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Tumor necrosis factor receptor superfamily member 1A (Tumor necrosis factor receptor 1) (TNF-R1) (Tumor necrosis factor receptor type I) (TNF-RI) (TNFR-I) (p55) (p60) (CD antigen CD120a)

 TNR1A_BOVIN             Reviewed;         471 AA.
O19131; Q2HJ72;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
22-NOV-2017, entry version 132.
RecName: Full=Tumor necrosis factor receptor superfamily member 1A;
AltName: Full=Tumor necrosis factor receptor 1;
Short=TNF-R1;
AltName: Full=Tumor necrosis factor receptor type I;
Short=TNF-RI;
Short=TNFR-I;
AltName: Full=p55;
AltName: Full=p60;
AltName: CD_antigen=CD120a;
Flags: Precursor;
Name=TNFRSF1A; Synonyms=TNFR1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Aorta;
PubMed=9613449; DOI=10.1016/S0165-2427(97)00136-0;
Lee E.-K., Kehrli M.E. Jr., Taylor M.J.;
"Cloning and sequencing of cDNA encoding bovine tumor necrosis factor
(TNF)-receptor I.";
Vet. Immunol. Immunopathol. 61:379-385(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Uterus;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Receptor for TNFSF2/TNF-alpha and homotrimeric
TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits
caspase-8 to the activated receptor. The resulting death-inducing
signaling complex (DISC) performs caspase-8 proteolytic activation
which initiates the subsequent cascade of caspases (aspartate-
specific cysteine proteases) mediating apoptosis (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Binding of TNF to the extracellular domain leads to
homotrimerization. The aggregated death domains provide a novel
molecular interface that interacts specifically with the death
domain of TRADD. Various TRADD-interacting proteins such as TRAFS,
RIPK1 and possibly FADD, are recruited to the complex by their
association with TRADD. This complex activates at least two
distinct signaling cascades, apoptosis and NF-kappa-B signaling.
Interacts with BAG4, BABAM2, FEM1B, GRB2, SQSTM1 and TRPC4AP.
Interacts directly with NOL3 (via CARD domain); inhibits TNF-
signaling pathway (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P25118}.
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Golgi apparatus membrane {ECO:0000250}; Single-pass type
I membrane protein {ECO:0000250}.
-!- DOMAIN: Both the cytoplasmic membrane-proximal region and the C-
terminal region containing the death domain are involved in the
interaction with TRPC4AP. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; U90937; AAB65143.1; -; mRNA.
EMBL; BC113278; AAI13279.1; -; mRNA.
RefSeq; NP_777099.1; NM_174674.2.
UniGene; Bt.3890; -.
ProteinModelPortal; O19131; -.
SMR; O19131; -.
STRING; 9913.ENSBTAP00000005522; -.
PaxDb; O19131; -.
PRIDE; O19131; -.
GeneID; 282527; -.
KEGG; bta:282527; -.
CTD; 7132; -.
eggNOG; ENOG410IXBX; Eukaryota.
eggNOG; ENOG4111YG2; LUCA.
HOGENOM; HOG000133001; -.
HOVERGEN; HBG058842; -.
InParanoid; O19131; -.
KO; K03158; -.
Proteomes; UP000009136; Unplaced.
GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0043120; F:tumor necrosis factor binding; IBA:GO_Central.
GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; ISS:UniProtKB.
GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0006952; P:defense response; ISS:UniProtKB.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; ISS:UniProtKB.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006693; P:prostaglandin metabolic process; IEA:InterPro.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
CDD; cd08313; Death_TNFR1; 1.
CDD; cd10576; TNFRSF1A; 1.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
InterPro; IPR020419; TNFR_1A.
InterPro; IPR033994; TNFRSF1A_death.
InterPro; IPR033993; TNFRSF1A_N.
Pfam; PF00531; Death; 1.
Pfam; PF00020; TNFR_c6; 2.
PRINTS; PR01918; TNFACTORR1A.
SMART; SM00005; DEATH; 1.
SMART; SM00208; TNFR; 3.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS00652; TNFR_NGFR_1; 3.
PROSITE; PS50050; TNFR_NGFR_2; 3.
2: Evidence at transcript level;
Apoptosis; Cell membrane; Complete proteome; Disulfide bond;
Glycoprotein; Golgi apparatus; Membrane; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 471 Tumor necrosis factor receptor
superfamily member 1A.
/FTId=PRO_0000034542.
TOPO_DOM 22 210 Extracellular. {ECO:0000255}.
TRANSMEM 211 233 Helical. {ECO:0000255}.
TOPO_DOM 234 471 Cytoplasmic. {ECO:0000255}.
REPEAT 43 82 TNFR-Cys 1.
REPEAT 83 125 TNFR-Cys 2.
REPEAT 126 166 TNFR-Cys 3.
REPEAT 167 195 TNFR-Cys 4.
DOMAIN 372 457 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
REGION 340 360 N-SMase activation domain (NSD).
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 145 145 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 58 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 59 72 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 62 81 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 84 99 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 102 117 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 105 125 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 127 143 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 146 158 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 149 166 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 168 179 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 182 194 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 185 190 {ECO:0000255|PROSITE-ProRule:PRU00206}.
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


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