TNR16_MOUSE
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 03-AUG-2022, entry version 172.
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: 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 ARNTL/BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus
CC (SCN) of the brain and in liver and of the genes involved in glucose
CC and 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};
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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 GlyGen; Q9Z0W1; 1 site.
DR iPTMnet; Q9Z0W1; -.
DR PhosphoSitePlus; Q9Z0W1; -.
DR jPOST; Q9Z0W1; -.
DR MaxQB; Q9Z0W1; -.
DR PaxDb; Q9Z0W1; -.
DR PeptideAtlas; Q9Z0W1; -.
DR PRIDE; Q9Z0W1; -.
DR ProteomicsDB; 260633; -. [Q9Z0W1-1]
DR ProteomicsDB; 341380; -.
DR Antibodypedia; 1461; 1617 antibodies from 50 providers.
DR DNASU; 18053; -.
DR Ensembl; ENSMUST00000000122; ENSMUSP00000000122; ENSMUSG00000000120. [Q9Z0W1-1]
DR GeneID; 18053; -.
DR KEGG; mmu:18053; -.
DR UCSC; uc007lam.2; mouse.
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; GECCMEC; -.
DR OrthoDB; 757160at2759; -.
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 77 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 222 other 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:0030135; C:coated 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:0005794; C:Golgi apparatus; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
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:0005634; C:nucleus; 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:0005791; C:rough endoplasmic reticulum; 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:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
DR GO; GO:0007411; P:axon guidance; IMP:MGI.
DR GO; GO:0001678; P:cellular glucose homeostasis; IMP:UniProtKB.
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: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:1901216; P:positive regulation of neuron death; 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 protein kinase B signaling; 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:0010941; P:regulation of cell death; ISO:MGI.
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:0009611; P:response to wounding; ISO:MGI.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:MGI.
DR GO; GO:0019233; P:sensory perception of pain; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
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; 2.
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 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
