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Reviewed, UniProtKB/Swiss-Prot P07174 (TNR16_RAT)

Last modified July 22, 2008. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tumor necrosis factor receptor superfamily member 16
Alternative name(s):
    Low-affinity nerve growth factor receptor
      Short name=NGF receptor
    Gp80-LNGFR
    p75 ICD
    Low affinity neurotrophin receptor p75NTR
    CD_antigen=CD271
Gene names
Name: Ngfr
Synonyms: Tnfrsf16
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length425 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.

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 ARMS and NTRK1. Can form a ternary complex with NTRK1 and ARMS and this complex is affected by the expression levels of ARMS. An increase in ARMS expression leads to a decreased association of NGFR and NTRK1. Interacts with LINGO1 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein.

Domain

Death domain is responsible for interaction with RANBP9.

The extracellular domain is responsible for interaction with NTRK1.

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 processApoptosis
Differentiation
Neurogenesis
   Cellular componentMembrane
   DomainRepeat
Signal
Transmembrane
   Molecular functionDevelopmental protein
Receptor
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure

Gene Ontology (GO)

None. [Check GOA]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 2929
Chain30 – 425396Tumor necrosis factor receptor superfamily member 16

Regions

Topological domain30 – 251222Extracellular Potential
Transmembrane252 – 27322 Potential
Topological domain274 – 425152Cytoplasmic Potential
Repeat32 – 6534TNFR-Cys 1
Repeat67 – 10842TNFR-Cys 2
Repeat109 – 14739TNFR-Cys 3
Repeat149 – 18941TNFR-Cys 4
Domain354 – 41966Death
Region327 – 34216Mediates interaction with ARMS
Compositional bias198 – 24952Ser/Thr-rich

Amino acid modifications

Glycosylation611N-linked (GlcNAc...) Potential
Glycosylation711N-linked (GlcNAc...) Potential
Disulfide bond33 ↔ 44 By similarity
Disulfide bond45 ↔ 58 By similarity
Disulfide bond48 ↔ 65 By similarity
Disulfide bond68 ↔ 84 By similarity
Disulfide bond87 ↔ 100 By similarity
Disulfide bond90 ↔ 108 By similarity
Disulfide bond110 ↔ 123 By similarity
Disulfide bond126 ↔ 139 By similarity
Disulfide bond129 ↔ 147 By similarity
Disulfide bond150 ↔ 165 By similarity
Disulfide bond168 ↔ 181 By similarity
Disulfide bond171 ↔ 189 By similarity

Secondary structure

......................................... 425
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07174-1 [UniParc].

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

FASTA42545,433
        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: 3027580] [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: 1446821] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
Tissue: Liver.
[3]"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: 11150334] [Abstract]
Cited for: INTERACTION WITH ARMS.
[4]"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: 15378608] [Abstract]
Cited for: INTERACTION WITH NTRK1 AND ARMS, DOMAIN.
[5]"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: 16498402] [Abstract]
Cited for: INTERACTION WITH BEX1.
[6]"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: 9305641] [Abstract]
Cited for: STRUCTURE BY NMR OF 334-418.

Cross-references

Sequence databases

X05137 mRNA. Translation: CAA28783.1.
X61269 Genomic DNA. No translation available.
PIRA26431.
RefSeqNP_036742.1.
UniGeneRn.10980

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1NGRNMR-A334-418[»]
1SG1X-ray2.40X30-190[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5715N.
IntActP07174.

PTM databases

PhosphoSiteP07174.

Genome annotation databases

EnsemblENSRNOG00000005392. Rattus norvegicus. [Contig view]
GeneID24596.
KEGGrno:24596.

Organism-specific databases

RGD3177. Ngfr.

Phylogenomic databases

HOVERGENP07174.

Gene expression databases

ArrayExpressP07174.
GermOnlineENSRNOG00000005392. Rattus norvegicus.

Family and domain databases

InterProIPR000488. Death.
IPR011029. DEATH_like.
IPR001368. TNFR_c6.
[Graphical view]
Gene3DG3DSA:1.10.533.10. DEATH_like. 1 hit.
PfamPF00531. Death. 1 hit.
PF00020. TNFR_c6. 4 hits.
[Graphical view]
SMARTSM00005. DEATH. 1 hit.
SM00208. TNFR. 4 hits.
[Graphical view]
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 3 hits.
PS50050. TNFR_NGFR_2. 4 hits.
[Graphical view]
ProDomP07174.
[Graphical view] [Entries sharing at least one domain]
BLOCKSSearch...

Other Resources

LinkHubP07174.
ProtoNetSearch...

Entry information

Entry nameTNR16_RAT
AccessionPrimary (citable) accession number: P07174
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: July 22, 2008
This is version 86 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents