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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_MOUSE             Reviewed;         454 AA.
P25118;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-MAY-1992, sequence version 1.
22-NOV-2017, entry version 175.
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=Tnfr-1, Tnfr1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1849278; DOI=10.1073/pnas.88.7.2830;
Lewis M., Tartaglia L.A., Lee A., Bennett G.L., Rice G.C., Wong G.H.,
Chen E.Y., Goeddel D.V.;
"Cloning and expression of cDNAs for two distinct murine tumor
necrosis factor receptors demonstrate one receptor is species
specific.";
Proc. Natl. Acad. Sci. U.S.A. 88:2830-2834(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1645445; DOI=10.1128/MCB.11.6.3020;
Goodwin R.G., Anderson D., Jerzy R., Davis T., Brannan C.I.,
Copeland N.G., Jenkins N.A., Smith C.A.;
"Molecular cloning and expression of the type 1 and type 2 murine
receptors for tumor necrosis factor.";
Mol. Cell. Biol. 11:3020-3026(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1647956; DOI=10.1002/eji.1830210710;
Barrett K., Taylor-Fishwick D.A., Cope A.P., Kissonerghis A.M.,
Gray P.W., Feldmann M., Foxwell B.M.J.;
"Cloning, expression and cross-linking analysis of the murine p55
tumor necrosis factor receptor.";
Eur. J. Immunol. 21:1649-1656(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
PubMed=1657766; DOI=10.1007/BF00211997;
Rothe J.G., Brockhaus M., Gentz R., Lesslauer W.;
"Molecular cloning and expression of the mouse Tnf receptor type b.";
Immunogenetics 34:338-340(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8188324; DOI=10.1007/BF00176168;
Bebo B.F., Linthicum D.S.;
"Nucleotide sequence of the TNF type I receptor from a mouse
endothelioma cell line.";
Immunogenetics 39:450-451(1994).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8381516; DOI=10.1016/0161-5890(93)90088-S;
Rothe J., Bluethmann H., Gentz R., Lesslauer W., Steinmetz M.;
"Genomic organization and promoter function of the murine tumor
necrosis factor receptor beta gene.";
Mol. Immunol. 30:165-175(1993).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C3H/He; TISSUE=Mesenchymal cell;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH NOL3.
PubMed=24440909; DOI=10.1038/cdd.2013.195;
Kung G., Dai P., Deng L., Kitsis R.N.;
"A novel role for the apoptosis inhibitor ARC in suppressing TNFalpha-
induced regulated necrosis.";
Cell Death Differ. 21:634-644(2014).
-!- 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 with DAB2IP (By similarity). Interacts directly with
NOL3 (via CARD domain); inhibits TNF-signaling pathway.
{ECO:0000250, ECO:0000269|PubMed:24440909}.
-!- INTERACTION:
Q9EQY0:Ern1; NbExp=2; IntAct=EBI-518014, EBI-5480799;
Q61160:Fadd; NbExp=2; IntAct=EBI-518014, EBI-524415;
Q60855:Ripk1; NbExp=4; IntAct=EBI-518014, EBI-529119;
Q31125:Slc39a7; NbExp=3; IntAct=EBI-518014, EBI-644519;
P01375:TNF (xeno); NbExp=3; IntAct=EBI-518014, EBI-359977;
P62991:Ubc; NbExp=2; IntAct=EBI-518014, EBI-413074;
-!- 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.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M60468; AAA39751.1; -; mRNA.
EMBL; M59377; AAA40464.1; -; mRNA.
EMBL; X59238; CAA41922.1; -; mRNA.
EMBL; X57796; CAA40936.1; -; mRNA.
EMBL; L26349; AAA59361.1; -; mRNA.
EMBL; M76656; AAA40465.1; -; Genomic_DNA.
EMBL; M88067; AAA40465.1; JOINED; Genomic_DNA.
EMBL; M76655; AAA40465.1; JOINED; Genomic_DNA.
EMBL; BC004599; AAH04599.1; -; mRNA.
EMBL; BC052675; AAH52675.1; -; mRNA.
CCDS; CCDS20550.1; -.
PIR; A38634; GQMST1.
RefSeq; NP_035739.2; NM_011609.4.
UniGene; Mm.1258; -.
UniGene; Mm.474976; -.
ProteinModelPortal; P25118; -.
SMR; P25118; -.
BioGrid; 204249; 13.
CORUM; P25118; -.
DIP; DIP-34532N; -.
IntAct; P25118; 27.
MINT; MINT-2631249; -.
