ID CASPC_RAT Reviewed; 420 AA.
AC Q920D5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=Caspase-12;
DE Short=CASP-12;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=Casp12;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Loisel T.P., Vaillancourt J., Roy S., Nicholson D.W.;
RT "Cloning of rat caspase-12 mRNA.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85 AND SER-90, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in the activation cascade of caspases responsible
CC for apoptosis execution. {ECO:0000250}.
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by two subunits (Potential). May interact
CC with TRAF2 (By similarity). {ECO:0000250, ECO:0000305}.
CC -!- INTERACTION:
CC Q920D5; O95786: RIGI; Xeno; NbExp=4; IntAct=EBI-1374296, EBI-995350;
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR EMBL; AF317633; AAL26897.1; -; mRNA.
DR RefSeq; NP_569106.1; NM_130422.1.
DR AlphaFoldDB; Q920D5; -.
DR SMR; Q920D5; -.
DR DIP; DIP-29839N; -.
DR IntAct; Q920D5; 5.
DR STRING; 10116.ENSRNOP00000071294; -.
DR MEROPS; C14.013; -.
DR iPTMnet; Q920D5; -.
DR PhosphoSitePlus; Q920D5; -.
DR PaxDb; 10116-ENSRNOP00000010244; -.
DR Ensembl; ENSRNOT00055009897; ENSRNOP00055007655; ENSRNOG00055006095.
DR Ensembl; ENSRNOT00060027358; ENSRNOP00060021950; ENSRNOG00060015916.
DR GeneID; 156117; -.
DR KEGG; rno:156117; -.
DR UCSC; RGD:621758; rat.
DR AGR; RGD:621758; -.
DR CTD; 100506742; -.
DR RGD; 621758; Casp12.
DR eggNOG; KOG3573; Eukaryota.
DR InParanoid; Q920D5; -.
DR OrthoDB; 2873736at2759; -.
DR PhylomeDB; Q920D5; -.
DR BRENDA; 3.4.22.B66; 5301.
DR PRO; PR:Q920D5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:RGD.
DR GO; GO:0004175; F:endopeptidase activity; IDA:RGD.
DR GO; GO:0002020; F:protease binding; IDA:RGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR GO; GO:0071287; P:cellular response to manganese ion; IEP:ParkinsonsUK-UCL.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISO:RGD.
DR GO; GO:0044346; P:fibroblast apoptotic process; ISO:RGD.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0001554; P:luteolysis; IEP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:0010663; P:positive regulation of striated muscle cell apoptotic process; IMP:RGD.
DR GO; GO:0016540; P:protein autoprocessing; IDA:RGD.
DR GO; GO:0030163; P:protein catabolic process; IDA:RGD.
DR GO; GO:0034059; P:response to anoxia; IEP:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0010041; P:response to iron(III) ion; IEP:RGD.
DR GO; GO:1904373; P:response to kainic acid; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0097264; P:self proteolysis; ISO:RGD.
DR CDD; cd08325; CARD_CASP1-like; 1.
DR CDD; cd00032; CASc; 1.
DR Gene3D; 3.40.50.1460; -; 1.
DR Gene3D; 3.30.70.1470; Caspase-like; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR011600; Pept_C14_caspase.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR47901; CASPASE RECRUITMENT DOMAIN-CONTAINING PROTEIN 18; 1.
DR PANTHER; PTHR47901:SF6; CASPASE-12; 1.
DR Pfam; PF00619; CARD; 1.
DR Pfam; PF00656; Peptidase_C14; 1.
DR PIRSF; PIRSF038001; Caspase_ICE; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; Caspase-like; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR PROSITE; PS50209; CARD; 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; Hydrolase; Phosphoprotein; Protease; Reference proteome;
KW Thiol protease; Zymogen.
FT PROPEP 1..?
FT /evidence="ECO:0000255"
FT /id="PRO_0000317444"
FT CHAIN ?..420
FT /note="Caspase-12"
FT /id="PRO_0000317445"
FT DOMAIN 1..92
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT REGION 93..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 251
FT /evidence="ECO:0000250"
FT ACT_SITE 299
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 420 AA; 47837 MW; E00809BBC61461AC CRC64;
MAAKRTHERD PIYKIKGLAK DMLDGVFDDL MDKNVLNGDE LLKIGEGASL ILSKAENLVE
SFFEKTEMAG KIFAGHIANS DKQLSLQFPS DDEEDELQKM FTPSSASESR GKVEDEEMEV
NVGVAHASHL MLTVPQGIQS TEVQDSLKLC SRDWFCTMKT ERAEEIYPVM EKEGRTRLAL
IICNKKFDYL FDRDDAETDI LNMKELLQNL GYSVVIKENL TAQEMETELM KFAGRPEHQS
SDSTFLVFMS HGILEGICGV KHRNKKPDVL HDDTIFTIFN NSNCPSLRNK PKILIMQACR
GRHTGTIWVS TSKGIATADT DEECVLSHRW NNSITKAHVE TDFIAFKSST PHNISWKVGK
SGSLFISKLI DCFKKYCWCY HLEEIFRKVQ YSFEVPGELT QMPTIERVSM TRYFYLFPGN
//
