FADD_BOVIN
ID FADD_BOVIN Reviewed; 209 AA.
AC Q645M6;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=FAS-associated death domain protein {ECO:0000303|PubMed:15670133};
DE AltName: Full=FAS-associating death domain-containing protein {ECO:0000303|PubMed:15670133};
GN Name=FADD {ECO:0000303|PubMed:15670133};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15670133; DOI=10.1111/j.1365-2052.2004.01207.x;
RA Szperka M.E., Connor E.E., Paape M.J., Williams J.L., Bannerman D.D.;
RT "Characterization of bovine FAS-associated death domain gene.";
RL Anim. Genet. 36:63-66(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal medulla;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q13158}.
CC -!- SUBUNIT: Can self-associate. Interacts with CFLAR, PEA15 and MBD4. When
CC phosphorylated, part of a complex containing HIPK3 and FAS. May
CC interact with MAVS/IPS1. Interacts with MOCV v-CFLAR protein and PIDD1.
CC Interacts (via death domain) with FAS (via death domain). Interacts
CC with CASP8 (By similarity). Interacts directly (via DED domain) with
CC NOL3 (via CARD domain); inhibits death-inducing signaling complex
CC (DISC) assembly by inhibiting the increase in FAS-FADD binding induced
CC by FAS activation. Interacts with RIPK1, TRADD and CASP8 (By
CC similarity). Component of the AIM2 PANoptosome complex, a multiprotein
CC complex that drives inflammatory cell death (PANoptosis) (By
CC similarity). Interacts with stimulated TNFRSF10B (By similarity).
CC {ECO:0000250|UniProtKB:Q13158, ECO:0000250|UniProtKB:Q61160}.
CC -!- DOMAIN: Contains a death domain involved in the binding of the
CC corresponding domain within Fas receptor.
CC {ECO:0000250|UniProtKB:Q13158}.
CC -!- DOMAIN: The interaction between the FAS and FADD death domains is
CC crucial for the formation of the death-inducing signaling complex
CC (DISC). {ECO:0000250|UniProtKB:Q13158}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY725483; AAU20801.1; -; mRNA.
DR EMBL; BC120180; AAI20181.1; -; mRNA.
DR RefSeq; NP_001007817.1; NM_001007816.1.
DR AlphaFoldDB; Q645M6; -.
DR SMR; Q645M6; -.
DR STRING; 9913.ENSBTAP00000024322; -.
DR PaxDb; Q645M6; -.
DR PRIDE; Q645M6; -.
DR Ensembl; ENSBTAT00000024322; ENSBTAP00000024322; ENSBTAG00000018274.
DR GeneID; 493720; -.
DR KEGG; bta:493720; -.
DR CTD; 8772; -.
DR VEuPathDB; HostDB:ENSBTAG00000018274; -.
DR VGNC; VGNC:28700; FADD.
DR eggNOG; ENOG502S2RV; Eukaryota.
DR GeneTree; ENSGT00390000002105; -.
DR HOGENOM; CLU_087961_0_0_1; -.
DR InParanoid; Q645M6; -.
DR OMA; CKMNLVA; -.
DR OrthoDB; 1619689at2759; -.
DR TreeFam; TF102046; -.
DR Reactome; R-BTA-3371378; Regulation by c-FLIP.
DR Reactome; R-BTA-5218900; CASP8 activity is inhibited.
DR Reactome; R-BTA-5357786; TNFR1-induced proapoptotic signaling.
DR Reactome; R-BTA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-BTA-5675482; Regulation of necroptotic cell death.
DR Reactome; R-BTA-69416; Dimerization of procaspase-8.
DR Reactome; R-BTA-75157; FasL/ CD95L signaling.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000018274; Expressed in ileocecal valve and 109 other tissues.
DR GO; GO:0031265; C:CD95 death-inducing signaling complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0097342; C:ripoptosome; ISS:UniProtKB.
DR GO; GO:0089720; F:caspase binding; ISS:UniProtKB.
DR GO; GO:0035877; F:death effector domain binding; IEA:Ensembl.
DR GO; GO:0005123; F:death receptor binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0071550; P:death-inducing signaling complex assembly; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048535; P:lymph node development; ISS:UniProtKB.
DR GO; GO:0097049; P:motor neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0097527; P:necroptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0070236; P:negative regulation of activation-induced cell death of T cells; ISS:UniProtKB.
DR GO; GO:0060546; P:negative regulation of necroptotic process; IEA:Ensembl.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; ISS:UniProtKB.
DR GO; GO:0002821; P:positive regulation of adaptive immune response; ISS:UniProtKB.
DR GO; GO:2000454; P:positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation; ISS:UniProtKB.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0060340; P:positive regulation of type I interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0048536; P:spleen development; ISS:UniProtKB.
DR GO; GO:0033077; P:T cell differentiation in thymus; ISS:UniProtKB.
DR GO; GO:0043029; P:T cell homeostasis; ISS:UniProtKB.
DR GO; GO:0048538; P:thymus development; ISS:UniProtKB.
DR GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IBA:GO_Central.
DR Gene3D; 1.10.533.10; -; 2.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR001875; DED_dom.
DR InterPro; IPR016729; FADD.
DR PANTHER; PTHR15077; PTHR15077; 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; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS50168; DED; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Immunity; Innate immunity; Phosphoprotein; Reference proteome.
FT CHAIN 1..209
FT /note="FAS-associated death domain protein"
FT /id="PRO_0000281928"
FT DOMAIN 3..81
FT /note="DED"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00065"
FT DOMAIN 97..181
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 187..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 209 AA; 23002 MW; 2EB6BA41F6DB0F9D CRC64;
MDPFLVLLHS VSAGLSSSDL TQLKFLCQNH ISKRKLELAQ SGLDLFTVLL QQNELNAEHT
ALLRELLCSL RRKDLLLRLD DFERGAAGGA APEDRDLRAA MEIICDNVGK DWRRLARHLG
VSDVKIEAIE EKYPRNLAEQ VRELLRVWKN STRENAAVSC LVGALRGCQL NVVADLIEED
QRARALQSGS ANPGSFTAWD SGSAAPGAS
