ID   CASP3_CANFA             Reviewed;         277 AA.
AC   Q8MKI5;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Caspase-3;
DE            Short=CASP-3;
DE            EC=3.4.22.56;
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   Canis familiaris (Dog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15187371; DOI=10.1292/jvms.66.563;
RA   Sano J., Oguma K., Kano R., Hasegawa A.;
RT   "Characterization of canine caspase-3.";
RL   J. Vet. Med. Sci. 66:563-567(2004).
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, -8 and -10 generates the
CC       two active subunits. Additional processing of the propeptides is
CC       likely due to the autocatalytic activity of the activated
CC       protease. Active heterodimers between the small subunit of
CC       caspase-7 protease and the large subunit of caspase-3 also occur
CC       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; AB085580; BAB92962.1; -; mRNA.
DR   RefSeq; NP_001003042.1; -.
DR   UniGene; Cfa.84; -.
DR   HSSP; P42574; 1PAU.
DR   MEROPS; C14.003; -.
DR   Ensembl; ENSCAFG00000007750; Canis familiaris.
DR   GeneID; 403567; -.
DR   KEGG; cfa:403567; -.
DR   HOVERGEN; Q8MKI5; -.
DR   BRENDA; 3.4.22.56; 463.
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_0000004557.
FT   PROPEP       10     28       By similarity.
FT                                /FTId=PRO_0000004558.
FT   CHAIN        29    175       Caspase-3 subunit p17 (By similarity).
FT                                /FTId=PRO_0000004559.
FT   CHAIN       176    277       Caspase-3 subunit p12 (By similarity).
FT                                /FTId=PRO_0000004560.
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;  31335 MW;  7094C76D868BDAB9 CRC64;
     MENTENSVDA KSFKNAETKI LHGSKSMDSG MSFDNSYKMD YPEMGLCIII NNKNFHKSTG
     MAPRSGTDVD AANLRETFTN LKYEVRNKND LTCEEILELM NSVSKEDHSK RSSFVCVLLS
     HGDEGIIFGT NGPVDLRKVT GFFRGDYCRS LTGKPKLFII QACRGTELDC GIETDSGIED
     DMACQKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC AMLKLYAHKL EFMHILTRVN
     RKVATEFESF SLDSAFHGKK QIPCIVSMLT KELYLYH
//