Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Z0W1 (TNR16_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tumor necrosis factor receptor superfamily member 16
Alternative name(s):
Low affinity neurotrophin receptor p75NTR
Low-affinity nerve growth factor receptor
Short name=NGF receptor
CD_antigen=CD271
Gene names
Name:Ngfr
Synonyms:Tnfrsf16
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. 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. Binds to rabies virus glycoprotein Gs. Ref.3

Subunit structure

Homodimer; disulfide-linked. Interacts with p75NTR-associated cell death executor. Interacts with TRAF2, TRAF4, TRAF6, PTPN13 and RANBP9. Interacts through TRAF6 with SQSTM1 which bridges NGFR to NTRK1. Interacts with BEX1 and NGFRAP1/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. Ref.2 Ref.3

Subcellular location

Membrane; Single-pass type I membrane protein By similarity.

Domain

Death domain is responsible for interaction with RANBP9 By similarity.

The extracellular domain is responsible for interaction with NTRK1 By similarity.

Post-translational modification

N- and O-glycosylated By similarity.

Phosphorylated on serine residues By similarity.

Sequence similarities

Contains 1 death domain.

Contains 4 TNFR-Cys repeats.

Ontologies

Keywords
   Biological processApoptosis
Differentiation
Neurogenesis
   Cellular componentMembrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionDevelopmental protein
Receptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

axon guidance

Inferred from mutant phenotype PubMed 11978834. Source: MGI

central nervous system development

Inferred from mutant phenotype PubMed 11978834. Source: MGI

detection of temperature stimulus

Inferred from mutant phenotype PubMed 1317267. Source: MGI

glucose homeostasis

Inferred from mutant phenotype Ref.3. Source: UniProtKB

hair follicle morphogenesis

Inferred from mutant phenotype PubMed 10588868. Source: MGI

intracellular protein transport

Inferred from mutant phenotype Ref.3. Source: UniProtKB

negative regulation of fibroblast growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 10588868. Source: MGI

negative regulation of hair follicle development

Inferred from mutant phenotype PubMed 10588868. Source: MGI

nerve development

Inferred from mutant phenotype PubMed 1317267. Source: MGI

positive regulation of apoptotic signaling pathway

Inferred from direct assay PubMed 10764727. Source: MGI

positive regulation of fibroblast proliferation

Inferred from mutant phenotype PubMed 10588868. Source: MGI

positive regulation of odontogenesis of dentin-containing tooth

Inferred from mutant phenotype PubMed 9268129. Source: MGI

regulation of gene expression

Inferred from mutant phenotype PubMed 10588868. Source: MGI

regulation of glucose import in response to insulin stimulus

Inferred from mutant phenotype Ref.3. Source: UniProtKB

skin development

Inferred from mutant phenotype PubMed 1317267. Source: MGI

   Cellular_componentcell surface

Inferred from direct assay PubMed 10021336. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 19295126. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 10536054. Source: MGI

   Molecular_functionRab GTPase binding

Inferred from direct assay Ref.3. Source: UniProtKB

death receptor activity

Inferred from direct assay PubMed 10764727. Source: MGI

nerve growth factor binding

Inferred from direct assay PubMed 1317267. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 By similarity
Chain22 – 417396Tumor necrosis factor receptor superfamily member 16
PRO_0000034592

Regions

Topological domain22 – 246225Extracellular Potential
Transmembrane247 – 26519Helical; Potential
Topological domain266 – 417152Cytoplasmic Potential
Repeat24 – 5734TNFR-Cys 1
Repeat59 – 10042TNFR-Cys 2
Repeat101 – 13939TNFR-Cys 3
Repeat141 – 18141TNFR-Cys 4
Domain346 – 41166Death
Region319 – 33416Mediates interaction with KIDINS220 By similarity
Compositional bias190 – 24152Ser/Thr-rich

