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

 CASP3_RAT               Reviewed;         277 AA.
P55213; P70543; P97699; Q62993;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
30-AUG-2017, entry version 157.
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=IRP;
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [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].
TISSUE=Brain;
PubMed=9030616;
Ni B., Wu X., Du Y., Su Y., Hamilton-Byrd E., Rockey P.K.,
Rosteck P. Jr., Poirier G.G., Paul S.M.;
"Cloning and expression of a rat brain interleukin-1beta-converting
enzyme (ICE)-related protease (IRP) and its possible role in apoptosis
of cultured cerebellar granule neurons.";
J. Neurosci. 17:1561-1569(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Heart;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-264.
Yakovlev A.G.;
"Cloning of the rat cysteine protease p32-beta.";
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 30-241.
TISSUE=Ovary;
PubMed=7588240; DOI=10.1210/endo.136.11.7588240;
Flaws J.A., Kugu K., Trbovich A.M., Desanti A., Tilly K.I.,
Hirshfield A.N., Tilly J.L.;
"Interleukin-1 beta-converting enzyme-related proteases (IRPs) and
mammalian cell death: dissociation of IRP-induced oligonucleosomal
endonuclease activity from morphological apoptosis in granulosa cells
of the ovarian follicle.";
Endocrinology 136:5042-5053(1995).
-!- 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).
{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}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Expressed in heart, brain, liver, and muscle
but not in kidney or testis.
-!- DEVELOPMENTAL STAGE: Highly expressed in neuron-enriched regions
of the developing brain, but down-regulated to low levels in the
adult brain.
-!- 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
-----------------------------------------------------------------------
EMBL; U49930; AAC52765.1; -; mRNA.
EMBL; U84410; AAB41792.1; -; mRNA.
EMBL; BC081854; AAH81854.1; -; mRNA.
EMBL; U58656; AAB02722.1; -; mRNA.
EMBL; U34685; AAC52261.1; -; mRNA.
PIR; I67437; I67437.
RefSeq; NP_037054.1; NM_012922.2.
RefSeq; XP_006253192.1; XM_006253130.3.
UniGene; Rn.10562; -.
ProteinModelPortal; P55213; -.
SMR; P55213; -.
ELM; P55213; -.
IntAct; P55213; 1.
MINT; MINT-2635470; -.
STRING; 10116.ENSRNOP00000014096; -.
ChEMBL; CHEMBL1075185; -.
MEROPS; C14.003; -.
iPTMnet; P55213; -.
PhosphoSitePlus; P55213; -.
PaxDb; P55213; -.
PRIDE; P55213; -.
Ensembl; ENSRNOT00000014095; ENSRNOP00000014096; ENSRNOG00000010475.
GeneID; 25402; -.
KEGG; rno:25402; -.
CTD; 836; -.
RGD; 2275; Casp3.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
HOGENOM; HOG000231878; -.
HOVERGEN; HBG050802; -.
InParanoid; P55213; -.
KO; K02187; -.
OMA; VDDDMAC; -.
OrthoDB; EOG091G05YD; -.
PhylomeDB; P55213; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.56; 5301.
Reactome; R-RNO-111459; Activation of caspases through apoptosome-mediated cleavage.
Reactome; R-RNO-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-RNO-2028269; Signaling by Hippo.
Reactome; R-RNO-205025; NADE modulates death signalling.
Reactome; R-RNO-211227; Activation of DNA fragmentation factor.
Reactome; R-RNO-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-RNO-351906; Apoptotic cleavage of cell adhesion proteins.
Reactome; R-RNO-418889; Ligand-independent caspase activation via DCC.
Reactome; R-RNO-449836; Other interleukin signaling.
PRO; PR:P55213; -.
Proteomes; UP000002494; Chromosome 16.
Bgee; ENSRNOG00000010475; -.
Genevisible; P55213; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0031264; C:death-inducing signaling complex; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:Ensembl.
GO; GO:0004861; F:cyclin-dependent protein serine/threonine kinase inhibitor activity; IEA:Ensembl.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0008234; F:cysteine-type peptidase activity; IDA:RGD.
GO; GO:0005123; F:death receptor binding; IPI:RGD.
GO; GO:0016005; F:phospholipase A2 activator activity; IMP:RGD.
