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Tumor necrosis factor receptor superfamily member 16 (Gp80-LNGFR) (Low affinity neurotrophin receptor p75NTR) (Low-affinity nerve growth factor receptor) (NGF receptor) (p75 ICD) (CD antigen CD271)

 TNR16_HUMAN             Reviewed;         427 AA.
P08138; B2R961; B4E096;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
22-NOV-2017, entry version 194.
RecName: Full=Tumor necrosis factor receptor superfamily member 16;
AltName: Full=Gp80-LNGFR;
AltName: Full=Low affinity neurotrophin receptor p75NTR;
AltName: Full=Low-affinity nerve growth factor receptor;
Short=NGF receptor;
AltName: Full=p75 ICD;
AltName: CD_antigen=CD271;
Flags: Precursor;
Name=NGFR; Synonyms=TNFRSF16;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3022937; DOI=10.1016/0092-8674(86)90619-7;
Johnson D., Lanahan A., Buck C.R., Sehgal A., Morgan C., Mercer E.,
Bothwell M., Chao M.;
"Expression and structure of the human NGF receptor.";
Cell 47:545-554(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cerebellum, and Thymus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
PubMed=2850481; DOI=10.1128/MCB.8.8.3160;
Sehgal A., Patil N., Chao M.;
"A constitutive promoter directs expression of the nerve growth factor
receptor gene.";
Mol. Cell. Biol. 8:3160-3167(1988).
[7]
INTERACTION WITH TRAF2; TRAF4 AND TRAF6.
PubMed=10514511; DOI=10.1074/jbc.274.42.30202;
Ye X., Mehlen P., Rabizadeh S., VanArsdale T., Zhang H., Shin H.,
Wang J.J.L., Leo E., Zapata J.M., Hauser C.A., Reed J.C.,
Bredesen D.E.;
"TRAF family proteins interact with the common neurotrophin receptor
and modulate apoptosis induction.";
J. Biol. Chem. 274:30202-30208(1999).
[8]
INTERACTION WITH TRAF6.
PubMed=9915784; DOI=10.1074/jbc.274.5.2597;
Khursigara G., Orlinick J.R., Chao M.V.;
"Association of the p75 neurotrophin receptor with TRAF6.";
J. Biol. Chem. 274:2597-2600(1999).
[9]
INTERACTION WITH PTPN13.
PubMed=10544233; DOI=10.1016/S0014-5793(99)01324-1;
Irie S., Hachiya T., Rabizadeh S., Maruyama W., Mukai J., Li Y.,
Reed J.C., Bredesen D.E., Sato T.A.;
"Functional interaction of Fas-associated phosphatase-1 (FAP-1) with
p75(NTR) and their effect on NF-kappaB activation.";
FEBS Lett. 460:191-198(1999).
[10]
INTERACTION WITH TRAF6 AND SQSTM1.
PubMed=11244088; DOI=10.1074/jbc.C000869200;
Wooten M.W., Seibenhener M.L., Mamidipudi V., Diaz-Meco M.T.,
Barker P.A., Moscat J.;
"The atypical protein kinase C-interacting protein p62 is a scaffold
for NF-kappaB activation by nerve growth factor.";
J. Biol. Chem. 276:7709-7712(2001).
[11]
INTERACTION WITH RANBP9.
TISSUE=Brain;
PubMed=12963025; DOI=10.1016/j.bbrc.2003.08.033;
Bai D., Chen H., Huang B.-R.;
"RanBPM is a novel binding protein for p75NTR.";
Biochem. Biophys. Res. Commun. 309:552-557(2003).
[12]
FUNCTION, AND INTERACTION WITH LINGO1.
PubMed=14966521; DOI=10.1038/nn1188;
Mi S., Lee X., Shao Z., Thill G., Ji B., Relton J., Levesque M.,
Allaire N., Perrin S., Sands B., Crowell T., Cate R.L., McCoy J.M.,
Pepinsky R.B.;
"LINGO-1 is a component of the Nogo-66 receptor/p75 signaling
complex.";
Nat. Neurosci. 7:221-228(2004).
[13]
STRUCTURE OF O-LINKED CARBOHYDRATE.
PubMed=8627329;
Chapman B.S., Eckart M.R., Kaufman S.E., Lapointe G.R.;
"O-linked oligosaccharide on the 75-kDa neurotrophin receptor.";
J. Neurochem. 66:1707-1716(1996).
[14]
INTERACTION WITH RTN4R.
