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Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]

 CASP3_SAIBB             Reviewed;         277 AA.
Q5IS99;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
23-MAY-2018, entry version 77.
RecName: Full=Caspase-3;
Short=CASP-3;
EC=3.4.22.56;
Contains:
RecName: Full=Caspase-3 subunit p17;
Contains:
RecName: Full=Caspase-3 subunit p12;
Flags: Precursor;
Name=CASP3;
Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Platyrrhini; Cebidae; Saimiriinae; Saimiri.
NCBI_TaxID=39432;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=15620360; DOI=10.1016/j.cell.2004.11.040;
Dorus S., Vallender E.J., Evans P.D., Anderson J.R., Gilbert S.L.,
Mahowald M., Wyckoff G.J., Malcom C.M., Lahn B.T.;
"Accelerated evolution of nervous system genes in the origin of Homo
sapiens.";
Cell 119:1027-1040(2004).
-!- 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. Involved in the
cleavage of huntingtin. 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 {ECO:0000250}.
-!- 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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EMBL; AY665229; AAV74267.1; -; mRNA.
RefSeq; NP_001266895.1; NM_001279966.1.
RefSeq; XP_010342651.1; XM_010344349.1.
RefSeq; XP_010342652.1; XM_010344350.1.
ProteinModelPortal; Q5IS99; -.
SMR; Q5IS99; -.
MEROPS; C14.003; -.
PRIDE; Q5IS99; -.
Ensembl; ENSSBOT00000027937; ENSSBOP00000011157; ENSSBOG00000022394.
GeneID; 101029697; -.
KEGG; sbq:101029697; -.
CTD; 836; -.
GeneTree; ENSGT00760000118912; -.
HOVERGEN; HBG050802; -.
KO; K02187; -.
Proteomes; UP000233220; Whole Genome Shotgun Assembly.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IEA:Ensembl.
GO; GO:0072734; P:cellular response to staurosporine; IEA:Ensembl.
GO; GO:0030218; P:erythrocyte differentiation; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
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_0000254879.
PROPEP 10 28 {ECO:0000250}.
/FTId=PRO_0000254880.
CHAIN 29 175 Caspase-3 subunit p17.
/FTId=PRO_0000254881.
CHAIN 176 277 Caspase-3 subunit p12.
/FTId=PRO_0000254882.
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}.
SEQUENCE 277 AA; 31394 MW; F4777B44E2823BD3 CRC64;
MENTENSVDS KSIKNSEPKI IHGSKSVDSG ISLDNSYKMD YPEMGLCIII NNKNFHKSTG
MASRSGTDVD AANLRETFMN LKYEVRNKND LTREEIVELM RNVSKEDHSK RSSFVCVLLS
HGEEGIIFGT NGPVDLKKIT SFFRGDCCRS LTGKPKLFII QACRGTELDC GIETDSGVDD
DMACHKIPVE ADFLYAYSTA PGYYSWRNSR DGSWFIQSLC AMLKQYAHKL EFMHILTRVN
RKVATEFESS SFDATFHAKK QIPCIVSMLT KELYFYQ


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