EMR2 EMR2 (egf-like module containing, mucin-like, hormone receptor-like 2)
Molecule TypeAntigen ExpressionMolecular Weight
Min / Max
Non-lineage Restricted Molecule
Multi-pass
Leukocyte
Myeloid Cell
Peripheral blood
Spleen
Lymph Node
Macrophage
Monocyte
Jurkat cell

Expression
EMR2 is restricted to myeloid cells.  The highest expression was found in peripheral blood leukocytes, followed by spleen and lymph nodes, intermediate to low levels of expression is in thymus, bone marrow, fetal liver, placenta and lung.  There is no expression in heart, brain skeletal muscle, kidney or pancreas.  Expression is also detected in monocyte/macrophage and Jurkat cell lines but not in other cell lines tested.

Structure
MOLECULAR FAMILY NAME: Belongs to the G-protein coupled receptor family.

EMR2 is a multi-pass 823 aa glycoprotein.  It contains an extracellular domain which contains 5 EGF-like domains which are nearly identical to those of CD97, a GPS domain and multiple N- and O-glycosylation sites, a 248 aa 7 transmembrane domains which are approximately 45% identical to those of CD97 and a 41 aa cytoplasmic domain which contains a cysteine-rich motif involved in proteolytic cleavage and 4 potential phosphorylation sites .  EGF domains 2 through 5 have calcium-binding sequences likely to play important roles in protein-protein interactions.  The EGF-like domains couple to the
TM7 domain via a mucin-like spacer.  EMR does not interact with the ligand CD55 (decoy accelerating factor for complement), unlike the related CD97 antigen, which indicates that these very closely related proteins likely have  nonredunant functions and the association between CD97 and CD55 is highly dependent on 3 or fewer amino acids and /or the more diverse spacer region.  EMR2 is proteolytically cleaved into 2 subunits, an extracellular α subunit and a seven transmembrane subunit.  Binding chondroitin sulfate is mediated by the fourth EGF domain.  The GSP domain is necessary but is not sufficient for receptor cleavage, which require the entire extracellular stalk. 

MOLECULAR MASS

POST-TRANSCRIPTIONAL MODIFICATION

Alternative splicing yields 1 isoform.  A soluble form is due to a fameshift which introduced a stop codon immediately before the first transmembrane is also detected.

POST-TRANSLATIONAL MODIFICATIONS

EMR2 has multiple N- and O-glycosylation sites.  EMR2 is proteolytocally cleaved into 2 subunits, an extracellular α subunit and a 7-transmembrane subunit.

Ligands
LIGANDS AND MOLECULES ASSOCIATED WITH EMR2: No information.

Function
EMR2 is a receptor and may be probably involved in cell attactment.  EMR2 forms a heterodimer, consisting of a large extracellular region non-covalently linked to the seven transmembrane moiety.  EMR2 interacts with chondroitin sulfate.

BIOCHEMICAL ACTIVITY: No information.

DISEASE RELEVANCE AND FUNCTION OF EMR2 IN INTACT ANIMAL: No information.

Comments
MOLECULAR INTERACTION-
 PROTEINS AND DNA ELEMENTS WHICH REGULATE TRANSCRIPTION OF EMR2: No information.

SUBSTRATES: No information.

ENZYMES WHICH MODIFY EMR2: No information.

Database accession numbers
AnimalPIRSWISSPROTEMGBL/GENBANK
 
HumanEntrezgene30817Q9UHX3
Antibodies

Revised June 25, 2008


Contact us: Webmaster |  509-335-9515 | Accessibility | Copyright | Policies
College of Veterinary Medicine Washington State University, Pullman, WA, 99164-7010 USA
Copyright 1995-2003 Washington State University