TNR16_HUMAN
ID TNR16_HUMAN Reviewed; 427 AA.
AC P08138; B2R961; B4E096;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 224.
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 {ECO:0000303|PubMed:3022937};
DE AltName: Full=p75 ICD;
DE AltName: CD_antigen=CD271;
DE Flags: Precursor;
GN Name=NGFR; Synonyms=TNFRSF16;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=3022937; DOI=10.1016/0092-8674(86)90619-7;
RA Johnson D., Lanahan A., Buck C.R., Sehgal A., Morgan C., Mercer E.,
RA Bothwell M., Chao M.;
RT "Expression and structure of the human NGF receptor.";
RL Cell 47:545-554(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX PubMed=2850481; DOI=10.1128/mcb.8.8.3160-3167.1988;
RA Sehgal A., Patil N., Chao M.;
RT "A constitutive promoter directs expression of the nerve growth factor
RT receptor gene.";
RL Mol. Cell. Biol. 8:3160-3167(1988).
RN [7]
RP 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 [8]
RP INTERACTION WITH TRAF6.
RX PubMed=9915784; DOI=10.1074/jbc.274.5.2597;
RA Khursigara G., Orlinick J.R., Chao M.V.;
RT "Association of the p75 neurotrophin receptor with TRAF6.";
RL J. Biol. Chem. 274:2597-2600(1999).
RN [9]
RP INTERACTION WITH PTPN13.
RX PubMed=10544233; DOI=10.1016/s0014-5793(99)01324-1;
RA Irie S., Hachiya T., Rabizadeh S., Maruyama W., Mukai J., Li Y., Reed J.C.,
RA Bredesen D.E., Sato T.A.;
RT "Functional interaction of Fas-associated phosphatase-1 (FAP-1) with
RT p75(NTR) and their effect on NF-kappaB activation.";
RL FEBS Lett. 460:191-198(1999).
RN [10]
RP INTERACTION WITH TRAF6 AND SQSTM1.
RX PubMed=11244088; DOI=10.1074/jbc.c000869200;
RA Wooten M.W., Seibenhener M.L., Mamidipudi V., Diaz-Meco M.T., Barker P.A.,
RA Moscat J.;
RT "The atypical protein kinase C-interacting protein p62 is a scaffold for
RT NF-kappaB activation by nerve growth factor.";
RL J. Biol. Chem. 276:7709-7712(2001).
RN [11]
RP INTERACTION WITH RANBP9.
RC TISSUE=Brain;
RX PubMed=12963025; DOI=10.1016/j.bbrc.2003.08.033;
RA Bai D., Chen H., Huang B.-R.;
RT "RanBPM is a novel binding protein for p75NTR.";
RL Biochem. Biophys. Res. Commun. 309:552-557(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH LINGO1.
RX PubMed=14966521; DOI=10.1038/nn1188;
RA Mi S., Lee X., Shao Z., Thill G., Ji B., Relton J., Levesque M.,
RA Allaire N., Perrin S., Sands B., Crowell T., Cate R.L., McCoy J.M.,
RA Pepinsky R.B.;
RT "LINGO-1 is a component of the Nogo-66 receptor/p75 signaling complex.";
RL Nat. Neurosci. 7:221-228(2004).
RN [13]
RP STRUCTURE OF O-LINKED CARBOHYDRATE.
RX PubMed=8627329; DOI=10.1046/j.1471-4159.1996.66041707.x;
RA Chapman B.S., Eckart M.R., Kaufman S.E., Lapointe G.R.;
RT "O-linked oligosaccharide on the 75-kDa neurotrophin receptor.";
RL J. Neurochem. 66:1707-1716(1996).
RN [14]
RP INTERACTION WITH RTN4R.
RX PubMed=19052207; DOI=10.1523/jneurosci.3828-08.2008;
RA Budel S., Padukkavidana T., Liu B.P., Feng Z., Hu F., Johnson S.,
RA Lauren J., Park J.H., McGee A.W., Liao J., Stillman A., Kim J.E.,
RA Yang B.Z., Sodi S., Gelernter J., Zhao H., Hisama F., Arnsten A.F.,
RA Strittmatter S.M.;
RT "Genetic variants of Nogo-66 receptor with possible association to
RT schizophrenia block myelin inhibition of axon growth.";
RL J. Neurosci. 28:13161-13172(2008).
RN [15]
RP INTERACTION WITH SORCS2 AND TRIO.
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 [16]
RP FUNCTION.
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP INTERACTION WITH SORCS2, AND FUNCTION.
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 [19] {ECO:0007744|PDB:2N80, ECO:0007744|PDB:2N83, ECO:0007744|PDB:2N97}
RP STRUCTURE BY NMR OF 330-427 IN COMPLEXES WITH RIPK2 AND ARHGDIA, FUNCTION,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF LYS-343; ASP-412 AND GLU-420.
RX PubMed=26646181; DOI=10.7554/elife.11692;
RA Lin Z., Tann J.Y., Goh E.T., Kelly C., Lim K.B., Gao J.F., Ibanez C.F.;
RT "Structural basis of death domain signaling in the p75 neurotrophin
RT receptor.";
RL Elife 4:e11692-e11692(2015).
CC -!- FUNCTION: Low affinity receptor which can bind to NGF, BDNF, NTF3, and
CC NTF4. Forms a heterodimeric receptor with SORCS2 that binds the
CC precursor forms of NGF, BDNF and NTF3 with high affinity, and has much
CC lower affinity for mature NGF and BDNF (PubMed:24908487). Plays an
CC important role in differentiation and survival of specific neuronal
CC populations during development (By similarity). Can mediate cell
CC survival as well as cell death of neural cells. Plays a role in the
CC inactivation of RHOA (PubMed:26646181). Plays a role in the regulation
CC of the translocation of GLUT4 to the cell surface in adipocytes and
CC skeletal muscle cells in response to insulin, probably by regulating
CC RAB31 activity, and thereby contributes to the regulation of insulin-
CC dependent glucose uptake (By similarity). Necessary for the circadian
CC oscillation of the clock genes ARNTL/BMAL1, PER1, PER2 and NR1D1 in the
CC suprachiasmatic nucleus (SCmgetaN) of the brain and in liver and of the
CC genes involved in glucose and lipid metabolism in the liver
CC (PubMed:23785138). {ECO:0000250, ECO:0000250|UniProtKB:Q9Z0W1,
CC ECO:0000269|PubMed:14966521, ECO:0000269|PubMed:23785138,
CC ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:26646181,
CC ECO:0000269|PubMed:3022937}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Heterodimer with
CC SORCS2. The extracellular domains of the heterodimer bind NGF
CC (PubMed:22155786, PubMed:24908487). The cytoplasmic region of the
CC heterodimer binds TRIO. NGF binding mediates dissociation of TRIO from
CC the receptor complex (PubMed:22155786). Interacts with RTN4R
CC (PubMed:19052207). Interacts with TRAF2, TRAF4, TRAF6, PTPN13 and
CC RANBP9 (PubMed:10514511, PubMed:9915784, PubMed:10544233,
CC PubMed:12963025). Interacts through TRAF6 with SQSTM1 which bridges
CC NGFR to NTRK1 (PubMed:11244088). Interacts with BEX1 (By similarity).
CC Interacts with BEX3 (By similarity). Interacts with KIDINS220 and
CC NTRK1. Can form a ternary complex with NTRK1 and KIDINS220 and this
CC complex is affected by the expression levels of KIDINS220. An increase
CC in KIDINS220 expression leads to a decreased association of NGFR and
CC NTRK1. Interacts with NTRK2; may regulate the ligand specificity of the
CC NTRK2 receptor (By similarity). Interacts (via death domain) with RAB31
CC (By similarity). Interacts with LINGO1 (PubMed:14966521). Interacts
CC with NRADD (By similarity). Interacts with MAGED1; the interaction
CC antagonizes the association NGFR:NTRK1 (By similarity). Interacts (via
CC death domain) with ARHGDIA and RIPK2 (PubMed:26646181).
CC {ECO:0000250|UniProtKB:P07174, ECO:0000250|UniProtKB:Q9Z0W1,
CC ECO:0000269|PubMed:10514511, ECO:0000269|PubMed:10544233,
CC ECO:0000269|PubMed:11244088, ECO:0000269|PubMed:12963025,
CC ECO:0000269|PubMed:14966521, ECO:0000269|PubMed:19052207,
CC ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:24908487,
CC ECO:0000269|PubMed:26646181, ECO:0000269|PubMed:9915784}.
