Tumor necrosis factor receptor superfamily member 1A precursor

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Reviewed, UniProtKB/Swiss-Prot P25118 (TNR1A_MOUSE)

Last modified June 16, 2009. Version 99. History...

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

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Names and origin

Protein names

Recommended name:
    Tumor necrosis factor receptor superfamily member 1A
Alternative name(s):
    p60
    TNF-R1
    TNF-RI
    TNFR-I
    p55
    CD_antigen=CD120a

Gene names

Name:	Tnfrsf1a
Synonyms:	Tnfr-1, Tnfr1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	454 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis By similarity.
Subunit structure	Binding of TNF to the extracellular domain leads to homotrimerization. The aggregated death domains provide a novel molecular interface that interacts specifically with the death domain of TRADD. Various TRADD-interacting proteins such as TRAFS, RIPK1 and possibly FADD, are recruited to the complex by their association with TRADD. This complex activates at least two distinct signaling cascades, apoptosis and NF-kappa-B signaling. Interacts with BAG4, BRE, FEM1B, GRB2, SQSTM1 and TRPC4AP. Interacts with DAB2IP By similarity.
Subcellular location	Membrane; Single-pass type I membrane protein.
Domain	Both the cytoplasmic membrane-proximal region and the C-terminal region containing the death domain are involved in the interaction with TRPC4AP.
Sequence similarities	Contains 1 death domain. Contains 4 TNFR-Cys repeats.

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Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Membrane
Domain	Repeat Signal Transmembrane
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW cytokine-mediated signaling pathway Inferred from mutant phenotype. Source: MGI inflammatory response Inferred from mutant phenotype. Source: MGI positive regulation of inflammatory response Inferred from mutant phenotype. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: MGI prostaglandin metabolic process Traceable author statement. Source: MGI
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane raft Inferred from direct assay. Source: UniProtKB plasma membrane Traceable author statement. Source: MGI
Molecular function	tumor necrosis factor receptor activity Ref.2 Inferred from mutant phenotype. Source: MGI
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
Kars	Q99MN1	1	EBI-518014,EBI-960115

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

Potential

Chain

22 – 454

433

Tumor necrosis factor receptor superfamily member 1A

PRO_0000034545

Regions

Topological domain

22 – 212

191

Extracellular Potential

Transmembrane

213 – 235

Potential

Topological domain

236 – 454

219

Cytoplasmic Potential

Repeat

43 – 82

TNFR-Cys 1

Repeat

83 – 125

TNFR-Cys 2

Repeat

126 – 166

TNFR-Cys 3

Repeat

167 – 196

TNFR-Cys 4

Domain

356 – 441

Death

Region

339 – 349

N-SMase activation domain (NSD)

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

151

N-linked (GlcNAc...) Potential

Glycosylation

202

N-linked (GlcNAc...) Potential

Disulfide bond

44 ↔ 58

By similarity

Disulfide bond

59 ↔ 72

By similarity

Disulfide bond

62 ↔ 81

By similarity

Disulfide bond

84 ↔ 99

By similarity

Disulfide bond

102 ↔ 117

By similarity

Disulfide bond

105 ↔ 125

By similarity

Disulfide bond

127 ↔ 143

By similarity

Disulfide bond

146 ↔ 158

By similarity

Disulfide bond

149 ↔ 166

By similarity

Disulfide bond

168 ↔ 179

By similarity

Disulfide bond

182 ↔ 195

By similarity

Disulfide bond

185 ↔ 191

By similarity

Experimental info

Sequence conflict

394

R → G in AAA40465. Ref.6

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Sequences

Sequence

Length

Mass (Da)

Tools

P25118-1 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 0710C2E8C3C2B6D9
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FASTA

454

50,130

        10         20         30         40         50         60 
MGLPTVPGLL LSLVLLALLM GIHPSGVTGL VPSLGDREKR DSLCPQGKYV HSKNNSICCT 

        70         80         90        100        110        120 
KCHKGTYLVS DCPSPGRDTV CRECEKGTFT ASQNYLRQCL SCKTCRKEMS QVEISPCQAD 

       130        140        150        160        170        180 
KDTVCGCKEN QFQRYLSETH FQCVDCSPCF NGTVTIPCKE TQNTVCNCHA GFFLRESECV 

       190        200        210        220        230        240 
PCSHCKKNEE CMKLCLPPPL ANVTNPQDSG TAVLLPLVIL LGLCLLSFIF ISLMCRYPRW 

       250        260        270        280        290        300 
RPEVYSIICR DPVPVKEEKA GKPLTPAPSP AFSPTSGFNP TLGFSTPGFS SPVSSTPISP 