GO; GO:0002020; F:protease binding; IPI:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0006915; P:apoptotic process; IMP:RGD.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0045165; P:cell fate commitment; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0072734; P:cellular response to staurosporine; IEA:Ensembl.
GO; GO:0030218; P:erythrocyte differentiation; IBA:GO_Central.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0034349; P:glial cell apoptotic process; IEP:RGD.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0021766; P:hippocampus development; IEP:RGD.
GO; GO:0035556; P:intracellular signal transduction; IMP:RGD.
GO; GO:0008627; P:intrinsic apoptotic signaling pathway in response to osmotic stress; IEA:Ensembl.
GO; GO:0030216; P:keratinocyte differentiation; IBA:GO_Central.
GO; GO:0007611; P:learning or memory; IMP:RGD.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0030889; P:negative regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0045736; P:negative regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
GO; GO:0030182; P:neuron differentiation; IEP:RGD.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0016485; P:protein processing; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; IDA:RGD.
GO; GO:0043200; P:response to amino acid; IEP:RGD.
GO; GO:0046677; P:response to antibiotic; IEP:RGD.
GO; GO:0032025; P:response to cobalt ion; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
GO; GO:0009749; P:response to glucose; IDA:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IDA:RGD.
GO; GO:0001666; P:response to hypoxia; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0010038; P:response to metal ion; IEP:RGD.
GO; GO:0035094; P:response to nicotine; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0009411; P:response to UV; IEA:Ensembl.
GO; GO:0010165; P:response to X-ray; IEP:RGD.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEP:RGD.
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.
2: Evidence at transcript level;
Acetylation; Apoptosis; Complete proteome; Cytoplasm; Hydrolase;
Phosphoprotein; Protease; Reference proteome; S-nitrosylation;
Thiol protease; Zymogen.
PROPEP 1 9 {ECO:0000250}.
/FTId=PRO_0000004589.
PROPEP 10 28 {ECO:0000250}.
/FTId=PRO_0000004590.
CHAIN 29 175 Caspase-3 subunit p17.
/FTId=PRO_0000004591.
CHAIN 176 277 Caspase-3 subunit p12.
/FTId=PRO_0000004592.
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:0000250|UniProtKB:P70677}.
MOD_RES 26 26 Phosphoserine.
{ECO:0000250|UniProtKB:P42574}.
MOD_RES 163 163 S-nitrosocysteine; in inhibited form.
{ECO:0000250|UniProtKB:P42574}.
CONFLICT 25 29 KSMDS -> QVD (in Ref. 4; AAB02722).
{ECO:0000305}.
CONFLICT 170 170 C -> S (in Ref. 5; AAC52261).
{ECO:0000305}.
CONFLICT 178 178 T -> A (in Ref. 5; AAC52261).
{ECO:0000305}.
CONFLICT 182 182 M -> V (in Ref. 5; AAC52261).
{ECO:0000305}.
CONFLICT 187 187 I -> K (in Ref. 5; AAC52261).
{ECO:0000305}.
CONFLICT 190 190 E -> G (in Ref. 2; AAB41792).
{ECO:0000305}.
CONFLICT 199 199 T -> S (in Ref. 5; AAC52261).
{ECO:0000305}.
CONFLICT 211 211 D -> G (in Ref. 5; AAC52261).
{ECO:0000305}.
CONFLICT 236 236 L -> I (in Ref. 4; AAB02722).
{ECO:0000305}.
CONFLICT 245 245 T -> M (in Ref. 2; AAB41792).
{ECO:0000305}.
SEQUENCE 277 AA; 31492 MW; ADABF418E2507402 CRC64;
MDNNETSVDS KSINNFETKT IHGSKSMDSG IYLDSSYKMD YPEMGLCIII NNKNFHKSTG
MSARNGTDVD AANLRETFMA LKYEVRNKND LTREEIMELM DSVSKEDHSK RSSFVCVILS
HGDEGVIFGT NGPVDLKKLT SFFRGDYCRS LTGKPKLFII QACRGTELDC GIETDSGTDD
DMACQKIPVE ADFLYAYSTA PGYYSWRNSR DGSWFIQSLC AMLKLYAHKL EFMHILTRVN
RKVATEFESF SLDATFHAKK QIPCIVSMLT KELYFYH


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