[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1038/325593a0; PubMed=3027580 [NCBI, ExPASy, EBI, Israel, Japan] Radeke M.J., Misko T.P., Hsu C., Herzenberg L.A., Shooter E.M.; "Gene transfer and molecular cloning of the rat nerve growth factor receptor."; Nature 325:593-597(1987).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22. TISSUE=Liver; DOI=10.1016/0378-1119(92)90128-C; PubMed=1446821 [NCBI, ExPASy, EBI, Israel, Japan] Metsis M., Timmusk T., Allikmets R., Saarma M., Persson H.; "Regulatory elements and transcriptional regulation by testosterone and retinoic acid of the rat nerve growth factor receptor promoter."; Gene 121:247-254(1992).
[3]	INTERACTION WITH ARMS. PubMed=11150334 [NCBI, ExPASy, EBI, Israel, Japan] Kong H., Boulter J., Weber J.L., Lai C., Chao M.V.; "An evolutionarily conserved transmembrane protein that is a novel downstream target of neurotrophin and ephrin receptors."; J. Neurosci. 21:176-185(2001).
[4]	INTERACTION WITH NTRK1 AND ARMS, AND DOMAIN. DOI=10.1002/jnr.20262; PubMed=15378608 [NCBI, ExPASy, EBI, Israel, Japan] Chang M.-S., Arevalo J.C., Chao M.V.; "Ternary complex with Trk, p75, and an ankyrin-rich membrane spanning protein."; J. Neurosci. Res. 78:186-192(2004).
[5]	INTERACTION WITH BEX1. DOI=10.1038/sj.emboj.7601017; PubMed=16498402 [NCBI, ExPASy, EBI, Israel, Japan] Vilar M., Murillo-Carretero M., Mira H., Magnusson K., Besset V., Ibanez C.F.; "Bex1, a novel interactor of the p75 neurotrophin receptor, links neurotrophin signaling to the cell cycle."; EMBO J. 25:1219-1230(2006).
[6]	STRUCTURE BY NMR OF 334-418. DOI=10.1093/emboj/16.16.4999; PubMed=9305641 [NCBI, ExPASy, EBI, Israel, Japan] Liepinsh E., Ilag L.L., Otting G., Ibanez C.F.; "NMR structure of the death domain of the p75 neurotrophin receptor."; EMBO J. 16:4999-5005(1997).

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: 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.
DOMAIN: The extracellular domain is responsible for interaction with NTRK1.
PTM: N- and O-glycosylated.
PTM: Phosphorylated on serine residues.
SIMILARITY: Contains 1 death domain.
SIMILARITY: Contains 4 TNFR-Cys repeats.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X05137; CAA28783.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X61269; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]

A26431; A26431.

NP_036742.1; -.

3D structure databases

PDB

1NGR; NMR; -; A=334-418.	[ExPASy / RCSB / EBI]
1SG1; X-ray; 2.40 A; X=30-190.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1NGR; -.
1SG1; -.

ModBase

P07174.

Protein-protein interaction databases

DIP

DIP:5715N; -.

IntAct

P07174; -.

PTM databases

PhosphoSite

P07174; -.

Organism-specific databases

RGD

3177; Ngfr.

Gene expression databases

ArrayExpress

P07174; -.

GermOnline

ENSRNOG00000005392; Rattus norvegicus.

Family and domain databases

InterPro

IPR000488; Death.
IPR011029; DEATH_like.
IPR001368; TNFR_c6.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.533.10; DEATH_like; 1.

Pfam

PF00531; Death; 1.
PF00020; TNFR_c6; 4.
Pfam graphical view of domain structure.

SMART

SM00005; DEATH; 1.
SM00208; TNFR; 4.
SMART graphical view of domain structure.

PROSITE

PS50017; DEATH_DOMAIN; 1.
PS00652; TNFR_NGFR_1; 3.
PS50050; TNFR_NGFR_2; 4.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P07174.

Genome annotation databases

Ensembl

ENSRNOG00000005392; Rattus norvegicus. [Contig view]

GeneID

24596; -.

KEGG

rno:24596; -.

Phylogenomic databases

HOVERGEN

P07174; -.

Other

P07174; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Apoptosis; Developmental protein; Differentiation; Glycoprotein; Membrane; Neurogenesis; Phosphoprotein; Receptor; Repeat; Signal; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 29`	`29`
`CHAIN`	`30 425`	`396`	`Tumor necrosis factor receptor superfamily member 16.`	`PRO_0000034593`
`TOPO_DOM`	`30 251`	`222`	`Extracellular (Potential).`
`TRANSMEM`	`252 273`	`22`	`Potential.`
`TOPO_DOM`	`274 425`	`152`	`Cytoplasmic (Potential).`
`REPEAT`	`32 65`	`34`	`TNFR-Cys 1.`
`REPEAT`	`67 108`	`42`	`TNFR-Cys 2.`
`REPEAT`	`109 147`	`39`	`TNFR-Cys 3.`
`REPEAT`	`149 189`	`41`	`TNFR-Cys 4.`
`DOMAIN`	`354 419`	`66`	`Death.`
`REGION`	`327 342`	`16`	`Mediates interaction with ARMS.`
`COMPBIAS`	`198 249`	`52`	`Ser/Thr-rich.`
`CARBOHYD`	`61 61`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`71 71`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`33 44`		`By similarity.`
`DISULFID`	`45 58`		`By similarity.`
`DISULFID`	`48 65`		`By similarity.`
`DISULFID`	`68 84`		`By similarity.`
`DISULFID`	`87 100`		`By similarity.`
`DISULFID`	`90 108`		`By similarity.`
`DISULFID`	`110 123`		`By similarity.`
`DISULFID`	`126 139`		`By similarity.`
`DISULFID`	`129 147`		`By similarity.`
`DISULFID`	`150 165`		`By similarity.`
`DISULFID`	`168 181`		`By similarity.`
`DISULFID`	`171 189`		`By similarity.`
`STRAND`	`52 56`	`5`
`STRAND`	`58 62`	`5`
`STRAND`	`64 67`	`4`
`TURN`	`70 72`	`3`
`STRAND`	`79 81`	`3`
`STRAND`	`94 98`	`5`
`STRAND`	`107 110`	`4`
`STRAND`	`114 116`	`3`
`TURN`	`118 120`	`3`
`STRAND`	`123 125`	`3`
`STRAND`	`133 137`	`5`
`STRAND`	`146 149`	`4`
`STRAND`	`160 162`	`3`
`TURN`	`343 345`	`3`
`HELIX`	`346 351`	`6`
`HELIX`	`356 363`	`8`
`HELIX`	`368 376`	`9`
`HELIX`	`380 387`	`8`
`HELIX`	`388 390`	`3`
`HELIX`	`396 405`	`10`
`HELIX`	`409 416`	`8`

Sequence information

Length: 425 AA [This is the length of the unprocessed precursor]

Molecular weight: 45433 Da [This is the MW of the unprocessed precursor]

CRC64: B2E152D94D3827F8 [This is a checksum on the sequence]

        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

P07174 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools