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Caspase-2 (CASP-2) (EC 3.4.22.55) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]

 CASP2_RAT               Reviewed;         452 AA.
P55215; O35398; O55194; Q9WUI6;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
06-DEC-2005, sequence version 3.
08-MAY-2019, entry version 166.
RecName: Full=Caspase-2;
Short=CASP-2;
EC=3.4.22.55;
AltName: Full=Protease ICH-1;
Contains:
RecName: Full=Caspase-2 subunit p18;
Contains:
RecName: Full=Caspase-2 subunit p13;
Contains:
RecName: Full=Caspase-2 subunit p12;
Flags: Precursor;
Name=Casp2; Synonyms=Ich1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9427555; DOI=10.1016/S0378-1119(97)00463-0;
Sato N., Milligan C.E., Uchiyama Y., Oppenheim R.W.;
"Cloning and expression of the cDNA encoding rat caspase-2.";
Gene 202:127-132(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
STRAIN=Sprague-Dawley; TISSUE=Brain;
PubMed=12067235; DOI=10.1046/j.1471-4159.2002.00781.x;
Jin K., Nagayama T., Mao X., Kawaguchi K., Hickey R.W.,
Greenberg D.A., Simon R.P., Graham S.H.;
"Two caspase-2 transcripts are expressed in rat hippocampus after
global cerebral ischemia.";
J. Neurochem. 81:25-35(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 67-324.
STRAIN=Sprague-Dawley; TISSUE=Kidney cortex;
PubMed=9530276;
Kaushal G.P., Singh A.B., Shah S.V.;
"Identification of gene family of caspases in rat kidney and altered
expression in ischemia-reperfusion injury.";
Am. J. Physiol. 274:F587-F595(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 198-379.
TISSUE=Ovary;
PubMed=7588240; DOI=10.1210/endo.136.11.7588240;
Flaws J.A., Kugu K., Trbovich A.M., Desanti A., Tilly K.I.,
Hirshfield A.N., Tilly J.L.;
"Interleukin-1 beta-converting enzyme-related proteases (IRPs) and
mammalian cell death: dissociation of IRP-induced oligonucleosomal
endonuclease activity from morphological apoptosis in granulosa cells
of the ovarian follicle.";
Endocrinology 136:5042-5053(1995).
[5]
INTERACTION WITH NOL3.
PubMed=16639714; DOI=10.1002/jcb.20946;
Zhang Y.Q., Herman B.;
"ARC protects rat cardiomyocytes against oxidative stress through
inhibition of caspase-2 mediated mitochondrial pathway.";
J. Cell. Biochem. 99:575-588(2006).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. Might function by either
activating some proteins required for cell death or inactivating
proteins necessary for cell survival (By similarity). Associates
with PIDD1 and CRADD to form the PIDDosome, a complex that
activates CASP2 and triggers apoptosis in response to genotoxic
stress (By similarity). {ECO:0000250|UniProtKB:P42575}.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for an Asp residue at P1, with 316-asp
being essential for proteolytic activity and has a preferred
cleavage sequence of Val-Asp-Val-Ala-Asp-|-.; EC=3.4.22.55;
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a p18 subunit and a p12
subunit. Forms a complex named the PIDDosome with PIDD1 and CRADD
(By similarity). Interacts with NOL3 (via CARD domain); inhibits
CASP2 activity in a phosphorylation-dependent manner
(PubMed:16639714). {ECO:0000250|UniProtKB:P42575,
ECO:0000269|PubMed:16639714}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=caspase-2L;
IsoId=P55215-1; Sequence=Displayed;
Name=2; Synonyms=caspase-2S;
IsoId=P55215-2; Sequence=VSP_016555, VSP_016556;
-!- DOMAIN: The CARD domain mediates a direct interaction with CRADD.
{ECO:0000250|UniProtKB:P42575}.
-!- PTM: The mature protease can process its own propeptide, but not
that of other caspases. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB82567.1; Type=Frameshift; Positions=137, 189; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U77933; AAB96379.1; -; mRNA.
EMBL; AF136231; AAD33684.1; -; mRNA.
EMBL; AF136232; AAD33685.1; -; mRNA.
EMBL; AF025671; AAB82567.1; ALT_FRAME; mRNA.
EMBL; U34684; AAC52260.1; -; mRNA.
PIR; I67436; I67436.
PIR; JC6507; JC6507.
RefSeq; NP_071967.2; NM_022522.2. [P55215-1]
SMR; P55215; -.
DIP; DIP-48602N; -.
IntAct; P55215; 2.
STRING; 10116.ENSRNOP00000022672; -.
MEROPS; C14.006; -.
iPTMnet; P55215; -.
PhosphoSitePlus; P55215; -.
jPOST; P55215; -.
PaxDb; P55215; -.
PRIDE; P55215; -.
Ensembl; ENSRNOT00000022672; ENSRNOP00000022672; ENSRNOG00000016707. [P55215-1]
GeneID; 64314; -.
KEGG; rno:64314; -.
UCSC; RGD:69274; rat. [P55215-1]
CTD; 835; -.
RGD; 69274; Casp2.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000156657; -.
HOGENOM; HOG000290714; -.
InParanoid; P55215; -.
KO; K02186; -.
OMA; VMVLMTH; -.
OrthoDB; 1092723at2759; -.
PhylomeDB; P55215; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.55; 5301.
Reactome; R-RNO-168638; NOD1/2 Signaling Pathway.
Reactome; R-RNO-205025; NADE modulates death signalling.
Reactome; R-RNO-6803207; TP53 Regulates Transcription of Caspase Activators and Caspases.
PRO; PR:P55215; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000016707; Expressed in 10 organ(s), highest expression level in spleen.
ExpressionAtlas; P55215; baseline and differential.
Genevisible; P55215; RN.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006915; P:apoptotic process; IMP:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; IEA:Ensembl.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IBA:GO_Central.
GO; GO:0001554; P:luteolysis; IEP:RGD.
GO; GO:0003407; P:neural retina development; IEP:RGD.
GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0012501; P:programmed cell death; TAS:RGD.
GO; GO:0016485; P:protein processing; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; TAS:RGD.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR035702; Caspase_2.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
PANTHER; PTHR10454:SF151; PTHR10454:SF151; 1.
Pfam; PF00619; CARD; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00114; CARD; 1.
SMART; SM00115; CASc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; Complete proteome;
Hydrolase; Phosphoprotein; Protease; Reference proteome;
Thiol protease; Zymogen.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P42575}.
PROPEP 2 169
/FTId=PRO_0000043403.
CHAIN 170 325 Caspase-2 subunit p18. {ECO:0000250}.
/FTId=PRO_0000044573.
PROPEP 326 333
/FTId=PRO_0000044574.
CHAIN 334 452 Caspase-2 subunit p13. {ECO:0000250}.
/FTId=PRO_0000004551.
CHAIN 348 452 Caspase-2 subunit p12. {ECO:0000250}.
/FTId=PRO_0000004552.
DOMAIN 32 121 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
ACT_SITE 277 277 {ECO:0000250}.
ACT_SITE 320 320 {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P42575}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000250|UniProtKB:P42575}.
MOD_RES 340 340 Phosphoserine.
{ECO:0000250|UniProtKB:P42575}.
VAR_SEQ 323 343 DETDRGVDQQDGKNHAQSPGC -> GAIGSLGPLLLFTAAT
ASLAL (in isoform 2).
{ECO:0000303|PubMed:12067235}.
/FTId=VSP_016555.
VAR_SEQ 344 452 Missing (in isoform 2).
{ECO:0000303|PubMed:12067235}.
/FTId=VSP_016556.
CONFLICT 145 145 C -> Y (in Ref. 3; AAB82567).
{ECO:0000305}.
CONFLICT 166 166 D -> H (in Ref. 3; AAB82567).
{ECO:0000305}.
CONFLICT 177 177 K -> E (in Ref. 3; AAB82567).
{ECO:0000305}.
CONFLICT 197 197 Q -> R (in Ref. 3; AAB82567).
{ECO:0000305}.
CONFLICT 340 340 S -> P (in Ref. 4; AAC52260).
{ECO:0000305}.
CONFLICT 348 349 AG -> TV (in Ref. 4; AAC52260).
{ECO:0000305}.
CONFLICT 367 367 G -> V (in Ref. 4; AAC52260).
{ECO:0000305}.
CONFLICT 373 373 G -> D (in Ref. 4; AAC52260).
{ECO:0000305}.
CONFLICT 376 377 AM -> PI (in Ref. 4; AAC52260).
{ECO:0000305}.
SEQUENCE 452 AA; 50728 MW; 03F9D096BB741CE3 CRC64;
MAASSGRSQS SLHRKGLMAA DRRSRILAVC GMHPDHQETL KKNRVVLAKQ LLLSELLEHL
LEKDIITLEM RELIQAKGGS FSQNVELLNL LPKRGPQAFD AFCEALRETR QGHLEDLLLT
TLSDIQHILP PLSCDYDSSL PFSVCESCPP HKQSRLSTDT MEHSLDNGDG PPCLQVKPCT
PEFYQAHYQL AYRLQSQPRG LALVMSNVHF TGEKDLEFRS GGDVDHTTLV TLFKLLGYNV
HVLYDQTAQE MQEKLQNFAQ LPAHRVTDSC IVALLSHGVE GGIYGVDGKL LQLQEVFRLF
DNANCPSLQN KPKMFFIQAC RGDETDRGVD QQDGKNHAQS PGCEESDAGK EELMKMRLPT
RSDMICGYAC LKGNAAMRNT KRGSWYIEAL TQVFSERACD MHVADMLVKV NALIKEREGY
APGTEFHRCK EMSEYCSTLC QQLYLFPGYP PT


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[Casp2 Ich1 Nedd-2 Nedd2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
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[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (IRP) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
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[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Casp7 Lice2 Mch3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (Cysteine protease LICE2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[Cflar Cash] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[CASP7 MCH3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (CMH-1) (ICE-like apoptotic protease 3) (ICE-LAP3) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[csp-2 Y73B6BL.7] Putative inactive caspase B [Cleaved into: Putative inactive caspase B subunit p31; Putative inactive caspase B subunit p17; Putative inactive caspase subunit p14]
[csp-1 Y48E1B.13] Caspase A (EC 3.4.22.36) [Cleaved into: Caspase A subunit p16; Caspase A subunit p14]
[Dredd DCP2 CG7486] Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10]
[CASP14] Caspase-14 (CASP-14) (EC 3.4.22.-) [Cleaved into: Caspase-14 subunit p17, mature form; Caspase-14 subunit p10, mature form; Caspase-14 subunit p20, intermediate form; Caspase-14 subunit p8, intermediate form]
[ORF1] Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[ORF1] Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]
[ORF1] Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]

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