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Entry version 187 (13 Nov 2019)
Sequence version 1 (01 Apr 1988)
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Protein

Tumor necrosis factor receptor superfamily member 16

Gene

Ngfr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Low affinity receptor which can bind to NGF, BDNF, NTF3, and NTF4 (PubMed:3027580, PubMed:15131306, PubMed:18596692). Forms a heterodimeric receptor with SORCS2 that binds the precursor forms of NGF, BDNF and NTF3 with high affinity, and has much lower affinity for mature NGF and BDNF (PubMed:24908487, PubMed:22155786). In response to proNGF binding, the heterodimeric receptor with SORCS2 activates a signaling cascade that leads to decreased Rac activity, reorganization of the actin cytoskeleton and neuronal growth cone collapse (PubMed:22155786). Plays an important role in differentiation and survival of specific neuronal populations during development (By similarity). Can mediate cell survival as well as cell death of neural cells (PubMed:10514511, PubMed:10985348, PubMed:24908487). Plays a role in the inactivation of RHOA (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 (By similarity). 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 (By similarity).By similarity7 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, Receptor
Biological processApoptosis, Biological rhythms, Differentiation, Neurogenesis

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-193634 Axonal growth inhibition (RHOA activation)
R-RNO-193692 Regulated proteolysis of p75NTR
R-RNO-205017 NFG and proNGF binds to p75NTR
R-RNO-205025 NADE modulates death signalling
R-RNO-205043 NRIF signals cell death from the nucleus
R-RNO-209543 p75NTR recruits signalling complexes
R-RNO-209560 NF-kB is activated and signals survival
R-RNO-209563 Axonal growth stimulation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Ngfr
Synonyms:Tnfrsf16
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3177 Ngfr

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini30 – 253ExtracellularCuratedAdd BLAST224
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei254 – 274Helical1 PublicationAdd BLAST21
Topological domaini275 – 425CytoplasmicCuratedAdd BLAST151

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi61N → D: Loss of a glycosylation site. 1 Publication1
Mutagenesisi257C → A: Alters mode of dimerization, but does not abolish dimerization. 1 Publication1
Mutagenesisi257C → I: No effect on dimerization. Loss of dimerization; when associated with I-266. 1 Publication1
Mutagenesisi262A → I: No effect on dimerization. 1 Publication1
Mutagenesisi266G → I: No effect on dimerization. Loss of dimerization; when associated with I-257. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 29Add BLAST29
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003459330 – 425Tumor necrosis factor receptor superfamily member 16Add BLAST396

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi33 ↔ 44PROSITE-ProRule annotationCombined sources
Disulfide bondi45 ↔ 58PROSITE-ProRule annotationCombined sources
Disulfide bondi48 ↔ 65PROSITE-ProRule annotationCombined sources
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi61N-linked (GlcNAc...) asparagineCombined sources1 Publication1
Disulfide bondi68 ↔ 84PROSITE-ProRule annotationCombined sources
Glycosylationi71N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi87 ↔ 100PROSITE-ProRule annotationCombined sources
Disulfide bondi90 ↔ 108PROSITE-ProRule annotationCombined sources
Disulfide bondi110 ↔ 123PROSITE-ProRule annotationCombined sources
Disulfide bondi126 ↔ 139PROSITE-ProRule annotationCombined sources
Disulfide bondi129 ↔ 147PROSITE-ProRule annotationCombined sources
Disulfide bondi150 ↔ 165PROSITE-ProRule annotationCombined sources
Disulfide bondi168 ↔ 181PROSITE-ProRule annotationCombined sources
Disulfide bondi171 ↔ 189PROSITE-ProRule annotationCombined sources
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei312PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Subject to intramembrane proteolytic cleavage by the gamma-secretase complex, giving rise to an intracellular fragment that is rapidly degraded via the proteasome.1 Publication
N- and O-glycosylated.1 Publication
Phosphorylated on serine residues.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P07174

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P07174

PRoteomics IDEntifications database

More...
PRIDEi
P07174

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07174

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P07174

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P07174

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P07174

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; disulfide-linked (PubMed:27056327). Heterodimer with SORCS2 (PubMed:27457814, PubMed:22155786, PubMed:24908487). The extracellular domains of the heterodimer bind NGF (PubMed:22155786, PubMed:24908487). The cytoplasmic region of the heterodimer binds TRIO. NGF binding mediates dissociation of TRIO from the receptor complex (PubMed:22155786).

