ID   CASP3_RABIT             Reviewed;         277 AA.
AC   Q8MJC3;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 48.
DE   RecName: Full=Caspase-3;
DE            Short=CASP-3;
DE            EC=3.4.22.56;
DE   AltName: Full=Apopain;
DE   AltName: Full=Cysteine protease CPP32;
DE   Contains:
DE     RecName: Full=Caspase-3 subunit p17;
DE   Contains:
DE     RecName: Full=Caspase-3 subunit p12;
DE   Flags: Precursor;
GN   Name=CASP3;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC   Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=98236830; PubMed=9575916;
RA   Wang H., Keiser J.A.;
RT   "Molecular characterization of rabbit CPP32 and its function in
RT   vascular smooth muscle cell apoptosis.";
RL   Am. J. Physiol. 274:H1132-H1140(1998).
CC   -!- FUNCTION: Involved in the activation cascade of caspases
CC       responsible for apoptosis execution. At the onset of apoptosis it
CC       proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a
CC       '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory
CC       element binding proteins (SREBPs) between the basic helix-loop-
CC       helix leucine zipper domain and the membrane attachment domain.
CC       Cleaves and activates caspase-6, -7 and -9 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Strict requirement for an Asp residue at
CC       positions P1 and P4. It has a preferred cleavage sequence of Asp-
CC       Xaa-Xaa-Asp-|- with a hydrophobic amino-acid residue at P2 and a
CC       hydrophilic amino-acid residue at P3, although Val or Ala are also
CC       accepted at this position.
CC   -!- SUBUNIT: Heterotetramer that consists of two anti-parallel
CC       arranged heterodimers, each one formed by a 17 kDa (p17) and a 12
CC       kDa (p12) subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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
CC       of caspase-7 protease and the large subunit of caspase-3 also
CC       occur and vice versa (By similarity).
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
CC       caspase activity. Fas therefore activates caspase-3 not only by
CC       inducing the cleavage of the caspase zymogen to its active
CC       subunits, but also by stimulating the denitrosylation of its
CC       active site thiol (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase C14A family.
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DR   EMBL; AF506008; AAM47195.1; -; mRNA.
DR   RefSeq; NP_001075586.1; -.
DR   UniGene; Ocu.2659; -.
DR   HSSP; P42574; 1PAU.
DR   MEROPS; C14.003; -.
DR   GeneID; 100008840; -.
DR   HOVERGEN; Q8MJC3; -.
DR   BRENDA; 3.4.22.56; 255.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptosis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR015470; Caspase_3_related.
DR   InterPro; IPR011600; Pept_C14_cat.
DR   InterPro; IPR001309; Pept_C14_ICE_p20.
DR   InterPro; IPR016129; Pept_C14_ICE_p20_AS.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR002398; Pept_C14_p45.
DR   InterPro; IPR015917; Pept_C14_p45_core.
DR   PANTHER; PTHR10454:SF30; Casp3_like; 1.
DR   PANTHER; PTHR10454; Pept_C14_p45; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00115; CASc; 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   2: Evidence at transcript level;
KW   Apoptosis; Cytoplasm; Hydrolase; Phosphoprotein; Protease;
KW   S-nitrosylation; Thiol protease; Zymogen.
FT   PROPEP        1      9       By similarity.
FT                                /FTId=PRO_0000004585.
FT   PROPEP       10     28       By similarity.
FT                                /FTId=PRO_0000004586.
FT   CHAIN        29    175       Caspase-3 subunit p17 (By similarity).
FT                                /FTId=PRO_0000004587.
FT   CHAIN       176    277       Caspase-3 subunit p12 (By similarity).
FT                                /FTId=PRO_0000004588.
FT   ACT_SITE    121    121       By similarity.
FT   ACT_SITE    163    163       By similarity.
FT   MOD_RES      26     26       Phosphoserine (By similarity).
FT   MOD_RES     163    163       S-nitrosocysteine; in inhibited form (By
FT                                similarity).
SQ   SEQUENCE   277 AA;  31653 MW;  7BA4B12E6D43629A CRC64;
     MENNETSVDA KSIKNLETQT IHGSKSMDSG KYLDNSYKMD YPEMGLCIII NNKNFHKNTG
     MSSRSGTDVN AANLGETFMN LKYEVRNKND LTREEIMELM YNVSKEDHSK RSSFICVILS
     HGDEGVIYGT NGPIELKKLT SFFRGDYCRS LTGKPKLFII QACRGTELDS GIETDSGVDY
     DMACQKIPVE ADFLYAYSTA PGYYSWRNSE EGSWFIQSLC AMLKEYAHKL EFMHILTRVN
     RKVATEFESY SLDATFHAKK QIPCIVSMLT KELYFYH
//