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Database: UniProt
Entry: Q95ND5
LinkDB: Q95ND5
Original site: Q95ND5 
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   11-JUN-2014, entry version 81.
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   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   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR029030; Caspase-like_dom.
DR   InterPro; IPR015470; Caspase_3.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR001309; Pept_C14_ICE_p20.
DR   InterPro; IPR016129; Pept_C14_ICE_p20_AS.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR015917; Pept_C14A_p45_core.
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   Acetylation; Apoptosis; Complete proteome; Cytoplasm; Hydrolase;
KW   Phosphoprotein; Protease; Reference proteome; S-nitrosylation;
KW   Thiol protease; 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       1      1       N-acetylmethionine (By similarity).
FT   MOD_RES      11     11       N6-acetyllysine (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
//
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