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Tumor necrosis factor receptor superfamily member 16 (Gp80-LNGFR) (Low affinity neurotrophin receptor p75NTR) (Low-affinity nerve growth factor receptor) (NGF receptor) (p75 ICD) (CD antigen CD271)

 TNR16_RAT               Reviewed;         425 AA.
P07174;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-APR-1988, sequence version 1.
20-JUN-2018, entry version 175.
RecName: Full=Tumor necrosis factor receptor superfamily member 16;
AltName: Full=Gp80-LNGFR;
AltName: Full=Low affinity neurotrophin receptor p75NTR;
AltName: Full=Low-affinity nerve growth factor receptor;
Short=NGF receptor;
AltName: Full=p75 ICD;
AltName: CD_antigen=CD271;
Flags: Precursor;
Name=Ngfr; Synonyms=Tnfrsf16;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3027580; DOI=10.1038/325593a0;
Radeke M.J., Misko T.P., Hsu C., Herzenberg L.A., Shooter E.M.;
"Gene transfer and molecular cloning of the rat nerve growth factor
receptor.";
Nature 325:593-597(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
TISSUE=Liver;
PubMed=1446821; DOI=10.1016/0378-1119(92)90128-C;
Metsis M., Timmusk T., Allikmets R., Saarma M., Persson H.;
"Regulatory elements and transcriptional regulation by testosterone
and retinoic acid of the rat nerve growth factor receptor promoter.";
Gene 121:247-254(1992).
[3]
INTERACTION WITH NTRK2.
PubMed=9927421; DOI=10.1093/emboj/18.3.616;
Bibel M., Hoppe E., Barde Y.A.;
"Biochemical and functional interactions between the neurotrophin
receptors trk and p75NTR.";
EMBO J. 18:616-622(1999).
[4]
FUNCTION IN APOPTOSIS, AND INTERACTION WITH MAGED1.
STRAIN=Sprague-Dawley; TISSUE=Neural crest;
PubMed=10985348; DOI=10.1016/S0896-6273(00)00036-2;
Salehi A.H., Roux P.P., Kubu C.J., Zeindler C., Bhakar A.,
Tannis L.-L., Verdi J.M., Barker P.A.;
"NRAGE, a novel MAGE protein, interacts with the p75 neurotrophin
receptor and facilitates nerve growth factor dependent apoptosis.";
Neuron 27:279-288(2000).
[5]
INTERACTION WITH KIDINS220.
PubMed=11150334;
Kong H., Boulter J., Weber J.L., Lai C., Chao M.V.;
"An evolutionarily conserved transmembrane protein that is a novel
downstream target of neurotrophin and ephrin receptors.";
J. Neurosci. 21:176-185(2001).
[6]
INTERACTION WITH NRADD.
PubMed=12095158; DOI=10.1385/NMM:1:3:153;
Frankowski H., Castro-Obregon S., del Rio G., Rao R.V., Bredesen D.E.;
"PLAIDD, a type II death domain protein that interacts with p75
neurotrophin receptor.";
NeuroMolecular Med. 1:153-170(2002).
[7]
INTERACTION WITH NTRK1 AND KIDINS220, AND DOMAIN.
PubMed=15378608; DOI=10.1002/jnr.20262;
Chang M.-S., Arevalo J.C., Chao M.V.;
"Ternary complex with Trk, p75, and an ankyrin-rich membrane spanning
protein.";
J. Neurosci. Res. 78:186-192(2004).
[8]
INTERACTION WITH BEX1.
PubMed=16498402; DOI=10.1038/sj.emboj.7601017;
Vilar M., Murillo-Carretero M., Mira H., Magnusson K., Besset V.,
Ibanez C.F.;
"Bex1, a novel interactor of the p75 neurotrophin receptor, links
neurotrophin signaling to the cell cycle.";
EMBO J. 25:1219-1230(2006).
[9]
STRUCTURE BY NMR OF 334-418.
PubMed=9305641; DOI=10.1093/emboj/16.16.4999;
Liepinsh E., Ilag L.L., Otting G., Ibanez C.F.;
"NMR structure of the death domain of the p75 neurotrophin receptor.";
EMBO J. 16:4999-5005(1997).
-!- FUNCTION: Plays a role in the regulation of the translocation of
GLUT4 to the cell surface in adipocytes and skeletal muscle cells
in response to insulin, probably by regulating RAB31 activity, and
thereby contributes to the regulation of insulin-dependent glucose
uptake. Low affinity receptor which can bind to NGF, BDNF, NT-3,
and NT-4. Can mediate cell survival as well as cell death of
neural cells. Necessary for the circadian oscillation of the clock
genes ARNTL/BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic
nucleus (SCN) of the brain and in liver and of the genes involved
in glucose and lipid metabolism in the liver.
{ECO:0000269|PubMed:10985348}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with p75NTR-
associated cell death executor. Interacts with RTN4R (By
similarity). Interacts with TRAF2, TRAF4, TRAF6, PTPN13 and
RANBP9. Interacts through TRAF6 with SQSTM1 which bridges NGFR to
NTRK1. Interacts with BEX1 and BEX3. Interacts with KIDINS220 and
NTRK1. Can form a ternary complex with NTRK1 and KIDINS220 and
this complex is affected by the expression levels of KIDINS220. An
increase in KIDINS220 expression leads to a decreased association
of NGFR and NTRK1. Interacts (via death domain) with RAB31.
Interacts with NTRK2; may regulate the ligand specificity of the
NTRK2 receptor. Interacts with LINGO1 and NRADD. Interacts with
MAGED1; the interaction antagonizes the association NGFR:NTRK1.
{ECO:0000250|UniProtKB:Q9Z0W1, ECO:0000269|PubMed:10985348,
ECO:0000269|PubMed:11150334, ECO:0000269|PubMed:12095158,
ECO:0000269|PubMed:15378608, ECO:0000269|PubMed:16498402,
ECO:0000269|PubMed:9927421}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-1038810, EBI-1038810;
P05067:APP (xeno); NbExp=2; IntAct=EBI-1038810, EBI-2431589;
Q3MKQ2:Bex1; NbExp=4; IntAct=EBI-1038810, EBI-8089575;
P01138:NGF (xeno); NbExp=3; IntAct=EBI-1038810, EBI-1028250;
P20783:NTF3 (xeno); NbExp=4; IntAct=EBI-1038810, EBI-1025994;
P35739:Ntrk1; NbExp=2; IntAct=EBI-1038810, EBI-976667;
Q12933:TRAF2 (xeno); NbExp=3; IntAct=EBI-1038810, EBI-355744;
Q9BUZ4:TRAF4 (xeno); NbExp=3; IntAct=EBI-1038810, EBI-3650647;
Q9Y4K3:TRAF6 (xeno); NbExp=2; IntAct=EBI-1038810, EBI-359276;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- DOMAIN: Death domain is responsible for interaction with RANBP9.
{ECO:0000269|PubMed:15378608}.
-!- DOMAIN: The extracellular domain is responsible for interaction
with NTRK1. {ECO:0000269|PubMed:15378608}.
-!- PTM: N- and O-glycosylated.
-!- PTM: Phosphorylated on serine residues.
-----------------------------------------------------------------------
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EMBL; X05137; CAA28783.1; -; mRNA.
EMBL; X61269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A26431; A26431.
RefSeq; NP_036742.2; NM_012610.2.
UniGene; Rn.10980; -.
PDB; 1NGR; NMR; -; A=334-418.
PDB; 1SG1; X-ray; 2.40 A; X=30-190.
PDB; 2MIC; NMR; -; A/B=245-284.
PDB; 2MJO; NMR; -; A/B=245-284.
PDB; 3BUK; X-ray; 2.60 A; C/D=30-190.
PDB; 3IJ2; X-ray; 3.75 A; X/Y=30-190.
PDB; 4F42; X-ray; 2.38 A; A=334-418.
PDB; 4F44; X-ray; 2.40 A; A/B=334-418.
PDBsum; 1NGR; -.
PDBsum; 1SG1; -.
PDBsum; 2MIC; -.
PDBsum; 2MJO; -.
PDBsum; 3BUK; -.
PDBsum; 3IJ2; -.
PDBsum; 4F42; -.
PDBsum; 4F44; -.
ProteinModelPortal; P07174; -.
SMR; P07174; -.
BioGrid; 246737; 11.
DIP; DIP-5715N; -.
IntAct; P07174; 20.
MINT; P07174; -.
STRING; 10116.ENSRNOP00000007268; -.
iPTMnet; P07174; -.
PhosphoSitePlus; P07174; -.
SwissPalm; P07174; -.
PaxDb; P07174; -.
PRIDE; P07174; -.
GeneID; 24596; -.
KEGG; rno:24596; -.
UCSC; RGD:3177; rat.
CTD; 4804; -.
RGD; 3177; Ngfr.
eggNOG; ENOG410IQFC; Eukaryota.
eggNOG; ENOG4111F3C; LUCA.
HOGENOM; HOG000059587; -.
HOVERGEN; HBG060431; -.
InParanoid; P07174; -.
KO; K02583; -.
PhylomeDB; P07174; -.
EvolutionaryTrace; P07174; -.
PMAP-CutDB; P07174; -.
PRO; PR:P07174; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0045334; C:clathrin-coated endocytic vesicle; IDA:RGD.
GO; GO:0030135; C:coated vesicle; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0032590; C:dendrite membrane; IDA:RGD.
GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0032809; C:neuronal cell body membrane; IDA:RGD.
GO; GO:0005635; C:nuclear envelope; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0043204; C:perikaryon; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
GO; GO:0001540; F:amyloid-beta binding; IPI:RGD.
GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0048406; F:nerve growth factor binding; IDA:RGD.
GO; GO:0043121; F:neurotrophin binding; IPI:RGD.
GO; GO:0005168; F:neurotrophin TRKA receptor binding; IPI:RGD.
GO; GO:0070678; F:preprotein binding; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0017137; F:Rab GTPase binding; ISS:UniProtKB.
GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; IBA:GO_Central.
GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0007411; P:axon guidance; IBA:GO_Central.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:RGD.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
GO; GO:0016525; P:negative regulation of angiogenesis; IMP:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0061000; P:negative regulation of dendritic spine development; IMP:RGD.
GO; GO:0051902; P:negative regulation of mitochondrial depolarization; IMP:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
GO; GO:0010977; P:negative regulation of neuron projection development; IDA:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:RGD.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:RGD.
GO; GO:0031643; P:positive regulation of myelination; IMP:RGD.
GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:RGD.
GO; GO:1901216; P:positive regulation of neuron death; IDA:RGD.
GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:RGD.
GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IDA:RGD.
GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IMP:RGD.
GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; IMP:RGD.
GO; GO:0010941; P:regulation of cell death; IDA:RGD.
GO; GO:2001273; P:regulation of glucose import in response to insulin stimulus; ISS:UniProtKB.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0009611; P:response to wounding; IMP:RGD.
GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
GO; GO:0007165; P:signal transduction; IDA:RGD.
GO; GO:0035914; P:skeletal muscle cell differentiation; IEP:RGD.
CDD; cd13416; TNFRSF16; 1.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
InterPro; IPR022325; TNFR_16.
InterPro; IPR034046; TNFRSF16_N.
Pfam; PF00531; Death; 1.
Pfam; PF00020; TNFR_c6; 3.
PRINTS; PR01966; TNFACTORR16.
SMART; SM00005; DEATH; 1.
SMART; SM00208; TNFR; 4.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS00652; TNFR_NGFR_1; 3.
PROSITE; PS50050; TNFR_NGFR_2; 4.
1: Evidence at protein level;
3D-structure; Apoptosis; Biological rhythms; Complete proteome;
Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
Membrane; Neurogenesis; Phosphoprotein; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 29
CHAIN 30 425 Tumor necrosis factor receptor
superfamily member 16.
/FTId=PRO_0000034593.
TOPO_DOM 30 251 Extracellular. {ECO:0000255}.
TRANSMEM 252 273 Helical. {ECO:0000255}.
TOPO_DOM 274 425 Cytoplasmic. {ECO:0000255}.
REPEAT 32 65 TNFR-Cys 1.
REPEAT 67 108 TNFR-Cys 2.
REPEAT 109 147 TNFR-Cys 3.
REPEAT 149 189 TNFR-Cys 4.
DOMAIN 354 419 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
REGION 327 342 Mediates interaction with KIDINS220.
COMPBIAS 198 249 Ser/Thr-rich.
MOD_RES 312 312 Phosphoserine.
{ECO:0000250|UniProtKB:P08138}.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 33 44 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 45 58 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 48 65 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 68 84 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 87 100 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 90 108 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 110 123 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 126 139 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 129 147 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 150 165 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 168 181 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 171 189 {ECO:0000255|PROSITE-ProRule:PRU00206}.
STRAND 40 45 {ECO:0000244|PDB:3BUK}.
STRAND 52 56 {ECO:0000244|PDB:1SG1}.
STRAND 58 62 {ECO:0000244|PDB:1SG1}.
STRAND 64 67 {ECO:0000244|PDB:1SG1}.
TURN 70 72 {ECO:0000244|PDB:1SG1}.
STRAND 79 81 {ECO:0000244|PDB:1SG1}.
STRAND 94 98 {ECO:0000244|PDB:1SG1}.
STRAND 107 110 {ECO:0000244|PDB:1SG1}.
STRAND 114 116 {ECO:0000244|PDB:1SG1}.
TURN 118 120 {ECO:0000244|PDB:1SG1}.
STRAND 123 125 {ECO:0000244|PDB:1SG1}.
STRAND 133 137 {ECO:0000244|PDB:1SG1}.
STRAND 146 149 {ECO:0000244|PDB:1SG1}.
STRAND 160 162 {ECO:0000244|PDB:1SG1}.
TURN 246 249 {ECO:0000244|PDB:2MIC}.
STRAND 250 253 {ECO:0000244|PDB:2MIC}.
HELIX 255 275 {ECO:0000244|PDB:2MIC}.
TURN 276 278 {ECO:0000244|PDB:2MIC}.
HELIX 337 339 {ECO:0000244|PDB:4F42}.
HELIX 342 351 {ECO:0000244|PDB:4F42}.
TURN 352 355 {ECO:0000244|PDB:4F42}.
HELIX 356 364 {ECO:0000244|PDB:4F42}.
HELIX 368 373 {ECO:0000244|PDB:4F42}.
HELIX 374 376 {ECO:0000244|PDB:4F42}.
STRAND 377 379 {ECO:0000244|PDB:4F42}.
HELIX 380 388 {ECO:0000244|PDB:4F42}.
STRAND 391 393 {ECO:0000244|PDB:4F44}.
HELIX 396 405 {ECO:0000244|PDB:4F42}.
HELIX 409 416 {ECO:0000244|PDB:4F42}.
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


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