CASP3_HUMAN
ID CASP3_HUMAN Reviewed; 277 AA.
AC P42574; A8K5M2; D3DP53; Q96AN1; Q96KP2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 238.
DE RecName: Full=Caspase-3;
DE Short=CASP-3;
DE EC=3.4.22.56 {ECO:0000269|PubMed:23152800, ECO:0000269|PubMed:23845944, ECO:0000269|PubMed:30878284, ECO:0000269|PubMed:33725486};
DE AltName: Full=Apopain {ECO:0000303|PubMed:8696339};
DE AltName: Full=Cysteine protease CPP32 {ECO:0000303|PubMed:7774019};
DE Short=CPP-32 {ECO:0000303|PubMed:7774019};
DE AltName: Full=Protein Yama {ECO:0000303|PubMed:7774019};
DE AltName: Full=SREBP cleavage activity 1;
DE Short=SCA-1;
DE Contains:
DE RecName: Full=Caspase-3 subunit p17;
DE Contains:
DE RecName: Full=Caspase-3 subunit p12;
DE Flags: Precursor;
GN Name=CASP3; Synonyms=CPP32;
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], AND VARIANT ASP-190.
RC TISSUE=T-cell;
RX PubMed=7983002; DOI=10.1016/s0021-9258(18)47344-9;
RA Fernandes-Alnemri T., Litwack G., Alnemri E.S.;
RT "CPP32, a novel human apoptotic protein with homology to Caenorhabditis
RT elegans cell death protein Ced-3 and mammalian interleukin-1 beta-
RT converting enzyme.";
RL J. Biol. Chem. 269:30761-30764(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=7774019; DOI=10.1016/0092-8674(95)90541-3;
RA Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D.R.,
RA Poirier G.G., Salvesen G.S., Dixit V.M.;
RT "Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable
RT protease that cleaves the death substrate poly(ADP-ribose) polymerase.";
RL Cell 81:801-809(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-190.
RX PubMed=15003516; DOI=10.1016/j.bbrc.2004.02.021;
RA Pelletier M., Cartron P.F., Delaval F., Meflah K., Vallette F.M.,
RA Oliver L.;
RT "Caspase 3 activation is controlled by a sequence located in the N-terminus
RT of its large subunit.";
RL Biochem. Biophys. Res. Commun. 316:93-99(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [8]
RP PROTEIN SEQUENCE OF 29-46 AND 176-193, FUNCTION, AND VARIANT ASP-190.
RX PubMed=7596430; DOI=10.1038/376037a0;
RA Nicholson D.W., Ali A., Thornberry N.A., Vaillancourt J.P., Ding C.K.,
RA Gallant M., Gareau Y., Griffin P.R., Labelle M., Lazebnik Y.A.,
RA Munday N.A., Raju S.M., Smulson M.E., Yamin T.-T., Li V.L., Miller D.K.;
RT "Identification and inhibition of the ICE/CED-3 protease necessary for
RT mammalian apoptosis.";
RL Nature 376:37-43(1995).
RN [9]
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 [10]
RP CLEAVAGE OF HUNTINGTIN, AND FUNCTION.
RX PubMed=8696339; DOI=10.1038/ng0896-442;
RA Goldberg Y.P., Nicholson D.W., Rasper D.M., Kalchman M.A., Koide H.B.,
RA Graham R.K., Bromm M., Kazemi-Esfarjani P., Thornberry N.A.,
RA Vaillancourt J.P., Hayden M.R.;
RT "Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is
RT modulated by the polyglutamine tract.";
RL Nat. Genet. 13:442-449(1996).
RN [11]
RP S-NITROSYLATION AT CYS-163.
RX PubMed=10213689; DOI=10.1126/science.284.5414.651;
RA Mannick J.B., Hausladen A., Liu L., Hess D.T., Zeng M., Miao Q.X.,
RA Kane L.S., Gow A.J., Stamler J.S.;
RT "Fas-induced caspase denitrosylation.";
RL Science 284:651-654(1999).
RN [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [14]
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 [15]
RP FUNCTION IN CELL ADHESION.
