RAIL-R3, also known as DcR1, was identified from EST data by two groups through searching for homologs of the TNFR1 death domain or the DR4 cysteine-rich domain (CRD).
Interacting protein(s): TRAIL (P7008F)
Related products: TNF-Receptor Superfamily
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Quick Specs
| Species: | Human |
| Catalog No.: | P7057F |
| Synonym: | CD263, TNFRSF10C, DCR1, LIT, MGC149501, MGC149502, TRID |
| Tag: | Mouse IgG2a |
| GenBank Accession: | NM_003841 |
| SwissPro Accession: | O14798 |
| Expression Host: | 293T |
| Construction: | Human TRAIL-R3 (S25-T161)-mouse IgG2a Fc |
| MW (calculated): | 42253.4 |
| MW (SDS-PAGE): | 45 Kd |
| Abs 0.1% (= 1 mg/ml): | 0.963 |
| Purity: | 95% |
Description
RAIL-R3, also known as DcR1, was identified from EST data by two groups through searching for homologs of the TNFR1 death domain or the DR4 cysteine-rich domain (CRD). TRAIL-R3 has a canonical cysteine-rich domain that is highly homologous to DR4 and DR5. Yet, it ends immediately after a short predicted transmembrane region. In addition, TRAIL-R3 contains five repeats rich in Thr, Ala, Pro, and Glu residues, also called TAPE repeat, immediately before the transmembrane region. The TAPE repeats are remarkably conserved diverging in only one out of the 15 aa positions. In addition, the TRAIL-R3 contains a carboxyl terminal stretch of 15 amino acids that is canonical for addition of GPI (glycosyl-phosphatidylinositol) anchor.
The TAPE repeats contains a significant number of O-glycosylation sites, as such while its apparent molecular weight (Mr) in SDS-PAGE (>180 kDa) is substantially larger than the expected 100 kDa. It is proposed that the TAPE repeats adapt an elongated, rigid structure facilitating expose of its ligand binding site away from the plane (therefore is more efficient for ligand binding) where the ligand-binding sites of DR4 and DR5 are present. While the transcripts of DR4 and DR5 can be detected in many tissues, those of TRAIL-R3 are restricted to skeletal muscle, peripheral blood lymphocytes and spleen.
As expected, as no death domain is present with its intracellular domain, TRAIL-R3 does not induce cytotoxic effect. In fact, overexpression of TRAIL-R3 prevents TRAIL-sensitive cells from apoptosis and cells can be re-sensitized by phospholipase treatment –consistent with the notion that TRAIL-R3 is GPI-anchored.
Amino Acid Sequence.
References
1. Sheridan JP, Marsters SA, Pitti RM, Gurney A, Skubatch M, et al. (1997) Control of TRAIL-induced apoptosis by a family of signaling and decoy receptors. Science 277:818-821.
2. Schneider P, Bodmer JL, Thome M, Hofmann K, Holler N, Tschopp J. (1997) Characterization of two receptors for TRAIL. FEBS Lett. 416:329-334.
3. Pan G, Ni J, Wei YF, Yu G, Gentz R, Dixit VM. (1997) An antagonist decoy receptor and a death domain-containing receptor for TRAIL. Science 277:815-818.
4. Falschlehner C, Emmerich CH, Gerlach B, Walczak H. (2007) TRAIL signalling: decisions between life and death. Int J Biochem Cell Biol. 39:1462-1475.