CASP7_MOUSE
ID CASP7_MOUSE Reviewed; 303 AA.
AC P97864; O08669;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Caspase-7;
DE Short=CASP-7;
DE EC=3.4.22.60 {ECO:0000269|PubMed:25231987};
DE AltName: Full=Apoptotic protease Mch-3;
DE AltName: Full=Cysteine protease LICE2;
DE Contains:
DE RecName: Full=Caspase-7 subunit p20;
DE Contains:
DE RecName: Full=Caspase-7 subunit p11;
DE Flags: Precursor;
GN Name=Casp7; Synonyms=Lice2, Mch3;
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 TISSUE=Skeletal muscle;
RX PubMed=9070923; DOI=10.1006/geno.1996.4548;
RA Juan T.S.-C., McNiece I.K., Argento J.M., Jenkins N.A., Gilbert D.J.,
RA Copeland N.G., Fletcher F.A.;
RT "Identification and mapping of Casp7, a cysteine protease resembling CPP32
RT beta, interleukin-1 beta converting enzyme, and CED-3.";
RL Genomics 40:86-93(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9125129; DOI=10.1006/bbrc.1997.6234;
RA Mukasa T., Khoroku Y., Tsukahara T., Momoi M.Y., Kimura I., Momoi T.;
RT "Wortmannin enhances CPP32-like activity during neuronal differentiation of
RT P19 embryonal carcinoma cells induced by retinoic acid.";
RL Biochem. Biophys. Res. Commun. 232:192-197(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Liver, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25231987; DOI=10.1074/jbc.m114.583419;
RA Suzuki J., Imanishi E., Nagata S.;
RT "Exposure of phosphatidylserine by Xk-related protein family members during
RT apoptosis.";
RL J. Biol. Chem. 289:30257-30267(2014).
RN [8]
RP FUNCTION.
RX PubMed=30878284; DOI=10.1016/j.molcel.2019.02.013;
RA Ning X., Wang Y., Jing M., Sha M., Lv M., Gao P., Zhang R., Huang X.,
RA Feng J.M., Jiang Z.;
RT "Apoptotic caspases suppress type i interferon production via the cleavage
RT of cGAS, MAVS, and IRF3.";
RL Mol. Cell 74:19-31(2019).
CC -!- FUNCTION: Involved in the activation cascade of caspases responsible
CC for apoptosis execution (By similarity). Cleaves and activates sterol
CC regulatory element binding proteins (SREBPs) (By similarity).
CC Overexpression promotes programmed cell death (By similarity). Cleaves
CC phospholipid scramblase proteins XKR4, XKR8 and XKR9 (PubMed:25231987).
CC Acts as an inhibitor of type I interferon production during virus-
CC induced apoptosis by mediating cleavage of antiviral proteins CGAS,
CC IRF3 and MAVS, thereby preventing cytokine overproduction
CC (PubMed:30878284). {ECO:0000250|UniProtKB:P55210,
CC ECO:0000269|PubMed:25231987, ECO:0000269|PubMed:30878284}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Strict requirement for an Asp residue at position P1 and has a
CC preferred cleavage sequence of Asp-Glu-Val-Asp-|-.; EC=3.4.22.60;
CC Evidence={ECO:0000269|PubMed:25231987};
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11)
CC subunit. Interacts with BIRC6/bruce (By similarity). Interacts with
CC HSPA5 (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P55210}.
CC -!- INTERACTION:
CC P97864; P11103: Parp1; NbExp=3; IntAct=EBI-5307197, EBI-642213;
CC P97864; P62270: Rps18; NbExp=4; IntAct=EBI-5307197, EBI-352460;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, lung, liver and kidney.
CC Low levels in spleen, skeletal muscle and testis. No expression in the
CC brain.
CC -!- PTM: Cleavages by granzyme B or caspase-10 generate the two active
CC subunits. Propeptide domains can also be cleaved efficiently by
CC caspase-3. Active heterodimers between the small subunit of caspase-7
CC and the large subunit of caspase-3, and vice versa, also occur (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC53068.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U67321; AAC53068.1; ALT_INIT; mRNA.
DR EMBL; D86353; BAA19730.1; -; mRNA.
DR EMBL; Y13088; CAA73530.1; -; mRNA.
DR EMBL; BC005428; AAH05428.1; -; mRNA.
DR CCDS; CCDS29915.1; -.
DR RefSeq; NP_031637.1; NM_007611.2.
DR RefSeq; XP_006526679.1; XM_006526616.3.
DR AlphaFoldDB; P97864; -.
DR SMR; P97864; -.
DR BioGRID; 198499; 7.
DR ComplexPortal; CPX-3947; Caspase-7 complex.
DR IntAct; P97864; 10.
DR STRING; 10090.ENSMUSP00000026062; -.
DR MEROPS; C14.004; -.
DR iPTMnet; P97864; -.
DR PhosphoSitePlus; P97864; -.
DR EPD; P97864; -.
DR jPOST; P97864; -.
DR PaxDb; P97864; -.
DR PeptideAtlas; P97864; -.
DR PRIDE; P97864; -.
DR ProteomicsDB; 265536; -.
DR Antibodypedia; 18528; 1073 antibodies from 45 providers.
DR DNASU; 12369; -.
DR Ensembl; ENSMUST00000026062; ENSMUSP00000026062; ENSMUSG00000025076.
DR GeneID; 12369; -.
DR KEGG; mmu:12369; -.
DR UCSC; uc008hyw.1; mouse.
DR CTD; 840; -.
DR MGI; MGI:109383; Casp7.
DR VEuPathDB; HostDB:ENSMUSG00000025076; -.
DR eggNOG; KOG3573; Eukaryota.
DR GeneTree; ENSGT00940000153232; -.
DR HOGENOM; CLU_036904_2_0_1; -.
DR InParanoid; P97864; -.
DR OMA; MQRSQTE; -.
DR OrthoDB; 984395at2759; -.
DR PhylomeDB; P97864; -.
DR TreeFam; TF102023; -.
DR BRENDA; 3.4.22.60; 3474.
DR Reactome; R-MMU-111459; Activation of caspases through apoptosome-mediated cleavage.
DR Reactome; R-MMU-111463; SMAC (DIABLO) binds to IAPs.
DR Reactome; R-MMU-111464; SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes.
DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-MMU-111469; SMAC, XIAP-regulated apoptotic response.
DR Reactome; R-MMU-264870; Caspase-mediated cleavage of cytoskeletal proteins.
DR BioGRID-ORCS; 12369; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Casp7; mouse.
DR PRO; PR:P97864; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P97864; protein.
DR Bgee; ENSMUSG00000025076; Expressed in intestinal villus and 216 other tissues.
DR ExpressionAtlas; P97864; baseline and differential.
DR Genevisible; P97864; MM.
DR GO; GO:0008303; C:caspase complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IDA:MGI.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
DR GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; ISO:MGI.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISO:MGI.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISO:MGI.
DR GO; GO:0072734; P:cellular response to staurosporine; ISO:MGI.
DR GO; GO:0097194; P:execution phase of apoptosis; IGI:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IC:ComplexPortal.
DR GO; GO:0044346; P:fibroblast apoptotic process; IGI:MGI.
DR GO; GO:0007507; P:heart development; IGI:MGI.
DR GO; GO:0006954; P:inflammatory response; IC:ComplexPortal.
DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IC:ComplexPortal.
DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0016485; P:protein processing; IDA:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0009411; P:response to UV; IGI:MGI.
DR CDD; cd00032; CASc; 1.
DR InterPro; IPR015471; Casp3/7.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
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:SF31; PTHR10454:SF31; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; SSF52129; 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; Cytoplasm; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Zymogen.
FT PROPEP 1..23
FT /evidence="ECO:0000250"
FT /id="PRO_0000004624"
FT CHAIN 24..198
FT /note="Caspase-7 subunit p20"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004625"
FT PROPEP 199..206
FT /evidence="ECO:0000250"
FT /id="PRO_0000004626"
FT CHAIN 207..303
FT /note="Caspase-7 subunit p11"
FT /evidence="ECO:0000250"
FT /id="PRO_0000004627"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /evidence="ECO:0000250"
FT ACT_SITE 186
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CONFLICT 10..11
FT /note="EL -> DW (in Ref. 2; BAA19730)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="A -> T (in Ref. 2; BAA19730)"
FT /evidence="ECO:0000305"
FT CONFLICT 48..49
FT /note="VR -> RQ (in Ref. 2; BAA19730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 34061 MW; 747787B5BDE5F744 CRC64;
MTDDQDCAAE LEKVDSSSED GVDAKPDRSS IISSILLKKK RNASAGPVRT GRDRVPTYLY
RMDFQKMGKC IIINNKNFDK ATGMDVRNGT DKDAGALFKC FQNLGFEVTV HNDCSCAKMQ
DLLRKASEED HSNSACFACV LLSHGEEDLI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL
FFIQACRGTE LDDGIQADSG PINDIDANPR NKIPVEADFL FAYSTVPGYY SWRNPGKGSW
FVQALCSILN EHGKDLEIMQ ILTRVNDRVA RHFESQSDDP RFNEKKQIPC MVSMLTKELY
FSR
