; RL Acta Crystallogr. D 69:1514-1521(2013). RN [50] {ECO:0007744|PDB:4JR1, ECO:0007744|PDB:4JR2} RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 57-303 IN COMPLEX WITH COVALENT RP INHIBITORS, AND MUTAGENESIS OF ASP-23 AND ASP-198. RX PubMed=23650375; DOI=10.1073/pnas.1306759110; RA Thomsen N.D., Koerber J.T., Wells J.A.; RT "Structural snapshots reveal distinct mechanisms of procaspase-3 and -7 RT activation."; RL Proc. Natl. Acad. Sci. U.S.A. 110:8477-8482(2013). RN [51] {ECO:0007744|PDB:4LSZ} RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) OF 24-198 AND 207-303 IN COMPLEX RP WITH DARPIN D7.18, AND ACTIVITY REGULATION. RX PubMed=24779913; DOI=10.1042/bj20131456; RA Fluetsch A., Ackermann R., Schroeder T., Lukarska M., Hausammann G.J., RA Weinert C., Briand C., Gruetter M.G.; RT "Combined inhibition of caspase 3 and caspase 7 by two highly selective RT DARPins slows down cellular demise."; RL Biochem. J. 461:279-290(2014). RN [52] {ECO:0007744|PDB:4ZVO, ECO:0007744|PDB:4ZVP, ECO:0007744|PDB:4ZVQ, ECO:0007744|PDB:4ZVR, ECO:0007744|PDB:4ZVS, ECO:0007744|PDB:4ZVT, ECO:0007744|PDB:4ZVU} RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-198 AND 199-303, FUNCTION, RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF 230-TYR--SER-234; 232-TRP--SER-234 RP AND GLN-276. RX PubMed=27032039; DOI=10.1021/acschembio.5b00971; RA Hill M.E., MacPherson D.J., Wu P., Julien O., Wells J.A., Hardy J.A.; RT "Reprogramming caspase-7 specificity by regio-specific mutations and RT selection provides alternate solutions for substrate recognition."; RL ACS Chem. Biol. 11:1603-1612(2016). RN [53] {ECO:0007744|PDB:5K20} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-198 AND 199-303, ACTIVITY RP REGULATION, PROTEOLYTIC CLEAVAGE, PHOSPHORYLATION AT SER-30; THR-173 AND RP SER-239, AND MUTAGENESIS OF SER-30; CYS-186; SER-239 AND CYS-290. RX PubMed=27889207; DOI=10.1016/j.str.2016.11.001; RA Eron S.J., Raghupathi K., Hardy J.A.; RT "Dual site phosphorylation of caspase-7 by PAK2 blocks apoptotic activity RT by two distinct mechanisms."; RL Structure 25:27-39(2017). RN [54] {ECO:0007744|PDB:7WZS} RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) OF 24-303 IN COMPLEX WITH RP C.VIOLACEUM COPC TOXIN, FUNCTION, PROTEOLYTIC CLEAVAGE, ADP-RIBOXANATION AT RP ARG-233 (MICROBIAL INFECTION), AND MUTAGENESIS OF ARG-233. RX PubMed=35446120; DOI=10.1128/mbio.00690-22; RA Liu Y., Zeng H., Hou Y., Li Z., Li L., Song X., Ding J., Shao F., Xu Y.; RT "Calmodulin binding activates chromobacterium CopC effector to ADP- RT riboxanate host apoptotic caspases."; RL MBio 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:8521391, PubMed:8567622, PubMed:8576161, PubMed:9070923, CC PubMed:16916640, PubMed:17646170, PubMed:18723680, PubMed:19581639, CC PubMed:11257230, PubMed:11257231, PubMed:11701129, PubMed:15314233). CC Has a marked preference for Asp-Glu-Val-Asp (DEVD) consensus sequences, CC with some plasticity for alternate non-canonical sequences CC (PubMed:12824163, PubMed:19581639, PubMed:20566630, PubMed:15314233, CC PubMed:17697120, PubMed:23897474, PubMed:23650375, PubMed:27032039). CC Its involvement in the different programmed cell death processes is CC probably determined by upstream proteases that activate CASP7 (By CC similarity). Acts as an effector caspase involved in the execution CC phase of apoptosis: following cleavage and activation by initiator CC caspases (CASP8, CASP9 and/or CASP10), mediates execution of apoptosis CC by catalyzing cleavage of proteins, such as CLSPN, PARP1, PTGES3 and CC YY1 (PubMed:10497198, PubMed:16123041, PubMed:16374543, CC PubMed:16916640, PubMed:18723680, PubMed:20566630, PubMed:21555521, CC PubMed:22184066, PubMed:22451931, PubMed:28863261, PubMed:31586028, CC PubMed:34156061, PubMed:27889207, PubMed:35338844, PubMed:35446120). CC Compared to CASP3, acts as a minor executioner caspase and cleaves a CC limited set of target proteins (PubMed:18723680). Acts as a key CC regulator of the inflammatory response in response to bacterial CC infection by catalyzing cleavage and activation of the sphingomyelin CC phosphodiesterase SMPD1 in the extracellular milieu, thereby promoting CC membrane repair (PubMed:21157428). Regulates pyroptosis in intestinal CC epithelial cells: cleaved and activated by CASP1 in response to CC S.typhimurium infection, promoting its secretion to the extracellular CC milieu, where it catalyzes activation of SMPD1, generating ceramides CC that repair membranes and counteract the action of gasdermin-D (GSDMD) CC pores (By similarity). Regulates granzyme-mediated programmed cell CC death in hepatocytes: cleaved and activated by granzyme B (GZMB) in CC response to bacterial infection, promoting its secretion to the CC extracellular milieu, where it catalyzes activation of SMPD1, CC generating ceramides that repair membranes and counteract the action of CC perforin (PRF1) pores (By similarity). Following cleavage by CASP1 in CC response to inflammasome activation, catalyzes processing and CC inactivation of PARP1, alleviating the transcription repressor activity CC of PARP1 (PubMed:22464733). Acts as an inhibitor of type I interferon CC production during virus-induced apoptosis by mediating cleavage of CC antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine CC overproduction (By similarity). Cleaves and activates sterol regulatory CC element binding proteins (SREBPs) (PubMed:8643593). Cleaves CC phospholipid scramblase proteins XKR4, XKR8 and XKR9 (By similarity). CC In case of infection, catalyzes cleavage of Kaposi sarcoma-associated CC herpesvirus protein ORF57, thereby preventing expression of viral lytic CC genes (PubMed:20159985). {ECO:0000250|UniProtKB:P97864, CC ECO:0000269|PubMed:10497198, ECO:0000269|PubMed:11257230, CC ECO:0000269|PubMed:11257231, ECO:0000269|PubMed:11701129, CC ECO:0000269|PubMed:12824163, ECO:0000269|PubMed:15314233, CC ECO:0000269|PubMed:16123041, ECO:0000269|PubMed:16374543, CC ECO:0000269|PubMed:16916640, ECO:0000269|PubMed:17646170, CC ECO:0000269|PubMed:17697120, ECO:0000269|PubMed:18723680, CC ECO:0000269|PubMed:19581639, ECO:0000269|PubMed:20159985, CC ECO:0000269|PubMed:20566630, ECO:0000269|PubMed:21157428, CC ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:22184066, CC ECO:0000269|PubMed:22451931, ECO:0000269|PubMed:22464733, CC ECO:0000269|PubMed:23650375, ECO:0000269|PubMed:23897474, CC ECO:0000269|PubMed:27032039, ECO:0000269|PubMed:27889207, CC ECO:0000269|PubMed:28863261, ECO:0000269|PubMed:31586028, CC ECO:0000269|PubMed:34156061, ECO:0000269|PubMed:35338844, CC ECO:0000269|PubMed:35446120, ECO:0000269|PubMed:8521391, CC ECO:0000269|PubMed:8567622, ECO:0000269|PubMed:8576161, CC ECO:0000269|PubMed:8643593, ECO:0000269|PubMed:9070923}. CC -!- FUNCTION: [Isoform Beta]: Lacks enzymatic activity. CC {ECO:0000269|PubMed:8521391}. 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:10497198, ECO:0000269|PubMed:11257230, CC ECO:0000269|PubMed:11701129, ECO:0000269|PubMed:12824163, CC ECO:0000269|PubMed:16123041, ECO:0000269|PubMed:16374543, CC ECO:0000269|PubMed:16916640, ECO:0000269|PubMed:17646170, CC ECO:0000269|PubMed:17697120, ECO:0000269|PubMed:18723680, CC ECO:0000269|PubMed:19581639, ECO:0000269|PubMed:19617626, CC ECO:0000269|PubMed:20566630, ECO:0000269|PubMed:22451931, CC ECO:0000269|PubMed:23650375, ECO:0000269|PubMed:23897474, CC ECO:0000269|PubMed:27032039, ECO:0000269|PubMed:31586028, CC ECO:0000269|PubMed:34156061}; CC -!- ACTIVITY REGULATION: During activation, the N-terminal disordered CC prodomain is removed by cleavage (PubMed:12824163, PubMed:16916640). CC Concomitantly, double cleavage gives rise to a large Caspase-7 subunit CC p20 and a small Caspase-7 subunit p11 (PubMed:16916640). The two large CC and two small subunits then assemble to form the active CASP7 complex CC (PubMed:16916640). Can be cleaved and activated by different caspases, CC depending on the context (PubMed:16916640). Cleaved and activated by CC initiator caspases (CASP8, CASP9 and/or CASP10), leading to execution CC phase of apoptosis (PubMed:16352606, PubMed:16916640). Inhibited by CC XIAP, which directly binds to the active site pocket and obstructs CC substrate entry (PubMed:16352606, PubMed:16916640, PubMed:11257230, CC PubMed:11257231). Cleavage and maturation by GZMB regulates granzyme- CC mediated programmed cell death (By similarity). Cleavage and maturation CC by CASP1 regulates pyroptosis (By similarity). Phosphorylation at Ser- CC 30 and Ser-239 by PAK2 inhibits its activity (PubMed:21555521, CC PubMed:27889207). Inhibited by isatin sulfonamides (PubMed:10821855). CC Inhibited by 2-(2,4-Dichlorophenoxy)- N-(2-mercapto-ethyl)-acetamide CC (DICA) and 5-Fluoro-1H-indole-2- carboxylic acid (2-mercapto-ethyl)- CC amide (FICA) allosteric inhibitors, which disrupt an interaction CC between Arg-187 and Tyr-223 (PubMed:15314233, PubMed:19581639). CC Specifically inhibited by DARPin D7.18 and D7.43, which specifically CC bind to the precursor CASP7 