ID TNR16_MOUSE Reviewed; 427 AA. AC Q9Z0W1; Q8CFT3; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 03-JUL-2019, sequence version 2. DT 24-JAN-2024, entry version 180. DE RecName: Full=Tumor necrosis factor receptor superfamily member 16; DE AltName: Full=Low affinity neurotrophin receptor p75NTR {ECO:0000303|PubMed:9857182}; DE AltName: Full=Low-affinity nerve growth factor receptor; DE Short=NGF receptor; DE AltName: Full=Low-affinity nerve growth factor receptor p75NGFR; DE AltName: Full=Low-affinity nerve growth factor receptor p75NGR; DE AltName: CD_antigen=CD271; DE Flags: Precursor; GN Name=Ngfr; Synonyms=Tnfrsf16; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Eye {ECO:0000312|EMBL:AAH38365.1}; 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). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-427 (ISOFORM 1), FUNCTION (MICROBIAL RP INFECTION), AND INTERACTION WITH RABIES VIRUS GLYCOPROTEIN (MICROBIAL RP INFECTION). RC STRAIN=A; RX PubMed=9857182; DOI=10.1093/emboj/17.24.7250; RA Tuffereau C., Benejean J., Blondel D., Kieffer B., Flamand A.; RT "Low-affinity nerve-growth factor receptor (p75NTR) can serve as a receptor RT for rabies virus."; RL EMBO J. 17:7250-7259(1998). RN [4] RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=1317267; DOI=10.1016/0092-8674(92)90286-l; RA Lee K.F., Li E., Huber L.J., Landis S.C., Sharpe A.H., Chao M.V., RA Jaenisch R.; RT "Targeted mutation of the gene encoding the low affinity NGF receptor p75 RT leads to deficits in the peripheral sensory nervous system."; RL Cell 69:737-749(1992). RN [5] RP DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH NTRK2, SUBCELLULAR RP LOCATION, GLYCOSYLATION, ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE, AND RP TISSUE SPECIFICITY. RX PubMed=11559852; DOI=10.1038/nn730; RA von Schack D., Casademunt E., Schweigreiter R., Meyer M., Bibel M., RA Dechant G.; RT "Complete ablation of the neurotrophin receptor p75NTR causes defects both RT in the nervous and the vascular system."; RL Nat. Neurosci. 4:977-978(2001). RN [6] RP INTERACTION WITH BEX3. RX PubMed=11830582; DOI=10.1074/jbc.m106342200; RA Mukai J., Shoji S., Kimura M.T., Okubo S., Sano H., Suvanto P., Li Y., RA Irie S., Sato T.-A.; RT "Structure-function analysis of NADE: identification of regions that RT mediate nerve growth factor-induced apoptosis."; RL J. Biol. Chem. 277:13973-13982(2002). RN [7] RP FUNCTION, INTERACTION WITH SORCS2; TRIO AND NGF, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. 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 [8] RP INTERACTION WITH RTN4R. RX PubMed=22923615; DOI=10.1074/jbc.m112.389916; RA Nakaya N., Sultana A., Lee H.S., Tomarev S.I.; RT "Olfactomedin 1 interacts with the Nogo A receptor complex to regulate axon RT growth."; RL J. Biol. Chem. 287:37171-37184(2012). RN [9] RP FUNCTION, AND INTERACTION WITH RAB31. RX PubMed=22460790; DOI=10.1073/pnas.1103638109; RA Baeza-Raja B., Li P., Le Moan N., Sachs B.D., Schachtrup C., Davalos D., RA Vagena E., Bridges D., Kim C., Saltiel A.R., Olefsky J.M., Akassoglou K.; RT "p75 neurotrophin receptor regulates glucose homeostasis and insulin RT sensitivity."; RL Proc. Natl. Acad. Sci. U.S.A. 109:5838-5843(2012). RN [10] RP FUNCTION, AND INDUCTION. RX PubMed=23785138; DOI=10.1523/jneurosci.2757-12.2013; RA Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F., RA Sassone-Corsi P., Ptacek L.J., Akassoglou K.; RT "p75 neurotrophin receptor is a clock gene that regulates oscillatory RT components of circadian and metabolic networks."; RL J. Neurosci. 33:10221-10234(2013). RN [11] RP FUNCTION, AND INTERACTION WITH SORCS2. 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 FUNCTION, INTERACTION WITH SORCS2, AND TISSUE SPECIFICITY. 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] RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION. RX PubMed=29909994; DOI=10.1016/j.neuron.2018.05.024; RA Giza J.I., Kim J., Meyer H.C., Anastasia A., Dincheva I., Zheng C.I., RA Lopez K., Bains H., Yang J., Bracken C., Liston C., Jing D., RA Hempstead B.L., Lee F.S.; RT "The BDNF Val66Met Prodomain Disassembles Dendritic Spines Altering Fear RT Extinction Circuitry and Behavior."; RL Neuron 99:163-178(2018). CC -!- FUNCTION: Low affinity neurotrophin receptor which can bind to mature CC NGF, BDNF, NTF3, and NTF4 (PubMed:11559852, PubMed:1317267). Forms a CC heterodimeric receptor with SORCS2 that binds the precursor forms of CC NGF (proNGF), BDNF (proBDNF) and NTF3 (proNT3) with high affinity, and CC has much lower affinity for mature NGF and BDNF (PubMed:22155786, CC PubMed:24908487, PubMed:27457814). Plays an important role in CC differentiation and survival of specific neuronal populations during CC development (PubMed:1317267, PubMed:11559852). Can mediate cell CC survival as well as cell death of neural cells (PubMed:1317267, CC PubMed:11559852, PubMed:24908487). The heterodimeric receptor formed CC with SORCS2 plays a role in proBDNF-dependent synaptic plasticity, in CC hippocampal long term depression (LTD) and long term potentiation (LTP) CC (PubMed:27457814). Plays a role in the inactivation of RHOA (By CC similarity). Plays a role in the regulation of the translocation of CC GLUT4 to the cell surface in adipocytes and skeletal muscle cells in CC response to insulin, probably by regulating RAB31 activity, and thereby CC contributes to the regulation of insulin-dependent glucose uptake CC (PubMed:22460790). Necessary for the circadian oscillation of the clock CC genes BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCN) CC of the brain and in liver and of the genes involved in glucose and CC lipid metabolism in the liver (PubMed:23785138). {ECO:0000250, CC ECO:0000250|UniProtKB:P08138, ECO:0000269|PubMed:11559852, CC ECO:0000269|PubMed:1317267, ECO:0000269|PubMed:22155786, CC ECO:0000269|PubMed:22460790, ECO:0000269|PubMed:23785138, CC ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:27457814}. CC -!- FUNCTION: (Microbial infection) Cell surface receptor for rabies virus CC glycoprotein Gs. {ECO:0000269|PubMed:9857182}. CC -!- FUNCTION: [Isoform 2]: Does not bind NGF, BDNF, NTF3, and NTF4. CC {ECO:0000269|PubMed:11559852}. CC -!- SUBUNIT: Homodimer; disulfide-linked. Heterodimer with SORCS2 CC (PubMed:22155786, PubMed:24908487, PubMed:27457814). The extracellular CC domains of the heterodimer bind NGF. The cytoplasmic region of the CC heterodimer binds TRIO. NGF binding mediates dissociation of TRIO from CC the receptor complex (PubMed:22155786). Interacts with TRAF2, TRAF4, CC TRAF6, PTPN13 and RANBP9. Interacts through TRAF6 with SQSTM1 which CC bridges NGFR to NTRK1. Interacts with BEX1 (By similarity). Interacts CC with BEX3 (PubMed:11830582). Interacts with KIDINS220 and NTRK1. Can CC form a ternary complex with NTRK1 and KIDINS220 and this complex is CC affected by the expression levels of KIDINS220. An increase in CC KIDINS220 expression leads to a decreased association of NGFR and CC NTRK1. Interacts (via death domain) with RAB31 (PubMed:22460790). CC Interacts with NTRK2; may regulate the ligand specificity of the NTRK2 CC receptor (PubMed:11559852). Interacts with LINGO1. Interacts with CC NRADD. Interacts with MAGED1; the interaction antagonizes the CC association NGFR:NTRK1 (By similarity). Interacts with RTN4R CC (PubMed:22923615). Interacts (via death domain) with ARHGDIA and RIPK2 CC (By similarity). {ECO:0000250|UniProtKB:P07174, CC ECO:0000250|UniProtKB:P08138, ECO:0000269|PubMed:11559852, CC ECO:0000269|PubMed:11830582, ECO:0000269|PubMed:22155786, CC ECO:0000269|PubMed:22460790, ECO:0000269|PubMed:22923615, CC ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:27457814}. CC -!- SUBUNIT: (Microbial infection) Binds to rabies virus glycoprotein Gs. CC {ECO:0000269|PubMed:9857182}. CC -!- INTERACTION: CC Q9Z0W1; Q9EPR5: Sorcs2; NbExp=4; IntAct=EBI-4411273, EBI-9915438; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11559852, CC ECO:0000269|PubMed:1317267, ECO:0000269|PubMed:22155786, CC ECO:0000269|PubMed:9857182}; 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:0000269|PubMed:29909994}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Z0W1-1; Sequence=Displayed; CC Name=2; Synonyms=s-p75 {ECO:0000303|PubMed:11559852}; CC IsoId=Q9Z0W1-2; Sequence=Not described; CC -!- TISSUE SPECIFICITY: Detected in Schwann cells (PubMed:11559852). CC Detected in embryonic brain, in hippocampus neurons (at protein level) CC (PubMed:22155786, PubMed:27457814). Detected in brain and spinal cord CC (PubMed:11559852). {ECO:0000269|PubMed:11559852, CC ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:27457814}. CC -!- DEVELOPMENTAL STAGE: Detected in embryonic large blood vessels at 11.5 CC dpc. {ECO:0000269|PubMed:11559852}. CC -!- INDUCTION: Expression oscillates in a circadian manner in the CC suprachiasmatic nucleus (SCN) of the brain and in liver. Expression CC seen at higher levels during the light period and lower during the dark CC period. {ECO:0000269|PubMed:23785138}. CC -!- DOMAIN: The death domain mediates interaction with RANBP9 (By CC similarity). It also mediates interaction with ARHGDIA and RIPK2 (By CC similarity). {ECO:0000250|UniProtKB:P07174, CC ECO:0000250|UniProtKB:P08138}. CC -!- DOMAIN: The extracellular domain is responsible for interaction with CC NTRK1. {ECO:0000250}. CC -!- PTM: N-glycosylated (PubMed:11559852). O-glycosylated. {ECO:0000250, CC ECO:0000269|PubMed:11559852}. CC -!- PTM: Phosphorylated on serine residues. {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Embryos are present at the expected Mendelian CC rate at 15.5 dpc, but mutant mice display about 40% perinatal CC lethality. At 11.5 dpc, mutant embryos display mildly to severely CC dilated blood vessels with thinner walls. The dorsal aorta is CC particularly affected. Many embryos show massive dilatations, ruptures CC and blood leakage. Surviving animals display small size and hind limb CC ataxia at 13 days after birth. When held by their tails, they respond CC by stretching their hind legs pointing upwards. The diameter of their CC sciatic nerve is strongly reduced. At 3 days after birth, the number of CC Schwann cells is strongly reduced in sciatic nerve from mutant mice. CC Likewise, the number of sensory neurons in dorsal root ganglia is CC strongly reduced (PubMed:11559852). The initially reported gene CC disruption experiment finds that mice are born at the expected CC Mendelian rate, are fertile, and have no visible phenotype when young. CC However, after 4 months mutant mice develop skin alterations with CC severe ulcers on all extremities. Already before the onset of symptoms, CC mutant mice display decreased skin innervation and smaller dorsal root CC ganglia, plus impaired heat sensitivity (PubMed:11559852). CC {ECO:0000269|PubMed:11559852}. CC -!- MISCELLANEOUS: [Isoform 2]: Minor isoform that lacks exon 3. CC {ECO:0000305|PubMed:11559852}. CC -!- CAUTION: The initial gene disruption experiment found a less pronounced CC phenotype than that reported in a later study (PubMed:1317267, CC PubMed:11559852). Both experiments disrupt expression of isoform 1 and CC NGF binding (PubMed:1317267, PubMed:11559852). The differences may be CC due to the presence of isoform 2; its expression is disrupted in the CC later experiment, but not in the initial experiment (PubMed:11559852). CC {ECO:0000269|PubMed:11559852, ECO:0000269|PubMed:1317267}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD17943.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL662875; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC038365; AAH38365.1; -; mRNA. DR EMBL; AF105292; AAD17943.1; ALT_INIT; mRNA. DR CCDS; CCDS25279.1; -. [Q9Z0W1-1] DR RefSeq; NP_150086.2; NM_033217.3. [Q9Z0W1-1] DR AlphaFoldDB; Q9Z0W1; -. DR BMRB; Q9Z0W1; -. DR SMR; Q9Z0W1; -. DR CORUM; Q9Z0W1; -. DR IntAct; Q9Z0W1; 6. DR MINT; Q9Z0W1; -. DR STRING; 10090.ENSMUSP00000000122; -. DR BindingDB; Q9Z0W1; -. DR ChEMBL; CHEMBL4523515; -. DR GlyCosmos; Q9Z0W1; 1 site, No reported glycans. DR GlyGen; Q9Z0W1; 1 site. DR iPTMnet; Q9Z0W1; -. DR PhosphoSitePlus; Q9Z0W1; -. DR jPOST; Q9Z0W1; -. DR MaxQB; Q9Z0W1; -. DR PaxDb; 10090-ENSMUSP00000000122; -. DR PeptideAtlas; Q9Z0W1; -. DR ProteomicsDB; 260633; -. [Q9Z0W1-1] DR ProteomicsDB; 341380; -. DR Antibodypedia; 1461; 1784 antibodies from 50 providers. DR DNASU; 18053; -. DR Ensembl; ENSMUST00000000122.7; ENSMUSP00000000122.7; ENSMUSG00000000120.7. [Q9Z0W1-1] DR GeneID; 18053; -. DR KEGG; mmu:18053; -. DR UCSC; uc007lam.2; mouse. DR AGR; MGI:97323; -. DR CTD; 4804; -. DR