STRING; 10090.ENSMUSP00000032491; -.
iPTMnet; P25118; -.
PhosphoSitePlus; P25118; -.
PaxDb; P25118; -.
PeptideAtlas; P25118; -.
PRIDE; P25118; -.
Ensembl; ENSMUST00000032491; ENSMUSP00000032491; ENSMUSG00000030341.
GeneID; 21937; -.
KEGG; mmu:21937; -.
UCSC; uc009dul.2; mouse.
CTD; 7132; -.
MGI; MGI:1314884; Tnfrsf1a.
eggNOG; ENOG410IXBX; Eukaryota.
eggNOG; ENOG4111YG2; LUCA.
GeneTree; ENSGT00530000064001; -.
HOGENOM; HOG000133001; -.
HOVERGEN; HBG058842; -.
InParanoid; P25118; -.
KO; K03158; -.
OMA; GCLEDIE; -.
OrthoDB; EOG091G07LE; -.
PhylomeDB; P25118; -.
TreeFam; TF333916; -.
Reactome; R-MMU-5357786; TNFR1-induced proapoptotic signaling.
Reactome; R-MMU-5357905; Regulation of TNFR1 signaling.
Reactome; R-MMU-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-MMU-5626978; TNFR1-mediated ceramide production.
Reactome; R-MMU-5669034; TNFs bind their physiological receptors.
Reactome; R-MMU-75893; TNF signaling.
PRO; PR:P25118; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000030341; -.
ExpressionAtlas; P25118; baseline and differential.
Genevisible; P25118; MM.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:MGI.
GO; GO:0043235; C:receptor complex; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0043120; F:tumor necrosis factor binding; IBA:GO_Central.
GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; IMP:MGI.
GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:MGI.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IMP:MGI.
GO; GO:0006952; P:defense response; IMP:MGI.
GO; GO:0042742; P:defense response to bacterium; IMP:MGI.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IMP:MGI.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
GO; GO:0050728; P:negative regulation of inflammatory response; ISO:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:MGI.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
GO; GO:0006693; P:prostaglandin metabolic process; TAS:MGI.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
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; 3.
PRINTS; PR01918; TNFACTORR1A.
SMART; SM00005; DEATH; 1.
SMART; SM00208; TNFR; 4.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS00652; TNFR_NGFR_1; 3.
PROSITE; PS50050; TNFR_NGFR_2; 3.
1: Evidence at protein 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 22 454 Tumor necrosis factor receptor
superfamily member 1A.
/FTId=PRO_0000034545.
TOPO_DOM 22 212 Extracellular. {ECO:0000255}.
TRANSMEM 213 235 Helical. {ECO:0000255}.
TOPO_DOM 236 454 Cytoplasmic. {ECO:0000255}.
REPEAT 43 82 TNFR-Cys 1.
REPEAT 83 125 TNFR-Cys 2.
REPEAT 126 166 TNFR-Cys 3.
REPEAT 167 196 TNFR-Cys 4.
DOMAIN 356 441 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
REGION 339 349 N-SMase activation domain (NSD).
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 151 151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 202 202 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 182 195 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 185 191 {ECO:0000255|PROSITE-ProRule:PRU00206}.
CONFLICT 394 394 R -> G (in Ref. 6; AAA40465).
{ECO:0000305}.
SEQUENCE 454 AA; 50130 MW; 0710C2E8C3C2B6D9 CRC64;
MGLPTVPGLL LSLVLLALLM GIHPSGVTGL VPSLGDREKR DSLCPQGKYV HSKNNSICCT
KCHKGTYLVS DCPSPGRDTV CRECEKGTFT ASQNYLRQCL SCKTCRKEMS QVEISPCQAD
KDTVCGCKEN QFQRYLSETH FQCVDCSPCF NGTVTIPCKE TQNTVCNCHA GFFLRESECV
PCSHCKKNEE CMKLCLPPPL ANVTNPQDSG TAVLLPLVIL LGLCLLSFIF ISLMCRYPRW
RPEVYSIICR DPVPVKEEKA GKPLTPAPSP AFSPTSGFNP TLGFSTPGFS SPVSSTPISP
IFGPSNWHFM PPVSEVVPTQ GADPLLYESL CSVPAPTSVQ KWEDSAHPQR PDNADLAILY
AVVDGVPPAR WKEFMRFMGL SEHEIERLEM QNGRCLREAQ YSMLEAWRRR TPRHEDTLEV
VGLVLSKMNL AGCLENILEA LRNPAPSSTT RLPR


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