Tumor necrosis factor receptor superfamily member 16 precursor

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P07174 (TNR16_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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 names

Name:	Ngfr
Synonyms:	Tnfrsf16

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 By similarity. 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.
Subunit structure	Homodimer; disulfide-linked. Interacts with p75NTR-associated cell death executor. Interacts with NGFRAP1/BEX3. Interacts with TRAF2, TRAF4, TRAF6, PTPN13 and RANBP9. Interacts through TRAF6 with SQSTM1 which bridges NGFR to NTRK1 By similarity. Interacts with BEX1. 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 with LINGO1. Interacts (via death domain) with RAB31 By similarity. Interacts with NTRK2; may regulate the ligand specificity of the NTRK2 receptor. Interacts with NRADD. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7
Subcellular location	Membrane; Single-pass type I membrane protein.
Domain	Death domain is responsible for interaction with RANBP9. Ref.6 The extracellular domain is responsible for interaction with NTRK1. Ref.6
Post-translational modification	N- and O-glycosylated. Phosphorylated on serine residues.
Sequence similarities	Contains 1 death domain. Contains 4 TNFR-Cys repeats.

Ontologies

Keywords
Biological process	Apoptosis Differentiation Neurogenesis
Cellular component	Membrane
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Developmental protein Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW cellular response to oxidative stress Inferred from mutant phenotype PubMed 19457114. Source: RGD glucose homeostasis Inferred from sequence or structural similarity. Source: UniProtKB induction of apoptosis Inferred from direct assay PubMed 12408842. Source: RGD intracellular protein transport Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of mitochondrial depolarization Inferred from mutant phenotype PubMed 19457114. Source: RGD negative regulation of neuron apoptotic process Inferred from mutant phenotype PubMed 11438587. Source: RGD negative regulation of neuron projection development Inferred from direct assay PubMed 18786176. Source: RGD positive regulation of MAPK cascade Inferred from direct assay PubMed 12929129. Source: RGD positive regulation of Rho protein signal transduction Inferred from direct assay PubMed 18786176. Source: RGD positive regulation of myelination Inferred from mutant phenotype PubMed 12424382. Source: RGD positive regulation of neuron death Inferred from direct assay PubMed 20943663. Source: RGD positive regulation of protein kinase B signaling cascade Inferred from direct assay PubMed 19457114. Source: RGD positive regulation of synaptic transmission, cholinergic Inferred from mutant phenotype PubMed 18256260. Source: RGD positive regulation of synaptic transmission, glutamatergic Inferred from mutant phenotype PubMed 18256260. Source: RGD regulation of glucose import in response to insulin stimulus Inferred from sequence or structural similarity. Source: UniProtKB regulation of reactive oxygen species metabolic process Inferred from mutant phenotype PubMed 19457114. Source: RGD response to lipopolysaccharide Inferred from expression pattern PubMed 21084570. Source: RGD response to wounding Inferred from mutant phenotype PubMed 12408842. Source: RGD sensory perception of pain Inferred from mutant phenotype PubMed 20060234. Source: RGD signal transduction Inferred from direct assay PubMed 12408842. Source: RGD skeletal muscle cell differentiation Inferred from expression pattern PubMed 16723531. Source: RGD
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 9521535. Source: RGD clathrin-coated endocytic vesicle Inferred from direct assay PubMed 17897318. Source: RGD dendrite membrane Inferred from direct assay PubMed 9521535. Source: RGD external side of plasma membrane Inferred from direct assay PubMed 9521535. Source: RGD integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane raft Inferred from direct assay PubMed 17433308. Source: RGD neuronal cell body membrane Inferred from direct assay PubMed 9521535. Source: RGD nuclear envelope Inferred from direct assay PubMed 9521535. Source: RGD perikaryon Inferred from direct assay PubMed 9767155. Source: RGD rough endoplasmic reticulum Inferred from direct assay PubMed 9521535. Source: RGD
Molecular_function	Rab GTPase binding Inferred from sequence or structural similarity. Source: UniProtKB beta-amyloid binding Inferred from physical interaction PubMed 19334058. Source: RGD nerve growth factor binding Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APP	P05067	2	EBI-1038810,EBI-2431589	From a different organism.
TRAF2	Q12933	3	EBI-1038810,EBI-355744	From a different organism.
TRAF4	Q9BUZ4	3	EBI-1038810,EBI-3650647	From a different organism.
TRAF6	Q9Y4K3	2	EBI-1038810,EBI-359276	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

