TRADD_BOVIN
ID TRADD_BOVIN Reviewed; 312 AA.
AC Q2KI74;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Tumor necrosis factor receptor type 1-associated DEATH domain protein {ECO:0000305};
DE Short=TNFR1-associated DEATH domain protein {ECO:0000250|UniProtKB:Q15628};
DE AltName: Full=TNFRSF1A-associated via death domain {ECO:0000250|UniProtKB:Q15628};
GN Name=TRADD {ECO:0000250|UniProtKB:Q15628};
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 [LARGE SCALE MRNA].
RC STRAIN=Hereford {ECO:0000312|EMBL:AAI12744.1};
RC TISSUE=Hypothalamus {ECO:0000312|EMBL:AAI12744.1};
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Adapter molecule for TNFRSF1A/TNFR1 that specifically
CC associates with the cytoplasmic domain of activated TNFRSF1A/TNFR1
CC mediating its interaction with FADD. Overexpression of TRADD leads to
CC two major TNF-induced responses, apoptosis and activation of NF-kappa-B
CC (By similarity). The nuclear form acts as a tumor suppressor by
CC preventing ubiquitination and degradation of isoform p19ARF/ARF of
CC CDKN2A by TRIP12: acts by interacting with TRIP12, leading to disrupt
CC interaction between TRIP12 and isoform p19ARF/ARF of CDKN2A (By
CC similarity). {ECO:0000250|UniProtKB:Q15628,
CC ECO:0000250|UniProtKB:Q3U0V2}.
CC -!- SUBUNIT: Stimulation of TNF-alpha receptor TNFRSF1A leads to the
CC formation of two distinct signaling complexes. Plasma membrane-bound
CC complex I is composed of TNFRSF1A, TRADD, RIPK1, TRAF2 and BIRC2/c-IAP1
CC or BIRC3 which interacts with CHUCK/IKK-alpha, IKBKB/IKK-beta and
CC IKBKG/IKK-gamma promoting cell survival. Subsequently, TRADD, RIPK1 and
CC TRAF2 dissociate from TNFRSF1A and form cytoplasmic complex II with
CC FADD and caspase CASP8 promoting cell apoptosis. Within complex I,
CC interacts with TNFRSF1A/TNFR1, TRAF2 and kinase RIPK1. Within complex
CC I, interacts with TRPC4AP; the interaction promotes NF-kappa B
CC activation. UXT1 associates with complex I; the interaction prevents
CC the formation of complex II. Within complex I Interacts with scaffold
CC protein DAB2IP. Interacts with autophagy receptor SQSTM1 (By
CC similarity). Interacts with E3 ligase TRIP12 (By similarity). Interacts
CC with kinase HIPK2. Interacts with keratin KRT14. Interacts with keratin
CC KRT18 (By similarity). Interacts with keratins KRT16 and KRT17 (By
CC similarity). Interacts with FADD (By similarity). Interacts with TOMM70
CC (By similarity). {ECO:0000250|UniProtKB:Q15628,
CC ECO:0000250|UniProtKB:Q3U0V2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q3U0V2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q15628}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q15628}. Note=Shuttles between the cytoplasm and
CC the nucleus. {ECO:0000250|UniProtKB:Q3U0V2}.
CC -!- DOMAIN: Requires the intact death domain to associate with
CC TNFRSF1A/TNFR1. {ECO:0000250|UniProtKB:Q15628}.
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DR EMBL; BC112743; AAI12744.1; -; mRNA.
DR RefSeq; NP_001039361.1; NM_001045896.2.
DR RefSeq; XP_010812732.1; XM_010814430.2.
DR AlphaFoldDB; Q2KI74; -.
DR SMR; Q2KI74; -.
DR STRING; 9913.ENSBTAP00000016776; -.
DR PaxDb; Q2KI74; -.
DR PRIDE; Q2KI74; -.
DR Ensembl; ENSBTAT00000016776; ENSBTAP00000016776; ENSBTAG00000012642.
DR GeneID; 504707; -.
DR KEGG; bta:504707; -.
DR CTD; 8717; -.
DR VEuPathDB; HostDB:ENSBTAG00000012642; -.
DR VGNC; VGNC:36269; TRADD.
DR eggNOG; ENOG502RXWE; Eukaryota.
DR GeneTree; ENSGT00390000002016; -.
DR HOGENOM; CLU_052183_0_0_1; -.
DR InParanoid; Q2KI74; -.
DR OMA; QPCSRFL; -.
DR OrthoDB; 1024816at2759; -.
DR TreeFam; TF331882; -.
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-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-BTA-5675482; Regulation of necroptotic cell death.
DR Reactome; R-BTA-69416; Dimerization of procaspase-8.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000012642; Expressed in digestive system secreted substance and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0002947; C:tumor necrosis factor receptor superfamily complex; IBA:GO_Central.
DR GO; GO:0070513; F:death domain binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IBA:GO_Central.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0051798; P:positive regulation of hair follicle development; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 3.30.70.680; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR035712; TRADD.
DR InterPro; IPR009095; TRADD_N.
DR InterPro; IPR036729; TRADD_N_sf.
DR PANTHER; PTHR14913; PTHR14913; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF09034; TRADD_N; 1.
DR SMART; SM00005; DEATH; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF55044; SSF55044; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Cytoskeleton; Nucleus; Reference proteome.
FT CHAIN 1..312
FT /note="Tumor necrosis factor receptor type 1-associated
FT DEATH domain protein"
FT /id="PRO_0000291658"
FT DOMAIN 215..305
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 166..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..289
FT /note="Interaction with KRT14 and KRT18"
FT /evidence="ECO:0000250|UniProtKB:Q15628"
FT MOTIF 147..163
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250|UniProtKB:Q3U0V2"
FT MOTIF 231..244
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q3U0V2"
FT COMPBIAS 166..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 312 AA; 34292 MW; BFB1F26AD5D9DCE7 CRC64;
MAAGPNGLEE WVGSAYLFVE SSLDKVVLSD AYAHQQQKVA MYGALQTALA ESGGSPDVLQ
MLKIHRSDPQ LIVQLRFSGR QACSRFLRAY REGALRATLQ GCLARALALN SVPLQLELRA
GAEQLDALLT NEERCLNCIC AQKPDRLRDE ELTELENALR NLTCGSAGGQ GSDVQGTPAP
LQSLAPSPPE EKPPPPQPGQ TFLFQGQPIV NRPLNLQDQQ KFARSVGLKW RKVGRSLQRS
CRALRDPALD SLAYEYERDG LYEQAFQLLR RFVQAEGRRA TLQRLVEALE ENELTSLAED
LLGLANPDGS LA