MGI; MGI:97323; Ngfr. DR VEuPathDB; HostDB:ENSMUSG00000000120; -. DR eggNOG; ENOG502QWPN; Eukaryota. DR GeneTree; ENSGT00730000110974; -. DR HOGENOM; CLU_052667_0_1_1; -. DR InParanoid; Q9Z0W1; -. DR OMA; YSCQDKQ; -. DR OrthoDB; 4222274at2759; -. DR TreeFam; TF106466; -. DR Reactome; R-MMU-193634; Axonal growth inhibition (RHOA activation). DR Reactome; R-MMU-193692; Regulated proteolysis of p75NTR. DR Reactome; R-MMU-205017; NFG and proNGF binds to p75NTR. DR Reactome; R-MMU-205025; NADE modulates death signalling. DR Reactome; R-MMU-205043; NRIF signals cell death from the nucleus. DR Reactome; R-MMU-209543; p75NTR recruits signalling complexes. DR Reactome; R-MMU-209560; NF-kB is activated and signals survival. DR Reactome; R-MMU-209563; Axonal growth stimulation. DR BioGRID-ORCS; 18053; 4 hits in 82 CRISPR screens. DR ChiTaRS; Ngfr; mouse. DR PRO; PR:Q9Z0W1; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; Q9Z0W1; Protein. DR Bgee; ENSMUSG00000000120; Expressed in dorsal root ganglion and 224 other cell types or tissues. DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL. DR GO; GO:0005911; C:cell-cell junction; IDA:MGI. DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0032590; C:dendrite membrane; ISO:MGI. DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell. DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI. DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell. DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO. DR GO; GO:0032809; C:neuronal cell body membrane; ISO:MGI. DR GO; GO:0005635; C:nuclear envelope; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0043204; C:perikaryon; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0014069; C:postsynaptic density; IDA:MGI. DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI. DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI. DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB. DR GO; GO:0015026; F:coreceptor activity; ISO:MGI. DR GO; GO:0005035; F:death receptor activity; IDA:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0048406; F:nerve growth factor binding; IDA:MGI. DR GO; GO:0043121; F:neurotrophin binding; ISO:MGI. DR GO; GO:0005168; F:neurotrophin TRKA receptor binding; ISO:MGI. DR GO; GO:0070678; F:preprotein binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0007411; P:axon guidance; IMP:MGI. DR GO; GO:1904646; P:cellular response to amyloid-beta; ISO:MGI. DR GO; GO:0034599; P:cellular response to oxidative stress; ISO:MGI. DR GO; GO:0007417; P:central nervous system development; IMP:MGI. DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB. DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB. DR GO; GO:0016048; P:detection of temperature stimulus; IMP:MGI. DR GO; GO:0035907; P:dorsal aorta development; IMP:UniProtKB. DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IMP:MGI. DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI. DR GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB. DR GO; GO:0001942; P:hair follicle development; IMP:MGI. DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI. DR GO; GO:0001678; P:intracellular glucose homeostasis; IMP:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; IMP:UniProtKB. DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI. DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; ISO:MGI. DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI. DR GO; GO:0061000; P:negative regulation of dendritic spine development; ISO:MGI. DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI. DR GO; GO:0051799; P:negative regulation of hair follicle development; IMP:MGI. DR GO; GO:0051902; P:negative regulation of mitochondrial depolarization; ISO:MGI. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI. DR GO; GO:0010977; P:negative regulation of neuron projection development; ISO:MGI. DR GO; GO:0021675; P:nerve development; IMP:MGI. DR GO; GO:0051402; P:neuron apoptotic process; ISO:MGI. DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IDA:MGI. DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISO:MGI. DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI. DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI. DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI. DR GO; GO:0031643; P:positive regulation of myelination; ISO:MGI. DR GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; ISO:MGI. DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI. DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI. DR GO; GO:0042488; P:positive regulation of odontogenesis of dentin-containing tooth; IMP:MGI. DR GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:MGI. DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:MGI. DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISO:MGI. DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; ISO:MGI. DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISO:MGI. DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IDA:SynGO. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:MGI. DR GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI. DR GO; GO:0043588; P:skin development; IMP:MGI. DR CDD; cd08311; Death_p75NR; 1. DR CDD; cd13416; TNFRSF16; 1. DR Gene3D; 6.10.250.1780; -; 1. DR Gene3D; 1.10.533.10; Death Domain, Fas; 1. DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 4. 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 PANTHER; PTHR46605; TUMOR NECROSIS FACTOR RECEPTOR; 1. DR PANTHER; PTHR46605:SF3; TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 16; 1. 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; DEATH domain; 1. DR SUPFAM; SSF57586; TNF receptor-like; 4. 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 Alternative splicing; 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..31 FT /evidence="ECO:0000255" FT CHAIN 32..427 FT /note="Tumor necrosis factor receptor superfamily member FT 16" FT /id="PRO_0000034592" FT TOPO_DOM 32..254 FT /note="Extracellular" FT /evidence="ECO:0000305" FT TRANSMEM 255..275 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 276..427 FT /note="Cytoplasmic" FT /evidence="ECO:0000305" FT REPEAT 34..67 FT /note="TNFR-Cys 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT REPEAT 69..110 FT /note="TNFR-Cys 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT REPEAT 111..149 FT /note="TNFR-Cys 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT REPEAT 151..191 FT /note="TNFR-Cys 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DOMAIN 356..421 FT /note="Death" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064" FT REGION 197..223 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 284..334 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 329..344 FT /note="Mediates interaction with KIDINS220" FT /evidence="ECO:0000250" FT COMPBIAS 204..218 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 308..334 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 314 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P08138" FT CARBOHYD 63 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 35..46 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 47..60 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 50..67 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 70..86 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 89..102 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 92..110 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 112..125 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 128..141 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 131..149 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 152..167 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 170..183 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT DISULFID 173..191 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206" FT CONFLICT 329 FT /note="G -> A (in Ref. 3; AAD17943)" SQ SEQUENCE 427 AA; 45647 MW; 7AC73263F7B31436 CRC64; MRRAGAACSA MDRLRLLLLL LLLLGVSFGG AKETCSTGMY THSGECCKAC NLGEGVAQPC GANQTVCEPC LDSVTFSDVV SATEPCKPCT ECLGLQSMSA PCVEADDAVC RCSYGYYQDE ETGRCEACSV CGVGSGLVFS CQDKQNTVCE ECPEGTYSDE ANHVDPCLPC TVCEDTERQL RECTPWADAE CEEIPGRWIT RSTPPEGSDV TTPSTQEPEA PPERDLIAST VADTVTTVMG SSQPVVTRGT ADNLIPVYCS ILAAVVVGLV AYIAFKRWNS CKQNKQGANS RPVNQTPPPE GEKLHSDSGI SVDSQSLHDQ QTHTQTASGQ ALKGDGNLYS SLPLTKREEV EKLLNGDTWR HLAGELGYQP EHIDSFTHEA CPVRALLASW GAQDSATLDA LLAALRRIQR ADIVESLCSE STATSPV //