Chain

30 – 425

396

Tumor necrosis factor receptor superfamily member 16

PRO_0000034593

Regions

Topological domain

30 – 251

222

Extracellular Potential

Transmembrane

252 – 273

Helical; Potential

Topological domain

274 – 425

152

Cytoplasmic Potential

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

Region

327 – 342

Mediates interaction with KIDINS220

Compositional bias

198 – 249

Ser/Thr-rich

Amino acid modifications

Modified residue

294

Phosphothreonine By similarity

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

N-linked (GlcNAc...) Potential

Disulfide bond

33 ↔ 44

By similarity

Disulfide bond

45 ↔ 58

By similarity

Disulfide bond

48 ↔ 65

By similarity

Disulfide bond

68 ↔ 84

By similarity

Disulfide bond

87 ↔ 100

By similarity

Disulfide bond

90 ↔ 108

By similarity

Disulfide bond

110 ↔ 123

By similarity

Disulfide bond

126 ↔ 139

By similarity

Disulfide bond

129 ↔ 147

By similarity

Disulfide bond

150 ↔ 165

By similarity

Disulfide bond

168 ↔ 181

By similarity

Disulfide bond

171 ↔ 189

By similarity

Secondary structure

425

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P07174 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: B2E152D94D3827F8
Show »

FASTA

425

45,433

        10         20         30         40         50         60 
MRRAGAACSA MDRLRLLLLL ILGVSSGGAK ETCSTGLYTH SGECCKACNL GEGVAQPCGA 

        70         80         90        100        110        120 
NQTVCEPCLD NVTFSDVVSA TEPCKPCTEC LGLQSMSAPC VEADDAVCRC AYGYYQDEET 

       130        140        150        160        170        180 
GHCEACSVCE VGSGLVFSCQ DKQNTVCEEC PEGTYSDEAN HVDPCLPCTV CEDTERQLRE 

       190        200        210        220        230        240 
CTPWADAECE EIPGRWIPRS TPPEGSDSTA PSTQEPEVPP EQDLVPSTVA DMVTTVMGSS 

       250        260        270        280        290        300 
QPVVTRGTTD NLIPVYCSIL AAVVVGLVAY IAFKRWNSCK QNKQGANSRP VNQTPPPEGE 

       310        320        330        340        350        360 
KLHSDSGISV DSQSLHDQQT HTQTASGQAL KGDGNLYSSL PLTKREEVEK LLNGDTWRHL 

       370        380        390        400        410        420 
AGELGYQPEH IDSFTHEACP VRALLASWGA QDSATLDALL AALRRIQRAD IVESLCSEST 


ATSPV

« Hide

References

[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]	"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.
[5]	"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.
[6]	"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.
[7]	"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.
[8]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05137 mRNA. Translation: CAA28783.1.
X61269 Genomic DNA. No translation available.

IPI

IPI00204445.

PIR

A26431.

RefSeq

NP_036742.2. NM_012610.2.

UniGene

Rn.10980.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NGR	NMR	-	A	334-418	[»]
1SG1	X-ray	2.40	X	30-190	[»]
3BUK	X-ray	2.60	C/D	30-190	[»]
3IJ2	X-ray	3.75	X/Y	30-190	[»]

ProteinModelPortal

P07174.

SMR

P07174. Positions 31-190, 334-418.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5715N.

IntAct

P07174. 11 interactions.

MINT

MINT-128759.

STRING

10116.ENSRNOP00000007268.

PTM databases

PhosphoSite

P07174.

Proteomic databases

PaxDb

P07174.

PRIDE

P07174.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

24596.

KEGG

rno:24596.

UCSC

RGD:3177. rat.

Organism-specific databases

CTD

4804.

RGD

3177. Ngfr.

Phylogenomic databases

eggNOG

NOG39106.

HOGENOM

HOG000059587.

HOVERGEN

HBG060431.

InParanoid

P07174.

K02583.

OrthoDB

EOG4ZKJM8.

Enzyme and pathway databases

Reactome

REACT_111984. Signal Transduction.

Gene expression databases

Genevestigator

P07174.

GermOnline

ENSRNOG00000005392. Rattus norvegicus.

Family and domain databases

Gene3D

1.10.533.10. 1 hit.

InterPro

IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022325. TNFR_16.
[Graphical view]

Pfam

PF00531. Death. 1 hit.
PF00020. TNFR_c6. 3 hits.
[Graphical view]

PRINTS

PR01966. TNFACTORR16.

SMART

SM00005. DEATH. 1 hit.
SM00208. TNFR. 4 hits.
[Graphical view]

SUPFAM

SSF47986. DEATH_like. 1 hit.

PROSITE

PS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 3 hits.
PS50050. TNFR_NGFR_2. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07174.

NextBio

603794.

PMAP-CutDB

P07174.

Entry information

Entry name

TNR16_RAT

Accession

Primary (citable) accession number: P07174

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	April 1, 1988
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents