CFLAR (Mus musculus)
Description [+]
- Synonyms: CFLAR, CASP8 AND FADD-LIKE APOPTOSIS REGULATOR, 2310024N18RIK, A430105C05RIK, C-FLIP, CASH, CASPER, FLIP
- Species: Metazoa;Bilateria;Deuterostoma;Chordata;Vertebrata;Mammalia;Rodentia; Mus musculus
- Short gene description: CASP8 and FADD-like apoptosis regulator Precursor (Cellular FLICE-like inhibitory protein)(c-FLIP)(Caspase-eight-related protein)(Casper)(Caspase-like apoptosis regulatory protein)(CLARP)(MACH-related inducer of toxicity)(MRIT)(Caspase homolog)(CASH)(Inhibitor of FLICE)(I-FLICE)(FADD-like antiapoptotic molecule 1)(FLAME-1)(Usurpin) [Contains CASP8 and FADD-like apoptosis regulator subunit p43;CASP8 and FADD-like apoptosis regulator subunit p12] [Source:UniProtKB/Swiss-Prot;Acc:O35732]
- Family: caspase Death effector domain-containing protein : other
- Process: apoptosis,
- Pathways: extrinsic pathway,
- Criteria: manually curated
- Curator comment:
- WIKI: CFLAR-M_musculus
References [+]
- Requirement for Casper (c-FLIP) in regulation of death receptor-induced apoptosis and embryonic development.
- Yeh WC, Itie A, Elia AJ, Ng M, Shu HB, Wakeham A, Mirtsos C, Suzuki N, Bonnard M, Goeddel DV, Mak TW
- Casper (c-FLIP) associates with FADD and caspase-8 in signaling complexes downstream of death receptors like Fas. We generated Casper-deficient mice and cells and noted a duality in the physiological functions of this molecule. casper-/- embryos do not survive past day 10.5 of embryogenesis and exhibit impaired heart development. This phenotype is reminiscent of that reported for FADD-/- and caspase-8-/- embryos. However, unlike FADD-/- and caspase-8-/- cells, casper-/- embryonic fibroblasts are highly sensitive to FasL- or TNF-induced apoptosis and show rapid induction of caspase activities. NF-kappaB and JNK/SAPK activation is intact in TNF-stimulated casper-/- cells. These results suggest that Casper has two distinct roles: to cooperate with FADD and caspase-8 during embryonic development and to mediate cytoprotection against death factor-induced apoptosis. Immunity. 2000 Jun;12(6):633-42.
Structure & Sequence [+]
Pfam domains:
(Pfam is a large collection of protein families.)
Source | Domain Name | Start | End |
---|---|---|---|
PFAM A | DED | 7 | 84 |
PFAM A | DED | 98 | 181 |
PFAM A | Peptidase_C14 | 257 | 481 |
Protein sequence [+]
Cflar | Mus musculus | 10090 | length:484
MAQSPVSAEVIHQVEECLDEDEKEMMLFLCRDVTENLAAPNVRDLLDSLSERGQLSFATL
AELLYRVRRFDLLKRILKTDKATVEDHLRRNPHLVSDYRVLLMEIGESLDQNDVSSLVFL
TRDYTGRGKIAKDKSFLDLVIELEKLNLIASDQLNLLEKCLKNIHRIDLNTKIQKYTQSS
QGARSNMNTLQASLPKLSIKPSVLYLKLQNGRSKEPRFVEYRDSQRTLVKTSIQESGAFL
PPHIREETYRMQSKPLGICLIIDCIGNDTKYLQETFTSLGYHIQLFLFPKSHDITQIVRR
YASMAQHQDYDSFACVLVSLGGSQSMMGRDQVHSGFSLDHVKNMFTGDTCPSLRGKPKLF
FIQNYESLGSQLEDSSLEVDGPSIKNVDSKPLQPRHCTTHPEADIFWSLCTADVSHLEKP
SSSSSVYLQKLSQQLKQGRRRPLVDLHVELMDKVYAWNSGVSSKEKYSLSLQHTLRKKLI
LAPT
AELLYRVRRFDLLKRILKTDKATVEDHLRRNPHLVSDYRVLLMEIGESLDQNDVSSLVFL
TRDYTGRGKIAKDKSFLDLVIELEKLNLIASDQLNLLEKCLKNIHRIDLNTKIQKYTQSS
QGARSNMNTLQASLPKLSIKPSVLYLKLQNGRSKEPRFVEYRDSQRTLVKTSIQESGAFL
PPHIREETYRMQSKPLGICLIIDCIGNDTKYLQETFTSLGYHIQLFLFPKSHDITQIVRR
YASMAQHQDYDSFACVLVSLGGSQSMMGRDQVHSGFSLDHVKNMFTGDTCPSLRGKPKLF
FIQNYESLGSQLEDSSLEVDGPSIKNVDSKPLQPRHCTTHPEADIFWSLCTADVSHLEKP
SSSSSVYLQKLSQQLKQGRRRPLVDLHVELMDKVYAWNSGVSSKEKYSLSLQHTLRKKLI
LAPT
Structure links:
Evolution [+]
View protein alignment and tree with Jalview:  
Explore tree at phylomeDB:   Click here.
Homologs list [+]
Name | Relationship | Species |
---|
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Gene Ontology [+]
GO id | Name | Ontology type | Evidence |
---|---|---|---|
GO:0006508 | proteolysis | biological_proccess | IEA |
GO:0043066 | negative regulation of apoptosis | biological_proccess | IMP |
GO:0043154 | negative regulation of caspase activity | biological_proccess | IMP |
GO:0042981 | regulation of apoptosis | biological_proccess | IEA |
GO:0006916 | anti-apoptosis | biological_proccess | IEA |
GO:0006915 | apoptosis | biological_proccess | RCA |
GO:0042981 | regulation of apoptosis | biological_proccess | RCA |
GO:0006915 | apoptosis | biological_proccess | IEA |
GO:0043123 | positive regulation of I-kappaB kinase/NF-kappaB cascade | biological_proccess | IEA |
GO:0004197 | cysteine-type endopeptidase activity | mollecular_function | IEA |
GO:0005515 | protein binding | mollecular_function | IEA |
GO:0008234 | cysteine-type peptidase activity | mollecular_function | IEA |
GO:0005737 | cytoplasm | cell_component | IDA |
Check GO Evidence Codes here
KEGG Pathways [+]
Curated Isoforms [+]
Info from The Vertebrate Genome Annotation (VEGA) database.
(*) Canonical transcript and translation forms.
Information from other databases [+]
- Gene info from MGI [?] MGI:1336166
- Ensembl genome browser [?] : ENSMUSG00000026031
- Expression info from Arrayexpress [?] : ENSMUSG00000026031
- Protein expression from Protein Atlas: [?] ENSMUSG00000026031
- Community gene edition from Wikigenes: [?] 100046787
Click on [?] for more information.