CFLAR_PONAB
ID CFLAR_PONAB Reviewed; 480 AA.
AC Q5RD56;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=CASP8 and FADD-like apoptosis regulator;
DE Contains:
DE RecName: Full=CASP8 and FADD-like apoptosis regulator subunit p43;
DE Contains:
DE RecName: Full=CASP8 and FADD-like apoptosis regulator subunit p12;
DE Flags: Precursor;
GN Name=CFLAR;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Apoptosis regulator protein which may function as a crucial
CC link between cell survival and cell death pathways in mammalian cells.
CC Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic
CC fragment (p43) is likely retained in the death-inducing signaling
CC complex (DISC) thereby blocking further recruitment and processing of
CC caspase-8 at the complex. Full length and shorter isoforms have been
CC shown either to induce apoptosis or to reduce TNFRSF-triggered
CC apoptosis. Lacks enzymatic (caspase) activity (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: TNFRSF6 stimulation triggers recruitment to the death-inducing
CC signaling complex (DISC) formed by TNFRSF6, FADD and CASP8 (By
CC similarity). A proteolytic fragment (p43) stays associated with the
CC DISC (By similarity). Interacts with RIPK1 (By similarity).
CC {ECO:0000250|UniProtKB:O15519, ECO:0000250|UniProtKB:O35732}.
CC -!- DOMAIN: The caspase domain lacks the active site residues involved in
CC catalysis.
CC -!- PTM: Proteolytically processed by CASP8 generating subunit p43 and p12.
CC {ECO:0000250|UniProtKB:O35732}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR EMBL; CR858062; CAH90301.1; -; mRNA.
DR RefSeq; NP_001125140.1; NM_001131668.1.
DR AlphaFoldDB; Q5RD56; -.
DR SMR; Q5RD56; -.
DR STRING; 9601.ENSPPYP00000014600; -.
DR MEROPS; C14.971; -.
DR GeneID; 100172025; -.
DR KEGG; pon:100172025; -.
DR CTD; 8837; -.
DR eggNOG; KOG3573; Eukaryota.
DR InParanoid; Q5RD56; -.
DR OrthoDB; 939331at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR CDD; cd00032; CASc; 1.
DR Gene3D; 1.10.533.10; -; 2.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR001875; DED_dom.
DR InterPro; IPR002398; Pept_C14.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR Pfam; PF01335; DED; 2.
DR SMART; SM00115; CASc; 1.
DR SMART; SM00031; DED; 2.
DR SUPFAM; SSF47986; SSF47986; 2.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
DR PROSITE; PS50168; DED; 2.
PE 2: Evidence at transcript level;
KW Apoptosis; Reference proteome; Repeat.
FT CHAIN 1..376
FT /note="CASP8 and FADD-like apoptosis regulator subunit p43"
FT /id="PRO_0000045838"
FT CHAIN 377..480
FT /note="CASP8 and FADD-like apoptosis regulator subunit p12"
FT /evidence="ECO:0000250|UniProtKB:O35732"
FT /id="PRO_0000045839"
FT DOMAIN 1..73
FT /note="DED 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065"
FT DOMAIN 92..170
FT /note="DED 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065"
FT REGION 1..435
FT /note="Not proteolytically processed and involved in
FT apoptosis inhibition"
FT /evidence="ECO:0000250"
FT REGION 1..305
FT /note="Interaction with CASP8 propeptide"
FT /evidence="ECO:0000250|UniProtKB:O15519"
FT REGION 1..227
FT /note="Interaction with FADD"
FT /evidence="ECO:0000250|UniProtKB:O15519"
FT REGION 1..195
FT /note="Interaction with CASP8"
FT /evidence="ECO:0000250|UniProtKB:O15519"
FT REGION 192..480
FT /note="Interaction with TRAF1 and TRAF2"
FT /evidence="ECO:0000250|UniProtKB:O15519"
FT REGION 192..435
FT /note="Interaction with CASP3"
FT /evidence="ECO:0000250|UniProtKB:O15519"
FT REGION 217..480
FT /note="Interaction with CASP8 subunits p18 and p10"
FT /evidence="ECO:0000250|UniProtKB:O15519"
FT REGION 263..358
FT /note="Caspase"
FT REGION 370..480
FT /note="Interaction with CASP8"
FT /evidence="ECO:0000250|UniProtKB:O15519"
FT SITE 369..370
FT /note="Cleavage; by CASP8"
FT /evidence="ECO:0000250|UniProtKB:O35732"
FT SITE 376..377
FT /note="Cleavage; by CASP8"
FT /evidence="ECO:0000250|UniProtKB:O35732"
SQ SEQUENCE 480 AA; 55360 MW; 6013B8292092FE8B CRC64;
MSAEVIHQVE EALDTDEKEM LLFSCRDVAI DVVPPNVRDL LDILRERGKL SVGDLAELLY
RVRRFDLLKR ILKMDRKAVE THLLRNPHLV SDYRVLMAEI GEDLDKSDVS SLIFLMKDYM
GRGKISKEKS FLDLVVELEK LNLVAPDQLD LLEKCLKNIH RIDLKTKIQK YKQSVQGAGT
SYRNVLQAAI QKSFKDPSNN FRLHNGRSKE QRLKEQLGTQ QEPVKKSIQE SEAFLPQSVP
EERYKMKSKP LGICLIIDCI GNETELLRDT FTSLGYEVQK FLHLSMHGIS QILGQFACMP
EHRDYDSFVC VLVSRGGSQS VYGVDQTHSG LPLHHIRRMF MGDSCPYLAG KPKIFFIQNY
VVSEGQLEDS SLLEVDGPAM KNVEFKAQKR GLCTVHREAD FFWSLCTADV SLLEWSHSSP
SLYLQCLSQK LRQERKRPLL DLHIELNGYM YDWNSRVSAK EKYYVWLQHT LRKKLIPSYT