CC -!- INTERACTION:
CC P08138; P05067: APP; NbExp=2; IntAct=EBI-1387782, EBI-77613;
CC P08138; PRO_0000000093 [P05067]: APP; NbExp=2; IntAct=EBI-1387782, EBI-2431589;
CC P08138; P33681: CD80; NbExp=3; IntAct=EBI-1387782, EBI-1031024;
CC P08138; Q96FE5: LINGO1; NbExp=2; IntAct=EBI-1387782, EBI-719955;
CC P08138; P01138: NGF; NbExp=2; IntAct=EBI-1387782, EBI-1028250;
CC P08138; PRO_0000019600 [P01138]: NGF; NbExp=2; IntAct=EBI-1387782, EBI-9249861;
CC P08138; Q9Y467: SALL2; NbExp=3; IntAct=EBI-1387782, EBI-746180;
CC P08138; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1387782, EBI-5235340;
CC P08138; Q9UNE7: STUB1; NbExp=3; IntAct=EBI-1387782, EBI-357085;
CC P08138; O75509: TNFRSF21; NbExp=4; IntAct=EBI-1387782, EBI-2313231;
CC P08138; P25233: Ndn; Xeno; NbExp=3; IntAct=EBI-1387782, EBI-1801080;
CC P08138; Q9CPR8: Nsmce3; Xeno; NbExp=3; IntAct=EBI-1387782, EBI-5529102;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:3022937};
CC Single-pass type I membrane protein {ECO:0000305}. Perikaryon
CC {ECO:0000250|UniProtKB:Q9Z0W1}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:Q9Z0W1}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q9Z0W1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P08138-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P08138-2; Sequence=VSP_056850;
CC -!- DOMAIN: The death domain mediates interaction with RANBP9 (By
CC similarity). It also mediates interaction with ARHGDIA and RIPK2
CC (PubMed:26646181). {ECO:0000250|UniProtKB:P07174,
CC ECO:0000269|PubMed:26646181}.
CC -!- DOMAIN: The extracellular domain is responsible for interaction with
CC NTRK1. {ECO:0000250}.
CC -!- PTM: N- and O-glycosylated.
CC -!- PTM: O-linked glycans consist of Gal(1-3)GalNAc core elongated by 1 or
CC 2 NeuNAc.
CC -!- PTM: Phosphorylated on serine residues.
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DR EMBL; M14764; AAB59544.1; -; mRNA.
DR EMBL; AK303278; BAG64358.1; -; mRNA.
DR EMBL; AK313654; BAG36408.1; -; mRNA.
DR EMBL; AC006487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC015656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94677.1; -; Genomic_DNA.
DR EMBL; BC050309; AAH50309.1; -; mRNA.
DR EMBL; M21621; AAA36363.1; -; Genomic_DNA.
DR CCDS; CCDS11549.1; -. [P08138-1]
DR PIR; A25218; GQHUN.
DR RefSeq; NP_002498.1; NM_002507.3. [P08138-1]
DR PDB; 2N80; NMR; -; A=334-427.
DR PDB; 2N83; NMR; -; A=330-427.
DR PDB; 2N97; NMR; -; A/B=330-427.
DR PDB; 3EWV; X-ray; 2.60 A; E=396-412.
DR PDB; 5ZGG; NMR; -; A/B=244-277.
DR PDB; 7CSQ; NMR; -; A=330-427.
DR PDBsum; 2N80; -.
DR PDBsum; 2N83; -.
DR PDBsum; 2N97; -.
DR PDBsum; 3EWV; -.
DR PDBsum; 5ZGG; -.
DR PDBsum; 7CSQ; -.
DR AlphaFoldDB; P08138; -.
DR BMRB; P08138; -.
DR SMR; P08138; -.
DR BioGRID; 110870; 58.
DR CORUM; P08138; -.
DR DIP; DIP-406N; -.
DR IntAct; P08138; 25.
DR MINT; P08138; -.
DR STRING; 9606.ENSP00000172229; -.
DR BindingDB; P08138; -.
DR ChEMBL; CHEMBL4762; -.
DR DrugCentral; P08138; -.
DR GuidetoPHARMACOLOGY; 1888; -.
DR TCDB; 9.B.87.4.1; the selenoprotein p receptor (selp-receptor) family.
DR GlyConnect; 611; 3 N-Linked glycans (1 site), 2 O-Linked glycans.
DR GlyGen; P08138; 2 sites, 6 N-linked glycans (1 site), 4 O-linked glycans (1 site).
DR iPTMnet; P08138; -.
DR PhosphoSitePlus; P08138; -.
DR BioMuta; NGFR; -.
DR DMDM; 128156; -.
DR EPD; P08138; -.
DR jPOST; P08138; -.
DR MassIVE; P08138; -.
DR MaxQB; P08138; -.
DR PaxDb; P08138; -.
DR PeptideAtlas; P08138; -.
DR PRIDE; P08138; -.
DR ProteomicsDB; 52073; -. [P08138-1]
DR ProteomicsDB; 5660; -.
DR Antibodypedia; 1461; 1617 antibodies from 50 providers.
DR DNASU; 4804; -.
DR Ensembl; ENST00000172229.8; ENSP00000172229.3; ENSG00000064300.9. [P08138-1]
DR Ensembl; ENST00000504201.1; ENSP00000421731.1; ENSG00000064300.9. [P08138-2]
DR GeneID; 4804; -.
DR KEGG; hsa:4804; -.
DR MANE-Select; ENST00000172229.8; ENSP00000172229.3; NM_002507.4; NP_002498.1.
DR UCSC; uc002ioz.5; human. [P08138-1]
DR CTD; 4804; -.
DR DisGeNET; 4804; -.
DR GeneCards; NGFR; -.
DR HGNC; HGNC:7809; NGFR.
DR HPA; ENSG00000064300; Low tissue specificity.
DR MIM; 162010; gene.
DR neXtProt; NX_P08138; -.
DR OpenTargets; ENSG00000064300; -.
DR PharmGKB; PA31615; -.
DR VEuPathDB; HostDB:ENSG00000064300; -.
DR eggNOG; ENOG502QWPN; Eukaryota.
DR GeneTree; ENSGT00730000110974; -.
DR HOGENOM; CLU_052667_0_1_1; -.
DR InParanoid; P08138; -.
DR OMA; GECCMEC; -.
DR OrthoDB; 757160at2759; -.
DR PhylomeDB; P08138; -.
DR TreeFam; TF106466; -.
DR PathwayCommons; P08138; -.
DR Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-193670; p75NTR negatively regulates cell cycle via SC1.
DR Reactome; R-HSA-193681; Ceramide signalling.
DR Reactome; R-HSA-193692; Regulated proteolysis of p75NTR.
DR Reactome; R-HSA-205017; NFG and proNGF binds to p75NTR.
DR Reactome; R-HSA-205025; NADE modulates death signalling.
DR Reactome; R-HSA-205043; NRIF signals cell death from the nucleus.
DR Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
DR Reactome; R-HSA-209560; NF-kB is activated and signals survival.
DR Reactome; R-HSA-209563; Axonal growth stimulation.
DR SignaLink; P08138; -.
DR SIGNOR; P08138; -.
DR BioGRID-ORCS; 4804; 13 hits in 1073 CRISPR screens.
DR ChiTaRS; NGFR; human.
DR EvolutionaryTrace; P08138; -.
DR GeneWiki; Low-affinity_nerve_growth_factor_receptor; -.
DR GenomeRNAi; 4804; -.
DR Pharos; P08138; Tclin.
DR PRO; PR:P08138; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P08138; protein.
DR Bgee; ENSG00000064300; Expressed in tibial nerve and 119 other tissues.
DR Genevisible; P08138; HS.
DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; NAS:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0001540; F:amyloid-beta binding; TAS:ARUK-UCL.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0015026; F:coreceptor activity; IDA:UniProtKB.
DR GO; GO:0005035; F:death receptor activity; IGI:ARUK-UCL.
DR GO; GO:0048406; F:nerve growth factor binding; ISS:UniProtKB.
DR GO; GO:0043121; F:neurotrophin binding; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; IEA:Ensembl.
DR GO; GO:0001678; P:cellular glucose homeostasis; ISS:UniProtKB.
DR GO; GO:1904646; P:cellular response to amyloid-beta; IDA:ARUK-UCL.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0016048; P:detection of temperature stimulus; IEA:Ensembl.
DR GO; GO:0035907; P:dorsal aorta development; IEA:Ensembl.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0031069; P:hair follicle morphogenesis; IEA:Ensembl.
DR GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
DR GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IGI:BHF-UCL.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:ARUK-UCL.
DR GO; GO:0040037; P:negative regulation of fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051799; P:negative regulation of hair follicle development; IEA:Ensembl.
DR GO; GO:0021675; P:nerve development; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IGI:ARUK-UCL.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:2001235; P:positive regulation of apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0042488; P:positive regulation of odontogenesis of dentin-containing tooth; IEA:Ensembl.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:BHF-UCL.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
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 3D-structure; Alternative splicing; Apoptosis; Biological rhythms;
KW Cell membrane; Cell projection; Developmental protein; Differentiation;
KW Disulfide bond; Glycoprotein; Membrane; Neurogenesis; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Synapse; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..28
FT CHAIN 29..427
FT /note="Tumor necrosis factor receptor superfamily member
FT 16"
FT /id="PRO_0000034591"
FT TOPO_DOM 29..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 31..64
FT /note="TNFR-Cys 1"
FT REPEAT 66..107
FT /note="TNFR-Cys 2"
FT REPEAT 108..146
FT /note="TNFR-Cys 3"
FT REPEAT 148..188
FT /note="TNFR-Cys 4"
FT DOMAIN 344..421
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 194..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 281..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..341
FT /note="Mediates interaction with KIDINS220"
FT /evidence="ECO:0000250"
FT COMPBIAS 200..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..328
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT /id="CAR_000231"
FT DISULFID 32..43
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 44..57
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 47..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 67..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 86..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 89..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 109..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 125..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 128..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 149..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 167..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 170..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT VAR_SEQ 1..94
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056850"
FT VARIANT 205
FT /note="S -> L (in dbSNP:rs2072446)"
FT /id="VAR_020010"
FT MUTAGEN 343
FT /note="K->A: Decreased interaction with ARHGDIA."
FT /evidence="ECO:0000269|PubMed:26646181"
FT MUTAGEN 412
FT /note="D->A: Decreased interaction with ARHGDIA."
FT /evidence="ECO:0000269|PubMed:26646181"
FT MUTAGEN 420
FT /note="E->A: Decreased interaction with ARHGDIA."
FT /evidence="ECO:0000269|PubMed:26646181"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:5ZGG"
FT HELIX 252..276
FT /evidence="ECO:0007829|PDB:5ZGG"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:2N80"
FT HELIX 341..351
FT /evidence="ECO:0007829|PDB:2N80"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:7CSQ"
FT HELIX 358..366
FT /evidence="ECO:0007829|PDB:2N80"
FT HELIX 370..377
FT /evidence="ECO:0007829|PDB:2N80"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2N80"
FT HELIX 382..390
FT /evidence="ECO:0007829|PDB:2N80"
FT HELIX 398..409
FT /evidence="ECO:0007829|PDB:3EWV"
FT HELIX 411..417
FT /evidence="ECO:0007829|PDB:2N80"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:2N80"
FT STRAND 421..423
FT /evidence="ECO:0007829|PDB:2N80"
SQ SEQUENCE 427 AA; 45183 MW; B09FA143FB3D625B CRC64;
MGAGATGRAM DGPRLLLLLL LGVSLGGAKE ACPTGLYTHS GECCKACNLG EGVAQPCGAN
QTVCEPCLDS VTFSDVVSAT EPCKPCTECV GLQSMSAPCV EADDAVCRCA YGYYQDETTG
RCEACRVCEA GSGLVFSCQD KQNTVCEECP DGTYSDEANH VDPCLPCTVC EDTERQLREC
TRWADAECEE IPGRWITRST PPEGSDSTAP STQEPEAPPE QDLIASTVAG VVTTVMGSSQ
PVVTRGTTDN LIPVYCSILA AVVVGLVAYI AFKRWNSCKQ NKQGANSRPV NQTPPPEGEK
LHSDSGISVD SQSLHDQQPH TQTASGQALK GDGGLYSSLP PAKREEVEKL LNGSAGDTWR
HLAGELGYQP EHIDSFTHEA CPVRALLASW ATQDSATLDA LLAALRRIQR ADLVESLCSE
STATSPV