and prevent its processing and activation CC (PubMed:24779913). {ECO:0000250|UniProtKB:P97864, CC ECO:0000269|PubMed:10821855, ECO:0000269|PubMed:11257230, CC ECO:0000269|PubMed:11257231, ECO:0000269|PubMed:12824163, CC ECO:0000269|PubMed:15314233, ECO:0000269|PubMed:16352606, CC ECO:0000269|PubMed:16916640, ECO:0000269|PubMed:19581639, CC ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:24779913, CC ECO:0000269|PubMed:27889207}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=10 uM for a DEVD peptide {ECO:0000269|PubMed:19581639}; CC Note=kcat is 0.51 sec(-1) for a DEVD peptide. CC {ECO:0000269|PubMed:19581639}; 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 (PubMed:16916640, PubMed:20566630, PubMed:11701129, CC PubMed:11752425). Interacts with XIAP (via its second BIR domain); CC inhibiting CASP7 activity (PubMed:16916640, PubMed:11257230, CC PubMed:11257231). Interacts with BIRC6/bruce (PubMed:15200957). CC Interacts with ATXN3 (short isoform 1) (PubMed:30455355). Interacts CC with HSPA5 (PubMed:26045166). {ECO:0000269|PubMed:11257230, CC ECO:0000269|PubMed:11257231, ECO:0000269|PubMed:11701129, CC ECO:0000269|PubMed:11752425, ECO:0000269|PubMed:15200957, CC ECO:0000269|PubMed:16916640, ECO:0000269|PubMed:20566630, CC ECO:0000269|PubMed:26045166, ECO:0000269|PubMed:30455355}. CC -!- INTERACTION: CC P55210; Q13490: BIRC2; NbExp=2; IntAct=EBI-523958, EBI-514538; CC P55210; P83105: HTRA4; NbExp=6; IntAct=EBI-523958, EBI-21776319; CC P55210; P42858: HTT; NbExp=12; IntAct=EBI-523958, EBI-466029; CC P55210; Q8N4N3-2: KLHL36; NbExp=3; IntAct=EBI-523958, EBI-10973851; CC P55210; P43364: MAGEA11; NbExp=3; IntAct=EBI-523958, EBI-739552; CC P55210; Q16236: NFE2L2; NbExp=2; IntAct=EBI-523958, EBI-2007911; CC P55210; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-523958, EBI-740897; CC P55210; Q13177: PAK2; NbExp=6; IntAct=EBI-523958, EBI-1045887; CC P55210; P27986-2: PIK3R1; NbExp=3; IntAct=EBI-523958, EBI-9090282; CC P55210; P21673: SAT1; NbExp=6; IntAct=EBI-523958, EBI-711613; CC P55210; Q86WV1-2: SKAP1; NbExp=3; IntAct=EBI-523958, EBI-11995314; CC P55210; P17405: SMPD1; NbExp=6; IntAct=EBI-523958, EBI-7095800; CC P55210; P98170: XIAP; NbExp=3; IntAct=EBI-523958, EBI-517127; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:12824163, CC ECO:0000305|PubMed:21555521, ECO:0000305|PubMed:8576161}. Nucleus CC {ECO:0000269|PubMed:19617626, ECO:0000269|PubMed:21555521}. Secreted, CC extracellular space {ECO:0000250|UniProtKB:P97864}. Note=Following CC cleavage and activation by CASP1 or granzyme B (GZMB), secreted into CC the extracellular milieu by passing through the gasdermin-D (GSDMD) CC pores or perforin (PRF1) pore, respectively. CC {ECO:0000250|UniProtKB:P97864}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=Alpha {ECO:0000303|PubMed:8521391}; CC IsoId=P55210-1; Sequence=Displayed; CC Name=Beta {ECO:0000303|PubMed:8521391}; CC IsoId=P55210-2; Sequence=VSP_000807; CC Name=Alpha' {ECO:0000303|PubMed:9070923}; Synonyms=Beta CC {ECO:0000303|PubMed:9070923}; CC IsoId=P55210-3; Sequence=VSP_000806; CC Name=4; CC IsoId=P55210-4; Sequence=VSP_045325; CC -!- TISSUE SPECIFICITY: Highly expressed in lung, skeletal muscle, liver, CC kidney, spleen and heart, and moderately in testis. No expression in CC the brain. {ECO:0000269|PubMed:8576161}. CC -!- DOMAIN: The exosite polybasic region mediates non-specific RNA-binding, CC acting as a bridge for RNA-binding target proteins, such as PARP1 CC (PubMed:22451931, PubMed:31586028, PubMed:34156061). The exosite is CC also required for interaction with non-RNA-binding proteins, such as CC Hsp90 co-chaperone PTGES3 (PubMed:34156061). CC {ECO:0000269|PubMed:22451931, ECO:0000269|PubMed:31586028, CC ECO:0000269|PubMed:34156061}. CC -!- PTM: Cleavage by different proteases, such as granzyme B (GZMB), CC caspase-1 (CASP1), caspase-8 (CASP8), caspase-9 (CASP9) or caspase-10 CC (CASP10) generate the two active subunits (PubMed:9852092, CC PubMed:12824163, PubMed:16352606, PubMed:16916640, PubMed:35338844, CC PubMed:35446120). Its involvement in different programmed cell death CC processes is probably specified by the protease that activates CASP7 CC (PubMed:9852092, PubMed:16916640). Cleaved and activated by initiator CC caspases (CASP8, CASP9 and/or CASP10), leading to execution phase of CC apoptosis (PubMed:16352606, PubMed:16916640, PubMed:21555521, CC PubMed:27889207). Cleavage and maturation by GZMB regulates granzyme- CC mediated programmed cell death (By