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Protein

Tumor necrosis factor receptor superfamily member 16

Gene

Ngfr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  • beta-amyloid binding Source: RGD
  • nerve growth factor binding Source: RGD
  • neurotrophin binding Source: RGD
  • neurotrophin TRKA receptor binding Source: RGD
  • preprotein binding Source: RGD
  • protein homodimerization activity Source: RGD
  • Rab GTPase binding Source: UniProtKB
  • tumor necrosis factor-activated receptor activity Source: GO_Central

GO - Biological processi

  • apoptotic signaling pathway Source: GO_Central
  • axon guidance Source: GO_Central
  • cellular response to oxidative stress Source: RGD
  • circadian regulation of gene expression Source: UniProtKB
  • glucose homeostasis Source: UniProtKB
  • immune response Source: GO_Central
  • inflammatory response Source: GO_Central
  • intracellular protein transport Source: UniProtKB
  • negative regulation of angiogenesis Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of cell cycle Source: Reactome
  • negative regulation of dendritic spine development Source: RGD
  • negative regulation of mitochondrial depolarization Source: RGD
  • negative regulation of neuron apoptotic process Source: RGD
  • negative regulation of neuron projection development Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of excitatory postsynaptic potential Source: RGD
  • positive regulation of MAPK cascade Source: RGD
  • positive regulation of myelination Source: RGD
  • positive regulation of neural precursor cell proliferation Source: RGD
  • positive regulation of neuron death Source: RGD
  • positive regulation of neuron differentiation Source: RGD
  • positive regulation of neuron projection development Source: RGD
  • positive regulation of protein kinase B signaling Source: RGD
  • positive regulation of Rho protein signal transduction Source: RGD
  • positive regulation of synaptic transmission, cholinergic Source: RGD
  • positive regulation of synaptic transmission, glutamatergic Source: RGD
  • regulation of cell death Source: RGD
  • regulation of glucose import in response to insulin stimulus Source: UniProtKB
  • regulation of reactive oxygen species metabolic process Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to wounding Source: RGD
  • sensory perception of pain Source: RGD
  • signal transduction Source: RGD
  • skeletal muscle cell differentiation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Receptor

Keywords - Biological processi

Apoptosis, Biological rhythms, Differentiation, Neurogenesis

Enzyme and pathway databases

ReactomeiR-RNO-193648. NRAGE signals death through JNK.
R-RNO-193670. p75NTR negatively regulates cell cycle via SC1.
R-RNO-193681. Ceramide signalling.
R-RNO-209543. p75NTR recruits signalling complexes.

Names & Taxonomyi

Protein namesi
Recommended name:
Tumor necrosis factor receptor superfamily member 16
Alternative name(s):
Gp80-LNGFR
Low affinity neurotrophin receptor p75NTR
Low-affinity nerve growth factor receptor
Short name:
NGF receptor
p75 ICD
CD_antigen: CD271
Gene namesi
Name:Ngfr
Synonyms:Tnfrsf16
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3177. Ngfr.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 251222ExtracellularSequence analysisAdd
BLAST
Transmembranei252 – 27322HelicalSequence analysisAdd
BLAST
Topological domaini274 – 425152CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • clathrin-coated endocytic vesicle Source: RGD
  • coated vesicle Source: RGD
  • cytoplasm Source: RGD
  • dendrite membrane Source: RGD
  • external side of plasma membrane Source: RGD
  • Golgi apparatus Source: RGD
  • integral component of plasma membrane Source: GO_Central
  • membrane raft Source: RGD
  • mitochondrion Source: RGD
  • neuronal cell body membrane Source: RGD
  • nuclear envelope Source: RGD
  • nucleus Source: RGD
  • perikaryon Source: RGD
  • plasma membrane Source: RGD
  • rough endoplasmic reticulum Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Add
BLAST
Chaini30 – 425396Tumor necrosis factor receptor superfamily member 16PRO_0000034593Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 44PROSITE-ProRule annotation
Disulfide bondi45 ↔ 58PROSITE-ProRule annotation
Disulfide bondi48 ↔ 65PROSITE-ProRule annotation
Glycosylationi61 – 611N-linked (GlcNAc...)Sequence analysis
Disulfide bondi68 ↔ 84PROSITE-ProRule annotation
Glycosylationi71 – 711N-linked (GlcNAc...)Sequence analysis
Disulfide bondi87 ↔ 100PROSITE-ProRule annotation
Disulfide bondi90 ↔ 108PROSITE-ProRule annotation
Disulfide bondi110 ↔ 123PROSITE-ProRule annotation
Disulfide bondi126 ↔ 139PROSITE-ProRule annotation
Disulfide bondi129 ↔ 147PROSITE-ProRule annotation
Disulfide bondi150 ↔ 165PROSITE-ProRule annotation
Disulfide bondi168 ↔ 181PROSITE-ProRule annotation
Disulfide bondi171 ↔ 189PROSITE-ProRule annotation
Modified residuei312 – 3121PhosphoserineBy similarity

Post-translational modificationi

N- and O-glycosylated.
Phosphorylated on serine residues.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP07174.
PRIDEiP07174.

PTM databases

iPTMnetiP07174.
PhosphoSiteiP07174.
SwissPalmiP07174.

Miscellaneous databases

PMAP-CutDBP07174.

Interactioni

Subunit structurei

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.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPP050672EBI-1038810,EBI-2431589From a different organism.
Bex1Q3MKQ24EBI-1038810,EBI-8089575
NGFP011382EBI-1038810,EBI-1028250From a different organism.
TRAF2Q129333EBI-1038810,EBI-355744From a different organism.
TRAF4Q9BUZ43EBI-1038810,EBI-3650647From a different organism.
TRAF6Q9Y4K32EBI-1038810,EBI-359276From a different organism.

GO - Molecular functioni

  • nerve growth factor binding Source: RGD
  • neurotrophin binding Source: RGD
  • neurotrophin TRKA receptor binding Source: RGD
  • preprotein binding Source: RGD
  • protein homodimerization activity Source: RGD
  • Rab GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi246737. 11 interactions.
DIPiDIP-5715N.
IntActiP07174. 15 interactions.
MINTiMINT-128759.
STRINGi10116.ENSRNOP00000007268.

Structurei

Secondary structure

1
425
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi40 – 456Combined sources
Beta strandi52 – 565Combined sources
Beta strandi58 – 625Combined sources
Beta strandi64 – 674Combined sources
Turni70 – 723Combined sources
Beta strandi79 – 813Combined sources
Beta strandi94 – 985Combined sources
Beta strandi107 – 1104Combined sources
Beta strandi114 – 1163Combined sources
Turni118 – 1203Combined sources
Beta strandi123 – 1253Combined sources
Beta strandi133 – 1375Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi160 – 1623Combined sources
Turni246 – 2494Combined sources
Beta strandi250 – 2534Combined sources
Helixi255 – 27521Combined sources
Turni276 – 2783Combined sources
Helixi337 – 3393Combined sources
Helixi342 – 35110Combined sources
Turni352 – 3554Combined sources
Helixi356 – 3649Combined sources
Helixi368 – 3736Combined sources
Helixi374 – 3763Combined sources
Beta strandi377 – 3793Combined sources
Helixi380 – 3889Combined sources
Beta strandi391 – 3933Combined sources
Helixi396 – 40510Combined sources
Helixi409 – 4168Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NGRNMR-A334-418[»]
1SG1X-ray2.40X30-190[»]
2MICNMR-A/B245-284[»]
2MJONMR-A/B245-284[»]
3BUKX-ray2.60C/D30-190[»]
3IJ2X-ray3.75X/Y30-190[»]
4F42X-ray2.38A334-418[»]
4F44X-ray2.40A/B334-418[»]
ProteinModelPortaliP07174.
SMRiP07174. Positions 31-190, 334-418.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07174.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati32 – 6534TNFR-Cys 1Add
BLAST
Repeati67 – 10842TNFR-Cys 2Add
BLAST
Repeati109 – 14739TNFR-Cys 3Add
BLAST
Repeati149 – 18941TNFR-Cys 4Add
BLAST
Domaini354 – 41966DeathPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni327 – 34216Mediates interaction with KIDINS220Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi198 – 24952Ser/Thr-richAdd
BLAST

Domaini

Death domain is responsible for interaction with RANBP9.1 Publication
The extracellular domain is responsible for interaction with NTRK1.1 Publication

Sequence similaritiesi

Contains 1 death domain.PROSITE-ProRule annotation
Contains 4 TNFR-Cys repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IQFC. Eukaryota.
ENOG4111F3C. LUCA.
HOGENOMiHOG000059587.
HOVERGENiHBG060431.
InParanoidiP07174.
KOiK02583.
PhylomeDBiP07174.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022325. TNFR_16.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00020. TNFR_c6. 3 hits.
[Graphical view]
PRINTSiPR01966. TNFACTORR16.
SMARTiSM00005. DEATH. 1 hit.
SM00208. TNFR. 4 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 3 hits.
PS50050. TNFR_NGFR_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07174-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRAGAACSA MDRLRLLLLL ILGVSSGGAK ETCSTGLYTH SGECCKACNL
60 70 80 90 100
GEGVAQPCGA NQTVCEPCLD NVTFSDVVSA TEPCKPCTEC LGLQSMSAPC
110 120 130 140 150
VEADDAVCRC AYGYYQDEET GHCEACSVCE VGSGLVFSCQ DKQNTVCEEC
160 170 180 190 200
PEGTYSDEAN HVDPCLPCTV CEDTERQLRE CTPWADAECE EIPGRWIPRS
210 220 230 240 250
TPPEGSDSTA PSTQEPEVPP EQDLVPSTVA DMVTTVMGSS QPVVTRGTTD
260 270 280 290 300
NLIPVYCSIL AAVVVGLVAY IAFKRWNSCK QNKQGANSRP VNQTPPPEGE
310 320 330 340 350
KLHSDSGISV DSQSLHDQQT HTQTASGQAL KGDGNLYSSL PLTKREEVEK
360 370 380 390 400
LLNGDTWRHL AGELGYQPEH IDSFTHEACP VRALLASWGA QDSATLDALL
410 420
AALRRIQRAD IVESLCSEST ATSPV
Length:425
Mass (Da):45,433
Last modified:April 1, 1988 - v1
Checksum:iB2E152D94D3827F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05137 mRNA. Translation: CAA28783.1.
X61269 Genomic DNA. No translation available.
PIRiA26431.
RefSeqiNP_036742.2. NM_012610.2.
UniGeneiRn.10980.

Genome annotation databases

GeneIDi24596.
KEGGirno:24596.
UCSCiRGD:3177. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05137 mRNA. Translation: CAA28783.1.
X61269 Genomic DNA. No translation available.
PIRiA26431.
RefSeqiNP_036742.2. NM_012610.2.
UniGeneiRn.10980.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NGRNMR-A334-418[»]
1SG1X-ray2.40X30-190[»]
2MICNMR-A/B245-284[»]
2MJONMR-A/B245-284[»]
3BUKX-ray2.60C/D30-190[»]
3IJ2X-ray3.75X/Y30-190[»]
4F42X-ray2.38A334-418[»]
4F44X-ray2.40A/B334-418[»]
ProteinModelPortaliP07174.
SMRiP07174. Positions 31-190, 334-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246737. 11 interactions.
DIPiDIP-5715N.
IntActiP07174. 15 interactions.
MINTiMINT-128759.
STRINGi10116.ENSRNOP00000007268.

PTM databases

iPTMnetiP07174.
PhosphoSiteiP07174.
SwissPalmiP07174.

Proteomic databases

PaxDbiP07174.
PRIDEiP07174.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24596.
KEGGirno:24596.
UCSCiRGD:3177. rat.

Organism-specific databases

CTDi4804.
RGDi3177. Ngfr.

Phylogenomic databases

eggNOGiENOG410IQFC. Eukaryota.
ENOG4111F3C. LUCA.
HOGENOMiHOG000059587.
HOVERGENiHBG060431.
InParanoidiP07174.
KOiK02583.
PhylomeDBiP07174.

Enzyme and pathway databases

ReactomeiR-RNO-193648. NRAGE signals death through JNK.
R-RNO-193670. p75NTR negatively regulates cell cycle via SC1.
R-RNO-193681. Ceramide signalling.
R-RNO-209543. p75NTR recruits signalling complexes.

Miscellaneous databases

EvolutionaryTraceiP07174.
PMAP-CutDBP07174.
PROiP07174.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022325. TNFR_16.
[Graphical view]
PfamiPF00531. Death. 1 hit.
PF00020. TNFR_c6. 3 hits.
[Graphical view]
PRINTSiPR01966. TNFACTORR16.
SMARTiSM00005. DEATH. 1 hit.
SM00208. TNFR. 4 hits.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 3 hits.
PS50050. TNFR_NGFR_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Gene transfer and molecular cloning of the rat nerve growth factor receptor."
    Radeke M.J., Misko T.P., Hsu C., Herzenberg L.A., Shooter E.M.
    Nature 325:593-597(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Regulatory elements and transcriptional regulation by testosterone and retinoic acid of the rat nerve growth factor receptor promoter."
    Metsis M., Timmusk T., Allikmets R., Saarma M., Persson H.
    Gene 121:247-254(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
    Tissue: Liver.
  3. "Biochemical and functional interactions between the neurotrophin receptors trk and p75NTR."
    Bibel M., Hoppe E., Barde Y.A.
    EMBO J. 18:616-622(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NTRK2.
  4. "NRAGE, a novel MAGE protein, interacts with the p75 neurotrophin receptor and facilitates nerve growth factor dependent apoptosis."
    Salehi A.H., Roux P.P., Kubu C.J., Zeindler C., Bhakar A., Tannis L.-L., Verdi J.M., Barker P.A.
    Neuron 27:279-288(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, INTERACTION WITH MAGED1.
    Strain: Sprague-Dawley.
    Tissue: Neural crest.
  5. "An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors."
    Kong H., Boulter J., Weber J.L., Lai C., Chao M.V.
    J. Neurosci. 21:176-185(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KIDINS220.
  6. "PLAIDD, a type II death domain protein that interacts with p75 neurotrophin receptor."
    Frankowski H., Castro-Obregon S., del Rio G., Rao R.V., Bredesen D.E.
    NeuroMolecular Med. 1:153-170(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NRADD.
  7. "Ternary complex with Trk, p75, and an ankyrin-rich membrane spanning protein."
    Chang M.-S., Arevalo J.C., Chao M.V.
    J. Neurosci. Res. 78:186-192(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NTRK1 AND KIDINS220, DOMAIN.
  8. "Bex1, a novel interactor of the p75 neurotrophin receptor, links neurotrophin signaling to the cell cycle."
    Vilar M., Murillo-Carretero M., Mira H., Magnusson K., Besset V., Ibanez C.F.
    EMBO J. 25:1219-1230(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BEX1.
  9. "NMR structure of the death domain of the p75 neurotrophin receptor."
    Liepinsh E., Ilag L.L., Otting G., Ibanez C.F.
    EMBO J. 16:4999-5005(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 334-418.

Entry informationi

Entry nameiTNR16_RAT
AccessioniPrimary (citable) accession number: P07174
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: July 6, 2016
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.