|CD311||EMRI (Epidermal growth factor-like module-containing, mucin-like hormone receptor 1)|
|Molecule Type||Antigen Expression||Molecular Weight|
Min / Max
|Non-lineage Restricted Molecule|
Type 3 glycoprotein, 7 span
|98 / 98|
CD322 is widely expressed with increased levels in peripheral blood mononuclear cells and macrophage cells but is weak in solid tumor-derived cell lines.
|MOLECULAR FAMILY NAME: Belongs to the G-protein coupled receptor 2 family.|
CD311 is a multi-pass type-3 7-span 886 aa glycoprotein. It contains a 20 aa signal sequence, a 579 aa N-terminal extracellular domain which contains 6 Ca++ binding EGF-like domains followed by a 283 aa domain of which 27 aa are serine and 25 aa are threonine, a feature reminiscent of mucin-like, single span, integral membrane glycoproteins with adhesive properties, and 1 GPS domain. The serine/threonine-rich domain is predicted to be heavily O-glycosylated resulting in a rigid stem-like structure. A G-protein-coupled receptor (GPS) is located in the stem-like structure however, it is unknown if CD311 is cleaved into two subunits. There are 13 potential N-linked glycosylation sites: 8 are found within the EGF domains, 3 in the stem-like structure and 1 in the first extracellular loop. CD311 contains 7 transmembranes-spanning hydrophobic domains with 283 aa and a C-terminal cytoplasmic domain which contains 4 potential protein kinase C phosphorylation sites, 2 sites which are located in the intracellular loop, one of those is a potential casein kinase II phosphorylation site and 2 sites occur within the C-terminal cytoplasmic domain. CD311 family members are characterized by a variable number of N-terminal epidermal growth factor (EGF) domains follwed by 7 transmembrane-spanning hydrophobic domains that bear homology to the equivalent region in G-protein-coupled peptide hormone receptor family members. Because of its unique characteristics, CD311 has been designated as a putative EGF module-containing, mucin-like hormone receptor EMRI.
Alternative splicing yields 4 isoforms. The isoforms arise from alternative RNA splicing.
CD311 has 13 potential N-linked glycosylation sites, 8 are found in the EGF domains, 3 in the stem-like structure and 1 in the first extracellular loop.
|LIGANDS AND MOLECULE ASSOCIATED WITH CD311: No information.|
|The function of CD311 is unknown but is thought to be a macrophage-specific marker. Expression of F4/80 is on tissue macrophages but weak expression in peripheral blood monocytes suggesting that there is a role cell-cell interactions and may have a role in the terminal differentiation of macrophages. The mouse homologue F4/80 (emr1) has an extra EGF-like domain and has a RGD motif in the extracellular domain that the human protein does not have. The RGD domain may mediate integrin binding and therefore may play a role in cell adhesion. F4/80 knochout mice are physiologically normal and no abnormality has as yet been detected.|
BIOCHEMICAL ACTIVITY: No information.
DISEASE RELEVANCE AND FUNCTION OF CD311 IN INTACT ANIMAL: No information.
PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCIPTION OF CD311: No information.
SUBSTRATES: No information.
ENZYMES WHICH MODIFY CD311: No information.
Database accession numbers
Revised June 25, 2008