TNR1A_BOVIN
ID TNR1A_BOVIN Reviewed; 471 AA.
AC O19131; Q2HJ72;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 1A;
DE AltName: Full=Tumor necrosis factor receptor 1;
DE Short=TNF-R1;
DE AltName: Full=Tumor necrosis factor receptor type I;
DE Short=TNF-RI;
DE Short=TNFR-I;
DE AltName: Full=p55;
DE AltName: Full=p60;
DE AltName: CD_antigen=CD120a;
DE Flags: Precursor;
GN Name=TNFRSF1A; Synonyms=TNFR1;
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].
RC TISSUE=Aorta;
RX PubMed=9613449; DOI=10.1016/s0165-2427(97)00136-0;
RA Lee E.-K., Kehrli M.E. Jr., Taylor M.J.;
RT "Cloning and sequencing of cDNA encoding bovine tumor necrosis factor
RT (TNF)-receptor I.";
RL Vet. Immunol. Immunopathol. 61:379-385(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for TNFSF2/TNF-alpha and homotrimeric
CC TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8
CC to the activated receptor. The resulting death-inducing signaling
CC complex (DISC) performs caspase-8 proteolytic activation which
CC initiates the subsequent cascade of caspases (aspartate-specific
CC cysteine proteases) mediating apoptosis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binding of TNF to the extracellular domain leads to
CC homotrimerization. The aggregated death domains provide a novel
CC molecular interface that interacts specifically with the death domain
CC of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and
CC possibly FADD, are recruited to the complex by their association with
CC TRADD. This complex activates at least two distinct signaling cascades,
CC apoptosis and NF-kappa-B signaling. Interacts with BAG4, BABAM2, FEM1B,
CC GRB2, SQSTM1 and TRPC4AP. Interacts directly with NOL3 (via CARD
CC domain); inhibits TNF-signaling pathway. Interacts with SH3RF2, TRADD
CC and RIPK1. SH3RF2 facilitates the recruitment of RIPK1 and TRADD to
CC TNFRSF1A in a TNF-alpha-dependent process. Interacts with PGLYRP1; this
CC interaction is important for cell death induction. Interacts (via death
CC domain) with MADD (via death domain) (By similarity).
CC {ECO:0000250|UniProtKB:P19438, ECO:0000250|UniProtKB:P25118}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Golgi apparatus membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: Both the cytoplasmic membrane-proximal region and the C-
CC terminal region containing the death domain are involved in the
CC interaction with TRPC4AP. {ECO:0000250}.
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DR EMBL; U90937; AAB65143.1; -; mRNA.
DR EMBL; BC113278; AAI13279.1; -; mRNA.
DR RefSeq; NP_777099.1; NM_174674.2.
DR AlphaFoldDB; O19131; -.
DR SMR; O19131; -.
DR STRING; 9913.ENSBTAP00000005522; -.
DR PaxDb; O19131; -.
DR GeneID; 282527; -.
DR KEGG; bta:282527; -.
DR CTD; 7132; -.
DR eggNOG; ENOG502S050; Eukaryota.
DR InParanoid; O19131; -.
DR OrthoDB; 726174at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0043120; F:tumor necrosis factor binding; IBA:GO_Central.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006952; P:defense response; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006693; P:prostaglandin metabolic process; IEA:InterPro.
DR CDD; cd08313; Death_TNFR1; 1.
DR CDD; cd10576; TNFRSF1A; 1.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR InterPro; IPR020419; TNFR_1A.
DR InterPro; IPR033994; TNFRSF1A_death.
DR InterPro; IPR033993; TNFRSF1A_N.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF00020; TNFR_c6; 2.
DR PRINTS; PR01918; TNFACTORR1A.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00208; TNFR; 3.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
DR PROSITE; PS00652; TNFR_NGFR_1; 3.
DR PROSITE; PS50050; TNFR_NGFR_2; 3.
PE 2: Evidence at transcript level;
KW Apoptosis; Cell membrane; Disulfide bond; Glycoprotein; Golgi apparatus;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000250|UniProtKB:P19438"
FT CHAIN 30..471
FT /note="Tumor necrosis factor receptor superfamily member
FT 1A"
FT /id="PRO_0000034542"
FT TOPO_DOM 30..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..233
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..471
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 43..82
FT /note="TNFR-Cys 1"
FT REPEAT 83..125
FT /note="TNFR-Cys 2"
FT REPEAT 126..166
FT /note="TNFR-Cys 3"
FT REPEAT 167..195
FT /note="TNFR-Cys 4"
FT DOMAIN 372..457
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 340..360
FT /note="N-SMase activation domain (NSD)"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 59..72
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 62..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 84..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 102..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 105..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 127..143
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 146..158
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 149..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 168..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 182..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 185..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
SQ SEQUENCE 471 AA; 51368 MW; 5243EF514DFE81C4 CRC64;
MGLPTVPGLL LPLVLPALLA DVYPAGVQGL VPHPGDLEKR ESPCPQGKYN HPQNSTICCT
KCHKGTYLYN DCPGPGRDTD CRVCAPGTYT ALENHLRRCL SCSRCRDEMF QVEISPCVVD
RDTVCGCRKN QYREYWGETG FRCLNCSLCP NGTVNIPCQE RQDTICHCHM GFFLKGAKCI
SCHDCKNKEC EKLCPTRPST GKDSQDPGTT VLLPLVIVFG LCLASFASVV LACRYQRWKP
KLYSIICGQS TLVKEGEPEL LVPAPGFNPT TTICFSSTPS SSPVSIPPYI SCDRSNFGAV
ASPSSETAPP HLKAGPILPG PPASTHLCTP GPPASTHLCT PGPPASTHLC TPVQKWEASA
PSAPDQLADA DPATLYAVVD GVPPSRWKEL VRRLGLSEHE IERLELENGR HLREAQYSML
AAWRRRTPRR EATLELLGRV LRDMDLLGCL ENIEEALGGA ARLASEPRLL W
