TNR16_RAT
ID TNR16_RAT Reviewed; 425 AA.
AC P07174;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Tumor necrosis factor receptor superfamily member 16;
DE AltName: Full=Gp80-LNGFR;
DE AltName: Full=Low affinity neurotrophin receptor p75NTR;
DE AltName: Full=Low-affinity nerve growth factor receptor;
DE Short=NGF receptor;
DE AltName: Full=p75 ICD;
DE AltName: CD_antigen=CD271;
DE Flags: Precursor;
GN Name=Ngfr; Synonyms=Tnfrsf16;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=3027580; DOI=10.1038/325593a0;
RA Radeke M.J., Misko T.P., Hsu C., Herzenberg L.A., Shooter E.M.;
RT "Gene transfer and molecular cloning of the rat nerve growth factor
RT receptor.";
RL Nature 325:593-597(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RC TISSUE=Liver;
RX PubMed=1446821; DOI=10.1016/0378-1119(92)90128-c;
RA Metsis M., Timmusk T., Allikmets R., Saarma M., Persson H.;
RT "Regulatory elements and transcriptional regulation by testosterone and
RT retinoic acid of the rat nerve growth factor receptor promoter.";
RL Gene 121:247-254(1992).
RN [3]
RP INTERACTION WITH NTRK2.
RX PubMed=9927421; DOI=10.1093/emboj/18.3.616;
RA Bibel M., Hoppe E., Barde Y.A.;
RT "Biochemical and functional interactions between the neurotrophin receptors
RT trk and p75NTR.";
RL EMBO J. 18:616-622(1999).
RN [4]
RP FUNCTION, AND INTERACTION WITH TRAF2; TRAF4 AND TRAF6.
RX PubMed=10514511; DOI=10.1074/jbc.274.42.30202;
RA Ye X., Mehlen P., Rabizadeh S., VanArsdale T., Zhang H., Shin H.,
RA Wang J.J.L., Leo E., Zapata J.M., Hauser C.A., Reed J.C., Bredesen D.E.;
RT "TRAF family proteins interact with the common neurotrophin receptor and
RT modulate apoptosis induction.";
RL J. Biol. Chem. 274:30202-30208(1999).
RN [5]
RP FUNCTION IN APOPTOSIS, AND INTERACTION WITH MAGED1.
RC STRAIN=Sprague-Dawley; TISSUE=Neural crest;
RX PubMed=10985348; DOI=10.1016/s0896-6273(00)00036-2;
RA Salehi A.H., Roux P.P., Kubu C.J., Zeindler C., Bhakar A., Tannis L.-L.,
RA Verdi J.M., Barker P.A.;
RT "NRAGE, a novel MAGE protein, interacts with the p75 neurotrophin receptor
RT and facilitates nerve growth factor dependent apoptosis.";
RL Neuron 27:279-288(2000).
RN [6]
RP INTERACTION WITH KIDINS220.
RX PubMed=11150334; DOI=10.1523/jneurosci.21-01-00176.2001;
RA Kong H., Boulter J., Weber J.L., Lai C., Chao M.V.;
RT "An evolutionarily conserved transmembrane protein that is a novel
RT downstream target of neurotrophin and ephrin receptors.";
RL J. Neurosci. 21:176-185(2001).
RN [7]
RP INTERACTION WITH NRADD.
RX PubMed=12095158; DOI=10.1385/nmm:1:3:153;
RA Frankowski H., Castro-Obregon S., del Rio G., Rao R.V., Bredesen D.E.;
RT "PLAIDD, a type II death domain protein that interacts with p75
RT neurotrophin receptor.";
RL NeuroMolecular Med. 1:153-170(2002).
RN [8]
RP INTERACTION WITH NTRK1 AND KIDINS220, AND DOMAIN.
RX PubMed=15378608; DOI=10.1002/jnr.20262;
RA Chang M.-S., Arevalo J.C., Chao M.V.;
RT "Ternary complex with Trk, p75, and an ankyrin-rich membrane spanning
RT protein.";
RL J. Neurosci. Res. 78:186-192(2004).
RN [9]
RP INTERACTION WITH BEX1.
RX PubMed=16498402; DOI=10.1038/sj.emboj.7601017;
RA Vilar M., Murillo-Carretero M., Mira H., Magnusson K., Besset V.,
RA Ibanez C.F.;
RT "Bex1, a novel interactor of the p75 neurotrophin receptor, links
RT neurotrophin signaling to the cell cycle.";
RL EMBO J. 25:1219-1230(2006).
RN [10]
RP FUNCTION, INTERACTION WITH TRIO; SORCS2 AND NGF, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22155786; DOI=10.1126/scisignal.2002060;
RA Deinhardt K., Kim T., Spellman D.S., Mains R.E., Eipper B.A., Neubert T.A.,
RA Chao M.V., Hempstead B.L.;
RT "Neuronal growth cone retraction relies on proneurotrophin receptor
RT signaling through Rac.";
RL Sci. Signal. 4:RA82-RA82(2011).
RN [11]
RP INTERACTION WITH SORCS2, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24908487; DOI=10.1016/j.neuron.2014.04.022;
RA Glerup S., Olsen D., Vaegter C.B., Gustafsen C., Sjoegaard S.S., Hermey G.,
RA Kjolby M., Molgaard S., Ulrichsen M., Boggild S., Skeldal S.,
RA Fjorback A.N., Nyengaard J.R., Jacobsen J., Bender D., Bjarkam C.R.,
RA Soerensen E.S., Fuechtbauer E.M., Eichele G., Madsen P., Willnow T.E.,
RA Petersen C.M., Nykjaer A.;
RT "SorCS2 regulates dopaminergic wiring and is processed into an apoptotic
RT two-chain receptor in peripheral glia.";
RL Neuron 82:1074-1087(2014).
RN [12]
RP INTERACTION WITH SORCS2.
RX PubMed=27457814; DOI=10.1038/mp.2016.108;
RA Glerup S., Bolcho U., Moelgaard S., Boeggild S., Vaegter C.B., Smith A.H.,
RA Nieto-Gonzalez J.L., Ovesen P.L., Pedersen L.F., Fjorback A.N., Kjolby M.,
RA Login H., Holm M.M., Andersen O.M., Nyengaard J.R., Willnow T.E.,
RA Jensen K., Nykjaer A.;
RT "SorCS2 is required for BDNF-dependent plasticity in the hippocampus.";
RL Mol. Psychiatry 21:1740-1751(2016).
RN [13] {ECO:0007744|PDB:1NGR}
RP STRUCTURE BY NMR OF 334-418.
RX PubMed=9305641; DOI=10.1093/emboj/16.16.4999;
RA Liepinsh E., Ilag L.L., Otting G., Ibanez C.F.;
RT "NMR structure of the death domain of the p75 neurotrophin receptor.";
RL EMBO J. 16:4999-5005(1997).
RN [14] {ECO:0007744|PDB:1SG1}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 30-190 IN COMPLEX WITH NGF,
RP FUNCTION, AND DISULFIDE BONDS.
RX PubMed=15131306; DOI=10.1126/science.1095190;
RA He X.L., Garcia K.C.;
RT "Structure of nerve growth factor complexed with the shared neurotrophin
RT receptor p75.";
RL Science 304:870-875(2004).
RN [15] {ECO:0007744|PDB:3BUK}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 30-190 IN COMPLEX WITH NTF3,
RP FUNCTION, GLYCOSYLATION AT ASN-61, AND DISULFIDE BONDS.
RX PubMed=18596692; DOI=10.1038/nature07089;
RA Gong Y., Cao P., Yu H.J., Jiang T.;
RT "Crystal structure of the neurotrophin-3 and p75NTR symmetrical complex.";
RL Nature 454:789-793(2008).
RN [16] {ECO:0007744|PDB:3IJ2}
RP X-RAY CRYSTALLOGRAPHY (3.75 ANGSTROMS) OF 30-190 OF MUTANT ASP-61 IN
RP COMPLEX WITH NGF, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BONDS,
RP GLYCOSYLATION AT ASN-61, AND MUTAGENESIS OF ASN-61.
