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Q9EPU5 (TNR21_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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 21
Alternative name(s):
Death receptor 6
CD_antigen=CD358
Gene names
Name:Tnfrsf21
Synonyms:Dr6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May activate NF-kappa-B and promote apoptosis By similarity. May activate JNK and be involved in T-cell differentiation. Required for both normal cell body death and axonal pruning. Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP). N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6). Ref.4 Ref.5

Subunit structure

Associates with TRADD By similarity. Interacts with N-APP. Ref.5

Subcellular location

Membrane; Single-pass type I membrane protein Probable.

Tissue specificity

Ubiquitous. Highly expressed in adult spleen, thymus, testis, prostate, ovary, small intestine, colon, brain, lung and kidney, and in fetal brain, liver and lung. Detected at lower levels in adult peripheral blood leukocytes, lung, and in fetal muscle, heart, kidney, small intestine and skin. Detected in T-cells, B-cells and monocytes. In T-cells expression is highest in Th0 cells, intermediate in Th2 cells and lower in Th1 cells. Expressed at low levels in proliferating progenitors in the spinal cord, but is highly expressed by differentiating neurons within the spinal cord and adjacent dorsal root ganglia. Expressed by developing neurons as they differentiate and enter a pro-apoptotic state. Expressed by both cell bodies and axons. Ref.5

Induction

Activated by a cleaved N-terminal fragment of APP (N-APP). Trophic-factor deprivation triggers beta-secretase-dependent cleavage of APP to release N-APP. Ref.5

Sequence similarities

Contains 1 death domain.

Contains 4 TNFR-Cys repeats.

Caution

It is uncertain whether Met-1 or Met-25 is the initiator.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentMembrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processneuron apoptotic process

Inferred from mutant phenotype Ref.5. Source: UniProtKB

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentaxon

Inferred from direct assay Ref.5. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: Compara

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4141 Potential
Chain42 – 655614Tumor necrosis factor receptor superfamily member 21
PRO_0000034603

Regions

Topological domain42 – 349308Extracellular Potential
Transmembrane350 – 37021Helical; Potential
Topological domain371 – 655285Cytoplasmic Potential
Repeat50 – 8839TNFR-Cys 1
Repeat90 – 13142TNFR-Cys 2
Repeat133 – 16735TNFR-Cys 3
Repeat170 – 21142TNFR-Cys 4
Domain415 – 49884Death

Amino acid modifications

Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation1411N-linked (GlcNAc...) Potential
Glycosylation2521N-linked (GlcNAc...) Potential
Glycosylation2571N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation2891N-linked (GlcNAc...) Potential
Disulfide bond67 ↔ 80 By similarity
Disulfide bond70 ↔ 88 By similarity
Disulfide bond91 ↔ 106 By similarity
Disulfide bond109 ↔ 123 By similarity
Disulfide bond113 ↔ 131 By similarity
Disulfide bond133 ↔ 144 By similarity
Disulfide bond150 ↔ 168 By similarity
Disulfide bond171 ↔ 186 By similarity
Disulfide bond192 ↔ 211 By similarity

Experimental info

Sequence conflict3521W → L in AAG38115. Ref.1
Sequence conflict5231M → I in AAH16420. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9EPU5 [UniParc].

Last modified May 27, 2002. Version 2.
Checksum: 5EC7C51C7C99EFF7

FASTA65571,983
        10         20         30         40         50         60 
MGTRASSITA LASCSRTAGQ VGATMVAGSL LLLGFLSTIT AQPEQKTLSL PGTYRHVDRT 

        70         80         90        100        110        120 
TGQVLTCDKC PAGTYVSEHC TNMSLRVCSS CPAGTFTRHE NGIERCHDCS QPCPWPMIER 

       130        140        150        160        170        180 
LPCAALTDRE CICPPGMYQS NGTCAPHTVC PVGWGVRKKG TENEDVRCKQ CARGTFSDVP 

       190        200        210        220        230        240 
SSVMKCKAHT DCLGQNLEVV KPGTKETDNV CGMRLFFSST NPPSSGTVTF SHPEHMESHD 

       250        260        270        280        290        300 
VPSSTYEPQG MNSTDSNSTA SVRTKVPSGI EEGTVPDNTS STSGKEGTNR TLPNPPQVTH 

       310        320        330        340        350        360 
QQAPHHRHIL KLLPSSMEAT GEKSSTAIKA PKRGHPRQNA HKHFDINEHL PWMIVLFLLL 

       370        380        390        400        410        420 
VLVLIVVCSI RKSSRTLKKG PRQDPSAIVE KAGLKKSLTP TQNREKWIYY RNGHGIDILK 

       430        440        450        460        470        480 
LVAAQVGSQW KDIYQFLCNA SEREVAAFSN GYTADHERAY AALQHWTIRG PEASLAQLIS 

       490        500        510        520        530        540 
ALRQHRRNDV VEKIRGLMED TTQLETDKLA LPMSPSPLSP SPMPSPNVKL ENSTLLTVEP 

       550        560        570        580        590        600 
SPLDKNKCFF VDESEPLLRC DSTSSGSSAL SRNGSFITKE KKDTVLRQVR LDPCDLQPIF 

       610        620        630        640        650 
DDMLHILNPE ELRVIEEIPQ AEDKLDRLFE IIGVKSQEAS QTLLDSVYSH LPDLL

« Hide

References

« Hide 'large scale' references
[1]"Mouse DR6: mouse homolog of human TNFR-related death receptor-6 (DR6)."
Isogai D., Ichino M., Yoshinari M., Yamaura A., Kurokawa F., Minami M.
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Kidney.
[2]"Murine DR6: murine TNFR-related death receptor-6."
Kim V., Machleidt T., Shi W.-X., Wang X., Cai Z.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Kidney.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[4]"Impaired c-Jun amino terminal kinase activity and T cell differentiation in death receptor 6-deficient mice."
Zhao H., Yan M., Wang H., Erickson S., Grewal I.S., Dixit V.M.
J. Exp. Med. 194:1441-1448(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"APP binds DR6 to trigger axon pruning and neuron death via distinct caspases."
Nikolaev A., McLaughlin T., O'Leary D.D.M., Tessier-Lavigne M.
Nature 457:981-989(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY, INTERACTION WITH APP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF322069 mRNA. Translation: AAG38115.1.
AY043489 mRNA. Translation: AAK74193.1.
BC016420 mRNA. Translation: AAH16420.1.
IPIIPI00110366.
RefSeqNP_848704.1. NM_178589.3.
UniGeneMm.200792.

3D structure databases

ProteinModelPortalQ9EPU5.
SMRQ9EPU5. Positions 52-212, 569-655.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-59733N.

PTM databases

PhosphoSiteQ9EPU5.

Proteomic databases

PaxDbQ9EPU5.
PRIDEQ9EPU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024708; ENSMUSP00000024708; ENSMUSG00000023915.
GeneID94185.
KEGGmmu:94185.

Organism-specific databases

CTD27242.
MGIMGI:2151075. Tnfrsf21.

Phylogenomic databases

eggNOGNOG42658.
GeneTreeENSGT00680000099809.
HOGENOMHOG000136852.
HOVERGENHBG054218.
InParanoidQ9EPU5.
KOK05157.
OMAGLKKSMT.
OrthoDBEOG47SSDR.

Gene expression databases

ArrayExpressQ9EPU5.
BgeeQ9EPU5.
GenevestigatorQ9EPU5.
GermOnlineENSMUSG00000023915. Mus musculus.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR001368. TNFR/NGFR_Cys_rich_reg.
IPR022330. TNFR_21.
[Graphical view]
PfamPF00531. Death. 1 hit.
[Graphical view]
PRINTSPR01971. TNFACTORR21.
SMARTSM00005. DEATH. 1 hit.
SM00208. TNFR. 4 hits.
[Graphical view]
SUPFAMSSF47986. DEATH_like. 1 hit.
PROSITEPS50017. DEATH_DOMAIN. 1 hit.
PS00652. TNFR_NGFR_1. 1 hit.
PS50050. TNFR_NGFR_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTNFRSF21. mouse.
NextBio352147.
SOURCESearch...

Entry information

Entry nameTNR21_MOUSE
AccessionPrimary (citable) accession number: Q9EPU5
Secondary accession number(s): Q91W77, Q91XH9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 27, 2002
Last modified: May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

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