TNR1A_RAT
ID TNR1A_RAT Reviewed; 461 AA.
AC P22934; Q5U1X6; Q91V30; Q91Y93;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 178.
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=Tnfr-1, Tnfr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1702293; DOI=10.1089/dna.1990.9.705;
RA Himmler A., Maurer-Fogy I., Kroenke M., Scheurich P., Pfizenmaier K.,
RA Lantz M., Olsson I., Hauptmann R., Stratowa C., Adolf G.R.;
RT "Molecular cloning and expression of human and rat tumor necrosis factor
RT receptor chain (p60) and its soluble derivative, tumor necrosis factor-
RT binding protein.";
RL DNA Cell Biol. 9:705-715(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-230 AND PRO-295.
RC STRAIN=ACI/SegHsd, BB(DR)/Wor, Brown Norway/SsNHsd, DA/Bkl, F344/NHsd, and
RC LEW/NHsd;
RX PubMed=11486281; DOI=10.1007/s002510100338;
RA Furuya T., Salstrom J.L., Joe B., Hashiramoto A., Dobbins D.E.,
RA Wilder R.L., Remmers E.F.;
RT "Polymorphisms of the tumor necrosis factor receptor type 1 locus among
RT autoimmune susceptible and resistant inbred rat strains.";
RL Immunogenetics 53:427-429(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-230 AND PRO-295.
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 with DAB2IP. Interacts directly
CC with NOL3 (via CARD domain); inhibits TNF-signaling pathway. Interacts
CC with SH3RF2, TRADD and RIPK1. SH3RF2 facilitates the recruitment of
CC RIPK1 and TRADD to TNFRSF1A in a TNF-alpha-dependent process. Interacts
CC with PGLYRP1; this interaction is important for cell death induction.
CC Interacts (via death domain) with MADD (via death domain) (By
CC similarity). {ECO:0000250|UniProtKB:P19438,
CC 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}.
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DR EMBL; M63122; AAA42256.1; -; mRNA.
DR EMBL; AF329976; AAK53562.1; -; mRNA.
DR EMBL; AF329977; AAK53563.1; -; mRNA.
DR EMBL; AF329978; AAK53564.1; -; mRNA.
DR EMBL; AF329979; AAK53565.1; -; mRNA.
DR EMBL; AF329980; AAK53566.1; -; mRNA.
DR EMBL; AF329981; AAK53567.1; -; mRNA.
DR EMBL; BC086413; AAH86413.1; -; mRNA.
DR PIR; B36555; GQRTT1.
DR RefSeq; NP_037223.1; NM_013091.1.
DR AlphaFoldDB; P22934; -.
DR SMR; P22934; -.
DR BioGRID; 247654; 2.
DR IntAct; P22934; 1.
DR STRING; 10116.ENSRNOP00000042371; -.
DR GlyGen; P22934; 3 sites.
DR PhosphoSitePlus; P22934; -.
DR PaxDb; P22934; -.
DR GeneID; 25625; -.
DR KEGG; rno:25625; -.
DR UCSC; RGD:621237; rat.
DR CTD; 7132; -.
DR RGD; 621237; Tnfrsf1a.
DR eggNOG; ENOG502S050; Eukaryota.
DR InParanoid; P22934; -.
DR OrthoDB; 726174at2759; -.
DR PhylomeDB; P22934; -.
DR TreeFam; TF333916; -.
DR Reactome; R-RNO-5357786; TNFR1-induced proapoptotic signaling.
DR Reactome; R-RNO-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-RNO-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-RNO-5626978; TNFR1-mediated ceramide production.
DR Reactome; R-RNO-5669034; TNFs bind their physiological receptors.
DR Reactome; R-RNO-75893; TNF signaling.
DR PRO; PR:P22934; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
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; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0002020; F:protease binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0043120; F:tumor necrosis factor binding; IPI:RGD.
DR GO; GO:0005031; F:tumor necrosis factor receptor activity; IMP:RGD.
DR GO; GO:0003176; P:aortic valve development; ISO:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISO:RGD.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006952; P:defense response; ISS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0006954; P:inflammatory response; IEP:RGD.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0010614; P:negative regulation of cardiac muscle hypertrophy; ISO:RGD.
DR GO; GO:0003332; P:negative regulation of extracellular matrix constituent secretion; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:RGD.
DR GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR GO; GO:1902339; P:positive regulation of apoptotic process involved in morphogenesis; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:RGD.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:RGD.
DR GO; GO:0006693; P:prostaglandin metabolic process; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0003177; P:pulmonary valve development; ISO:RGD.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:RGD.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; ISO:RGD.
DR GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; ISO:RGD.
DR GO; GO:0043279; P:response to alkaloid; IEP:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; IEP:RGD.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:RGD.
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; 3.
DR PRINTS; PR01918; TNFACTORR1A.
DR SMART; SM00005; DEATH; 1.
DR SMART; SM00208; TNFR; 4.
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..461
FT /note="Tumor necrosis factor receptor superfamily member
FT 1A"
FT /id="PRO_0000034547"
FT TOPO_DOM 30..211
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..234
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 235..461
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..196
FT /note="TNFR-Cys 4"
FT DOMAIN 363..448
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 344..354
FT /note="N-SMase activation domain (NSD)"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
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..195
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 185..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VARIANT 230
FT /note="I -> V (in strain: LEW/NHsd, ACI/SegHsd, DA/Bkl and
FT F344/NHsd)"
FT /evidence="ECO:0000269|PubMed:11486281,
FT ECO:0000269|PubMed:15489334"
FT VARIANT 295
FT /note="H -> P (in strain: LEW/NHsd, ACI/SegHsd, DA/Bkl,
FT F344/NHsd and BN/SsNHsd)"
FT /evidence="ECO:0000269|PubMed:11486281,
FT ECO:0000269|PubMed:15489334"
SQ SEQUENCE 461 AA; 50969 MW; EB23C05450FBD202 CRC64;
MGLPIVPGLL LSLVLLALLM GIHPSGVTGL VPSLGDREKR DNLCPQGKYA HPKNNSICCT
KCHKGTYLVS DCPSPGQETV CEVCDKGTFT ASQNHVRQCL SCKTCRKEMF QVEISPCKAD
MDTVCGCKKN QFQRYLSETH FQCVDCSPCF NGTVTIPCKE KQNTVCNCHA GFFLSGNECT
PCSHCKKNQE CMKLCLPPVA NVTNPQDSGT AVLLPLVIFL GLCLLFFICI SLLCRYPQWR
PRVYSIICRD SAPVKEVEGE GIVTKPLTPA SIPAFSPNPG FNPTLGFSTT PRFSHPVSST
PISPVFGPSN WHNFVPPVRE VVPTQGADPL LYGSLNPVPI PAPVRKWEDV VAAQPQRLDT
ADPAMLYAVV DGVPPTRWKE FMRLLGLSEH EIERLELQNG RCLREAHYSM LEAWRRRTPR
HEATLDVVGR VLCDMNLRGC LENIRETLES PAHSSTTHLP R