RX PubMed=20036257; DOI=10.1016/j.jmb.2009.12.030;
RA Feng D., Kim T., Ozkan E., Light M., Torkin R., Teng K.K., Hempstead B.L.,
RA Garcia K.C.;
RT "Molecular and structural insight into proNGF engagement of p75NTR and
RT sortilin.";
RL J. Mol. Biol. 396:967-984(2010).
RN [17] {ECO:0007744|PDB:2MIC, ECO:0007744|PDB:2MJO}
RP STRUCTURE BY NMR OF 244-284, SUBUNIT, PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS
RP OF CYS-257; ALA-262 AND GLY-266.
RX PubMed=27056327; DOI=10.1074/jbc.m116.723585;
RA Nadezhdin K.D., Garcia-Carpio I., Goncharuk S.A., Mineev K.S.,
RA Arseniev A.S., Vilar M.;
RT "Structural Basis of p75 Transmembrane Domain Dimerization.";
RL J. Biol. Chem. 291:12346-12357(2016).
CC -!- FUNCTION: Low affinity receptor which can bind to NGF, BDNF, NTF3, and
CC NTF4 (PubMed:3027580, PubMed:15131306, PubMed:18596692). Forms a
CC heterodimeric receptor with SORCS2 that binds the precursor forms of
CC NGF, BDNF and NTF3 with high affinity, and has much lower affinity for
CC mature NGF and BDNF (PubMed:24908487, PubMed:22155786). In response to
CC proNGF binding, the heterodimeric receptor with SORCS2 activates a
CC signaling cascade that leads to decreased Rac activity, reorganization
CC of the actin cytoskeleton and neuronal growth cone collapse
CC (PubMed:22155786). Plays an important role in differentiation and
CC survival of specific neuronal populations during development (By
CC similarity). Can mediate cell survival as well as cell death of neural
CC cells (PubMed:10514511, PubMed:10985348, PubMed:24908487). Plays a role
CC in the inactivation of RHOA (By similarity). Plays a role in the
CC regulation of the translocation of GLUT4 to the cell surface in
CC adipocytes and skeletal muscle cells in response to insulin, probably
CC by regulating RAB31 activity, and thereby contributes to the regulation
CC of insulin-dependent glucose uptake (By similarity). Necessary for the
CC circadian oscillation of the clock genes ARNTL/BMAL1, PER1, PER2 and
CC NR1D1 in the suprachiasmatic nucleus (SCN) of the brain and in liver
CC and of the genes involved in glucose and lipid metabolism in the liver
CC (By similarity). {ECO:0000250|UniProtKB:P08138,
CC ECO:0000250|UniProtKB:Q9Z0W1, ECO:0000269|PubMed:10514511,
CC ECO:0000269|PubMed:10985348, ECO:0000269|PubMed:15131306,
CC ECO:0000269|PubMed:18596692, ECO:0000269|PubMed:22155786,
CC ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:3027580}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:27056327). Heterodimer
CC with SORCS2 (PubMed:27457814, PubMed:22155786, PubMed:24908487). The
CC extracellular domains of the heterodimer bind NGF (PubMed:22155786,
CC PubMed:24908487). The cytoplasmic region of the heterodimer binds TRIO.
CC NGF binding mediates dissociation of TRIO from the receptor complex
CC (PubMed:22155786). Interacts with RTN4R (By similarity). Interacts with
CC TRAF2, TRAF4 and TRAF6 (PubMed:10514511). Interacts with PTPN13 and
CC RANBP9. Interacts through TRAF6 with SQSTM1 which bridges NGFR to NTRK1
CC (By similarity). Interacts with BEX1 (PubMed:16498402). Interacts with
CC BEX3 (By similarity). Interacts with KIDINS220 and NTRK1. Can form a
CC ternary complex with NTRK1 and KIDINS220 and this complex is affected
CC by the expression levels of KIDINS220. An increase in KIDINS220
CC expression leads to a decreased association of NGFR and NTRK1
CC (PubMed:11150334, PubMed:15378608). Interacts (via death domain) with
CC RAB31 (By similarity). Interacts with NTRK2; may regulate the ligand
CC specificity of the NTRK2 receptor (PubMed:9927421). Interacts with
CC LINGO1 (By similarity). Interacts with NRADD (PubMed:12095158).
