Open Access Articles- Top Results for GPR98


SymbolsGPR98 ; FEB4; MASS1; USH2B; USH2C; VLGR1; VLGR1b
External IDsOMIM602851 MGI1274784 HomoloGene19815 IUPHAR: 189 GeneCards: GPR98 Gene
RNA expression pattern
File:PBB GE GPR98 gnf1h01727 s at tn.png
File:PBB GE GPR98 gnf1h07403 at tn.png
File:PBB GE GPR98 gnf1h07404 at tn.png
More reference expression data
RefSeq (mRNA)NM_032119NM_054053
RefSeq (protein)NP_115495NP_473394
Location (UCSC)Chr 5:
89.83 – 90.46 Mb
Chr 13:
81.1 – 81.63 Mb
PubMed search[1][2]

G protein-coupled receptor 98, also known as GPR98 or VLGR1, is a protein that in humans is encoded by the GPR98 gene.[1] Several alternatively spliced transcripts have been described.[1]

The adhesion GPCR Very Large GPCR receptor 1 (Vlg1R1) is the largest GPCR known, with a size of 6300 amino acids and consisting of 90 exons.[2] There are 8 splice variants of VlgR1, named VlgR1a-1e and Mass1.1-1.3. The N-terminus consists of 5800 amino acids containing 35 Calx-beta domains, one pentraxin domain, and one epilepsy associated repeat. Mutations of VlgR1 have been shown to result in Usher's syndrome. Knockouts of Vlgr1 in mice have been shown to phenocopy Usher's syndrome and lead to audigoenic seizures.


This gene encodes a member of the adhesion-GPCR family of receptors.[3] The protein binds calcium and is expressed in the central nervous system. It is also known as very large G-protein coupled receptor 1 because it is 6300 residues long. It contains a C-terminal 7-transmembrane receptor domain, whereas the large N-terminal segment (5900 residues) includes 35 calcium binding Calx-beta domains, and 6 EAR domains.


The Sea Urchin genome has a homolog of VLGR1 in it.[4]

Clinical significance

Mutations in this gene are associated with Usher syndrome 2 and familial febrile seizures.[1]


  1. ^ a b c "Entrez Gene: GPR98 G protein-coupled receptor 98". 
  2. ^ Sun JP, Li R, Ren HZ, Xu AT, Yu X, Xu ZG. The very large g protein coupled receptor (vlgr1) in hair cells.J Mol Neurosci. 2013 May;50(1):204-14. doi: 10.1007/s12031-012-9911-5. Epub 2012 Nov 20.
  3. ^ Stacey M, Yona S (2011). AdhesionGPCRs: Structure to Function (Advances in Experimental Medicine and Biology). Berlin: Springer. ISBN 1-4419-7912-3. 
  4. ^ Charles A. Whittakera, Karl-Frederik Bergerone, James Whittlec, Bruce P. Brandhorste, Robert D. Burked, Richard O. Hynes. The echinoderm adhesome. Developmental Biology. Volume 300, Issue 1, 1 December 2006, Pages 252–266.

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