Interacts with RTN4R (By similarity).

Interacts with TRAF2, TRAF4 and TRAF6 (PubMed:10514511).

Interacts with PTPN13 and RANBP9.

Interacts through TRAF6 with SQSTM1 which bridges NGFR to NTRK1 (By similarity).

Interacts with BEX1 (PubMed:16498402).

Interacts with BEX3 (By similarity).

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 (PubMed:11150334, PubMed:15378608).

Interacts (via death domain) with RAB31 (By similarity).

Interacts with NTRK2; may regulate the ligand specificity of the NTRK2 receptor (PubMed:9927421).

Interacts with LINGO1 (By similarity).

Interacts with NRADD (PubMed:12095158).

Interacts with MAGED1; the interaction antagonizes the association NGFR:NTRK1 (PubMed:10985348).

Interacts (via death domain) with ARHGDIA and RIPK2 (By similarity).

By similarity11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
246737, 13 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P07174

Database of interacting proteins

More...
DIPi
DIP-5715N

Protein interaction database and analysis system

More...
IntActi
P07174, 20 interactors

Molecular INTeraction database

More...
MINTi
P07174

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000007268

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1425
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P07174

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P07174

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati32 – 65TNFR-Cys 1Add BLAST34
Repeati67 – 108TNFR-Cys 2Add BLAST42
Repeati109 – 147TNFR-Cys 3Add BLAST39
Repeati149 – 189TNFR-Cys 4Add BLAST41
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini354 – 419DeathPROSITE-ProRule annotationAdd BLAST66

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni327 – 342Mediates interaction with KIDINS220Add BLAST16

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi198 – 249Ser/Thr-richAdd BLAST52

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Death domain is responsible for interaction with RANBP9. It also mediates interaction with ARHGDIA and RIPK2 (By similarity).By similarity1 Publication
The extracellular domain is responsible for interaction with NTRK1.1 Publication

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IQFC Eukaryota
ENOG4111F3C LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000059587

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07174

KEGG Orthology (KO)

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KOi
K02583

Database of Orthologous Groups

More...
OrthoDBi
757160at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P07174

Family and domain databases

Conserved Domains Database

More...
CDDi
cd13416 TNFRSF16, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain
IPR001368 TNFR/NGFR_Cys_rich_reg
IPR041448 TNFR16_TM
IPR022325 TNFR_16
IPR034046 TNFRSF16_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00531 Death, 1 hit
PF18422 TNFR_16_TM, 1 hit
PF00020 TNFR_c6, 3 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01966 TNFACTORR16

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00005 DEATH, 1 hit
SM00208 TNFR, 4 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47986 SSF47986, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50017 DEATH_DOMAIN, 1 hit
PS00652 TNFR_NGFR_1, 3 hits
PS50050 TNFR_NGFR_2, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P07174-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRRAGAACSA MDRLRLLLLL ILGVSSGGAK ETCSTGLYTH SGECCKACNL
60 70 80 90 100
GEGVAQPCGA NQTVCEPCLD NVTFSDVVSA TEPCKPCTEC LGLQSMSAPC
110 120 130 140 150
VEADDAVCRC AYGYYQDEET GHCEACSVCE VGSGLVFSCQ DKQNTVCEEC
160 170 180 190 200
PEGTYSDEAN HVDPCLPCTV CEDTERQLRE CTPWADAECE EIPGRWIPRS
210 220 230 240 250
TPPEGSDSTA PSTQEPEVPP EQDLVPSTVA DMVTTVMGSS QPVVTRGTTD
260 270 280 290 300
NLIPVYCSIL AAVVVGLVAY IAFKRWNSCK QNKQGANSRP VNQTPPPEGE
310 320 330 340 350
KLHSDSGISV DSQSLHDQQT HTQTASGQAL KGDGNLYSSL PLTKREEVEK
360 370 380 390 400
LLNGDTWRHL AGELGYQPEH IDSFTHEACP VRALLASWGA QDSATLDALL
410 420
AALRRIQRAD IVESLCSEST ATSPV
Length:425
Mass (Da):45,433
Last modified:April 1, 1988 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB2E152D94D3827F8
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V6P1G3V6P1_RAT
Nerve growth factor receptor (TNFR ...
Ngfr rCG_34900
425Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X05137 mRNA Translation: CAA28783.1
X61269 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