RX PubMed=21357690; DOI=10.1074/jbc.m110.195461;
RA Cabrera J.R., Bouzas-Rodriguez J., Tauszig-Delamasure S., Mehlen P.;
RT "RET modulates cell adhesion via its cleavage by caspase in sympathetic
RT neurons.";
RL J. Biol. Chem. 286:14628-14638(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [17]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23152800; DOI=10.1371/journal.pone.0048770;
RA Sen T., Sen N., Noordhuis M.G., Ravi R., Wu T.C., Ha P.K., Sidransky D.,
RA Hoque M.O.;
RT "OGDHL is a modifier of AKT-dependent signaling and NF-kappaB function.";
RL PLoS ONE 7:e48770-e48770(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [19]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23845944; DOI=10.1126/science.1236758;
RA Suzuki J., Denning D.P., Imanishi E., Horvitz H.R., Nagata S.;
RT "Xk-Related protein 8 and CED-8 promote phosphatidylserine exposure in
RT apoptotic cells.";
RL Science 341:403-406(2013).
RN [20]
RP FUNCTION, AND CATALYTIC ACTIVITY.
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 [21]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=33725486; DOI=10.1016/j.molcel.2021.02.025;
RA Maruoka M., Zhang P., Mori H., Imanishi E., Packwood D.M., Harada H.,
RA Kosako H., Suzuki J.;
RT "Caspase cleavage releases a nuclear protein fragment that stimulates
RT phospholipid scrambling at the plasma membrane.";
RL Mol. Cell 81:1397-1410(2021).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-277.
RX PubMed=8673606; DOI=10.1038/nsb0796-619;
RA Rotonda J., Nicholson D.W., Fazil K.M., Gallant M., Gareau Y., Labelle M.,
RA Peterson E.P., Rasper D.M., Ruel R., Vaillancourt J.P., Thornberry N.A.,
RA Becker J.W.;
RT "The three-dimensional structure of apopain/CPP32, a key mediator of
RT apoptosis.";
RL Nat. Struct. Biol. 3:619-625(1996).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 35-173 AND 185-277.
RX PubMed=9045680; DOI=10.1074/jbc.272.10.6539;
RA Mittl P.R.E., di Marco S., Krebs J.F., Bai X., Karanewsky D.S.,
RA Priestle J.P., Tomaselli K.J., Gruetter M.G.;
RT "Structure of recombinant human CPP32 in complex with the tetrapeptide
RT acetyl-Asp-Val-Ala-Asp fluoromethyl ketone.";
RL J. Biol. Chem. 272:6539-6547(1997).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
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).
CC -!- FUNCTION: Involved in the activation cascade of caspases responsible
CC for apoptosis execution (PubMed:7596430). At the onset of apoptosis it
CC proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-
CC Asp-|-Gly-217' bond (PubMed:7774019). Cleaves and activates sterol
CC regulatory element binding proteins (SREBPs) between the basic helix-
CC loop-helix leucine zipper domain and the membrane attachment domain.
CC Cleaves and activates caspase-6, -7 and -9 (PubMed:7596430). Involved
CC in the cleavage of huntingtin (PubMed:8696339). Triggers cell adhesion
CC in sympathetic neurons through RET cleavage (PubMed:21357690). Cleaves
CC and inhibits serine/threonine-protein kinase AKT1 in response to
CC oxidative stress (PubMed:23152800). Acts as an inhibitor of type I
CC interferon production during virus-induced apoptosis by mediating
CC cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing
CC cytokine overproduction (PubMed:30878284). Cleaves XRCC4 and
CC phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to
CC promote phosphatidylserine exposure on apoptotic cell surface
CC (PubMed:23845944, PubMed:33725486). {ECO:0000269|PubMed:21357690,
CC ECO:0000269|PubMed:23152800, ECO:0000269|PubMed:23845944,
CC ECO:0000269|PubMed:30878284, ECO:0000269|PubMed:33725486,
CC ECO:0000269|PubMed:7596430, ECO:0000269|PubMed:7774019,
CC ECO:0000269|PubMed:8696339}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Strict requirement for an Asp residue at positions P1 and P4.
CC It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a
CC hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid
CC residue at P3, although Val or Ala are also accepted at this
CC position.; EC=3.4.22.56; Evidence={ECO:0000269|PubMed:23152800,
CC ECO:0000269|PubMed:23845944, ECO:0000269|PubMed:30878284,
CC ECO:0000269|PubMed:33725486};
CC -!- ACTIVITY REGULATION: Inhibited by isatin sulfonamides.
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12)
CC subunit. Interacts with BIRC6/bruce. {ECO:0000269|PubMed:15200957}.