PubMed=19052207; DOI=10.1523/JNEUROSCI.3828-08.2008;
Budel S., Padukkavidana T., Liu B.P., Feng Z., Hu F., Johnson S.,
Lauren J., Park J.H., McGee A.W., Liao J., Stillman A., Kim J.E.,
Yang B.Z., Sodi S., Gelernter J., Zhao H., Hisama F., Arnsten A.F.,
Strittmatter S.M.;
"Genetic variants of Nogo-66 receptor with possible association to
schizophrenia block myelin inhibition of axon growth.";
J. Neurosci. 28:13161-13172(2008).
[15]
FUNCTION.
PubMed=23785138; DOI=10.1523/JNEUROSCI.2757-12.2013;
Baeza-Raja B., Eckel-Mahan K., Zhang L., Vagena E., Tsigelny I.F.,
Sassone-Corsi P., Ptacek L.J., Akassoglou K.;
"p75 neurotrophin receptor is a clock gene that regulates oscillatory
components of circadian and metabolic networks.";
J. Neurosci. 33:10221-10234(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- 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. 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. {ECO:0000250, ECO:0000269|PubMed:14966521,
ECO:0000269|PubMed:23785138}.
-!- SUBUNIT: Homodimer; disulfide-linked. Interacts with p75NTR-
associated cell death executor. Interacts with RTN4R. 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 with NTRK2; may regulate the ligand specificity of the
NTRK2 receptor. Interacts (via death domain) with RAB31. Interacts
with LINGO1 and NRADD. Interacts with MAGED1; the interaction
antagonizes the association NGFR:NTRK1.
{ECO:0000250|UniProtKB:Q9Z0W1, ECO:0000269|PubMed:10514511,
ECO:0000269|PubMed:10544233, ECO:0000269|PubMed:11244088,
ECO:0000269|PubMed:12963025, ECO:0000269|PubMed:14966521,
ECO:0000269|PubMed:19052207, ECO:0000269|PubMed:9915784}.
-!- INTERACTION:
P05067:APP; NbExp=2; IntAct=EBI-1387782, EBI-77613;
P33681:CD80; NbExp=3; IntAct=EBI-1387782, EBI-1031024;
P25233:Ndn (xeno); NbExp=3; IntAct=EBI-1387782, EBI-1801080;
P01138:NGF; NbExp=2; IntAct=EBI-1387782, EBI-1028250;
Q9CPR8:Nsmce3 (xeno); NbExp=3; IntAct=EBI-1387782, EBI-5529102;
Q9Y467:SALL2; NbExp=3; IntAct=EBI-1387782, EBI-746180;
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P08138-1; Sequence=Displayed;
Name=2;
IsoId=P08138-2; Sequence=VSP_056850;
Note=No experimental confirmation available.;
-!- DOMAIN: Death domain is responsible for interaction with RANBP9.
-!- DOMAIN: The extracellular domain is responsible for interaction
with NTRK1. {ECO:0000250}.
-!- PTM: N- and O-glycosylated.
-!- PTM: O-linked glycans consist of Gal(1-3)GalNAc core elongated by
1 or 2 NeuNAc.
-!- PTM: Phosphorylated on serine residues.
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EMBL; M14764; AAB59544.1; -; mRNA.
EMBL; AK303278; BAG64358.1; -; mRNA.
EMBL; AK313654; BAG36408.1; -; mRNA.
EMBL; AC006487; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC015656; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471109; EAW94677.1; -; Genomic_DNA.
EMBL; BC050309; AAH50309.1; -; mRNA.
EMBL; M21621; AAA36363.1; -; Genomic_DNA.
CCDS; CCDS11549.1; -. [P08138-1]
PIR; A25218; GQHUN.
RefSeq; NP_002498.1; NM_002507.3. [P08138-1]
UniGene; Hs.415768; -.
UniGene; Hs.681726; -.
PDB; 2N80; NMR; -; A=334-427.
PDB; 2N83; NMR; -; A=330-427.
PDB; 2N97; NMR; -; A/B=330-427.
PDB; 3EWV; X-ray; 2.60 A; E=396-412.
PDBsum; 2N80; -.
PDBsum; 2N83; -.
PDBsum; 2N97; -.
PDBsum; 3EWV; -.
ProteinModelPortal; P08138; -.
SMR; P08138; -.
BioGrid; 110870; 37.
CORUM; P08138; -.
DIP; DIP-406N; -.
IntAct; P08138; 20.
MINT; MINT-107412; -.
STRING; 9606.ENSP00000172229; -.
BindingDB; P08138; -.
ChEMBL; CHEMBL4762; -.
GuidetoPHARMACOLOGY; 1888; -.
iPTMnet; P08138; -.
PhosphoSitePlus; P08138; -.
UniCarbKB; P08138; -.
BioMuta; NGFR; -.
DMDM; 128156; -.
EPD; P08138; -.
MaxQB; P08138; -.
PaxDb; P08138; -.
PeptideAtlas; P08138; -.
PRIDE; P08138; -.
DNASU; 4804; -.
Ensembl; ENST00000172229; ENSP00000172229; ENSG00000064300. [P08138-1]
Ensembl; ENST00000504201; ENSP00000421731; ENSG00000064300. [P08138-2]
GeneID; 4804; -.
KEGG; hsa:4804; -.
UCSC; uc002ioz.5; human. [P08138-1]
CTD; 4804; -.
DisGeNET; 4804; -.
EuPathDB; HostDB:ENSG00000064300.8; -.
GeneCards; NGFR; -.
HGNC; HGNC:7809; NGFR.
HPA; CAB000143; -.
HPA; CAB001995; -.
HPA; HPA004765; -.
MIM; 162010; gene.
neXtProt; NX_P08138; -.
OpenTargets; ENSG00000064300; -.
PharmGKB; PA31615; -.
eggNOG; ENOG410IQFC; Eukaryota.
eggNOG; ENOG4111F3C; LUCA.
GeneTree; ENSGT00730000110974; -.
HOGENOM; HOG000059587; -.
HOVERGEN; HBG060431; -.
InParanoid; P08138; -.
KO; K02583; -.
OMA; AQPCGAN; -.
OrthoDB; EOG091G0M0X; -.
PhylomeDB; P08138; -.
TreeFam; TF106466; -.
Reactome; R-HSA-193634; Axonal growth inhibition (RHOA activation).
Reactome; R-HSA-193648; NRAGE signals death through JNK.
Reactome; R-HSA-193670; p75NTR negatively regulates cell cycle via SC1.
Reactome; R-HSA-193681; Ceramide signalling.
Reactome; R-HSA-193692; Regulated proteolysis of p75NTR.
Reactome; R-HSA-205017; NFG and proNGF binds to p75NTR.
Reactome; R-HSA-205025; NADE modulates death signalling.
Reactome; R-HSA-205043; NRIF signals cell death from the nucleus.
Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
Reactome; R-HSA-209560; NF-kB is activated and signals survival.
Reactome; R-HSA-209563; Axonal growth stimulation.
SignaLink; P08138; -.
SIGNOR; P08138; -.
ChiTaRS; NGFR; human.
EvolutionaryTrace; P08138; -.
GeneWiki; Low-affinity_nerve_growth_factor_receptor; -.
GenomeRNAi; 4804; -.
PMAP-CutDB; P08138; -.
PRO; PR:P08138; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000064300; -.
CleanEx; HS_NGFR; -.
Genevisible; P08138; HS.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; NAS:ARUK-UCL.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
GO; GO:0015026; F:coreceptor activity; IDA:UniProtKB.
GO; GO:0005035; F:death receptor activity; IGI:ARUK-UCL.
GO; GO:0048406; F:nerve growth factor binding; ISS:UniProtKB.
GO; GO:0043121; F:neurotrophin binding; ISS:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; ISS:UniProtKB.
GO; GO:0004872; F:receptor activity; TAS:ProtInc.
GO; GO:0004871; F:signal transducer activity; TAS:ProtInc.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
GO; GO:0005031; F:tumor necrosis factor-activated receptor activity; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:BHF-UCL.
GO; GO:0097190; P:apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0007411; P:axon guidance; IBA:GO_Central.
GO; GO:1904646; P:cellular response to amyloid-beta; IDA:ARUK-UCL.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0006886; P:intracellular protein transport; ISS:UniProtKB.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
GO; GO:0050771; P:negative regulation of axonogenesis; TAS:Reactome.
GO; GO:1903588; P:negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis; IGI:BHF-UCL.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
GO; GO:0010977; P:negative regulation of neuron projection development; IBA:GO_Central.
