GCGR
entrez
2642
canonical
uniprot
P47871
canonical
ensembl
ENSG00000215644
resolver
ensembl
ENSG00000288269
resolver
ensp
ENSP00000383558
resolver
ensp
ENSP00000500297
resolver
ensp
ENSP00000523107
resolver
ensp
ENSP00000523109
resolver
ensp
ENSP00000523114
resolver
ensp
ENSP00000523115
resolver
ensp
ENSP00000523116
resolver
ensp
ENSP00000523117
resolver
ensp
ENSP00000523121
resolver
ensp
ENSP00000523124
resolver
ensp
ENSP00000523134
resolver
ensp
ENSP00000627579
resolver
ensp
ENSP00000627580
resolver
enst
ENST00000400723
resolver
enst
ENST00000671794
resolver
enst
ENST00000853050
resolver
enst
ENST00000853055
resolver
enst
ENST00000853056
resolver
enst
ENST00000853057
resolver
enst
ENST00000853058
resolver
enst
ENST00000853062
resolver
enst
ENST00000853065
resolver
enst
ENST00000853075
resolver
enst
ENST00000957520
resolver
enst
ENST00000957521
resolver
genesymbol
GCGR
resolver
hgnc
HGNC:4192
resolver
uniprot
Q2M3M5
resolver
uniprot_entry
GLR_HUMAN
resolver
uniprot_sec
Q2M3M5
resolver
amino_acid_sequence
MPPCQPQRPLLLLLLLLACQPQVPSAQVMDFLFEKWKLYGDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPANTTANISCPWYLPWHHKVQHRFVFKRCGPDGQWVRGPRGQPWRDASQCQMDGEEIEVQKEVAKMYSSFQVMYTVGYSLSLGALLLALAILGGLSKLHCTRNAIHANLFASFVLKASSVLVIDGLLRTRYSQKIGDDLSVSTWLSDGAVAGCRVAAVFMQYGIVANYCWLLVEGLYLHNLLGLATLPERSFFSLYLGIGWGAPMLFVVPWAVVKCLFENVQCWTSNDNMGFWWILRFPVFLAILINFFIFVRIVQLLVAKLRARQMHHTDYKFRLAKSTLTLIPLLGVHEVVFAFVTDEHAQGTLRSAKLFFDLFLSSFQGLLVAVLYCFLNKEVQSELRRRWHRWRLGKVLWEERNTSNHRASSSPGHGPPSKELQFGRGGGSQDSSAETPLAGGLPRLAESPF
uniprot
proteins
disease_involvement
DISEASE: Mahvash disease (MVAH) [MIM:619290]: An autosomal recessive disorder characterized by alpha-cell hyperplasia of the pancreas, hyperglucagonemia without glucagonoma syndrome, aminoacidemia, and occasional hypoglycemia. The disease may lead to glucagonomas and/or primitive neuroectodermal tumors. {ECO:0000269|PubMed:19657311, ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:25695890, ECO:0000269|PubMed:30032256, ECO:0000269|PubMed:30294546, ECO:0000269|PubMed:32677665}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: G protein-coupled receptor for glucagon that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase (PubMed:32193322, PubMed:38346960). Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system. {ECO:0000269|PubMed:19657311, ECO:0000269|PubMed:22908259, ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451, ECO:0000269|PubMed:30294546, ECO:0000269|PubMed:32193322, ECO:0000269|PubMed:32677665, ECO:0000269|PubMed:38346960, ECO:0000269|PubMed:7507321, ECO:0000269|PubMed:9287038}.
uniprot
proteins
mass_dalton
54009
uniprot
proteins
mutagenesis
MUTAGEN 36; /note="W->A: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 63; /note="D->A: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 65; /note="Y->A: Strongly reduced affinity for glucagon. Increased constitutive signaling via G proteins."; /evidence="ECO:0000269|PubMed:22908259"; MUTAGEN 113; /note="Q->A,N: No effect on affinity for glucagon."; /evidence="ECO:0000269|PubMed:22908259"; MUTAGEN 113; /note="Q->C: Causes the formation of an artifactual disulfide bond that abolishes glucagon binding; when associated with C-209."; /evidence="ECO:0000269|PubMed:28514451"; MUTAGEN 113; /note="Q->E: Strongly reduced affinity for glucagon."; /evidence="ECO:0000269|PubMed:22908259"; MUTAGEN 130; /note="V->C: Causes the formation of an artifactual disulfide bond that interferes with glucagon binding; when associated with C-210."; /evidence="ECO:0000269|PubMed:28514451"; MUTAGEN 135; /note="A->P: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 145; /note="Y->A: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 149; /note="Y->A: Abolishes expression at cell surface and glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 198; /note="L->A: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 201; /note="R->D: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 202; /note="Y->A: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 208; /note="D->Q: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 209; /note="D->C: Causes the formation of an artifactual disulfide bond that abolishes glucagon binding; when associated with C-113."; /evidence="ECO:0000269|PubMed:28514451"; MUTAGEN 210; /note="L->C: Causes the formation of an artifactual disulfide bond that interferes with glucagon binding; when associated with C-130."; /evidence="ECO:0000269|PubMed:28514451"; MUTAGEN 215; /note="W->L: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 232; /note="Q->L: Abolishes expression at cell surface and glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 233; /note="Y->A: Abolishes glucagon binding. Strongly reduces expression at the cell surface."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 286; /note="K->L: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 290; /note="E->A: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 294; /note="C->A,S: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 295; /note="W->A,H: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 304; /note="W->Q: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 339; /note="H->A: Notable decrease of glucagon potency in GNAI1 activation but only slight alteration of GNAS activation."; /evidence="ECO:0000269|PubMed:32193322"; MUTAGEN 350; /note="S->A: Strongly decreases affinity for synthetic antagonist."; /evidence="ECO:0000269|PubMed:28514451"; MUTAGEN 353; /note="T->A: Loss of synthetic antagonist binding."; /evidence="ECO:0000269|PubMed:28514451"; MUTAGEN 382; /note="L->A: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 386; /note="L->F: Abolishes glucagon binding."; /evidence="ECO:0000269|PubMed:23863937"; MUTAGEN 404; /note="N->A: More than 30 fold reduction of glucagon-induced GNAS activation but no effect on GNAI1 activation."; /evidence="ECO:0000269|PubMed:32193322
uniprot
proteins
post_translational_modification
PTM: Ligand-binding promotes phosphorylation of serine residues in the C-terminal cytoplasmic domain. Phosphorylation is important for receptor endocytosis after ligand-binding. {ECO:0000269|PubMed:9287038}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16221670
uniprot
proteins
pubmed
19657311
uniprot
proteins
pubmed
22908259
uniprot
proteins
pubmed
23863937
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25695890
uniprot
proteins
pubmed
27111510
uniprot
proteins
pubmed
28514451
uniprot
proteins
pubmed
30032256
uniprot
proteins
pubmed
30294546
uniprot
proteins
pubmed
32193322
uniprot
proteins
pubmed
32677665
uniprot
proteins
pubmed
38346960
uniprot
proteins
pubmed
7507321
uniprot
proteins
pubmed
7589886
uniprot
proteins
pubmed
8020989
uniprot
proteins
pubmed
8144028
uniprot
proteins
pubmed
9287038
uniprot
proteins
sequence_length
477
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19657311, ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451, ECO:0000269|PubMed:30294546, ECO:0000269|PubMed:32677665, ECO:0000269|PubMed:7507321, ECO:0000269|PubMed:9287038}; Multi-pass membrane protein {ECO:0000269|PubMed:19657311, ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451, ECO:0000269|PubMed:7507321, ECO:0000269|PubMed:9287038}. Note=Is rapidly internalized after ligand-binding. {ECO:0000269|PubMed:9287038}.
uniprot
proteins
transmembrane_region
TRANSMEM 137..161; /note="Helical; Name=1"; /evidence="ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451"; TRANSMEM 174..198; /note="Helical; Name=2"; /evidence="ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451"; TRANSMEM 226..249; /note="Helical; Name=3"; /evidence="ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451"; TRANSMEM 264..285; /note="Helical; Name=4"; /evidence="ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451"; TRANSMEM 304..326; /note="Helical; Name=5"; /evidence="ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451"; TRANSMEM 351..369; /note="Helical; Name=6"; /evidence="ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451"; TRANSMEM 382..402; /note="Helical; Name=7"; /evidence="ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510, ECO:0000269|PubMed:28514451
uniprot
proteins