CC -!- INTERACTION:
CC P42574; O43823: AKAP8; NbExp=5; IntAct=EBI-524064, EBI-1237481;
CC P42574; Q9Y243: AKT3; NbExp=2; IntAct=EBI-524064, EBI-296115;
CC P42574; P05067: APP; NbExp=4; IntAct=EBI-524064, EBI-77613;
CC P42574; P54252: ATXN3; NbExp=9; IntAct=EBI-524064, EBI-946046;
CC P42574; P55212: CASP6; NbExp=2; IntAct=EBI-524064, EBI-718729;
CC P42574; P55211: CASP9; NbExp=2; IntAct=EBI-524064, EBI-516799;
CC P42574; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-524064, EBI-25840379;
CC P42574; P42858: HTT; NbExp=9; IntAct=EBI-524064, EBI-466029;
CC P42574; Q00987: MDM2; NbExp=2; IntAct=EBI-524064, EBI-389668;
CC P42574; O60551: NMT2; NbExp=2; IntAct=EBI-524064, EBI-3920273;
CC P42574; P09874: PARP1; NbExp=2; IntAct=EBI-524064, EBI-355676;
CC P42574; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-524064, EBI-12288855;
CC P42574; P10599: TXN; NbExp=6; IntAct=EBI-524064, EBI-594644;
CC P42574; Q9BYP7: WNK3; NbExp=2; IntAct=EBI-524064, EBI-1182602;
CC P42574; P98170: XIAP; NbExp=4; IntAct=EBI-524064, EBI-517127;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highly expressed in lung, spleen, heart, liver and
CC kidney. Moderate levels in brain and skeletal muscle, and low in
CC testis. Also found in many cell lines, highest expression in cells of
CC the immune system.
CC -!- PTM: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10
CC generates the two active subunits. Additional processing of the
CC propeptides is likely due to the autocatalytic activity of the
CC activated protease. Active heterodimers between the small subunit of
CC caspase-7 protease and the large subunit of caspase-3 also occur and
CC vice versa.
CC -!- PTM: S-nitrosylated on its catalytic site cysteine in unstimulated
CC human cell lines and denitrosylated upon activation of the Fas
CC apoptotic pathway, associated with an increase in intracellular caspase
CC activity. Fas therefore activates caspase-3 not only by inducing the
CC cleavage of the caspase zymogen to its active subunits, but also by
CC stimulating the denitrosylation of its active site thiol.
CC {ECO:0000269|PubMed:10213689}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/casp3/";
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DR EMBL; U13737; AAA65015.1; -; mRNA.
DR EMBL; U13738; AAB60355.1; -; mRNA.
DR EMBL; U26943; AAA74929.1; -; mRNA.
DR EMBL; AJ413269; CAC88866.1; -; mRNA.
DR EMBL; AK291337; BAF84026.1; -; mRNA.
DR EMBL; AY219866; AAO25654.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04673.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04674.1; -; Genomic_DNA.
DR EMBL; CH471056; EAX04675.1; -; Genomic_DNA.
DR EMBL; BC016926; AAH16926.1; -; mRNA.
DR CCDS; CCDS3836.1; -.
DR PIR; A55315; A55315.
DR RefSeq; NP_004337.2; NM_004346.3.
DR RefSeq; NP_116786.1; NM_032991.2.
DR RefSeq; XP_011530603.1; XM_011532301.1.
DR PDB; 1CP3; X-ray; 2.30 A; A/B=1-277.
DR PDB; 1GFW; X-ray; 2.80 A; A=29-175, B=181-277.
DR PDB; 1I3O; X-ray; 2.70 A; A/C=1-175, B/D=176-277.
DR PDB; 1NME; X-ray; 1.60 A; A=29-174, B=186-277.
DR PDB; 1NMQ; X-ray; 2.40 A; A/B=29-277.
DR PDB; 1NMS; X-ray; 1.70 A; A/B=29-277.
DR PDB; 1PAU; X-ray; 2.50 A; A=29-175, B=176-277.
DR PDB; 1QX3; X-ray; 1.90 A; A=29-277.
DR PDB; 1RE1; X-ray; 2.50 A; A=29-175, B=176-277.
DR PDB; 1RHJ; X-ray; 2.20 A; A/C=29-175, B/D=176-277.
DR PDB; 1RHK; X-ray; 2.50 A; A=29-175, B=176-277.
DR PDB; 1RHM; X-ray; 2.50 A; A/C=29-175, B/D=176-277.
DR PDB; 1RHQ; X-ray; 3.00 A; A/D=29-175, B/E=176-277.
DR PDB; 1RHR; X-ray; 3.00 A; A=29-175, B=176-277.
DR PDB; 1RHU; X-ray; 2.51 A; A=29-175, B=176-277.
DR PDB; 2C1E; X-ray; 1.77 A; A=29-175, B=176-277.
DR PDB; 2C2K; X-ray; 1.87 A; A=29-175, B=176-277.
DR PDB; 2C2M; X-ray; 1.94 A; A=29-175, B=176-277.
DR PDB; 2C2O; X-ray; 2.45 A; A=29-175, B=176-277.
DR PDB; 2CDR; X-ray; 1.70 A; A=29-175, B=176-277.
DR PDB; 2CJX; X-ray; 1.70 A; A=29-175, B=176-277.
DR PDB; 2CJY; X-ray; 1.67 A; A=29-175, B=176-277.
DR PDB; 2CNK; X-ray; 1.75 A; A=29-175, B=176-277.
DR PDB; 2CNL; X-ray; 1.67 A; A=29-175, B=176-277.
DR PDB; 2CNN; X-ray; 1.70 A; A=29-175, B=176-277.
DR PDB; 2CNO; X-ray; 1.95 A; A=29-175, B=176-277.
DR PDB; 2DKO; X-ray; 1.06 A; A=29-174, B=175-277.
DR PDB; 2H5I; X-ray; 1.69 A; A=29-174, B=184-277.
DR PDB; 2H5J; X-ray; 2.00 A; A/C=29-174, B/D=184-277.
DR PDB; 2H65; X-ray; 2.30 A; A/C=29-174, B/D=184-277.
DR PDB; 2J30; X-ray; 1.40 A; A=29-277.
DR PDB; 2J31; X-ray; 1.50 A; A=29-277.
DR PDB; 2J32; X-ray; 1.30 A; A=29-277.
DR PDB; 2J33; X-ray; 2.00 A; A=29-277.
DR PDB; 2XYG; X-ray; 1.54 A; A=29-174, B=185-277.
DR PDB; 2XYH; X-ray; 1.89 A; A=29-174, B=185-277.
DR PDB; 2XYP; X-ray; 1.86 A; A=29-174, B=185-277.
DR PDB; 2XZD; X-ray; 2.10 A; A/C=27-175, B/D=176-277.
DR PDB; 2XZT; X-ray; 2.70 A; A/C=29-175, B/D=176-277.
DR PDB; 2Y0B; X-ray; 2.10 A; A/C=29-175, B/D=176-277.
DR PDB; 3DEH; X-ray; 2.50 A; A/B/C/D=29-277.
DR PDB; 3DEI; X-ray; 2.80 A; A/B/C/D=29-277.
DR PDB; 3DEJ; X-ray; 2.60 A; A/B/C/D=29-277.
DR PDB; 3DEK; X-ray; 2.40 A; A/B/C/D=29-277.
DR PDB; 3EDQ; X-ray; 1.61 A; A/C=29-175, B/D=176-277.
DR PDB; 3GJQ; X-ray; 2.60 A; A/C=29-175, B/D=176-277.
DR PDB; 3GJR; X-ray; 2.20 A; A/C=29-175, B/D=176-277.
DR PDB; 3GJS; X-ray; 1.90 A; A/C=29-175, B/D=176-277.
DR PDB; 3GJT; X-ray; 2.20 A; A/C=29-175, B/D=176-277.
DR PDB; 3H0E; X-ray; 2.00 A; A/B=29-277.
DR PDB; 3ITN; X-ray; 1.63 A; A=29-277.
DR PDB; 3KJF; X-ray; 2.00 A; A=29-175, B=176-277.
DR PDB; 3PCX; X-ray; 1.50 A; A=29-277.
DR PDB; 3PD0; X-ray; 2.00 A; A=29-277.
DR PDB; 3PD1; X-ray; 1.62 A; A=29-277.
DR PDB; 4DCJ; X-ray; 1.70 A; A/D=29-175, B/E=176-277.
DR PDB; 4DCO; X-ray; 1.70 A; A/D=29-175, B/E=176-277.
DR PDB; 4DCP; X-ray; 1.70 A; A/D=29-175, B/E=176-277.
DR PDB; 4EHA; X-ray; 1.70 A; A/C=1-277.
DR PDB; 4EHD; X-ray; 1.58 A; A=1-277.
DR PDB; 4EHF; X-ray; 1.66 A; A=1-277.
DR PDB; 4EHH; X-ray; 1.78 A; A=1-277.
DR PDB; 4EHK; X-ray; 1.67 A; A/C=1-277.
DR PDB; 4EHL; X-ray; 1.80 A; A/C=1-277.
DR PDB; 4EHN; X-ray; 1.69 A; A=1-277.
DR PDB; 4JJE; X-ray; 1.48 A; A=29-277.
DR PDB; 4JQY; X-ray; 2.50 A; A/B=34-277.
DR PDB; 4JQZ; X-ray; 2.89 A; A/B=34-277.
DR PDB; 4JR0; X-ray; 1.80 A; A/B=34-277.
DR PDB; 4PRY; X-ray; 1.70 A; A=1-277.
DR PDB; 4PS0; X-ray; 1.63 A; A/B=1-277.
DR PDB; 4QTX; X-ray; 1.97 A; A=1-277.
DR PDB; 4QTY; X-ray; 1.60 A; A=29-277.
DR PDB; 4QU0; X-ray; 1.95 A; A=1-277.
DR PDB; 4QU5; X-ray; 1.91 A; A=1-277.
DR PDB; 4QU8; X-ray; 1.72 A; A=1-277.
DR PDB; 4QU9; X-ray; 1.56 A; A=1-277.
DR PDB; 4QUA; X-ray; 1.89 A; A=1-277.
DR PDB; 4QUB; X-ray; 1.69 A; A=1-277.
DR PDB; 4QUD; X-ray; 2.00 A; A/B=1-277.
DR PDB; 4QUE; X-ray; 1.84 A; A/C=1-277.
DR PDB; 4QUG; X-ray; 1.92 A; A/C=1-277.
DR PDB; 4QUH; X-ray; 1.76 A; A/C=1-277.
DR PDB; 4QUI; X-ray; 1.76 A; A/B=1-277.
DR PDB; 4QUJ; X-ray; 1.50 A; A=1-277.
DR PDB; 4QUL; X-ray; 1.90 A; A/C=1-277.
DR PDB; 5I9B; X-ray; 1.80 A; A=1-277.
DR PDB; 5I9T; X-ray; 1.95 A; A/C=1-277.
DR PDB; 5IAB; X-ray; 1.79 A; A/C=1-277.
DR PDB; 5IAE; X-ray; 1.55 A; A/C=1-277.
DR PDB; 5IAG; X-ray; 1.98 A; A=1-277.
DR PDB; 5IAJ; X-ray; 1.58 A; A=1-277.
DR PDB; 5IAK; X-ray; 1.82 A; A=1-277.
DR PDB; 5IAN; X-ray; 2.70 A; A=1-277.
DR PDB; 5IAR; X-ray; 1.76 A; A=1-277.
DR PDB; 5IAS; X-ray; 1.54 A; A=1-277.
DR PDB; 5IBC; X-ray; 1.66 A; A=1-277.
DR PDB; 5IBP; X-ray; 1.38 A; A=1-277.
DR PDB; 5IBR; X-ray; 1.74 A; A/C=1-277.
DR PDB; 5IC4; X-ray; 2.65 A; A/C/E/G=1-175, B/D/F/H=176-276.
DR PDBsum; 1CP3; -.
DR PDBsum; 1GFW; -.
DR PDBsum; 1I3O; -.
DR PDBsum; 1NME; -.
DR PDBsum; 1NMQ; -.
DR PDBsum; 1NMS; -.
DR PDBsum; 1PAU; -.
DR PDBsum; 1QX3; -.
DR PDBsum; 1RE1; -.
DR PDBsum; 1RHJ; -.
DR PDBsum; 1RHK; -.
DR PDBsum; 1RHM; -.
DR PDBsum; 1RHQ; -.
DR PDBsum; 1RHR; -.
DR PDBsum; 1RHU; -.
DR PDBsum; 2C1E; -.
DR PDBsum; 2C2K; -.
DR PDBsum; 2C2M; -.
DR PDBsum; 2C2O; -.
DR PDBsum; 2CDR; -.
DR PDBsum; 2CJX; -.
DR PDBsum; 2CJY; -.
DR PDBsum; 2CNK; -.
DR PDBsum; 2CNL; -.
DR PDBsum; 2CNN; -.
DR PDBsum; 2CNO; -.
DR PDBsum; 2DKO; -.
DR PDBsum; 2H5I; -.
DR PDBsum; 2H5J; -.
DR PDBsum; 2H65; -.
DR PDBsum; 2J30; -.
DR PDBsum; 2J31; -.
DR PDBsum; 2J32; -.
DR PDBsum; 2J33; -.
DR PDBsum; 2XYG; -.
DR PDBsum; 2XYH; -.
DR PDBsum; 2XYP; -.
DR PDBsum; 2XZD; -.
DR PDBsum; 2XZT; -.
DR PDBsum; 2Y0B; -.
DR PDBsum; 3DEH; -.
DR PDBsum; 3DEI; -.
DR PDBsum; 3DEJ; -.
DR PDBsum; 3DEK; -.
DR PDBsum; 3EDQ; -.
DR PDBsum; 3GJQ; -.
DR PDBsum; 3GJR; -.
DR PDBsum; 3GJS; -.
DR PDBsum; 3GJT; -.
DR PDBsum; 3H0E; -.
DR PDBsum; 3ITN; -.
DR PDBsum; 3KJF; -.
DR PDBsum; 3PCX; -.
DR PDBsum; 3PD0; -.
DR PDBsum; 3PD1; -.
DR PDBsum; 4DCJ; -.
DR PDBsum; 4DCO; -.
DR PDBsum; 4DCP; -.
DR PDBsum; 4EHA; -.
DR PDBsum; 4EHD; -.
DR PDBsum; 4EHF; -.
DR PDBsum; 4EHH; -.
DR PDBsum; 4EHK; -.
DR PDBsum; 4EHL; -.
DR PDBsum; 4EHN; -.
DR PDBsum; 4JJE; -.
DR PDBsum; 4JQY; -.
DR PDBsum; 4JQZ; -.
DR PDBsum; 4JR0; -.
DR PDBsum; 4PRY; -.
DR PDBsum; 4PS0; -.
DR PDBsum; 4QTX; -.
DR PDBsum; 4QTY; -.
DR PDBsum; 4QU0; -.
DR PDBsum; 4QU5; -.
DR PDBsum; 4QU8; -.
DR PDBsum; 4QU9; -.
DR PDBsum; 4QUA; -.
DR PDBsum; 4QUB; -.
DR PDBsum; 4QUD; -.
DR PDBsum; 4QUE; -.
DR PDBsum; 4QUG; -.
DR PDBsum; 4QUH; -.
DR PDBsum; 4QUI; -.
DR PDBsum; 4QUJ; -.
DR PDBsum; 4QUL; -.
DR PDBsum; 5I9B; -.
DR PDBsum; 5I9T; -.
DR PDBsum; 5IAB; -.
DR PDBsum; 5IAE; -.
DR PDBsum; 5IAG; -.
DR PDBsum; 5IAJ; -.
DR PDBsum; 5IAK; -.
DR PDBsum; 5IAN; -.
DR PDBsum; 5IAR; -.
DR PDBsum; 5IAS; -.
DR PDBsum; 5IBC; -.
DR PDBsum; 5IBP; -.
DR PDBsum; 5IBR; -.
DR PDBsum; 5IC4; -.
DR AlphaFoldDB; P42574; -.
DR SMR; P42574; -.
DR BioGRID; 107286; 116.
DR ComplexPortal; CPX-970; Caspase-3 complex.
DR DIP; DIP-268N; -.
DR ELM; P42574; -.
DR IntAct; P42574; 64.
DR MINT; P42574; -.
DR STRING; 9606.ENSP00000311032; -.
DR BindingDB; P42574; -.
DR ChEMBL; CHEMBL2334; -.
DR DrugBank; DB08498; (1S)-1-(3-chlorophenyl)-2-oxo-2-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]ethyl acetate.
DR DrugBank; DB08497; (1S)-2-oxo-1-phenyl-2-[(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-5-yl)amino]ethyl acetate.
DR DrugBank; DB08213; 1-METHYL-5-(2-PHENOXYMETHYL-PYRROLIDINE-1-SULFONYL)-1H-INDOLE-2,3-DIONE.
DR DrugBank; DB06862; 2-HYDROXY-5-(2-MERCAPTO-ETHYLSULFAMOYL)-BENZOIC ACID.
DR DrugBank; DB08251; 4-[5-(2-CARBOXY-1-FORMYL-ETHYLCARBAMOYL)-PYRIDIN-3-YL]-BENZOIC ACID.
DR DrugBank; DB03124; 5-[4-(1-Carboxymethyl-2-Oxo-Propylcarbamoyl)-Benzylsulfamoyl]-2-Hydroxy-Benzoic Acid.
DR DrugBank; DB08229; [N-(3-dibenzylcarbamoyl-oxiranecarbonyl)-hydrazino]-acetic acid.
DR DrugBank; DB00945; Acetylsalicylic acid.