CC Interacts with MAGED1; the interaction antagonizes the association
CC NGFR:NTRK1 (PubMed:10985348). Interacts (via death domain) with ARHGDIA
CC and RIPK2 (By similarity). {ECO:0000250|UniProtKB:P08138,
CC ECO:0000250|UniProtKB:Q9Z0W1, ECO:0000269|PubMed:10514511,
CC ECO:0000269|PubMed:10985348, ECO:0000269|PubMed:11150334,
CC ECO:0000269|PubMed:12095158, ECO:0000269|PubMed:15378608,
CC ECO:0000269|PubMed:16498402, ECO:0000269|PubMed:22155786,
CC ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:27056327,
CC ECO:0000269|PubMed:27457814, ECO:0000269|PubMed:9927421}.
CC -!- INTERACTION:
CC P07174; Q3MKQ2: Bex1; NbExp=4; IntAct=EBI-1038810, EBI-8089575;
CC P07174; P07174: Ngfr; NbExp=2; IntAct=EBI-1038810, EBI-1038810;
CC P07174; P35739: Ntrk1; NbExp=2; IntAct=EBI-1038810, EBI-976667;
CC P07174; PRO_0000000093 [P05067]: APP; Xeno; NbExp=2; IntAct=EBI-1038810, EBI-2431589;
CC P07174; P01138: NGF; Xeno; NbExp=3; IntAct=EBI-1038810, EBI-1028250;
CC P07174; P20783: NTF3; Xeno; NbExp=4; IntAct=EBI-1038810, EBI-1025994;
CC P07174; Q12933: TRAF2; Xeno; NbExp=3; IntAct=EBI-1038810, EBI-355744;
CC P07174; Q9BUZ4: TRAF4; Xeno; NbExp=3; IntAct=EBI-1038810, EBI-3650647;
CC P07174; Q9Y4K3: TRAF6; Xeno; NbExp=2; IntAct=EBI-1038810, EBI-359276;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20036257,
CC ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:24908487,
CC ECO:0000269|PubMed:3027580}; Single-pass type I membrane protein
CC {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:22155786}. Cell
CC projection, growth cone {ECO:0000269|PubMed:22155786}. Cell projection,
CC dendritic spine {ECO:0000250|UniProtKB:Q9Z0W1}.
CC -!- DOMAIN: Death domain is responsible for interaction with RANBP9. It
CC also mediates interaction with ARHGDIA and RIPK2 (By similarity).
CC {ECO:0000250|UniProtKB:P08138, ECO:0000269|PubMed:15378608}.
CC -!- DOMAIN: The extracellular domain is responsible for interaction with
CC NTRK1. {ECO:0000269|PubMed:15378608}.
CC -!- PTM: Subject to intramembrane proteolytic cleavage by the gamma-
CC secretase complex, giving rise to an intracellular fragment that is
CC rapidly degraded via the proteasome. {ECO:0000269|PubMed:27056327}.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:20036257}.
CC -!- PTM: Phosphorylated on serine residues.
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DR EMBL; X05137; CAA28783.1; -; mRNA.
DR EMBL; X61269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; A26431; A26431.
DR RefSeq; NP_036742.2; NM_012610.2.
DR PDB; 1NGR; NMR; -; A=334-418.
DR PDB; 1SG1; X-ray; 2.40 A; X=30-190.
DR PDB; 2MIC; NMR; -; A/B=245-284.
DR PDB; 2MJO; NMR; -; A/B=245-284.
DR PDB; 3BUK; X-ray; 2.60 A; C/D=30-190.
DR PDB; 3IJ2; X-ray; 3.75 A; X/Y=30-190.
DR PDB; 4F42; X-ray; 2.38 A; A=334-418.
DR PDB; 4F44; X-ray; 2.40 A; A/B=334-418.
DR PDBsum; 1NGR; -.
DR PDBsum; 1SG1; -.
DR PDBsum; 2MIC; -.
DR PDBsum; 2MJO; -.
DR PDBsum; 3BUK; -.
DR PDBsum; 3IJ2; -.
DR PDBsum; 4F42; -.
