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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]

 CFLAR_MOUSE             Reviewed;         484 AA.
O35732; D3Z0W6; O35707; O35733;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
05-JUL-2017, entry version 160.
RecName: Full=CASP8 and FADD-like apoptosis regulator;
AltName: Full=Caspase homolog;
Short=CASH;
AltName: Full=Caspase-eight-related protein;
Short=Casper;
AltName: Full=Caspase-like apoptosis regulatory protein;
Short=CLARP;
AltName: Full=Cellular FLICE-like inhibitory protein;
Short=c-FLIP;
AltName: Full=FADD-like antiapoptotic molecule 1;
Short=FLAME-1;
AltName: Full=Inhibitor of FLICE;
Short=I-FLICE;
AltName: Full=MACH-related inducer of toxicity;
Short=MRIT;
AltName: Full=Usurpin;
Contains:
RecName: Full=CASP8 and FADD-like apoptosis regulator subunit p43;
Contains:
RecName: Full=CASP8 and FADD-like apoptosis regulator subunit p12;
Flags: Precursor;
Name=Cflar; Synonyms=Cash;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver;
PubMed=9289491; DOI=10.1074/jbc.272.32.19641;
Goltsev Y.V., Kovalenko A.V., Arnold E., Varfolomeev E.E.,
Brodianskii V.M., Wallach D.;
"CASH, a novel caspase homologue with death effector domains.";
J. Biol. Chem. 272:19641-19644(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
PubMed=9217161; DOI=10.1038/40657;
Irmler M., Thome M., Hahne M., Schneider P., Hofmann K., Steiner V.,
Bodmer J.-L., Schroeter M., Burns K., Mattmann C., Rimoldi D.,
French L.E., Tschopp J.;
"Inhibition of death receptor signals by cellular FLIP.";
Nature 388:190-195(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
FUNCTION.
PubMed=10894163; DOI=10.1016/S1074-7613(00)80214-9;
Yeh W.-C., Itie A., Elia A.J., Ng M., Shu H.-B., Wakeham A.,
Mirtsos C., Suzuki N., Bonnard M., Goeddel D.V., Mak T.W.;
"Requirement for Casper (c-FLIP) in regulation of death receptor-
induced apoptosis and embryonic development.";
Immunity 12:633-642(2000).
[5]
FUNCTION.
PubMed=10602037;
DOI=10.1002/1521-4141(200001)30:1<155::AID-IMMU155>3.0.CO;2-X;
Wang J., Lobito A.A., Shen F., Hornung F., Winoto A., Lenardo M.J.;
"Inhibition of Fas-mediated apoptosis by the B cell antigen receptor
through c-FLIP.";
Eur. J. Immunol. 30:155-163(2000).
-!- FUNCTION: Apoptosis regulator protein which may function as a
crucial link between cell survival and cell death pathways in
mammalian cells. Acts as an inhibitor of TNFRSF6 mediated
apoptosis. A proteolytic fragment (p43) is likely retained in the
death-inducing signaling complex (DISC) thereby blocking further
recruitment and processing of caspase-8 at the complex. Full
length and shorter isoforms have been shown either to induce
apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic
(caspase) activity (By similarity). {ECO:0000250,
ECO:0000269|PubMed:10602037, ECO:0000269|PubMed:10894163}.
-!- SUBUNIT: TNFRSF6 stimulation triggers recruitment to the death-
inducing signaling complex (DISC) formed by TNFRSF6, FADD and
caspase-8. A proteolytic fragment (p43) stays associated with the
DISC (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=FLIP-L, CASH alpha;
IsoId=O35732-1; Sequence=Displayed;
Name=2; Synonyms=FLIP-S, CASH beta;
IsoId=O35732-2; Sequence=VSP_000842, VSP_000843;
-!- TISSUE SPECIFICITY: Highly expressed in heart.
-!- DEVELOPMENTAL STAGE: At embryonic days E9.5 and E10.5 highest
expression in developing heart.
-!- INDUCTION: Isoform 1 but not isoform 2 is activated by BCR cross-
linking in primary B-cells.
-!- DOMAIN: The caspase domain lacks the active site residues involved
in catalysis.
-!- PTM: Proteolytically processed; probably by caspase-8. Processing
likely occurs at the DISC and generates subunit p43 and p12 (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y14041; CAA74368.1; -; mRNA.
EMBL; Y14042; CAA74369.1; -; mRNA.
EMBL; U97076; AAC53281.1; -; mRNA.
EMBL; AC112968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001276633.1; NM_001289704.2.
RefSeq; NP_997536.1; NM_207653.5.
RefSeq; XP_006495698.1; XM_006495635.3.
RefSeq; XP_011236722.1; XM_011238420.2.
RefSeq; XP_011236723.1; XM_011238421.2.
RefSeq; XP_011236724.1; XM_011238422.1.
RefSeq; XP_011236725.1; XM_011238423.2.
RefSeq; XP_017169048.1; XM_017313559.1.
UniGene; Mm.336848; -.
UniGene; Mm.486313; -.
ProteinModelPortal; O35732; -.
SMR; O35732; -.
BioGrid; 198686; 7.
IntAct; O35732; 2.
STRING; 10090.ENSMUSP00000065107; -.
MEROPS; C14.974; -.
iPTMnet; O35732; -.
PhosphoSitePlus; O35732; -.
MaxQB; O35732; -.
PaxDb; O35732; -.
PRIDE; O35732; -.
Ensembl; ENSMUST00000097722; ENSMUSP00000095329; ENSMUSG00000026031. [O35732-1]
GeneID; 12633; -.
KEGG; mmu:12633; -.
CTD; 8837; -.
MGI; MGI:1336166; Cflar.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00530000064199; -.
HOGENOM; HOG000069972; -.
HOVERGEN; HBG050918; -.
InParanoid; O35732; -.
KO; K04724; -.
OMA; YDWNSRV; -.
OrthoDB; EOG091G05YD; -.
Reactome; R-MMU-3371378; Regulation by c-FLIP.
Reactome; R-MMU-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-MMU-5218900; CASP8 activity is inhibited.
Reactome; R-MMU-69416; Dimerization of procaspase-8.
Reactome; R-MMU-75158; TRAIL signaling.
ChiTaRS; Cflar; mouse.
PRO; PR:O35732; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026031; -.
CleanEx; MM_CFLAR; -.
ExpressionAtlas; O35732; baseline and differential.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031264; C:death-inducing signaling complex; ISO:MGI.
GO; GO:0097342; C:ripoptosome; ISO:MGI.
GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
GO; GO:0016504; F:peptidase activator activity; IDA:MGI.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IGI:MGI.
GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:1901740; P:negative regulation of myoblast fusion; IMP:BHF-UCL.
GO; GO:0060546; P:negative regulation of necroptotic process; IGI:MGI.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:BHF-UCL.
GO; GO:0060544; P:regulation of necroptotic process; ISO:MGI.
GO; GO:0014842; P:regulation of skeletal muscle satellite cell proliferation; IMP:BHF-UCL.
GO; GO:0014732; P:skeletal muscle atrophy; IMP:BHF-UCL.
GO; GO:0007519; P:skeletal muscle tissue development; IMP:BHF-UCL.
GO; GO:0043403; P:skeletal muscle tissue regeneration; IMP:BHF-UCL.
GO; GO:0014866; P:skeletal myofibril assembly; IMP:BHF-UCL.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR001875; DED_dom.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
Pfam; PF01335; DED; 2.
SMART; SM00115; CASc; 1.
SMART; SM00031; DED; 2.
SUPFAM; SSF47986; SSF47986; 2.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS50208; CASPASE_P20; 1.
PROSITE; PS50168; DED; 2.
2: Evidence at transcript level;
Alternative splicing; Apoptosis; Complete proteome;
Reference proteome; Repeat.
CHAIN 1 380 CASP8 and FADD-like apoptosis regulator
subunit p43. {ECO:0000250}.
/FTId=PRO_0000004680.
CHAIN 381 484 CASP8 and FADD-like apoptosis regulator
subunit p12. {ECO:0000250}.
/FTId=PRO_0000004681.
DOMAIN 6 78 DED 1. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
DOMAIN 97 172 DED 2. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
REGION 268 363 Caspase.
COMPBIAS 421 425 Poly-Ser.
VAR_SEQ 208 218 LQNGRSKEPRF -> VSLEPVYGVPA (in isoform
2). {ECO:0000303|PubMed:9289491}.
/FTId=VSP_000842.
VAR_SEQ 219 484 Missing (in isoform 2).
{ECO:0000303|PubMed:9289491}.
/FTId=VSP_000843.
CONFLICT 121 121 T -> TRIT (in Ref. 1; CAA74369/CAA74368).
{ECO:0000305}.
CONFLICT 201 207 PSVLYLK -> YNSR (in Ref. 1; CAA74368 and
2; AAC53281). {ECO:0000305}.
SEQUENCE 484 AA; 55155 MW; B272DE6DB2861C86 CRC64;
MAQSPVSAEV IHQVEECLDE DEKEMMLFLC RDVTENLAAP NVRDLLDSLS ERGQLSFATL
AELLYRVRRF DLLKRILKTD KATVEDHLRR NPHLVSDYRV LLMEIGESLD QNDVSSLVFL
TRDYTGRGKI AKDKSFLDLV IELEKLNLIA SDQLNLLEKC LKNIHRIDLN TKIQKYTQSS
QGARSNMNTL QASLPKLSIK PSVLYLKLQN GRSKEPRFVE YRDSQRTLVK TSIQESGAFL
PPHIREETYR MQSKPLGICL IIDCIGNDTK YLQETFTSLG YHIQLFLFPK SHDITQIVRR
YASMAQHQDY DSFACVLVSL GGSQSMMGRD QVHSGFSLDH VKNMFTGDTC PSLRGKPKLF
FIQNYESLGS QLEDSSLEVD GPSIKNVDSK PLQPRHCTTH PEADIFWSLC TADVSHLEKP
SSSSSVYLQK LSQQLKQGRR RPLVDLHVEL MDKVYAWNSG VSSKEKYSLS LQHTLRKKLI
LAPT


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