ID CASP3_PIG Reviewed; 277 AA.
AC Q95ND5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-APR-2013, entry version 73.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11440638; DOI=10.1089/107999001750277880;
RA Muneta Y., Shimojima Y., Mori Y.;
RT "Porcine caspase-3: its cloning and activity during apoptosis of PK15
RT cells induced by porcine Fas ligand.";
RL J. Interferon Cytokine Res. 21:409-415(2001).
RN [2]
RP INTERACTION WITH ASFIVIRUS A224L.
RX PubMed=11222676; DOI=10.1128/JVI.75.6.2535-2543.2001;
RA Nogal M.L., Gonzalez de Buitrago G., Rodriguez C., Cubelos B.,
RA Carrascosa A.L., Salas M.L., Revilla Y.;
RT "African swine fever virus IAP homologue inhibits caspase activation
RT and promotes cell survival in mammalian cells.";
RL J. Virol. 75:2535-2543(2001).
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. Triggers cell adhesion
CC in sympathetic neurons through RET cleavage (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). Subunit p17 interacts with
CC asfivirus A224L protein. Interacts with BIRC6/bruce (By
CC 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; AB029345; BAB55544.1; -; mRNA.
DR RefSeq; NP_999296.1; NM_214131.1.
DR UniGene; Ssc.15886; -.
DR ProteinModelPortal; Q95ND5; -.
DR SMR; Q95ND5; 29-277.
DR STRING; 9823.ENSSSCP00000016724; -.
DR MEROPS; C14.003; -.
DR PaxDb; Q95ND5; -.
DR GeneID; 397244; -.
DR KEGG; ssc:397244; -.
DR CTD; 836; -.
DR eggNOG; NOG279444; -.
DR HOGENOM; HOG000231878; -.
DR HOVERGEN; HBG050802; -.
DR KO; K02187; -.
DR OrthoDB; EOG4CZBGR; -.
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:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR015470; Caspase_3.
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; PTHR10454; 1.
DR PANTHER; PTHR10454:SF30; PTHR10454:SF30; 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 1: Evidence at protein level;
KW Apoptosis; Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein;
KW Protease; Reference proteome; S-nitrosylation; Thiol protease;
KW Zymogen.
FT PROPEP 1 9 By similarity.
FT /FTId=PRO_0000004581.
FT PROPEP 10 28 By similarity.
FT /FTId=PRO_0000004582.
FT CHAIN 29 175 Caspase-3 subunit p17 (By similarity).
FT /FTId=PRO_0000004583.
FT CHAIN 176 277 Caspase-3 subunit p12 (By similarity).
FT /FTId=PRO_0000004584.
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; 31379 MW; 616C0F56141B012B CRC64;
MENNKTSVDS KSIKTLETKI LHGSKSMDSG ISLDVSYKMD YPEMGLCIII NNKNFDKNTG
MACRSGTDVD AANLRETFTN LKYEVRNKND LTREEILELM HSVSKEDHSK RSSFICVLLS
HGEEGKIFGT NGPVDLKKLT SFFRGDCCRT LTGKPKLFII QACRGTELDC GIETDSGTED
DMACQKIPVE ADFLYAYSTA PGYYSWRNSK DGSWFIQSLC AALKQYVHKL ELMHILTRVN
RKVAVEFESF STDSTFHAKK QIPCIVSMLT KELYFYH
//