similarity). Cleaved and activated CC by CASP1 in response to bacterial infection (By similarity). Propeptide CC domains can also be cleaved efficiently by CASP3 (PubMed:8755496). CC Active heterodimers between the small subunit of caspase-7 and the CC large subunit of CASP3, and vice versa, also occur (PubMed:8755496). CC Also cleaved at the N-terminus at alternative sites by CAPN1, leading CC to its activation (PubMed:19617626). {ECO:0000250|UniProtKB:P97864, CC ECO:0000269|PubMed:12824163, ECO:0000269|PubMed:16352606, CC ECO:0000269|PubMed:16916640, ECO:0000269|PubMed:19617626, CC ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207, CC ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120, CC ECO:0000269|PubMed:8755496, ECO:0000269|PubMed:9852092}. CC -!- PTM: Phosphorylation at Ser-30 and Ser-239 by PAK2 inhibits its CC activity (PubMed:21555521, PubMed:27889207). Phosphorylation at Ser-30 CC prevents cleavage and activation by initiator caspase CASP9, while CC phosphorylation at Ser-239 prevents thiol protease activity by CC preventing substrate-binding (PubMed:21555521, PubMed:27889207). CC {ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207}. CC -!- PTM: (Microbial infection) ADP-riboxanation by C.violaceum CopC blocks CC CASP7 processing, preventing CASP7 activation and ability to recognize CC and cleave substrates. {ECO:0000269|PubMed:35338844, CC ECO:0000269|PubMed:35446120}. CC -!- SIMILARITY: Belongs to the peptidase C14A family. {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; U37448; AAC50303.1; -; mRNA. DR EMBL; U37449; AAC50304.1; -; mRNA. DR EMBL; U39613; AAC50346.1; -; mRNA. DR EMBL; U40281; AAC50352.1; -; mRNA. DR EMBL; U67319; AAC51152.1; -; mRNA. DR EMBL; U67320; AAC51153.1; -; mRNA. DR EMBL; U67206; AAF21460.1; -; mRNA. DR EMBL; BT006683; AAP35329.1; -; mRNA. DR EMBL; AB451281; BAG70095.1; -; mRNA. DR EMBL; AB451413; BAG70227.1; -; mRNA. DR EMBL; AK298964; BAG61059.1; -; mRNA. DR EMBL; AL592546; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL627395; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471066; EAW49494.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49495.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49498.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49496.1; -; Genomic_DNA. DR EMBL; CH471066; EAW49497.1; -; Genomic_DNA. DR EMBL; BC015799; AAH15799.1; -; mRNA. DR CCDS; CCDS58096.1; -. [P55210-4] DR CCDS; CCDS7580.1; -. [P55210-3] DR CCDS; CCDS7581.1; -. [P55210-1] DR CCDS; CCDS7582.1; -. [P55210-2] DR RefSeq; NP_001218.1; NM_001227.4. [P55210-1] DR RefSeq; NP_001253985.1; NM_001267056.1. [P55210-1] DR RefSeq; NP_001253986.1; NM_001267057.1. DR RefSeq; NP_001253987.1; NM_001267058.1. [P55210-4] DR RefSeq; NP_001307840.1; NM_001320911.1. DR RefSeq; NP_203124.1; NM_033338.5. [P55210-3] DR RefSeq; NP_203125.1; NM_033339.4. [P55210-1] DR RefSeq; NP_203126.1; NM_033340.3. [P55210-2] DR PDB; 1F1J; X-ray; 2.35 A; A/B=2-303. DR PDB; 1GQF; X-ray; 2.90 A; A/B=47-303. DR PDB; 1I4O; X-ray; 2.40 A; A/B=24-303. DR PDB; 1I51; X-ray; 2.45 A; A/C=51-198, B/D=199-303. DR PDB; 1K86; X-ray; 2.60 A; A/B=51-303. DR PDB; 1K88; X-ray; 2.70 A; A/B=51-303. DR PDB; 1KMC; X-ray; 2.90 A; A/B=1-303. DR PDB; 1SHJ; X-ray; 2.80 A; A/B=50-303. DR PDB; 1SHL; X-ray; 3.00 A; A/B=57-303. DR PDB; 2QL5; X-ray; 2.34 A; A/C=24-196, B/D=207-303. DR PDB; 2QL7; X-ray; 2.40 A; A/C=24-196, B/D=207-303. DR PDB; 2QL9; X-ray; 2.14 A; A/C=24-196, B/D=207-303. DR PDB; 2QLB; X-ray; 2.25 A; A/C=24-196, B/D=207-303. DR PDB; 2QLF; X-ray; 2.80 A; A/C=24-196, B/D=207-303. DR PDB; 2QLJ; X-ray; 2.60 A; A/C=24-196, B/D=207-303. DR PDB; 3EDR; X-ray; 2.45 A; A/C=24-196, B/D=207-303. DR PDB; 3H1P; X-ray; 2.61 A; A/B=50-303. DR PDB; 3IBC; X-ray; 2.75 A; A/C=24-196, B/D=207-303. DR PDB; 3IBF; X-ray; 2.50 A; A/C=24-196, B/D=207-303. DR PDB; 3R5K; X-ray; 2.86 A; A/B=1-303. DR PDB; 4FDL; X-ray; 2.80 A; A/B=2-303. DR PDB; 4FEA; X-ray; 3.79 A; A/B=57-303. DR PDB; 4HQ0; X-ray; 3.00 A; A/B=47-303. DR PDB; 4HQR; X-ray; 3.00 A; A/B=47-303. DR PDB; 4JB8; X-ray; 1.70 A; A=24-198, B=207-303. DR PDB; 4JJ8; X-ray; 2.94 A; A/B=57-303. DR PDB; 4JR1; X-ray; 2.15 A; A/B=57-303. DR PDB; 4JR2; X-ray; 1.65 A; A/B=57-303. DR PDB; 4LSZ; X-ray; 2.26 A; A/C=24-198, B/D=207-303. DR PDB; 4ZVO; X-ray; 2.85 A; A/C=1-198, B/D=199-303. DR PDB; 4ZVP; X-ray; 2.50 A; A/C=1-198, B/D=199-303. DR PDB; 4ZVQ; X-ray; 2.50 A; A/C=1-198, B/D=199-303. DR PDB; 4ZVR; X-ray; 2.30 A; A/C=1-198, B/D=199-303. DR PDB; 4ZVS; X-ray; 2.50 A; A/C=1-198, B/D=199-303. DR