ID A0A2Y9PNL8_DELLE Unreviewed; 211 AA.
AC A0A2Y9PNL8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=FAS-associated death domain protein {ECO:0000256|PIRNR:PIRNR018586};
DE AltName: Full=FAS-associating death domain-containing protein {ECO:0000256|PIRNR:PIRNR018586};
GN Name=FADD {ECO:0000313|RefSeq:XP_022446851.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022446851.1};
RN [1] {ECO:0000313|RefSeq:XP_022446851.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022446851.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Apoptotic adaptor molecule that recruits caspase-8 or
CC caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The
CC resulting aggregate called the death-inducing signaling complex (DISC)
CC performs caspase-8 proteolytic activation. Active caspase-8 initiates
CC the subsequent cascade of caspases mediating apoptosis. Involved in
CC interferon-mediated antiviral immune response, playing a role in the
CC positive regulation of interferon signaling.
CC {ECO:0000256|PIRNR:PIRNR018586}.
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DR RefSeq; XP_022446851.1; XM_022591143.2.
DR AlphaFoldDB; A0A2Y9PNL8; -.
DR STRING; 9749.A0A2Y9PNL8; -.
DR KEGG; dle:111183629; -.
DR InParanoid; A0A2Y9PNL8; -.
DR OrthoDB; 2960517at2759; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-UniRule.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002821; P:positive regulation of adaptive immune response; IEA:UniProtKB-UniRule.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd08306; Death_FADD; 1.
DR CDD; cd08336; DED_FADD; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 2.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR001875; DED_dom.
DR InterPro; IPR016729; FADD_DD.
DR InterPro; IPR049634; FADD_vert.
DR PANTHER; PTHR15077:SF9; FAS-ASSOCIATED DEATH DOMAIN PROTEIN; 1.
DR PANTHER; PTHR15077; FAS-ASSOCIATING DEATH DOMAIN-CONTAINING PROTEIN FADD; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF01335; DED; 1.
DR PIRSF; PIRSF018586; FADD; 1.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00031; DED; 1.
DR SUPFAM; SSF47986; DEATH domain; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS50168; DED; 1.
PE 4: Predicted;
KW Apoptosis {ECO:0000256|PIRNR:PIRNR018586};
KW Immunity {ECO:0000256|PIRNR:PIRNR018586};
KW Innate immunity {ECO:0000256|PIRNR:PIRNR018586};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT DOMAIN 3..81
FT /note="DED"
FT /evidence="ECO:0000259|PROSITE:PS50168"
FT DOMAIN 97..181
FT /note="Death"
FT /evidence="ECO:0000259|PROSITE:PS50017"
FT REGION 184..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 211 AA; 23691 MW; 10F889369630103E CRC64;
MDPFLVLLHS VSTGLSSSEL TELKFLCQSR VGKRKLERVQ SGLDLFSVLL EQNEMSPENT
VLLRELLVSL RRQDLLRRLD DFEAGAAGGA APEERDLRAA FDIICDNVGK DWRKLARHLR
VSDAKIEAIE EKYPRNLAEQ VRESLRVWKN SRRDDAAVSH LVRALRACRL NLVADLIEEG
QRARALQNES GDPVSLSESW DSDSPASGAS R
//
