GLP1R
entrez
2740
canonical
uniprot
P43220
canonical
ensembl
ENSG00000112164
resolver
ensp
ENSP00000362353
resolver
enst
ENST00000373256
resolver
genesymbol
GLP1R
resolver
hgnc
HGNC:4324
resolver
uniprot
A0A142FHB8
resolver
uniprot
Q2M229
resolver
uniprot
Q99669
resolver
uniprot_entry
A0A142FHB8_HUMAN
resolver
uniprot_entry
GLP1R_HUMAN
resolver
uniprot_sec
Q2M229
resolver
uniprot_sec
Q99669
resolver
activity_regulation
ACTIVITY REGULATION: The allosteric modulators NNC0640, PF-06372222 and MK-0893 inhibit the increase of intracellular cAMP levels in response to GLP-1. {ECO:0000269|PubMed:28514449}.
uniprot
proteins
amino_acid_sequence
MAGAPGPLRLALLLLGMVGRAGPRPQGATVSLWETVQKWREYRRQCQRSLTEDPPPATDLFCNRTFDEYACWPDGEPGSFVNVSCPWYLPWASSVPQGHVYRFCTAEGLWLQKDNSSLPWRDLSECEESKRGERSSPEEQLLFLYIIYTVGYALSFSALVIASAILLGFRHLHCTRNYIHLNLFASFILRALSVFIKDAALKWMYSTAAQQHQWDGLLSYQDSLSCRLVFLLMQYCVAANYYWLLVEGVYLYTLLAFSVLSEQWIFRLYVSIGWGVPLLFVVPWGIVKYLYEDEGCWTRNSNMNYWLIIRLPILFAIGVNFLIFVRVICIVVSKLKANLMCKTDIKCRLAKSTLTLIPLLGTHEVIFAFVMDEHARGTLRFIKLFTELSFTSFQGLMVAILYCFVNNEVQLEFRKSWERWRLEHLHIQRDSSMKPLKCPTSSLSSGATAGSSMYTATCQASCS
uniprot
proteins
function
FUNCTION: G protein-coupled receptor for glucagon-like peptide 1 (GLP-1) (PubMed:19861722, PubMed:26308095, PubMed:27196125, PubMed:28514449, PubMed:7517895, PubMed:8216285, PubMed:8405712). Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels (PubMed:19861722, PubMed:26308095, PubMed:27196125, PubMed:28514449, PubMed:7517895, PubMed:8216285, PubMed:8405712). Plays a role in regulating insulin secretion in response to GLP-1 (By similarity). {ECO:0000250|UniProtKB:O35659, ECO:0000269|PubMed:19861722, ECO:0000269|PubMed:26308095, ECO:0000269|PubMed:27196125, ECO:0000269|PubMed:28514449, ECO:0000269|PubMed:7517895, ECO:0000269|PubMed:8216285, ECO:0000269|PubMed:8405712}.
uniprot
proteins
mass_dalton
53026
uniprot
proteins
mutagenesis
MUTAGEN 32; /note="L->A: No effect on stimulation of cAMP accumulation and on GLP-1 binding."; /evidence="ECO:0000269|PubMed:19861722"; MUTAGEN 69; /note="Y->A: Abolishes stimulation of cAMP accumulation in response to GLP-1."; /evidence="ECO:0000269|PubMed:19861722"; MUTAGEN 88; /note="Y->A: Abolishes stimulation of cAMP accumulation in response to GLP-1."; /evidence="ECO:0000269|PubMed:19861722"; MUTAGEN 89; /note="L->A: Abolishes stimulation of cAMP accumulation in response to GLP-1."; /evidence="ECO:0000269|PubMed:19861722"; MUTAGEN 90; /note="P->A: Strongly decreased stimulation of cAMP accumulation in response to GLP-1."; /evidence="ECO:0000269|PubMed:19861722"; MUTAGEN 121; /note="R->A: Strongly decreased stimulation of cAMP accumulation in response to GLP-1."; /evidence="ECO:0000269|PubMed:19861722"; MUTAGEN 127; /note="E->A: No effect on stimulation of cAMP accumulation in response to GLP-1."; /evidence="ECO:0000269|PubMed:19861722"; MUTAGEN 128; /note="E->A: Slightly decreases stimulation of cAMP accumulation in response to GLP-1."; /evidence="ECO:0000269|PubMed:19861722"; MUTAGEN 128; /note="E->Q: No effect on stimulation of cAMP accumulation in response to GLP-1."; /evidence="ECO:0000269|PubMed:19861722"; MUTAGEN 176; /note="R->Q: Decreases sensitivity to GLP-1."; /evidence="ECO:0000269|PubMed:28514449"; MUTAGEN 317; /note="I->C: Causes the formation of an artifactual disulfide bond that abolishes signaling in response to GLP-1 binding; when associated with C-361."; /evidence="ECO:0000269|PubMed:28514449"; MUTAGEN 352; /note="S->A: Abolishes inhibition by negative allosteric modulators."; /evidence="ECO:0000269|PubMed:28514449"; MUTAGEN 355; /note="T->A: Abolishes inhibition by the negative allosteric modulators NNC0640 and PF-06372222, but does not abolish inhibition by MK-0893."; /evidence="ECO:0000269|PubMed:28514449"; MUTAGEN 361; /note="G->C: Causes the formation of an artifactual disulfide bond that abolishes signaling in response to GLP-1 binding; when associated with C-317."; /evidence="ECO:0000269|PubMed:28514449
uniprot
proteins
post_translational_modification
PTM: N-glycosylation enhances cell surface expression and lengthens receptor half-life by preventing degradation in the ER. {ECO:0000269|PubMed:22412906}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18287102
uniprot
proteins
pubmed
19861722
uniprot
proteins
pubmed
20869417
uniprot
proteins
pubmed
21901419
uniprot
proteins
pubmed
22412906
uniprot
proteins
pubmed
26308095
uniprot
proteins
pubmed
27196125
uniprot
proteins
pubmed
28514449
uniprot
proteins
pubmed
7517895
uniprot
proteins
pubmed
7843404
uniprot
proteins
pubmed
8216285
uniprot
proteins
pubmed
8404634
uniprot
proteins
pubmed
8405712
uniprot
proteins
pubmed
9213353
uniprot
proteins
sequence_length
463
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19861722, ECO:0000269|PubMed:26308095, ECO:0000269|PubMed:27196125, ECO:0000269|PubMed:28514449, ECO:0000269|PubMed:7517895, ECO:0000269|PubMed:8216285, ECO:0000269|PubMed:8405712}; Multi-pass membrane protein {ECO:0000269|PubMed:28514449}.
uniprot
proteins
transmembrane_region
TRANSMEM 140..164; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:28514449"; TRANSMEM 176..201; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:28514449"; TRANSMEM 228..251; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:28514449"; TRANSMEM 266..290; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:28514449"; TRANSMEM 306..328; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:28514449"; TRANSMEM 349..370; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:28514449"; TRANSMEM 384..404; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:28514449
uniprot
proteins