PDB; 4ZVT; X-ray; 2.85 A; A/C=1-198, B/D=199-303. DR PDB; 4ZVU; X-ray; 2.60 A; A/C=1-198, B/D=199-303. DR PDB; 5IC6; X-ray; 2.70 A; A/C=1-198, B/D=199-303. DR PDB; 5K20; X-ray; 2.20 A; A/C=1-198, B/D=199-303. DR PDB; 5V6U; X-ray; 2.80 A; A/B=1-303. DR PDB; 5V6Z; X-ray; 2.60 A; A/B=1-303. DR PDB; 7WZS; X-ray; 3.60 A; B=24-303. DR PDB; 8DGZ; X-ray; 2.80 A; A/B=2-303. DR PDB; 8DJ3; X-ray; 3.20 A; A/B=2-303. DR PDBsum; 1F1J; -. DR PDBsum; 1GQF; -. DR PDBsum; 1I4O; -. DR PDBsum; 1I51; -. DR PDBsum; 1K86; -. DR PDBsum; 1K88; -. DR PDBsum; 1KMC; -. DR PDBsum; 1SHJ; -. DR PDBsum; 1SHL; -. DR PDBsum; 2QL5; -. DR PDBsum; 2QL7; -. DR PDBsum; 2QL9; -. DR PDBsum; 2QLB; -. DR PDBsum; 2QLF; -. DR PDBsum; 2QLJ; -. DR PDBsum; 3EDR; -. DR PDBsum; 3H1P; -. DR PDBsum; 3IBC; -. DR PDBsum; 3IBF; -. DR PDBsum; 3R5K; -. DR PDBsum; 4FDL; -. DR PDBsum; 4FEA; -. DR PDBsum; 4HQ0; -. DR PDBsum; 4HQR; -. DR PDBsum; 4JB8; -. DR PDBsum; 4JJ8; -. DR PDBsum; 4JR1; -. DR PDBsum; 4JR2; -. DR PDBsum; 4LSZ; -. DR PDBsum; 4ZVO; -. DR PDBsum; 4ZVP; -. DR PDBsum; 4ZVQ; -. DR PDBsum; 4ZVR; -. DR PDBsum; 4ZVS; -. DR PDBsum; 4ZVT; -. DR PDBsum; 4ZVU; -. DR PDBsum; 5IC6; -. DR PDBsum; 5K20; -. DR PDBsum; 5V6U; -. DR PDBsum; 5V6Z; -. DR PDBsum; 7WZS; -. DR PDBsum; 8DGZ; -. DR PDBsum; 8DJ3; -. DR AlphaFoldDB; P55210; -. DR EMDB; EMD-27839; -. DR SMR; P55210; -. DR BioGRID; 107290; 67. DR ComplexPortal; CPX-2862; Caspase-7 complex. DR DIP; DIP-29973N; -. DR ELM; P55210; -. DR IntAct; P55210; 25. DR MINT; P55210; -. DR STRING; 9606.ENSP00000358327; -. DR BindingDB; P55210; -. DR ChEMBL; CHEMBL3468; -. DR DrugBank; DB05408; Emricasan. DR DrugBank; DB03384; Fica. DR DrugBank; DB06255; Incadronic acid. DR DrugCentral; P55210; -. DR GuidetoPHARMACOLOGY; 1623; -. DR MEROPS; C14.004; -. DR TCDB; 8.A.217.1.1; the apoptosis cell death regulator (acdr) family. DR iPTMnet; P55210; -. DR PhosphoSitePlus; P55210; -. DR BioMuta; CASP7; -. DR DMDM; 1730092; -. DR EPD; P55210; -. DR jPOST; P55210; -. DR MassIVE; P55210; -. DR MaxQB; P55210; -. DR PaxDb; 9606-ENSP00000358327; -. DR PeptideAtlas; P55210; -. DR ProteomicsDB; 56811; -. [P55210-1] DR ProteomicsDB; 56812; -. [P55210-2] DR ProteomicsDB; 56813; -. [P55210-3] DR Pumba; P55210; -. DR Antibodypedia; 18528; 1167 antibodies from 45 providers. DR DNASU; 840; -. DR Ensembl; ENST00000345633.8; ENSP00000298701.7; ENSG00000165806.21. [P55210-1] DR Ensembl; ENST00000369315.5; ENSP00000358321.1; ENSG00000165806.21. [P55210-1] DR Ensembl; ENST00000369318.8; ENSP00000358324.4; ENSG00000165806.21. [P55210-1] DR Ensembl; ENST00000369331.8; ENSP00000358337.3; ENSG00000165806.21. [P55210-2] DR Ensembl; ENST00000452490.3; ENSP00000398107.2; ENSG00000165806.21. [P55210-4] DR Ensembl; ENST00000614447.4; ENSP00000478285.1; ENSG00000165806.21. [P55210-2] DR Ensembl; ENST00000621345.4; ENSP00000480584.1; ENSG00000165806.21. [P55210-1] DR Ensembl; ENST00000621607.4; ENSP00000478999.1; ENSG00000165806.21. [P55210-3] DR GeneID; 840; -. DR KEGG; hsa:840; -. DR MANE-Select; ENST00000369318.8; ENSP00000358324.4; NM_001227.5; NP_001218.1. DR UCSC; uc001lam.5; human. [P55210-1] DR AGR; HGNC:1508; -. DR CTD; 840; -. DR DisGeNET; 840; -. DR GeneCards; CASP7; -. DR HGNC; HGNC:1508; CASP7. DR HPA; ENSG00000165806; Low tissue specificity. DR MIM; 601761; gene. DR neXtProt; NX_P55210; -. DR OpenTargets; ENSG00000165806; -. DR PharmGKB; PA26091; -. DR VEuPathDB; HostDB:ENSG00000165806; -. DR eggNOG; KOG3573; Eukaryota. DR GeneTree; ENSGT00940000153232; -. DR HOGENOM; CLU_1098210_0_0_1; -. DR InParanoid; P55210; -. DR OMA; AKDTHYK; -. DR OrthoDB; 2873736at2759; -. DR PhylomeDB; P55210; -. DR TreeFam; TF102023; -. DR BioCyc; MetaCyc:HS09288-MONOMER; -. DR BRENDA; 3.4.22.60; 2681. DR PathwayCommons; P55210; -. DR Reactome; R-HSA-111459; Activation of caspases through apoptosome-mediated cleavage. DR Reactome; R-HSA-111463; SMAC (DIABLO) binds to IAPs. DR Reactome; R-HSA-111464; SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes. DR Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins. DR Reactome; R-HSA-111469; SMAC, XIAP-regulated apoptotic response. DR Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins. DR SignaLink; P55210; -. DR SIGNOR; P55210; -. DR BioGRID-ORCS; 840; 17 hits in 1171 CRISPR screens. DR ChiTaRS; CASP7; human. DR EvolutionaryTrace; P55210; -. DR GeneWiki; Caspase_7; -. DR GenomeRNAi; 840; -. DR Pharos; P55210; Tchem. DR PRO; PR:P55210; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P55210; Protein. DR Bgee; ENSG00000165806; Expressed in rectum and 181 other cell types or tissues. DR ExpressionAtlas; P55210; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; TAS:UniProt. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:Ensembl. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB. DR GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB. DR GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:UniProtKB. DR GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc. DR GO; GO:0008233; F:peptidase activity; IDA:BHF-UCL. DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProt. DR GO; GO:0072734; P:cellular response to staurosporine; IMP:CAFA. DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl. DR GO; GO:0097194; P:execution phase of apoptosis; IDA:UniProt. DR GO; GO:0044346; P:fibroblast apoptotic process; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0070227; P:lymphocyte apoptotic process; ISS:UniProtKB. DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl. DR GO; GO:1905686; P:positive regulation of plasma membrane repair; IEA:Ensembl. DR GO; GO:0030163; P:protein catabolic process; IDA:UniProt. DR GO; GO:0051604; P:protein maturation; IDA:UniProt. DR GO; GO:0016485; P:protein processing; IEA:Ensembl. DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB. DR GO; GO:0009411; P:response to UV; IEA:Ensembl. DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl. DR CDD; cd00032; CASc; 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; 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. DR Genevisible; P55210; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Allosteric enzyme; Alternative splicing; KW Apoptosis; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protease; KW Reference proteome; RNA-binding; Secreted; Thiol protease; Zymogen. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT PROPEP 2..23 FT /note="N-terminally processed" FT /evidence="ECO:0000305|PubMed:12824163, FT ECO:0000305|PubMed:16916640, ECO:0000305|PubMed:23650375, FT ECO:0000305|PubMed:8755496" FT /id="PRO_0000004616" FT CHAIN 24..198 FT /note="Caspase-7 subunit p20" FT /evidence="ECO:0000305|PubMed:12824163, FT ECO:0000305|PubMed:16916640, ECO:0000305|PubMed:23650375, FT ECO:0000305|PubMed:27889207, ECO:0000305|PubMed:8755496" FT /id="PRO_0000004617" FT PROPEP 199..206 FT /evidence="ECO:0000305|PubMed:12824163, FT ECO:0000305|PubMed:16916640, ECO:0000305|PubMed:23650375, FT ECO:0000305|PubMed:27889207" FT /id="PRO_0000004618" FT CHAIN 207..303 FT /note="Caspase-7 subunit p11" FT /evidence="ECO:0000305|PubMed:12824163, FT ECO:0000305|PubMed:16916640, ECO:0000305|PubMed:27889207, FT ECO:0000305|PubMed:8755496" FT /id="PRO_0000004619" FT REGION 1..30 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 38..41 FT /note="Exosite" FT /evidence="ECO:0000269|PubMed:22451931, FT ECO:0000269|PubMed:31586028, ECO:0000269|PubMed:34156061" FT REGION 76..87 FT /note="Loop L1" FT /evidence="ECO:0000303|PubMed:23897474" FT REGION 187..196 FT /note="Loop L2" FT /evidence="ECO:0000303|PubMed:23897474" FT REGION 226..238 FT /note="Loop L3" FT /evidence="ECO:0000303|PubMed:23897474" FT REGION 274..288 FT /note="Loop L4" FT /evidence="ECO:0000303|PubMed:23897474" FT COMPBIAS 1..17 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 144 FT /evidence="ECO:0000269|PubMed:15314233" FT ACT_SITE 186 FT /evidence="ECO:0000269|PubMed:11701129, FT ECO:0000269|PubMed:15314233, ECO:0000269|PubMed:16916640" FT SITE 36..37 FT /note="Cleavage; by CAPN1" FT /evidence="ECO:0000269|PubMed:19617626" FT SITE 45..46 FT /note="Cleavage; by CAPN1" FT /evidence="ECO:0000269|PubMed:19617626" FT SITE 47..48 FT /note="Cleavage; by CAPN1" FT /evidence="ECO:0000269|PubMed:19617626" FT SITE 187 FT /note="Involved in allosteric regulation" FT /evidence="ECO:0000269|PubMed:15314233, FT ECO:0000269|PubMed:19581639" FT SITE 223 FT /note="Involved in allosteric regulation" FT /evidence="ECO:0000269|PubMed:15314233, FT ECO:0000269|PubMed:19581639" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT MOD_RES 30 FT /note="Phosphoserine; by PAK2" FT /evidence="ECO:0000269|PubMed:21555521, FT ECO:0000269|PubMed:27889207" FT MOD_RES 37 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 173 FT /note="Phosphothreonine; by PAK2" FT /evidence="ECO:0000269|PubMed:21555521, FT ECO:0000269|PubMed:27889207" FT MOD_RES 233 FT /note="(Microbial infection) ADP-riboxanated arginine" FT /evidence="ECO:0000269|PubMed:35338844, FT ECO:0000269|PubMed:35446120" FT MOD_RES 239 FT /note="Phosphoserine; by