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Disulfide bond25 ↔ 36 By similarity
Disulfide bond37 ↔ 50 By similarity
Disulfide bond40 ↔ 57 By similarity
Disulfide bond60 ↔ 76 By similarity
Disulfide bond79 ↔ 92 By similarity
Disulfide bond82 ↔ 100 By similarity
Disulfide bond102 ↔ 115 By similarity
Disulfide bond118 ↔ 131 By similarity
Disulfide bond121 ↔ 139 By similarity
Disulfide bond142 ↔ 157 By similarity
Disulfide bond160 ↔ 173 By similarity
Disulfide bond163 ↔ 181 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9Z0W1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 5D7A4510DB8AF9B2

FASTA41744,686
        10         20         30         40         50         60 
MDRLRLLLLL LLLLGVSFGG AKETCSTGMY THSGECCKAC NLGEGVAQPC GANQTVCEPC 

        70         80         90        100        110        120 
LDSVTFSDVV SATEPCKPCT ECLGLQSMSA PCVEADDAVC RCSYGYYQDE ETGRCEACSV 

       130        140        150        160        170        180 
CGVGSGLVFS CQDKQNTVCE ECPEGTYSDE ANHVDPCLPC TVCEDTERQL RECTPWADAE 

       190        200        210        220        230        240 
CEEIPGRWIT RSTPPEGSDV TTPSTQEPEA PPERDLIAST VADTVTTVMG SSQPVVTRGT 

       250        260        270        280        290        300 
ADNLIPVYCS ILAAVVVGLV AYIAFKRWNS CKQNKQGANS RPVNQTPPPE GEKLHSDSGI 

       310        320        330        340        350        360 
SVDSQSLHDQ QTHTQTASAQ ALKGDGNLYS SLPLTKREEV EKLLNGDTWR HLAGELGYQP 

       370        380        390        400        410 
EHIDSFTHEA CPVRALLASW GAQDSATLDA LLAALRRIQR ADIVESLCSE STATSPV 

« Hide

References

[1]"Low-affinity nerve-growth factor receptor (p75NTR) can serve as a receptor for rabies virus."
Tuffereau C., Benejean J., Blondel D., Kieffer B., Flamand A.
EMBO J. 17:7250-7259(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: A.
[2]"Structure-function analysis of NADE: identification of regions that mediate nerve growth factor-induced apoptosis."
Mukai J., Shoji S., Kimura M.T., Okubo S., Sano H., Suvanto P., Li Y., Irie S., Sato T.-A.
J. Biol. Chem. 277:13973-13982(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NGFRAP1.
[3]"p75 neurotrophin receptor regulates glucose homeostasis and insulin sensitivity."
Baeza-Raja B., Li P., Le Moan N., Sachs B.D., Schachtrup C., Davalos D., Vagena E., Bridges D., Kim C., Saltiel A.R., Olefsky J.M., Akassoglou K.
Proc. Natl. Acad. Sci. U.S.A. 109:5838-5843(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RAB31.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF105292 mRNA. Translation: AAD17943.1.
UniGeneMm.283893.

3D structure databases

ProteinModelPortalQ9Z0W1.
SMRQ9Z0W1. Positions 24-223, 326-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Z0W1. 5 interactions.
MINTMINT-243918.

PTM databases

PhosphoSiteQ9Z0W1.

Proteomic databases

PaxDbQ9Z0W1.
PRIDEQ9Z0W1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:97323. Ngfr.

Phylogenomic databases

eggNOGNOG39106.
HOVERGENHBG060431.
InParanoidQ9Z0W1.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

GenevestigatorQ9Z0W1.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022325. TNFR_16.
[Graphical view]
PfamPF00531. Death. 1 hit.
PF00020. TNFR_c6. 3 hits.
[Graphical view]
PRINTSPR01966. TNFACTORR16.
SMARTSM00005. DEATH. 1 hit.
SM00208. TNFR. 4 hits.
[Graphical view]
SUPFAMSSF47986. SSF47986. 1 hit.
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 3 hits.
PS50050. TNFR_NGFR_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

PROQ9Z0W1.
SOURCESearch...

Entry information

Entry nameTNR16_MOUSE
AccessionPrimary (citable) accession number: Q9Z0W1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot