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Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]

 CASP3_MOUSE             Reviewed;         277 AA.
P70677; O08668; Q8CHV5; Q9QWI4;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
30-AUG-2017, entry version 166.
RecName: Full=Caspase-3;
Short=CASP-3;
EC=3.4.22.56;
AltName: Full=Apopain;
AltName: Full=Cysteine protease CPP32;
Short=CPP-32;
AltName: Full=LICE;
AltName: Full=Protein Yama;
AltName: Full=SREBP cleavage activity 1;
Short=SCA-1;
Contains:
RecName: Full=Caspase-3 subunit p17;
Contains:
RecName: Full=Caspase-3 subunit p12;
Flags: Precursor;
Name=Casp3; Synonyms=Cpp32;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=8761296;
Juan T.S.-C., McNiece I.K., Jenkins N.A., Gilbert D.J., Copeland N.G.,
Fletcher F.A.;
"Molecular characterization of mouse and rat CPP32 beta gene encoding
a cysteine protease resembling interleukin-1 beta converting enzyme
and CED-3.";
Oncogene 13:749-755(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9070890; DOI=10.1006/bbrc.1996.6002;
Mukasa T., Urase K., Momoi M.Y., Kimura I., Momoi T.;
"Specific expression of CPP32 in sensory neurons of mouse embryos and
activation of CPP32 in the apoptosis induced by a withdrawal of NGF.";
Biochem. Biophys. Res. Commun. 231:770-774(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C3H/An;
PubMed=9038361; DOI=10.1016/S0014-5793(97)00026-4;
van de Craen M., Vandenabeele P., Declercq W., van den Brande I.,
van Loo G., Molemans F., Schotte P., van Criekinge W., Beyaert R.,
Fiers W.;
"Characterization of seven murine caspase family members.";
FEBS Lett. 403:61-69(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Fernandes-Alnemri T., Litwack G., Alnemri E.S.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 58-277.
Denis F., Alam A., Cohen L., Hartgers F., Braun M., Martinez O.,
Fortin J.-P., Sekaly R.-P.;
"Multiple pathways of apoptosis converging on the CPP32 protease.";
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. At the onset of apoptosis it
proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a
'216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory
element binding proteins (SREBPs) between the basic helix-loop-
helix leucine zipper domain and the membrane attachment domain.
Cleaves and activates caspase-6, -7 and -9. Triggers cell adhesion
in sympathetic neurons through RET cleavage (By similarity).
Cleaves IL-1 beta between an Asp and an Ala, releasing the mature
cytokine which is involved in a variety of inflammatory processes.
{ECO:0000250}.
-!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at
positions P1 and P4. It has a preferred cleavage sequence of Asp-
Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a
hydrophilic amino-acid residue at P3, although Val or Ala are also
accepted at this position.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 17 kDa (p17) and a 12
kDa (p12) subunit. Interacts with BIRC6/bruce. {ECO:0000250}.
-!- INTERACTION:
P42859:Htt; NbExp=2; IntAct=EBI-1790419, EBI-5327353;
P11103:Parp1; NbExp=3; IntAct=EBI-1790419, EBI-642213;
P62270:Rps18; NbExp=5; IntAct=EBI-1790419, EBI-352460;
Q96EK4:THAP11 (xeno); NbExp=2; IntAct=EBI-1790419, EBI-1790529;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Highest expression in spleen, lung, liver,
kidney and heart. Lower expression in brain, skeletal muscle and
testis.
-!- PTM: Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10
generates the two active subunits. Additional processing of the
propeptides is likely due to the autocatalytic activity of the
activated protease. Active heterodimers between the small subunit
of caspase-7 protease and the large subunit of caspase-3 also
occur and vice versa (By similarity). {ECO:0000250}.
-!- PTM: S-nitrosylated on its catalytic site cysteine in unstimulated
human cell lines and denitrosylated upon activation of the Fas
apoptotic pathway, associated with an increase in intracellular
caspase activity. Fas therefore activates caspase-3 not only by
inducing the cleavage of the caspase zymogen to its active
subunits, but also by stimulating the denitrosylation of its
active site thiol (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; U54803; AAC52768.1; -; Genomic_DNA.
EMBL; U54802; AAC52768.1; JOINED; Genomic_DNA.
EMBL; U49929; AAC52764.1; -; mRNA.
EMBL; D86352; BAA21727.1; -; mRNA.
EMBL; Y13086; CAA73528.1; -; mRNA.
EMBL; U19522; AAC53196.1; -; mRNA.
EMBL; BC038825; AAH38825.2; -; mRNA.
EMBL; U63720; AAD09504.1; -; mRNA.
CCDS; CCDS22294.1; -.
PIR; JC5410; JC5410.
RefSeq; NP_001271338.1; NM_001284409.1.
RefSeq; NP_033940.1; NM_009810.3.
RefSeq; XP_017168032.1; XM_017312543.1.
UniGene; Mm.34405; -.
ProteinModelPortal; P70677; -.
SMR; P70677; -.
BioGrid; 198497; 17.
DIP; DIP-44076N; -.
ELM; P70677; -.
IntAct; P70677; 9.
MINT; MINT-4050331; -.
STRING; 10090.ENSMUSP00000091238; -.
BindingDB; P70677; -.
ChEMBL; CHEMBL5632; -.
MEROPS; C14.003; -.
iPTMnet; P70677; -.
PhosphoSitePlus; P70677; -.
SwissPalm; P70677; -.
EPD; P70677; -.
MaxQB; P70677; -.
PaxDb; P70677; -.
PeptideAtlas; P70677; -.
PRIDE; P70677; -.
Ensembl; ENSMUST00000093517; ENSMUSP00000091238; ENSMUSG00000031628.
Ensembl; ENSMUST00000211115; ENSMUSP00000147767; ENSMUSG00000031628.
GeneID; 12367; -.
KEGG; mmu:12367; -.
UCSC; uc009lql.2; mouse.
CTD; 836; -.
MGI; MGI:107739; Casp3.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
HOGENOM; HOG000231878; -.
HOVERGEN; HBG050802; -.
InParanoid; P70677; -.
KO; K02187; -.
OMA; VDDDMAC; -.
OrthoDB; EOG091G05YD; -.
PhylomeDB; P70677; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.56; 3474.
Reactome; R-MMU-111459; Activation of caspases through apoptosome-mediated cleavage.
Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-MMU-2028269; Signaling by Hippo.
Reactome; R-MMU-205025; NADE modulates death signalling.
Reactome; R-MMU-211227; Activation of DNA fragmentation factor.
Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-MMU-351906; Apoptotic cleavage of cell adhesion proteins.
Reactome; R-MMU-418889; Ligand-independent caspase activation via DCC.
Reactome; R-MMU-449836; Other interleukin signaling.
ChiTaRS; Casp3; mouse.
PRO; PR:P70677; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031628; -.
CleanEx; MM_CASP3; -.
ExpressionAtlas; P70677; baseline and differential.
Genevisible; P70677; MM.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031264; C:death-inducing signaling complex; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:MGI.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IMP:MGI.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IDA:MGI.
GO; GO:0008234; F:cysteine-type peptidase activity; IDA:MGI.
GO; GO:0005123; F:death receptor binding; IEA:Ensembl.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0016005; F:phospholipase A2 activator activity; IEA:Ensembl.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IDA:MGI.
GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
GO; GO:0072734; P:cellular response to staurosporine; ISO:MGI.
GO; GO:0030218; P:erythrocyte differentiation; ISO:MGI.
GO; GO:0097194; P:execution phase of apoptosis; IDA:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; TAS:Reactome.
GO; GO:0034349; P:glial cell apoptotic process; IMP:MGI.
GO; GO:0007507; P:heart development; IGI:MGI.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; NAS:ParkinsonsUK-UCL.
GO; GO:0008627; P:intrinsic apoptotic signaling pathway in response to osmotic stress; IDA:CAFA.
GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0030889; P:negative regulation of B cell proliferation; IMP:MGI.
GO; GO:0045786; P:negative regulation of cell cycle; IMP:MGI.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:MGI.
GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:CAFA.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0016485; P:protein processing; IDA:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
GO; GO:0032025; P:response to cobalt ion; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
GO; GO:0010033; P:response to organic substance; IDA:MGI.
GO; GO:0009411; P:response to UV; IDA:MGI.
GO; GO:0009611; P:response to wounding; IDA:MGI.
GO; GO:0010165; P:response to X-ray; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom.
InterPro; IPR015470; Caspase_3.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454:SF178; PTHR10454:SF178; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Acetylation; Apoptosis; Complete proteome; Cytoplasm; Hydrolase;
Phosphoprotein; Protease; Reference proteome; S-nitrosylation;
Thiol protease; Zymogen.
PROPEP 1 9 {ECO:0000250}.
/FTId=PRO_0000004573.
PROPEP 10 28 {ECO:0000250}.
/FTId=PRO_0000004574.
CHAIN 29 175 Caspase-3 subunit p17.
/FTId=PRO_0000004575.
CHAIN 176 277 Caspase-3 subunit p12.
/FTId=PRO_0000004576.
ACT_SITE 121 121 {ECO:0000250}.
ACT_SITE 163 163 {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P42574}.
MOD_RES 11 11 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 163 163 S-nitrosocysteine; in inhibited form.
{ECO:0000250|UniProtKB:P42574}.
CONFLICT 63 65 SRS -> ARN (in Ref. 6; AAD09504).
{ECO:0000305}.
CONFLICT 231 231 E -> Q (in Ref. 6; AAD09504).
{ECO:0000305}.
CONFLICT 262 262 I -> F (in Ref. 6; AAD09504).
{ECO:0000305}.
SEQUENCE 277 AA; 31475 MW; CE91598F74826605 CRC64;
MENNKTSVDS KSINNFEVKT IHGSKSVDSG IYLDSSYKMD YPEMGICIII NNKNFHKSTG
MSSRSGTDVD AANLRETFMG LKYQVRNKND LTREDILELM DSVSKEDHSK RSSFVCVILS
HGDEGVIYGT NGPVELKKLT SFFRGDYCRS LTGKPKLFII QACRGTELDC GIETDSGTDE
EMACQKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC SMLKLYAHKL EFMHILTRVN
RKVATEFESF SLDSTFHAKK QIPCIVSMLT KELYFYH


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