PAK2" FT /evidence="ECO:0000269|PubMed:21555521, FT ECO:0000269|PubMed:27889207" FT VAR_SEQ 1..36 FT /note="MADDQGCIEEQGVEDSANEDSVDAKPDRSSFVPSLF -> MQRGLFSDGDT FT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045325" FT VAR_SEQ 1 FT /note="M -> MDCVGWPPGRKWHLEKNTSCGGSSGICASYVTQM (in isoform FT Alpha')" FT /evidence="ECO:0000303|PubMed:19054851, FT ECO:0000303|PubMed:8521391, ECO:0000303|PubMed:9070923" FT /id="VSP_000806" FT VAR_SEQ 149..303 FT /note="VIYGKDGVTPIKDLTAHFRGDRCKTLLEKPKLFFIQACRGTELDDGIQADSG FT PINDTDANPRYKIPVEADFLFAYSTVPGYYSWRSPGRGSWFVQALCSILEEHGKDLEIM FT QILTRVNDRVARHFESQSDDPHFHEKKQIPCVVSMLTKELYFSQ -> MESCSVTQAGV FT QRRDLGRLQPPPPRLAEGPSLMMASRPTRGPSMTQMLILDTRSQWKLTSSSPIPRFQAI FT TRGGAQEEAPGLCKPSAPSWRSTEKTWKSCRSSPG (in isoform Beta)" FT /evidence="ECO:0000303|PubMed:8521391" FT /id="VSP_000807" FT VARIANT 4 FT /note="D -> E (in dbSNP:rs11555408)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5" FT /id="VAR_048617" FT VARIANT 255 FT /note="D -> E (in dbSNP:rs2227310)" FT /id="VAR_048618" FT MUTAGEN 23 FT /note="D->A: Abolished cleavage at the N-terminus, leading FT to impaired activation and thiol protease activity. In FT P7-D2A mutant; abolished cleavage and activation, leading FT to decreased but mesureable activity; when associated with FT A-198." FT /evidence="ECO:0000269|PubMed:12824163, FT ECO:0000269|PubMed:22451931, ECO:0000269|PubMed:23650375, FT ECO:0000269|PubMed:34156061" FT MUTAGEN 30 FT /note="S->A: Abolished phosphorylation by PAK2; when FT associated with A-173 and A-239." FT /evidence="ECO:0000269|PubMed:21555521" FT MUTAGEN 30 FT /note="S->E: Mimics phosphorylation; does not affect thiol FT protease activity." FT /evidence="ECO:0000269|PubMed:27889207" FT MUTAGEN 38..41 FT /note="KKKK->AAAA: Decreased ability to cleave PARP1 and FT PTGES3." FT /evidence="ECO:0000269|PubMed:22451931, FT ECO:0000269|PubMed:28863261" FT MUTAGEN 38..41 FT /note="KKKK->AKKA: Decreased ability to cleave PARP1." FT /evidence="ECO:0000269|PubMed:31586028" FT MUTAGEN 39..40 FT /note="KK->AA: Does not affect ability to cleave PARP1." FT /evidence="ECO:0000269|PubMed:22451931, FT ECO:0000269|PubMed:31586028" FT MUTAGEN 39..40 FT /note="KK->EE: Decreased ability to cleave PARP1. Decreased FT RNA-binding." FT /evidence="ECO:0000269|PubMed:22451931, FT ECO:0000269|PubMed:31586028, ECO:0000269|PubMed:34156061" FT MUTAGEN 39 FT /note="K->E: Decreased ability to cleave PARP1." FT /evidence="ECO:0000269|PubMed:22451931" FT MUTAGEN 173 FT /note="T->A: Abolished phosphorylation by PAK2; when FT associated with A-30 and A-239." FT /evidence="ECO:0000269|PubMed:21555521" FT MUTAGEN 186 FT /note="C->A: Abolished thiol protease activity." FT /evidence="ECO:0000269|PubMed:11701129, FT ECO:0000269|PubMed:11752425, ECO:0000269|PubMed:12824163, FT ECO:0000269|PubMed:16916640, ECO:0000269|PubMed:27889207, FT ECO:0000269|PubMed:8576161" FT MUTAGEN 187 FT /note="R->K: Does not significantly affect thiol protease FT catalytic efficiency." FT /evidence="ECO:0000269|PubMed:19581639" FT MUTAGEN 187 FT /note="R->M,A,G: Reduced thiol protease catalytic FT efficiency." FT /evidence="ECO:0000269|PubMed:19581639" FT MUTAGEN 187 FT /note="R->W,N: Strongly reduced thiol protease catalytic FT efficiency." FT /evidence="ECO:0000269|PubMed:19581639" FT MUTAGEN 192 FT /note="D->A: Strongly reduced thiol protease activity." FT /evidence="ECO:0000269|PubMed:16916640" FT MUTAGEN 195..206 FT /note="IQADSGPINDTD->LVPRGS: In mutant II; prevents FT cleavage of loop L2 region; retains significant thiol FT protease activity." FT /evidence="ECO:0000269|PubMed:23897474" FT MUTAGEN 195..200 FT /note="IQADSG->LVPRGS: In mutant III; prevents cleavage of FT loop L2 region; abolished thiol protease activity." FT /evidence="ECO:0000269|PubMed:23897474" FT MUTAGEN 198..204 FT /note="DSGPIND->ASGPINDLVPRGS: In mutant IV; prevents FT cleavage of loop L2 region; retains significant thiol FT protease activity." FT /evidence="ECO:0000269|PubMed:23897474" FT MUTAGEN 198 FT /note="D->A: Strongly reduced cleavage and activation by FT initiator caspases. Abolished cleavage and activation by FT initiator caspases; when associated with A-206. In P7-D2A FT mutant; abolished cleavage and activation, leading to FT decreased but mesureable activity; when associated with FT A-23." FT /evidence="ECO:0000269|PubMed:12824163, FT ECO:0000269|PubMed:16916640, ECO:0000269|PubMed:23650375" FT MUTAGEN 206 FT /note="D->A: Reduced cleavage and activation by initiator FT