Biology:ADGRA2

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Short description: Protein-coding gene in the species Homo sapiens

A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example

Adhesion G protein-coupled receptor A2 is a protein that in humans is encoded by the ADGREA2 gene (previously GPR124).[1][2][3] It is a member of the adhesion-GPCR family of receptors. Family members are characterized by an extended extracellular region with a variable number of protein domains coupled to a TM7 domain via a domain known as the GPCR-Autoproteolysis INducing (GAIN) domain.[4][5][6]

Interactions

ADGRA2 has been shown to interact with DLG1[7] and is involved in the Wnt/β-catenin signaling pathway along with RECK.[8] ADGRA2 is the predicted target of several Group IV (+)ssRNA neuroinvasive viruses; proteolytic cleavage of ADGRA2 by these viral proteases may be important for entry into the brain.[9] ADGRA2 was predicted using SSHHPS.

Zebrafish embryos with Gpr124 loss of function demonstrate severe angiogenic deficiencies in the central nervous system.

References

  1. ↑ "Cell surface tumor endothelial markers are conserved in mice and humans". Cancer Research 61 (18): 6649–6655. September 2001. PMID 11559528. 
  2. ↑ "There exist at least 30 human G-protein-coupled receptors with long Ser/Thr-rich N-termini". Biochemical and Biophysical Research Communications 301 (3): 725–734. February 2003. doi:10.1016/S0006-291X(03)00026-3. PMID 12565841. 
  3. ↑ "Entrez Gene: GPR124 G protein-coupled receptor 124". https://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=25960. 
  4. ↑ AdhesionGPCRs: Structure to Function (Advances in Experimental Medicine and Biology). Berlin: Springer. 2011. ISBN 978-1-4419-7912-4. 
  5. ↑ "Novel human G protein-coupled receptors with long N-terminals containing GPS domains and Ser/Thr-rich regions". FEBS Letters 531 (3): 407–414. November 2002. doi:10.1016/S0014-5793(02)03574-3. PMID 12435584. 
  6. ↑ "A novel evolutionarily conserved domain of cell-adhesion GPCRs mediates autoproteolysis". The EMBO Journal 31 (6): 1364–1378. March 2012. doi:10.1038/emboj.2012.26. PMID 22333914. 
  7. ↑ "Direct binding of the human homologue of the Drosophila disc large tumor suppressor gene to seven-pass transmembrane proteins, tumor endothelial marker 5 (TEM5), and a novel TEM5-like protein". Oncogene 23 (22): 3889–3897. May 2004. doi:10.1038/sj.onc.1207495. PMID 15021905. 
  8. ↑ "Tip cell-specific requirement for an atypical Gpr124- and Reck-dependent Wnt/β-catenin pathway during brain angiogenesis". eLife 4. June 2015. doi:10.7554/eLife.06489. PMID 26051822. 
  9. ↑ "Automated SSHHPS Analysis Predicts a Potential Host Protein Target Common to Several Neuroinvasive (+)ssRNA Viruses". Viruses 15 (2): 542. February 2023. doi:10.3390/v15020542. PMID 36851756. 

Further reading

  • "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Research 9 (3): 99–106. June 2002. doi:10.1093/dnares/9.3.99. PMID 12168954. 
  • "Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research 7 (2): 143–150. April 2000. doi:10.1093/dnares/7.2.143. PMID 10819331. 
  • "Direct binding of the human homologue of the Drosophila disc large tumor suppressor gene to seven-pass transmembrane proteins, tumor endothelial marker 5 (TEM5), and a novel TEM5-like protein". Oncogene 23 (22): 3889–3897. May 2004. doi:10.1038/sj.onc.1207495. PMID 15021905. 
  • "The human and mouse repertoire of the adhesion family of G-protein-coupled receptors". Genomics 84 (1): 23–33. July 2004. doi:10.1016/j.ygeno.2003.12.004. PMID 15203201. 
  • "Proteolytically processed soluble tumor endothelial marker (TEM) 5 mediates endothelial cell survival during angiogenesis by linking integrin alpha(v)beta3 to glycosaminoglycans". The Journal of Biological Chemistry 281 (45): 34179–34188. November 2006. doi:10.1074/jbc.M605291200. PMID 16982628.