EMR2

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Egf-like module containing, mucin-like, hormone receptor-like 2
Protein EMR2 PDB 2bo2.png
PDB rendering based on 2bo2.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols EMR2 ; CD312
External IDs OMIM606100 HomoloGene113735 IUPHAR: EMR2 GeneCards: EMR2 Gene
RNA expression pattern
PBB GE EMR2 207610 s at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 30817 n/a
Ensembl ENSG00000127507 n/a
UniProt Q9UHX3 n/a
RefSeq (mRNA) NM_001271052 n/a
RefSeq (protein) NP_001257981 n/a
Location (UCSC) Chr 19:
14.84 – 14.89 Mb
n/a
PubMed search [1] n/a

EGF-like module-containing mucin-like hormone receptor-like 2 is a protein that in humans is encoded by the EMR2 gene. EMR2 has also been designated as CD312 (cluster of differentiation 312).

Structure and function[edit]

This gene encodes a member of the adhesion-GPCR receptor family [1] expressed predominantly by cells of the immune system. Family members are characterized by an extended extracellular region with a variable number of N-terminal protein modules coupled to a TM7 region via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.[2] In the case of EMR2 the N-terminal domains consist of alternatively spliced epidermal growth factor (EGF)-like domains.

This gene is closely linked to the gene encoding egf-like molecule containing mucin-like hormone receptor 3 on chromosome 19 EMR3. This protein does not interact with the complement regulatory protein, decay accelerating factor CD55, unlike the related CD97 antigen, and indicates that these very closely related proteins likely have nonredundant functions.


EGF-like module-containing mucin-like hormone receptor-like 2 (EMR2) is an adhesion GPCR that undergoes GPS autoproteolysis before being trafficked to the plasma membrane.[3] Mutations in the GPS have shown that EMR2 does not need to undergo autoproteolysis to be trafficked, but loses function. EMR2 has been shown to be necessary for in vitro cell migration.

Upon cleavage the N-terminus has been shown to associate with the 7TM, but to also dissociate, giving two possible functions. When the N-terminus dissociates it can be found in lipid rafts. Additionally, the cleaved EMR2 protein 7TM has been found to associate with EMR4 N-terminus.


See also[edit]

References[edit]

  1. ^ Stacey M, Yona S (2011). Adhesion-GPCRs: Structure to Function (Advances in Experimental Medicine and Biology). Berlin: Springer. ISBN 1-4419-7912-3. 
  2. ^ Araç D, Boucard AA, Bolliger MF, Nguyen J, Soltis SM, Südhof TC, Brunger AT (March 2012). "A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis". EMBO J. 31 (6): 1364–78. doi:10.1038/emboj.2012.26. PMC 3321182. PMID 22333914. 
  3. ^ Huang, Y. S., N. Y. Chiang, C. H. Hu, C. C. Hsiao, K. F. Cheng, W. P. Tsai, S. Yona, M. Stacey, S. Gordon, G. W. Chang, H. H. Lin. 2012. Activation of myeloid cell-specific adhesion class G protein-coupled receptor EMR2 via ligation-induced translocation and interaction of receptor subunits in lipid raft microdomains" Mol. Cell. Biol 32: 1408–1420.

Further reading[edit]

  • Lin HH, Stacey M, Hamann J, et al. (2000). "Human EMR2, a novel EGF-TM7 molecule on chromosome 19p13.1, is closely related to CD97". Genomics 67 (2): 188–200. doi:10.1006/geno.2000.6238. PMID 10903844. 
  • Lin HH, Stacey M, Saxby C, et al. (2001). "Molecular analysis of the epidermal growth factor-like short consensus repeat domain-mediated protein-protein interactions: dissection of the CD97-CD55 complex". J. Biol. Chem. 276 (26): 24160–9. doi:10.1074/jbc.M101770200. PMID 11297558. 
  • Kwakkenbos MJ, Chang GW, Lin HH, et al. (2002). "The human EGF-TM7 family member EMR2 is a heterodimeric receptor expressed on myeloid cells". J. Leukoc. Biol. 71 (5): 854–62. PMID 11994511. 
  • Stacey M, Chang GW, Davies JQ, et al. (2003). "The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans". Blood 102 (8): 2916–24. doi:10.1182/blood-2002-11-3540. PMID 12829604. 
  • Chang GW, Stacey M, Kwakkenbos MJ, et al. (2003). "Proteolytic cleavage of the EMR2 receptor requires both the extracellular stalk and the GPS motif". FEBS Lett. 547 (1–3): 145–50. doi:10.1016/S0014-5793(03)00695-1. PMID 12860403. 
  • Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19". Nature 428 (6982): 529–35. doi:10.1038/nature02399. PMID 15057824. 
  • Lin HH, Chang GW, Davies JQ, et al. (2004). "Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein-coupled receptor proteolytic site motif". J. Biol. Chem. 279 (30): 31823–32. doi:10.1074/jbc.M402974200. PMID 15150276. 
  • Bjarnadóttir TK, Fredriksson R, Höglund PJ, et al. (2005). "The human and mouse repertoire of the adhesion family of G-protein-coupled receptors". Genomics 84 (1): 23–33. doi:10.1016/j.ygeno.2003.12.004. PMID 15203201. 
  • Chang GW, Davies JQ, Stacey M, et al. (2007). "CD312, the human adhesion-GPCR EMR2, is differentially expressed during differentiation, maturation, and activation of myeloid cells". Biochem. Biophys. Res. Commun. 353 (1): 133–8. doi:10.1016/j.bbrc.2006.11.148. PMID 17174274. 

This article incorporates text from the United States National Library of Medicine, which is in the public domain.