|CD315||PTGFRN (prostaglandin F2 receptor negative), FPRP, CD9P-1, SMAP-6, KIAA1436|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
Type 1 glycoprotein
|135 / 135|
|CD315 is expressed on B cell subsets, activated monocytes, endothelial and epithelial cells, hepatocytes and megakaryocytes. Expression is detected in the ovary and lung. There is expression in keratinocytes and faintly in salivary glands but not in other tissues. There is a high expression in cancer cell lines derived from the colon or fibrosarcoma but not in their normal cell counterparts.|
|MOLECULAR FAMILY NAME: Belongs to the immunoglobulin gene family.|
CD315 is a single-pass type-1 854 aa glycoprotein. It contains a 25 aa signal sequence, an 807 aa extracellular domain which contains 6 Ig-V-type domains and 9 potential N-linked glycosylation sites, a 21 aa transmembrane domain and a 26 aa intracellular cytoplasmic domain. CD315 is a member of a novel Ig-like protein subfamily known as EWI (glutamine-tryptophan-isoleucine) with the Ig gene superfamily. Other members of this family include CD101, IgSF3 and CD316 and are characterized by a CxxxEWI motif not found in other Ig proteins, extracellular domains composed exclusively of V-type Ig-like domain and short cytoplasmic domains. The distal 2 Ig-like domains have the greatest homology between members of the EWI family. A stretch of basic charged amino acids in the cytoplasmic domain may act as binding sites for ERM proteins that are linked to the actin cytoskeletal.
POST-TRANSCRIPTIONAL MODIFICATION: No information.
CD315 has 9 potential N-linked glycosylation sites.
|LIGANDS AND MOLECULE ASSOCIATED WITH CD315|
CD315 seems to interact with CD63, CD82 and CD151.
|CD315 has been shown to associate specifically with CD81 and CD9 but not with other tetraspanin molecules. Recent studies have demonstrated that CD315 in association with CD81 is involved in regulating cell moltility and polarity. It seems to also interact with CD63, CD82, and CD151. The rat CD315 molecule was found to reduce the number of prostaglandin F2 (PGF-2) α-binding sites on COS cells transfected with the PGF-2 α receptor, and the bovine molecule was found to co-elute from multiple chromatographic proceduresd with bound tritiated PGF-2 α. CD315 inhibits the binding of PGF2-α to its specific FP receptor by decreasing the receptor number rather then the affinity constant. Functional coupling with the PGF2 α- receptor seems to occur. |
BIOCHEMICAL ACTIVITY: No information.
DISEASE RELEVANCE AND FUNCTION OF CD315 IN INTACT ANIMAL
CD315 is strongly expressed in a number of cancer cells suggesting a possible upregulation during tumorigenesis.
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF CD315: No information.
SUBSTRATES: No information.
ENZYMES WHICH MODIFY CD315: No information.
For further information see Charrin, S. et al (2001) J. Biol. Chem. 276: 14329-14337.
Database accession numbers
Revised June 25, 2008