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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;         481 AA.
O35732; D3Z0W6; O35707; O35733;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
25-OCT-2017, sequence version 3.
08-MAY-2019, entry version 174.
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, and Skin fibroblast;
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 9.5 and 10.5 dpc, highly expressed 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.
CCDS; CCDS14978.1; -. [O35732-1]
CCDS; CCDS35582.1; -. [O35732-2]
RefSeq; NP_001276633.1; NM_001289704.2. [O35732-1]
RefSeq; NP_997536.1; NM_207653.5. [O35732-1]
RefSeq; XP_006495698.1; XM_006495635.3. [O35732-1]
RefSeq; XP_011236722.1; XM_011238420.2. [O35732-1]
RefSeq; XP_011236723.1; XM_011238421.2. [O35732-1]
RefSeq; XP_011236724.1; XM_011238422.1. [O35732-1]
RefSeq; XP_011236725.1; XM_011238423.2. [O35732-1]
RefSeq; XP_017169048.1; XM_017313559.1. [O35732-1]
SMR; O35732; -.
BioGrid; 198686; 6.
IntAct; O35732; 2.
STRING; 10090.ENSMUSP00000109952; -.
MEROPS; C14.974; -.
iPTMnet; O35732; -.
PhosphoSitePlus; O35732; -.
PaxDb; O35732; -.
PRIDE; O35732; -.
Ensembl; ENSMUST00000069333; ENSMUSP00000065107; ENSMUSG00000026031. [O35732-1]
Ensembl; ENSMUST00000114309; ENSMUSP00000109948; ENSMUSG00000026031. [O35732-2]
Ensembl; ENSMUST00000114313; ENSMUSP00000109952; ENSMUSG00000026031. [O35732-1]
GeneID; 12633; -.
KEGG; mmu:12633; -.
CTD; 8837; -.
MGI; MGI:1336166; Cflar.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00530000064199; -.
HOGENOM; HOG000069972; -.
InParanoid; O35732; -.
KO; K04724; -.
OMA; VYDWNSR; -.
OrthoDB; 939331at2759; -.
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; Expressed in 292 organ(s), highest expression level in blood.
ExpressionAtlas; O35732; baseline and differential.
GO; GO:0031265; C:CD95 death-inducing signaling complex; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031264; C:death-inducing signaling complex; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0097342; C:ripoptosome; ISO:MGI.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0005123; F:death receptor binding; ISO:MGI.
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:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0006915; P:apoptotic process; ISO:MGI.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0071732; P:cellular response to nitric oxide; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
GO; GO:1903845; P:negative regulation of cellular response to transforming growth factor beta stimulus; ISO:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:MGI.
GO; GO:1904036; P:negative regulation of epithelial cell apoptotic process; ISO: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:1903944; P:negative regulation of hepatocyte apoptotic process; 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:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:1903055; P:positive regulation of extracellular matrix organization; ISO:MGI.
GO; GO:0072126; P:positive regulation of glomerular mesangial cell proliferation; ISO:MGI.
GO; GO:2000347; P:positive regulation of hepatocyte proliferation; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0010976; P:positive regulation of neuron projection development; ISO: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:0009617; P:response to bacterium; IEP:MGI.
GO; GO:0033574; P:response to testosterone; ISO:MGI.
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_sf.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001875; DED_dom.
InterPro; IPR002398; Pept_C14.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
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 1 377 CASP8 and FADD-like apoptosis regulator
subunit p43. {ECO:0000250}.
/FTId=PRO_0000004680.
CHAIN 378 481 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 265 360 Caspase.
COMPBIAS 418 422 Poly-Ser.
VAR_SEQ 205 215 LQNGRSKEPRF -> VSLEPVYGVPA (in isoform
2). {ECO:0000303|PubMed:9289491}.
/FTId=VSP_000842.
VAR_SEQ 216 481 Missing (in isoform 2).
{ECO:0000303|PubMed:9289491}.
/FTId=VSP_000843.
CONFLICT 121 121 T -> TRIT (in Ref. 1; CAA74369/CAA74368).
{ECO:0000305}.
SEQUENCE 481 AA; 54875 MW; 433E07E2E5FA5A05 CRC64;
MAQSPVSAEV IHQVEECLDE DEKEMMLFLC RDVTENLAAP NVRDLLDSLS ERGQLSFATL
AELLYRVRRF DLLKRILKTD KATVEDHLRR NPHLVSDYRV LLMEIGESLD QNDVSSLVFL
TRDYTGRGKI AKDKSFLDLV IELEKLNLIA SDQLNLLEKC LKNIHRIDLN TKIQKYTQSS
QGARSNMNTL QASLPKLSIK YNSRLQNGRS KEPRFVEYRD SQRTLVKTSI QESGAFLPPH
IREETYRMQS KPLGICLIID CIGNDTKYLQ ETFTSLGYHI QLFLFPKSHD ITQIVRRYAS
MAQHQDYDSF ACVLVSLGGS QSMMGRDQVH SGFSLDHVKN MFTGDTCPSL RGKPKLFFIQ
NYESLGSQLE DSSLEVDGPS IKNVDSKPLQ PRHCTTHPEA DIFWSLCTAD VSHLEKPSSS
SSVYLQKLSQ QLKQGRRRPL VDLHVELMDK VYAWNSGVSS KEKYSLSLQH TLRKKLILAP
T


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