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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

  • amyloid-beta binding Source: RGD
  • calmodulin binding Source: UniProtKB
  • coreceptor activity Source: RGD
  • death receptor activity Source: RGD
  • identical protein binding Source: IntAct
  • 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
  • ubiquitin protein ligase binding Source: RGD

GO - Biological processi

  • activation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
  • apoptotic signaling pathway Source: GO_Central
  • axon guidance Source: RGD
  • cellular response to oxidative stress Source: RGD
  • central nervous system development Source: RGD
  • circadian regulation of gene expression Source: UniProtKB
  • circadian rhythm Source: RGD
  • detection of temperature stimulus Source: RGD
  • dorsal aorta development Source: RGD
  • glucose homeostasis Source: UniProtKB
  • hair follicle morphogenesis Source: RGD
  • 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 blood vessel endothelial cell proliferation involved in sprouting angiogenesis Source: RGD
  • negative regulation of cell cycle Source: Reactome
  • negative regulation of dendritic spine development Source: RGD
  • negative regulation of fibroblast growth factor receptor signaling pathway Source: RGD
  • negative regulation of hair follicle 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
  • nerve development Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of apoptotic signaling pathway Source: RGD
  • positive regulation of excitatory postsynaptic potential Source: RGD
  • positive regulation of fibroblast proliferation 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 odontogenesis of dentin-containing tooth Source: RGD
  • positive regulation of pri-miRNA transcription from RNA polymerase II promoter Source: RGD
  • positive regulation of protein kinase B signaling Source: RGD
  • positive regulation of protein localization to nucleus 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 gene expression 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
  • Rho protein signal transduction Source: RGD
  • sensory perception of pain Source: RGD
  • signal transduction Source: RGD
  • skeletal muscle cell differentiation Source: RGD
  • skin development Source: RGD

Keywordsi

Molecular functionDevelopmental protein, Receptor
Biological processApoptosis, Biological rhythms, Differentiation, Neurogenesis

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3177. Ngfr.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini30 – 251ExtracellularSequence analysisAdd BLAST222
Transmembranei252 – 273HelicalSequence analysisAdd BLAST22
Topological domaini274 – 425CytoplasmicSequence analysisAdd BLAST152

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 29Add BLAST29
ChainiPRO_000003459330 – 425Tumor necrosis factor receptor superfamily member 16Add BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi33 ↔ 44PROSITE-ProRule annotation
Disulfide bondi45 ↔ 58PROSITE-ProRule annotation
Disulfide bondi48 ↔ 65PROSITE-ProRule annotation
Glycosylationi61N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi68 ↔ 84PROSITE-ProRule annotation
Glycosylationi71N-linked (GlcNAc...) asparagineSequence analysis1
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 residuei312PhosphoserineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP07174.
PRIDEiP07174.

PTM databases

iPTMnetiP07174.
PhosphoSitePlusiP07174.
SwissPalmiP07174.

Miscellaneous databases

PMAP-CutDBiP07174.

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

Show more details

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • 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
  • ubiquitin protein ligase binding Source: RGD

Protein-protein interaction databases

BioGridi246737. 11 interactors.
DIPiDIP-5715N.
IntActiP07174. 20 interactors.
MINTiMINT-128759.
STRINGi10116.ENSRNOP00000007268.

Structurei

Secondary structure

1425
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi40 – 45Combined sources6
Beta strandi52 – 56Combined sources5
Beta strandi58 – 62Combined sources5
Beta strandi64 – 67Combined sources4
Turni70 – 72Combined sources3
Beta strandi79 – 81Combined sources3
Beta strandi94 – 98Combined sources5
Beta strandi107 – 110Combined sources4
Beta strandi114 – 116Combined sources3
Turni118 – 120Combined sources3
Beta strandi123 – 125Combined sources3
Beta strandi133 – 137Combined sources5
Beta strandi146 – 149Combined sources4
Beta strandi160 – 162Combined sources3
Turni246 – 249Combined sources4
Beta strandi250 – 253Combined sources4
Helixi255 – 275Combined sources21
Turni276 – 278Combined sources3
Helixi337 – 339Combined sources3
Helixi342 – 351Combined sources10
Turni352 – 355Combined sources4
Helixi356 – 364Combined sources9
Helixi368 – 373Combined sources6
Helixi374 – 376Combined sources3
Beta strandi377 – 379Combined sources3
Helixi380 – 388Combined sources9
Beta strandi391 – 393Combined sources3
Helixi396 – 405Combined sources10
Helixi409 – 416Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07174.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati32 – 65TNFR-Cys 1Add BLAST34
Repeati67 – 108TNFR-Cys 2Add BLAST42
Repeati109 – 147TNFR-Cys 3Add BLAST39
Repeati149 – 189TNFR-Cys 4Add BLAST41
Domaini354 – 419DeathPROSITE-ProRule annotationAdd BLAST66

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni327 – 342Mediates interaction with KIDINS220Add BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi198 – 249Ser/Thr-richAdd BLAST52

Domaini

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

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

Family and domain databases

CDDicd13416. TNFRSF16. 1 hit.
InterProiView protein in InterPro
IPR011029. DEATH-like_dom_sf.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022325. TNFR_16.
IPR034046. TNFRSF16_N.
PfamiView protein in Pfam
PF00531. Death. 1 hit.
PF00020. TNFR_c6. 3 hits.
PRINTSiPR01966. TNFACTORR16.
SMARTiView protein in SMART
SM00005. DEATH. 1 hit.
SM00208. TNFR. 4 hits.
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiView protein in PROSITE
PS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 3 hits.
PS50050. TNFR_NGFR_2. 4 hits.

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.

Similar proteinsi

Entry informationi

Entry nameiTNR16_RAT
AccessioniPrimary (citable) accession number: P07174
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 22, 2017
This is version 170 of the entry and version 1 of the sequence. See 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