DR PDBsum; 4F44; -.
DR AlphaFoldDB; P07174; -.
DR BMRB; P07174; -.
DR SMR; P07174; -.
DR BioGRID; 246737; 15.
DR CORUM; P07174; -.
DR DIP; DIP-5715N; -.
DR IntAct; P07174; 20.
DR MINT; P07174; -.
DR STRING; 10116.ENSRNOP00000007268; -.
DR ChEMBL; CHEMBL4523169; -.
DR GlyGen; P07174; 2 sites.
DR iPTMnet; P07174; -.
DR PhosphoSitePlus; P07174; -.
DR SwissPalm; P07174; -.
DR jPOST; P07174; -.
DR PaxDb; P07174; -.
DR PRIDE; P07174; -.
DR GeneID; 24596; -.
DR KEGG; rno:24596; -.
DR UCSC; RGD:3177; rat.
DR CTD; 4804; -.
DR RGD; 3177; Ngfr.
DR eggNOG; ENOG502QWPN; Eukaryota.
DR InParanoid; P07174; -.
DR OrthoDB; 757160at2759; -.
DR PhylomeDB; P07174; -.
DR Reactome; R-RNO-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-RNO-193692; Regulated proteolysis of p75NTR.
DR Reactome; R-RNO-205017; NFG and proNGF binds to p75NTR.
DR Reactome; R-RNO-205025; NADE modulates death signalling.
DR Reactome; R-RNO-205043; NRIF signals cell death from the nucleus.
DR Reactome; R-RNO-209543; p75NTR recruits signalling complexes.
DR Reactome; R-RNO-209560; NF-kB is activated and signals survival.
DR Reactome; R-RNO-209563; Axonal growth stimulation.
DR EvolutionaryTrace; P07174; -.
DR PRO; PR:P07174; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:RGD.
DR GO; GO:0030135; C:coated vesicle; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
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:0032809; C:neuronal cell body membrane; IDA:RGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0001540; F:amyloid-beta binding; IPI:RGD.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0015026; F:coreceptor activity; ISO:RGD.
DR GO; GO:0005035; F:death receptor activity; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0048406; F:nerve growth factor binding; IDA:RGD.
DR GO; GO:0043121; F:neurotrophin binding; IPI:RGD.
DR GO; GO:0005168; F:neurotrophin TRKA receptor binding; IPI:RGD.
DR GO; GO:0070678; F:preprotein binding; IPI:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; ISO:RGD.
DR GO; GO:0001678; P:cellular glucose homeostasis; ISS:UniProtKB.
DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:RGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:RGD.
DR GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; ISO:RGD.
DR GO; GO:0016048; P:detection of temperature stimulus; ISO:RGD.
DR GO; GO:0035907; P:dorsal aorta development; ISO:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0031069; P:hair follicle morphogenesis; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0061000; P:negative regulation of dendritic spine development; IMP:RGD.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0051799; P:negative regulation of hair follicle development; ISO:RGD.
DR GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IMP:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:RGD.
DR GO; GO:0021675; P:nerve development; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:RGD.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; ISO:RGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:RGD.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0031643; P:positive regulation of myelination; IMP:RGD.
DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; IDA:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0042488; P:positive regulation of odontogenesis of dentin-containing tooth; ISO:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:RGD.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:RGD.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:RGD.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IMP:RGD.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:RGD.
DR GO; GO:0010941; P:regulation of cell death; IDA:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; IMP:RGD.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR GO; GO:0007165; P:signal transduction; IDA:RGD.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEP:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR CDD; cd13416; TNFRSF16; 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; IPR041448; TNFR16_TM.
DR InterPro; IPR022325; TNFR_16.
DR InterPro; IPR034046; TNFRSF16_N.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF18422; TNFR_16_TM; 1.
DR Pfam; PF00020; TNFR_c6; 3.
DR PRINTS; PR01966; TNFACTORR16.
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; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Biological rhythms; Cell membrane;
KW Cell projection; Developmental protein; Differentiation; Disulfide bond;
KW Glycoprotein; Membrane; Neurogenesis; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..29
FT CHAIN 30..425
FT /note="Tumor necrosis factor receptor superfamily member
FT 16"
FT /id="PRO_0000034593"
FT TOPO_DOM 30..253
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:27056327"
FT TOPO_DOM 275..425
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 32..65
FT /note="TNFR-Cys 1"
FT REPEAT 67..108
FT /note="TNFR-Cys 2"
FT REPEAT 109..147
FT /note="TNFR-Cys 3"
FT REPEAT 149..189
FT /note="TNFR-Cys 4"
FT DOMAIN 354..419
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 193..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..342
FT /note="Mediates interaction with KIDINS220"
FT COMPBIAS 202..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08138"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:20036257,
FT ECO:0007744|PDB:3BUK"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..44
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT DISULFID 45..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT DISULFID 48..65
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT DISULFID 68..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT DISULFID 87..100
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT DISULFID 90..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT DISULFID 110..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT DISULFID 126..139
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT DISULFID 129..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT DISULFID 150..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT DISULFID 168..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT DISULFID 171..189
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206,
FT ECO:0007744|PDB:1SG1, ECO:0007744|PDB:3BUK,
FT ECO:0007744|PDB:3IJ2"
FT MUTAGEN 61
FT /note="N->D: Loss of a glycosylation site."
FT /evidence="ECO:0000269|PubMed:20036257"
FT MUTAGEN 257
FT /note="C->A: Alters mode of dimerization, but does not
FT abolish dimerization."
FT /evidence="ECO:0000269|PubMed:27056327"
FT MUTAGEN 257
FT /note="C->I: No effect on dimerization. Loss of
FT dimerization; when associated with I-266."
FT /evidence="ECO:0000269|PubMed:27056327"
FT MUTAGEN 262
FT /note="A->I: No effect on dimerization."
FT /evidence="ECO:0000269|PubMed:27056327"
FT MUTAGEN 266
FT /note="G->I: No effect on dimerization. Loss of
FT dimerization; when associated with I-257."
FT /evidence="ECO:0000269|PubMed:27056327"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3BUK"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1SG1"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1SG1"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1SG1"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1SG1"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:1SG1"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:1SG1"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:1SG1"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1SG1"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1SG1"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:1SG1"
FT STRAND 133..137
FT /evidence="ECO:0007829|PDB:1SG1"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:1SG1"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1SG1"
FT TURN 246..249
FT /evidence="ECO:0007829|PDB:2MIC"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:2MIC"
FT HELIX 255..275
FT /evidence="ECO:0007829|PDB:2MIC"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:2MIC"
FT HELIX 337..339
FT /evidence="ECO:0007829|PDB:4F42"
FT HELIX 342..351
FT /evidence="ECO:0007829|PDB:4F42"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:4F42"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:4F42"
FT HELIX 368..373
FT /evidence="ECO:0007829|PDB:4F42"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:4F42"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:4F42"
FT HELIX 380..388
FT /evidence="ECO:0007829|PDB:4F42"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:4F44"
FT HELIX 396..405
FT /evidence="ECO:0007829|PDB:4F42"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:4F42"
SQ SEQUENCE 425 AA; 45433 MW; B2E152D94D3827F8 CRC64;
MRRAGAACSA MDRLRLLLLL ILGVSSGGAK ETCSTGLYTH SGECCKACNL GEGVAQPCGA
NQTVCEPCLD NVTFSDVVSA TEPCKPCTEC LGLQSMSAPC VEADDAVCRC AYGYYQDEET
GHCEACSVCE VGSGLVFSCQ DKQNTVCEEC PEGTYSDEAN HVDPCLPCTV CEDTERQLRE
CTPWADAECE EIPGRWIPRS TPPEGSDSTA PSTQEPEVPP EQDLVPSTVA DMVTTVMGSS
QPVVTRGTTD NLIPVYCSIL AAVVVGLVAY IAFKRWNSCK QNKQGANSRP VNQTPPPEGE
KLHSDSGISV DSQSLHDQQT HTQTASGQAL KGDGNLYSSL PLTKREEVEK LLNGDTWRHL
AGELGYQPEH IDSFTHEACP VRALLASWGA QDSATLDALL AALRRIQRAD IVESLCSEST
ATSPV