GO; GO:0051402; P:neuron apoptotic process; IGI:ARUK-UCL.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0050772; P:positive regulation of axonogenesis; TAS:Reactome.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:BHF-UCL.
GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; TAS:Reactome.
GO; GO:2001273; P:regulation of glucose import in response to insulin stimulus; ISS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
CDD; cd13416; TNFRSF16; 1.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR000488; Death_domain.
InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
InterPro; IPR022325; TNFR_16.
InterPro; IPR034046; TNFRSF16_N.
Pfam; PF00531; Death; 1.
Pfam; PF00020; TNFR_c6; 2.
PRINTS; PR01966; TNFACTORR16.
SMART; SM00005; DEATH; 1.
SMART; SM00208; TNFR; 4.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50017; DEATH_DOMAIN; 1.
PROSITE; PS00652; TNFR_NGFR_1; 3.
PROSITE; PS50050; TNFR_NGFR_2; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Biological rhythms;
Complete proteome; Developmental protein; Differentiation;
Disulfide bond; Glycoprotein; Membrane; Neurogenesis; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 28
CHAIN 29 427 Tumor necrosis factor receptor
superfamily member 16.
/FTId=PRO_0000034591.
TOPO_DOM 29 250 Extracellular. {ECO:0000255}.
TRANSMEM 251 272 Helical. {ECO:0000255}.
TOPO_DOM 273 427 Cytoplasmic. {ECO:0000255}.
REPEAT 31 64 TNFR-Cys 1.
REPEAT 66 107 TNFR-Cys 2.
REPEAT 108 146 TNFR-Cys 3.
REPEAT 148 188 TNFR-Cys 4.
DOMAIN 344 421 Death. {ECO:0000255|PROSITE-
ProRule:PRU00064}.
REGION 326 341 Mediates interaction with KIDINS220.
{ECO:0000250}.
COMPBIAS 197 248 Ser/Thr-rich.
MOD_RES 311 311 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
/FTId=CAR_000231.
DISULFID 32 43 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 44 57 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 47 64 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 67 83 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 86 99 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 89 107 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 109 122 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 125 138 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 128 146 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 149 164 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 167 180 {ECO:0000255|PROSITE-ProRule:PRU00206}.
DISULFID 170 188 {ECO:0000255|PROSITE-ProRule:PRU00206}.
VAR_SEQ 1 94 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056850.
VARIANT 205 205 S -> L (in dbSNP:rs2072446).
/FTId=VAR_020010.
HELIX 336 338 {ECO:0000244|PDB:2N80}.
HELIX 341 351 {ECO:0000244|PDB:2N80}.
HELIX 358 366 {ECO:0000244|PDB:2N80}.
HELIX 370 377 {ECO:0000244|PDB:2N80}.
STRAND 379 381 {ECO:0000244|PDB:2N80}.
HELIX 382 390 {ECO:0000244|PDB:2N80}.
HELIX 398 409 {ECO:0000244|PDB:3EWV}.
HELIX 411 417 {ECO:0000244|PDB:2N80}.
TURN 418 420 {ECO:0000244|PDB:2N80}.
STRAND 421 423 {ECO:0000244|PDB:2N80}.
SEQUENCE 427 AA; 45183 MW; B09FA143FB3D625B CRC64;
MGAGATGRAM DGPRLLLLLL LGVSLGGAKE ACPTGLYTHS GECCKACNLG EGVAQPCGAN
QTVCEPCLDS VTFSDVVSAT EPCKPCTECV GLQSMSAPCV EADDAVCRCA YGYYQDETTG
RCEACRVCEA GSGLVFSCQD KQNTVCEECP DGTYSDEANH VDPCLPCTVC EDTERQLREC
TRWADAECEE IPGRWITRST PPEGSDSTAP STQEPEAPPE QDLIASTVAG VVTTVMGSSQ
PVVTRGTTDN LIPVYCSILA AVVVGLVAYI AFKRWNSCKQ NKQGANSRPV NQTPPPEGEK
LHSDSGISVD SQSLHDQQPH TQTASGQALK GDGGLYSSLP PAKREEVEKL LNGSAGDTWR
HLAGELGYQP EHIDSFTHEA CPVRALLASW ATQDSATLDA LLAALRRIQR ADLVESLCSE
STATSPV


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