Gcgr
entrez
14527
canonical
uniprot
Q61606
canonical
ensembl
ENSMUSG00000025127
resolver
ensp
ENSMUSP00000026119
resolver
enst
ENSMUST00000026119
resolver
genesymbol
Gcgr
resolver
uniprot
Q3UN81
resolver
uniprot
Q63960
resolver
uniprot
Q8K0B5
resolver
uniprot_entry
GLR_MOUSE
resolver
uniprot_entry
Q3UN81_MOUSE
resolver
uniprot_sec
Q63960
resolver
uniprot_sec
Q8K0B5
resolver
amino_acid_sequence
MPLTQLHCPHLLLLLLVLSCLPEAPSAQVMDFLFEKWKLYSDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPPNTTANISCPWYLPWYHKVQHRLVFKRCGPDGQWVRGPRGQPWRNASQCQLDDEEIEVQKGVAKMYSSQQVMYTVGYSLSLGALLLALVILLGLRKLHCTRNYIHGNLFASFVLKAGSVLVIDWLLKTRYSQKIGDDLSVSVWLSDGAMAGCRVATVIMQYGIIANYCWLLVEGVYLYSLLSLATFSERSFFSLYLGIGWGAPLLFVIPWVVVKCLFENVQCWTSNDNMGFWWILRIPVFLALLINFFIFVHIIHLLVAKLRAHQMHYADYKFRLARSTLTLIPLLGVHEVVFAFVTDEHAQGTLRSTKLFFDLFLSSFQGLLVAVLYCFLNKEVQAELMRRWRQWQEGKALQEERLASSHGSHMAPAGPCHGDPCEKLQLMSAGSSSGTGCVPSMETSLASSLPRLADSPT
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. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system. {ECO:0000269|PubMed:12552113, ECO:0000269|PubMed:19046568, ECO:0000269|PubMed:32677665}.
uniprot
proteins
mass_dalton
54929
uniprot
proteins
mutagenesis
MUTAGEN 369; /note="V->M: Results in impaired glucagon binding and glucagon-mediated signaling. Homozygous mice show hyperglucagonemia with alpha-cell hyperplasia and enlargement of the pancreas."; /evidence="ECO:0000269|PubMed:32677665
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 (By similarity). {ECO:0000250|UniProtKB:P47871}.
uniprot
proteins
protein_family
G protein-coupled receptor 2 family
uniprot
proteins
pubmed
12552113
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16627579
uniprot
proteins
pubmed
19046568
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
32677665
uniprot
proteins
pubmed
7590348
uniprot
proteins
pubmed
8156917
uniprot
proteins
sequence_length
485
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12552113}; Multi-pass membrane protein {ECO:0000269|PubMed:12552113}. Note=Is rapidly internalized after ligand-binding. {ECO:0000250|UniProtKB:P47871}.
uniprot
proteins
transmembrane_region
TRANSMEM 138..162; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P47871"; TRANSMEM 175..199; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P47871"; TRANSMEM 227..250; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P47871"; TRANSMEM 265..286; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P47871"; TRANSMEM 305..327; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P47871"; TRANSMEM 352..370; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P47871"; TRANSMEM 383..403; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P47871
uniprot
proteins