|CD93||GR11, C1qR1, C1qRP (C1q receptor precursor)|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
Type 1 glycoprotein
|126 / 126|
110 / 110
|CD93 is expressed on NK cells, monocytes, granulocytes, AML blasts, myeloid cell lines, platelets and endothelial cells. It is not expressed on lymphocytes or red blood cells.|
|MOLECULAR FAMILY NAME|
CD93 is a single-pass type-1 O-sialoglycoprotein. It contains a 21 aa signal sequence, an 652 aa extracellular domain which contains a N-terminal C-type carbohydrate lectin domain followed by 5 epidermal growth factor (EGF-like) domains 3 of which may be calcium-binding domains, a 22 aa transmembrane domain and a 46 aa cytoplasmic domain which contains a potential tyrosine kinase phosphorylation site. Treatment of CD93+ with O-sialoglycoprotease selectively cleaves O-sialylated peptides and reduces the binding of all 4 anti-CD93 mAbs by greater than 90%. This suggests that CD93 is an O-sialoglycoprotein.
POST-TRANSCRIPTIONAL MODIFICATION: No information.
CD93 is N- and O-glycosylated.
|LIGANDS AND MOLECULES ASSOCIATED WITH CD93: No information.|
|CD93 was origionally identified as a myeloid cell-specific marker. It was once thought top be a receptor for C1q, but now is thought to be involved in intercellular adhesion and in the clearance of apoptotic cells. The intracellular cytoplasmic tail has been found to interact with moesin, a protein known to play a role in linking transmembrane proteins to the cytoskeleton and in the remodeling of the sktoskeleton.|
BIOCHEMICAL ACTIVITY: No information.
DISEASE RELEVANCE AND FUNCTION OF CD93 IN INTACT ANIMAL: No information.
|MOLECULAR INTERACTIONS -|
PROTEINS AND DNA ELEMENT WHICH REGULATE TRANSCRIPTION OF CD93: No information.
SUBSTRATES: No information.
ENZYMES WHICH MODIFY CD93: No information.
Database accession numbers
Revised June 25, 2008