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Database: UniProt
Entry: A0A2U4AUP3_TURTR
LinkDB: A0A2U4AUP3_TURTR
Original site: A0A2U4AUP3_TURTR 
ID   A0A2U4AUP3_TURTR        Unreviewed;       211 AA.
AC   A0A2U4AUP3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 2.
DT   27-MAR-2024, entry version 25.
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_019784651.2};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019784651.2};
RN   [1] {ECO:0000313|RefSeq:XP_019784651.2}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019784651.2};
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_019784651.2; XM_019929092.2.
DR   AlphaFoldDB; A0A2U4AUP3; -.
DR   InParanoid; A0A2U4AUP3; -.
DR   OrthoDB; 2960517at2759; -.
DR   Proteomes; UP000245320; Chromosome 8.
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   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:UP000245320}.
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;  23670 MW;  5D23550825BDC037 CRC64;
     MDPFLVLLHS VSLSLSSSEL TEFKFLCQSR VGKRKLELVQ SGLDLFNVLL EQNEMSRENT
     VLLRELLVSL RRQDLLRRLD DFEAGAAGGA APEERDLRAA FDIICDNVGK DWRKLARHLG
     VSDAKIEAIE EKYPRNLAEQ VRESLRVWKN SRRDDAAVSH LVRALRACRL NLVADLIEEG
     QRARALQSDS GDPVSLSESW DSDSPASGAS R
//
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