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PIRi
A26431

NCBI Reference Sequences

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RefSeqi
NP_036742.2, NM_012610.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
24596

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:24596

UCSC genome browser

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UCSCi
RGD:3177 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05137 mRNA Translation: CAA28783.1
X61269 Genomic DNA No translation available.
PIRiA26431
RefSeqiNP_036742.2, NM_012610.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NGRNMR-A334-418[»]
1SG1X-ray2.40X30-190[»]
2MICNMR-A/B245-284[»]
2MJONMR-A/B245-284[»]
3BUKX-ray2.60C/D30-190[»]
3IJ2X-ray3.75X/Y30-190[»]
4F42X-ray2.38A334-418[»]
4F44X-ray2.40A/B334-418[»]
SMRiP07174
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi246737, 13 interactors
CORUMiP07174
DIPiDIP-5715N
IntActiP07174, 20 interactors
MINTiP07174
STRINGi10116.ENSRNOP00000007268

PTM databases

iPTMnetiP07174
PhosphoSitePlusiP07174
SwissPalmiP07174

Proteomic databases

jPOSTiP07174
PaxDbiP07174
PRIDEiP07174

Genome annotation databases

GeneIDi24596
KEGGirno:24596
UCSCiRGD:3177 rat

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
4804
RGDi3177 Ngfr

Phylogenomic databases

eggNOGiENOG410IQFC Eukaryota
ENOG4111F3C LUCA
HOGENOMiHOG000059587
InParanoidiP07174
KOiK02583
OrthoDBi757160at2759
PhylomeDBiP07174

Enzyme and pathway databases

ReactomeiR-RNO-193634 Axonal growth inhibition (RHOA activation)
R-RNO-193692 Regulated proteolysis of p75NTR
R-RNO-205017 NFG and proNGF binds to p75NTR
R-RNO-205025 NADE modulates death signalling
R-RNO-205043 NRIF signals cell death from the nucleus
R-RNO-209543 p75NTR recruits signalling complexes
R-RNO-209560 NF-kB is activated and signals survival
R-RNO-209563 Axonal growth stimulation

Miscellaneous databases

EvolutionaryTraceiP07174
PMAP-CutDBiP07174

Protein Ontology

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PROi
PR:P07174

Family and domain databases

CDDicd13416 TNFRSF16, 1 hit
InterProiView protein in InterPro
IPR011029 DEATH-like_dom_sf
IPR000488 Death_domain
IPR001368 TNFR/NGFR_Cys_rich_reg
IPR041448 TNFR16_TM
IPR022325 TNFR_16
IPR034046 TNFRSF16_N
PfamiView protein in Pfam
PF00531 Death, 1 hit
PF18422 TNFR_16_TM, 1 hit
PF00020 TNFR_c6, 3 hits
PRINTSiPR01966 TNFACTORR16
SMARTiView protein in SMART
SM00005 DEATH, 1 hit
SM00208 TNFR, 4 hits
SUPFAMiSSF47986 SSF47986, 1 hit
PROSITEiView protein in PROSITE
PS50017 DEATH_DOMAIN, 1 hit
PS00652 TNFR_NGFR_1, 3 hits
PS50050 TNFR_NGFR_2, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTNR16_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P07174
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: April 1, 1988
Last modified: November 13, 2019
This is version 187 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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