GLP-1 receptor

GLP1R
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3C59, 3C5T, 3IOL, 4ZGM
Identifiers
Aliases	GLP1R, entrez:2740, glucagon-like peptide 1 receptor, GLP-1, GLP-1-R, GLP-1R, glucagon like peptide 1 receptor
External IDs	MGI: 99571 HomoloGene: 1558 GeneCards: GLP1R
Gene ontology Molecular function • G-protein coupled peptide receptor activity • G-protein coupled receptor activity • signal transducer activity • protein binding • glucagon receptor activity • transmembrane signaling receptor activity Cellular component • integral component of membrane • membrane • plasma membrane • intracellular Biological process • G-protein coupled receptor signaling pathway • regulation of heart contraction • regulation of insulin secretion • positive regulation of cytosolic calcium ion concentration • cellular response to glucagon stimulus • response to stress • activation of adenylate cyclase activity • cell surface receptor signaling pathway • positive regulation of blood pressure • learning or memory • cAMP-mediated signaling • signal transduction Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2740	14652
Ensembl	ENSG00000112164	ENSMUSG00000024027
UniProt	P43220	O35659
RefSeq (mRNA)	NM_002062	NM_021332
RefSeq (protein)	NP_002053	NP_067307.2 NP_067307
Location (UCSC)	Chr 6: 39.05 – 39.09 Mb	Chr 17: 30.9 – 30.94 Mb
PubMed search

3C59, 3C5T, 3IOL, 4ZGM

2740

14652

ENSG00000112164

ENSMUSG00000024027

P43220

O35659

NM_002062

NM_021332

NP_002053

NP_067307.2
NP_067307

The glucagon-like peptide 1 receptor (GLP1R) is a human gene which resides on chromosome 6. The protein encoded by this gene is a member of the glucagon receptor family of G protein-coupled receptors. GLP1R is composed of two domains, one extracellular (ECD) that binds the C-terminal helix of GLP-1, and one transmembrane (TMD) domain that binds the N-terminal region of GLP-1. In the TMD domain there is fulcrum of polar residues that regulates the biased signaling of the receptor while the transmembrane helical boundaries and extracellular surface are a trigger for biased agonism.

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