caspases. Abolished cleavage and activation by initiator FT caspases; when associated with A-198." FT /evidence="ECO:0000269|PubMed:12824163, FT ECO:0000269|PubMed:16916640" FT MUTAGEN 223 FT /note="Y->A,F,W,D,E: Does not significantly affect thiol FT protease catalytic efficiency." FT /evidence="ECO:0000269|PubMed:19581639" FT MUTAGEN 229 FT /note="Y->W: Strongly reduced thiol protease catalytic FT efficiency." FT /evidence="ECO:0000269|PubMed:19581639" FT MUTAGEN 230..234 FT /note="YSWRS->VSYRV: In esCasp-7 V3 mutant; promotes FT specificity toward alternate peptides with VEID, YVAD, FT WEHD, LETD or LEHD sequence; when associated with C-276. In FT esCasp-7 V4 mutant; promotes specificity toward alternate FT peptides with VEID, YVAD, WEHD, LETD or LEHD sequence; when FT associated with D-276." FT /evidence="ECO:0000269|PubMed:27032039" FT MUTAGEN 232..234 FT /note="WRS->HRE: In dsCasp-7 mutant; unable to cleave DEVD FT and VEID peptides; when associated with F-276." FT /evidence="ECO:0000269|PubMed:27032039" FT MUTAGEN 233 FT /note="R->A: Abolished ADP-riboxanation by C.violaceum FT CopC." FT /evidence="ECO:0000269|PubMed:35446120" FT MUTAGEN 239 FT /note="S->A: Abolished phosphorylation by PAK2; when FT associated with A-30 and A-173." FT /evidence="ECO:0000269|PubMed:21555521" FT MUTAGEN 239 FT /note="S->E: Mimics phosphorylation; leading to inactivate FT thiol protease activity." FT /evidence="ECO:0000269|PubMed:27889207" FT MUTAGEN 276 FT /note="Q->C: In esCasp-7 V3 mutant; promotes specificity FT toward alternate peptides with VEID, YVAD, WEHD, LETD or FT LEHD sequence; when associated with 230-V--V-234." FT /evidence="ECO:0000269|PubMed:27032039" FT MUTAGEN 276 FT /note="Q->D: In esCasp-7 V4 mutant; promotes specificity FT toward alternate peptides with VEID, YVAD, WEHD, LETD or FT LEHD sequence; when associated with 230-V--V-234." FT /evidence="ECO:0000269|PubMed:27032039" FT MUTAGEN 276 FT /note="Q->F: In dsCasp-7 mutant; unable to cleave DEVD sand FT VEID peptides; when associated with 232-H--E-234." FT /evidence="ECO:0000269|PubMed:27032039" FT MUTAGEN 290 FT /note="C->S: Decreased phosphorylation by PAK2." FT /evidence="ECO:0000269|PubMed:27889207" FT MUTAGEN 290 FT /note="C->T,N: Does not significantly affect thiol protease FT catalytic activity." FT /evidence="ECO:0000269|PubMed:19581639" FT CONFLICT 194 FT /note="G -> A (in Ref. 2; AAC50346)" FT /evidence="ECO:0000305" FT HELIX 56..58 FT /evidence="ECO:0007829|PDB:4JB8" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:4JR2" FT STRAND 68..74 FT /evidence="ECO:0007829|PDB:4JR2" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:4JR2" FT HELIX 90..104 FT /evidence="ECO:0007829|PDB:4JR2" FT STRAND 106..113 FT /evidence="ECO:0007829|PDB:4JR2" FT HELIX 116..127 FT /evidence="ECO:0007829|PDB:4JR2" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:1F1J" FT STRAND 137..143 FT /evidence="ECO:0007829|PDB:4JR2" FT STRAND 149..152 FT /evidence="ECO:0007829|PDB:4JR2" FT STRAND 155..158 FT /evidence="ECO:0007829|PDB:4JR2" FT HELIX 159..163 FT /evidence="ECO:0007829|PDB:4JR2" FT HELIX 164..166 FT /evidence="ECO:0007829|PDB:4JR2" FT TURN 168..170 FT /evidence="ECO:0007829|PDB:4JR2" FT HELIX 172..174 FT /evidence="ECO:0007829|PDB:4JR2" FT STRAND 179..185 FT /evidence="ECO:0007829|PDB:4JR2" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:4JB8" FT TURN 209..211 FT /evidence="ECO:0007829|PDB:4JR1" FT TURN 215..218 FT /evidence="ECO:0007829|PDB:4JR2" FT STRAND 219..225 FT /evidence="ECO:0007829|PDB:4JR2" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:4HQ0" FT STRAND 232..234 FT /evidence="ECO:0007829|PDB:4JR2" FT TURN 235..237 FT /evidence="ECO:0007829|PDB:4JR2" FT HELIX 240..252 FT /evidence="ECO:0007829|PDB:4JR2" FT TURN 253..255 FT /evidence="ECO:0007829|PDB:4JR2" FT HELIX 258..272 FT /evidence="ECO:0007829|PDB:4JR2" FT TURN 276..278 FT /evidence="ECO:0007829|PDB:4ZVO" FT HELIX 280..282 FT /evidence="ECO:0007829|PDB:4JR2" FT STRAND 290..293 FT /evidence="ECO:0007829|PDB:4JR2" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:4JR2" SQ SEQUENCE 303 AA; 34277 MW; CD373EE54A232CA4 CRC64; MADDQGCIEE QGVEDSANED SVDAKPDRSS FVPSLFSKKK KNVTMRSIKT TRDRVPTYQY NMNFEKLGKC IIINNKNFDK VTGMGVRNGT DKDAEALFKC FRSLGFDVIV YNDCSCAKMQ DLLKKASEED HTNAACFACI LLSHGEENVI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL FFIQACRGTE LDDGIQADSG PINDTDANPR YKIPVEADFL FAYSTVPGYY SWRSPGRGSW FVQALCSILE EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP HFHEKKQIPC VVSMLTKELY FSQ //