DR DrugBank; DB05408; Emricasan.
DR DrugBank; DB13751; Glycyrrhizic acid.
DR DrugBank; DB06255; Incadronic acid.
DR DrugBank; DB07696; methyl (3S)-3-[(tert-butoxycarbonyl)amino]-4-oxopentanoate.
DR DrugBank; DB01017; Minocycline.
DR DrugBank; DB08499; N-[3-(2-fluoroethoxy)phenyl]-N'-(1,3,4-trioxo-1,2,3,4-tetrahydroisoquinolin-6-yl)butanediamide.
DR DrugBank; DB00282; Pamidronic acid.
DR DrugCentral; P42574; -.
DR GuidetoPHARMACOLOGY; 1619; -.
DR MEROPS; C14.003; -.
DR GlyGen; P42574; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P42574; -.
DR MetOSite; P42574; -.
DR PhosphoSitePlus; P42574; -.
DR BioMuta; CASP3; -.
DR DMDM; 77416852; -.
DR OGP; P42574; -.
DR EPD; P42574; -.
DR jPOST; P42574; -.
DR MassIVE; P42574; -.
DR MaxQB; P42574; -.
DR PaxDb; P42574; -.
DR PeptideAtlas; P42574; -.
DR PRIDE; P42574; -.
DR ProteomicsDB; 55518; -.
DR ABCD; P42574; 3 sequenced antibodies.
DR Antibodypedia; 1222; 2462 antibodies from 54 providers.
DR CPTC; P42574; 1 antibody.
DR DNASU; 836; -.
DR Ensembl; ENST00000308394.9; ENSP00000311032.4; ENSG00000164305.19.
DR Ensembl; ENST00000523916.5; ENSP00000428929.1; ENSG00000164305.19.
DR GeneID; 836; -.
DR KEGG; hsa:836; -.
DR MANE-Select; ENST00000308394.9; ENSP00000311032.4; NM_004346.4; NP_004337.2.
DR UCSC; uc003iwh.3; human.
DR CTD; 836; -.
DR DisGeNET; 836; -.
DR GeneCards; CASP3; -.
DR HGNC; HGNC:1504; CASP3.
DR HPA; ENSG00000164305; Low tissue specificity.
DR MIM; 600636; gene.
DR neXtProt; NX_P42574; -.
DR OpenTargets; ENSG00000164305; -.
DR PharmGKB; PA26087; -.
DR VEuPathDB; HostDB:ENSG00000164305; -.
DR eggNOG; KOG3573; Eukaryota.
DR GeneTree; ENSGT00940000153232; -.
DR HOGENOM; CLU_036904_2_0_1; -.
DR InParanoid; P42574; -.
DR OMA; ADESYRM; -.
DR OrthoDB; 984395at2759; -.
DR PhylomeDB; P42574; -.
DR TreeFam; TF102023; -.
DR BRENDA; 3.4.22.56; 2681.
DR PathwayCommons; P42574; -.
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-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
DR Reactome; R-HSA-2028269; Signaling by Hippo.
DR Reactome; R-HSA-205025; NADE modulates death signalling.
DR Reactome; R-HSA-211736; Stimulation of the cell death response by PAK-2p34.
DR Reactome; R-HSA-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR Reactome; R-HSA-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-HSA-418889; Caspase activation via Dependence Receptors in the absence of ligand.
DR Reactome; R-HSA-449836; Other interleukin signaling.
DR Reactome; R-HSA-5620971; Pyroptosis.
DR SABIO-RK; P42574; -.
DR SignaLink; P42574; -.
DR SIGNOR; P42574; -.
DR BioGRID-ORCS; 836; 18 hits in 1082 CRISPR screens.
DR ChiTaRS; CASP3; human.
DR EvolutionaryTrace; P42574; -.
DR GeneWiki; Caspase_3; -.
DR GenomeRNAi; 836; -.
DR Pharos; P42574; Tchem.
DR PRO; PR:P42574; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P42574; protein.
DR Bgee; ENSG00000164305; Expressed in jejunal mucosa and 156 other tissues.
DR ExpressionAtlas; P42574; baseline and differential.
DR Genevisible; P42574; HS.
DR GO; GO:0008303; C:caspase complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031264; C:death-inducing signaling complex; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
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:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor 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:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:UniProtKB.
DR GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IMP:UniProtKB.
DR GO; GO:0005123; F:death receptor binding; IEA:Ensembl.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0016005; F:phospholipase A2 activator activity; IEA:Ensembl.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0061713; P:anterior neural tube closure; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:BHF-UCL.