       310        320        330        340        350        360 
IFGPSNWHFM PPVSEVVPTQ GADPLLYESL CSVPAPTSVQ KWEDSAHPQR PDNADLAILY 

       370        380        390        400        410        420 
AVVDGVPPAR WKEFMRFMGL SEHEIERLEM QNGRCLREAQ YSMLEAWRRR TPRHEDTLEV 

       430        440        450 
VGLVLSKMNL AGCLENILEA LRNPAPSSTT RLPR

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of cDNAs for two distinct murine tumor necrosis factor receptors demonstrate one receptor is species specific." Lewis M., Tartaglia L.A., Lee A., Bennett G.L., Rice G.C., Wong G.H., Chen E.Y., Goeddel D.V. Proc. Natl. Acad. Sci. U.S.A. 88:2830-2834(1991) [PubMed: 1849278] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Molecular cloning and expression of the type 1 and type 2 murine receptors for tumor necrosis factor." Goodwin R.G., Anderson D., Jerzy R., Davis T., Brannan C.I., Copeland N.G., Jenkins N.A., Smith C.A. Mol. Cell. Biol. 11:3020-3026(1991) [PubMed: 1645445] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning, expression and cross-linking analysis of the murine p55 tumor necrosis factor receptor." Barrett K., Taylor-Fishwick D.A., Cope A.P., Kissonerghis A.M., Gray P.W., Feldmann M., Foxwell B.M.J. Eur. J. Immunol. 21:1649-1656(1991) [PubMed: 1647956] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Molecular cloning and expression of the mouse Tnf receptor type b." Rothe J.G., Brockhaus M., Gentz R., Lesslauer W. Immunogenetics 34:338-340(1991) [PubMed: 1657766] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Spleen.
[5]	"Nucleotide sequence of the TNF type I receptor from a mouse endothelioma cell line." Bebo B.F., Linthicum D.S. Immunogenetics 39:450-451(1994) [PubMed: 8188324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Genomic organization and promoter function of the murine tumor necrosis factor receptor beta gene." Rothe J., Bluethmann H., Gentz R., Lesslauer W., Steinmetz M. Mol. Immunol. 30:165-175(1993) [PubMed: 8381516] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C3H/He. Tissue: Mesenchymal cell.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	M60468 mRNA. Translation: AAA39751.1. M59377 mRNA. Translation: AAA40464.1. X59238 mRNA. Translation: CAA41922.1. X57796 mRNA. Translation: CAA40936.1. L26349 mRNA. Translation: AAA59361.1. M76656, M88067, M76655 Genomic DNA. Translation: AAA40465.1. BC004599 mRNA. Translation: AAH04599.1. BC052675 mRNA. Translation: AAH52675.1.
IPI	IPI00317228.
PIR	GQMST1. A38634.
RefSeq	NP_035739.2.
UniGene	Mm.1258 Mm.474976
3D structure databases
HSSP	HSSP built from PDB template 1ICH based on UniProtKB P19438.
SMR	P25118. Positions 41-197, 357-441.
ModBase	Search...
Protein-protein interaction databases
IntAct	P25118. 19 interactions.
PTM databases
PhosphoSite	P25118.
Genome annotation databases
Ensembl	ENSMUSG00000030341. Mus musculus. [Contig view]
GeneID	21937.
KEGG	mmu:21937.
Organism-specific databases
MGI	MGI:1314884. Tnfrsf1a.
Phylogenomic databases
HOGENOM	P25118.
HOVERGEN	P25118.
OMA	P25118. CGCRKNQ.
Gene expression databases
Bgee	P25118.
GermOnline	ENSMUSG00000030341. Mus musculus.
Family and domain databases
InterPro	IPR000488. Death. IPR011029. DEATH-like. IPR001368. TNFR_Cys_rich_reg. [Graphical view]
Gene3D	G3DSA:1.10.533.10. DEATH_like. 1 hit.
Pfam	PF00531. Death. 1 hit. PF00020. TNFR_c6. 3 hits. [Graphical view]
SMART	SM00005. DEATH. 1 hit. SM00208. TNFR. 4 hits. [Graphical view]
PROSITE	PS50017. DEATH_DOMAIN. 1 hit. PS00652. TNFR_NGFR_1. 3 hits. PS50050. TNFR_NGFR_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	301546.
SOURCE	Search...

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Entry information

Entry name

TNR1A_MOUSE

Accession

Primary (citable) accession number: P25118

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	May 1, 1992
Last modified:	June 16, 2009
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents