CASPC_MOUSE
ID CASPC_MOUSE Reviewed; 419 AA.
AC O08736; Q3TT82;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Caspase-12;
DE Short=CASP-12;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=Casp12;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C3H/An;
RX PubMed=9038361; DOI=10.1016/s0014-5793(97)00026-4;
RA van de Craen M., Vandenabeele P., Declercq W., van den Brande I.,
RA van Loo G., Molemans F., Schotte P., van Criekinge W., Beyaert R.,
RA Fiers W.;
RT "Characterization of seven murine caspase family members.";
RL FEBS Lett. 403:61-69(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Ovary, and Uterus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N-3; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP INTERACTION WITH TRAF2.
RX PubMed=11278723; DOI=10.1074/jbc.m010677200;
RA Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., Tohyama M.;
RT "Activation of caspase-12, an endoplastic reticulum (ER) resident caspase,
RT through tumor necrosis factor receptor-associated factor 2-dependent
RT mechanism in response to the ER stress.";
RL J. Biol. Chem. 276:13935-13940(2001).
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). Interacts
CC with TRAF2 under resting conditions; this interaction is reduced in ER
CC stress conditions. {ECO:0000269|PubMed:11278723, ECO:0000305}.
CC -!- INTERACTION:
CC O08736; Q12933: TRAF2; Xeno; NbExp=6; IntAct=EBI-6140033, EBI-355744;
CC -!- TISSUE SPECIFICITY: Mainly expressed in skeletal muscle and lung.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR EMBL; Y13090; CAA73532.1; -; mRNA.
DR EMBL; AK077256; BAC36712.1; -; mRNA.
DR EMBL; AK161525; BAE36443.1; -; mRNA.
DR EMBL; BC028979; AAH28979.1; -; mRNA.
DR CCDS; CCDS22800.1; -.
DR RefSeq; NP_033938.3; NM_009808.4.
DR AlphaFoldDB; O08736; -.
DR SMR; O08736; -.
DR BioGRID; 198494; 3.
DR IntAct; O08736; 1.
DR STRING; 10090.ENSMUSP00000027009; -.
DR MEROPS; C14.013; -.
DR iPTMnet; O08736; -.
DR PhosphoSitePlus; O08736; -.
DR MaxQB; O08736; -.
DR PaxDb; O08736; -.
DR PRIDE; O08736; -.
DR ProteomicsDB; 283678; -.
DR Antibodypedia; 8737; 579 antibodies from 42 providers.
DR DNASU; 12364; -.
DR Ensembl; ENSMUST00000027009; ENSMUSP00000027009; ENSMUSG00000025887.
DR GeneID; 12364; -.
DR KEGG; mmu:12364; -.
DR UCSC; uc009obw.2; mouse.
DR CTD; 100506742; -.
DR MGI; MGI:1312922; Casp12.
DR VEuPathDB; HostDB:ENSMUSG00000025887; -.
DR eggNOG; KOG3573; Eukaryota.
DR GeneTree; ENSGT00940000162555; -.
DR InParanoid; O08736; -.
DR OMA; IIIMQAC; -.
DR OrthoDB; 1327703at2759; -.
DR PhylomeDB; O08736; -.
DR TreeFam; TF102023; -.
DR BRENDA; 3.4.22.B66; 3474.
DR BioGRID-ORCS; 12364; 4 hits in 71 CRISPR screens.
DR PRO; PR:O08736; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O08736; protein.
DR Bgee; ENSMUSG00000025887; Expressed in temporalis muscle and 134 other tissues.
DR ExpressionAtlas; O08736; baseline and differential.
DR Genevisible; O08736; MM.
DR GO; GO:0097169; C:AIM2 inflammasome complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0072557; C:IPAF inflammasome complex; IBA:GO_Central.
DR GO; GO:0072559; C:NLRP3 inflammasome complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; ISO:MGI.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IDA:MGI.
DR GO; GO:0044346; P:fibroblast apoptotic process; IDA:MGI.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IDA:ParkinsonsUK-UCL.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0010663; P:positive regulation of striated muscle cell apoptotic process; ISO:MGI.
DR GO; GO:0016540; P:protein autoprocessing; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
DR GO; GO:0097264; P:self proteolysis; IDA:ParkinsonsUK-UCL.
DR CDD; cd00032; CASc; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR035713; Caspase_12.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR002398; Pept_C14.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR PANTHER; PTHR10454:SF134; PTHR10454:SF134; 1.
DR Pfam; PF00619; CARD; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF52129; SSF52129; 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_0000004647"
FT CHAIN ?..419
FT /note="Caspase-12"
FT /id="PRO_0000004648"
FT DOMAIN 1..92
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT REGION 88..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 250
FT /evidence="ECO:0000250"
FT ACT_SITE 298
FT /evidence="ECO:0000250"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920D5"
SQ SEQUENCE 419 AA; 47854 MW; B94B0FED16B1CB40 CRC64;
MAARRTHERD PIYKIKGLAK DMLDGVFDDL VEKNVLNGDE LLKIGESASF ILNKAENLVE
NFLEKTDMAG KIFAGHIANS QEQLSLQFSN DEDDGPQKIC TPSSPSESKR KVEDDEMEVN
AGLAHESHLM LTAPHGLQSS EVQDTLKLCP RDQFCKIKTE RAKEIYPVME KEGRTRLALI
ICNKKFDYLF DRDNADTDIL NMQELLENLG YSVVLKENLT AQEMETELMQ FAGRPEHQSS
DSTFLVFMSH GILEGICGVK HRNKKPDVLH DDTIFKIFNN SNCRSLRNKP KILIMQACRG
RYNGTIWVST NKGIATADTD EERVLSCKWN NSITKAHVET DFIAFKSSTP HNISWKVGKT
GSLFISKLID CFKKYCWCYH LEEIFRKVQH SFEVPGELTQ MPTIERVSMT RYFYLFPGN