DR GO; GO:0007413; P:axonal fasciculation; IEA:Ensembl.
DR GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
DR GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
DR GO; GO:0072734; P:cellular response to staurosporine; IMP:CAFA.
DR GO; GO:1904019; P:epithelial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0030218; P:erythrocyte differentiation; IDA:UniProtKB.
DR GO; GO:0097194; P:execution phase of apoptosis; IDA:UniProtKB.
DR GO; GO:0044346; P:fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:0034349; P:glial cell apoptotic process; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IEA:Ensembl.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IC:ComplexPortal.
DR GO; GO:0008627; P:intrinsic apoptotic signaling pathway in response to osmotic stress; IEA:Ensembl.
DR GO; GO:0030216; P:keratinocyte differentiation; IBA:GO_Central.
DR GO; GO:0007611; P:learning or memory; IEA:Ensembl.
DR GO; GO:0071887; P:leukocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0001554; P:luteolysis; IEA:Ensembl.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IDA:MGI.
DR GO; GO:0030220; P:platelet formation; TAS:UniProtKB.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IDA:UniProtKB.
DR GO; GO:1902512; P:positive regulation of apoptotic DNA fragmentation; IDA:ComplexPortal.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:ComplexPortal.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0016241; P:regulation of macroautophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
DR GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
DR GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
DR GO; GO:0032025; P:response to cobalt ion; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0034612; P:response to tumor necrosis factor; TAS:BHF-UCL.
DR GO; GO:0009411; P:response to UV; IEA:Ensembl.
DR GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0051146; P:striated muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR CDD; cd00032; CASc; 1.
DR InterPro; IPR015471; Casp3/7.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR002398; Pept_C14.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR PANTHER; PTHR10454:SF31; PTHR10454:SF31; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Apoptosis; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Phosphoprotein; Protease; Reference proteome; S-nitrosylation;
KW Thiol protease; Zymogen.
FT PROPEP 1..9
FT /id="PRO_0000004569"
FT PROPEP 10..28
FT /evidence="ECO:0000269|PubMed:7596430"
FT /id="PRO_0000004570"
FT CHAIN 29..175
FT /note="Caspase-3 subunit p17"
FT /id="PRO_0000004571"
FT CHAIN 176..277
FT /note="Caspase-3 subunit p12"
FT /id="PRO_0000004572"
FT ACT_SITE 121
FT /evidence="ECO:0000250"
FT ACT_SITE 163
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P70677"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 163
FT /note="S-nitrosocysteine; in inhibited form"
FT /evidence="ECO:0000269|PubMed:10213689"
FT VARIANT 22
FT /note="H -> R (in dbSNP:rs35578277)"
FT /id="VAR_048616"
FT VARIANT 190
FT /note="E -> D (in dbSNP:rs1049210)"
FT /evidence="ECO:0000269|PubMed:15003516,
FT ECO:0000269|PubMed:7596430, ECO:0000269|PubMed:7983002"
FT /id="VAR_001401"
FT CONFLICT 31..36
FT /note="ISLDNS -> MSWDTG (in Ref. 3; CAC88866)"
FT /evidence="ECO:0000305"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:2DKO"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:2DKO"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:2DKO"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:2DKO"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:2DKO"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:1I3O"
FT STRAND 111..120
FT /evidence="ECO:0007829|PDB:2DKO"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:2DKO"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:2DKO"
FT HELIX 136..141
FT /evidence="ECO:0007829|PDB:2DKO"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:2DKO"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:2DKO"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:2DKO"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2DKO"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:2DKO"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:1NMS"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:2DKO"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:2DKO"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:2DKO"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:2DKO"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:2DKO"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:2DKO"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:2DKO"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:2DKO"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:2DKO"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2DKO"
SQ SEQUENCE 277 AA; 31608 MW; 2F35CD3BCF7FF64A CRC64;
MENTENSVDS KSIKNLEPKI IHGSESMDSG ISLDNSYKMD YPEMGLCIII NNKNFHKSTG
MTSRSGTDVD AANLRETFRN LKYEVRNKND LTREEIVELM RDVSKEDHSK RSSFVCVLLS
HGEEGIIFGT NGPVDLKKIT NFFRGDRCRS LTGKPKLFII QACRGTELDC GIETDSGVDD
DMACHKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC AMLKQYADKL EFMHILTRVN
RKVATEFESF SFDATFHAKK QIPCIVSMLT KELYFYH
