CD263 TNFRSF10c (tumor necrosis factor receptor superfamily member 10c), LIT, TRID, TRAIL-R3, DcR1
Molecule TypeAntigen ExpressionMolecular Weight
Min / Max
Non-lineage Restricted Molecule
GPI anchor
Peripheral blood
Lymphocyte
Placenta
Heart
Lung
Skeletal muscle
Spleen
NK Cell
Monocyte
Macrophage
Granulocyte
Epithelium
Hepatocyte
T Lymphocyte
B Lymphocyte
Brain
Neuron
Bile duct
65 / 65

Expression
CD263 is highly expressed in T and B lymphocytes, peripheral blood lymphocytes, NK cells, macrophages, monocytes, granulocytes, spleen, skeletal muscle, placenta, lung and heart.  Expression is higher in normal tissues but not in most cancer tumor cell lines.   Expression is found in hepatocytes and bile duct epithelium, neurons in the brain, germ and Leydig cells. 

Structure
MOLECULAR FAMILY NAME: Belongs to the tumor necrosis factor receptor family.

CD263 is a GPI-linked cell surface glycoprotein.  It contains a 23 aa N-terminal signal sequence, an extracellular domain which  contains 3 TNFR cysteine-rich repeats, 5 tandem TAPE repeats and 3 potential N-glycosylation sites and a transmembrane domain.  It lacks a cytoplasmic domain.  The signal sequence is a Has a N-terminal and a 23 aa propeptide at the C terminus which is removed in a mature form leaving a 190 aa mature protein.  CD263 is a plasma membrane-bound protein and appears to be glycosylphosphatidylinositol-linked. 

MOLECULAR MASS

POST-TRANSCRIPTIONAL MODIFICATION: No information.

POST-TRANSLATIONAL MODIFICATION

CD263 is N- and O-glycosylated.
      

Ligands

LIGANDS AND MOLECULE ASSOCIATED WITH CD263

CD263 binds CD253 (TRAIL).



Function
CD263 is a membrane receptor for the cytotoxic ligand CD253 and is thought to act as a decoy receptor.   It does not have a cytoplasmic death domain, and therefore is not capable of inducing apoptosis and is thought to function as an antagonistic receptor that protects cells from TRAIL-induced apoptosis by competing for binding with other TRAIL receptors.  Unlike other TRAIL receptors, CD261 (TRAIL-R1) and CD262 (TRAIL-R2), CD263 (TRAIL-R3) lacks the death domain and cannot transmit apoptotic signal to the cell upon TRAIL binding.  Normal tissues that express CD263 and CD264 (TRAIL-R4) are resistant to TRAIL-induced apoptosis even in the presence of apoptoic signaling receptors CD261 and CD262.  The role of CD263 in malignant tissue is unclear and various studies reveal conflicting results as to its importance in the control of TRAIL-mediated cell death in tumors. The gene for CD263 was found to be a p53-regulated DNA damage-inducible gene. 

BIOCHEMICAL ACTIVITY: No information.

DISEASE RELEVANCE AND FUNCTION OF CD263 IN INTACT ANIMAL

Expression is in many normal tissues but not in most cancer cell lines which may explain the specific sensitivity of cancer cells to the apoptosis-inducing activity of CD263. 



Comments
MOLECULAR INTERACTIONS-
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF CD263: No information.

SUBSTRATES: No information.

ENZYMES WHICH MODIFY CD263: No information.

ADDITIONAL INSIGHTS

For further information see Degli-Esposti, M. A. et al (1997) J. Exp. Med. 186: 1165-1170.


Database accession numbers
AnimalPIRSWISSPROTEMGBL/GENBANK
 
HumanEntrezgene 8794O14798
Antibodies

Revised June 25, 2008


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