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Glucagon receptor (GL-R)

 GLR_MOUSE               Reviewed;         485 AA.
Q61606; Q63960; Q8K0B5;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 145.
RecName: Full=Glucagon receptor;
Short=GL-R;
Flags: Precursor;
Name=Gcgr;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=7590348; DOI=10.1016/0378-1119(95)00472-I;
Burcelin R., Li J., Charron M.J.;
"Cloning and sequence analysis of the murine glucagon receptor-
encoding gene.";
Gene 164:305-310(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 324-458.
TISSUE=Brain;
PubMed=8156917; DOI=10.1210/endo.134.5.8156917;
Campos R.V., Lee Y.C., Drucker D.J.;
"Divergent tissue-specific and developmental expression of receptors
for glucagon and glucagon-like peptide-1 in the mouse.";
Endocrinology 134:2156-2164(1994).
[6]
DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12552113; DOI=10.1073/pnas.0237106100;
Gelling R.W., Du X.Q., Dichmann D.S., Romer J., Huang H., Cui L.,
Obici S., Tang B., Holst J.J., Fledelius C., Johansen P.B.,
Rossetti L., Jelicks L.A., Serup P., Nishimura E., Charron M.J.;
"Lower blood glucose, hyperglucagonemia, and pancreatic alpha cell
hyperplasia in glucagon receptor knockout mice.";
Proc. Natl. Acad. Sci. U.S.A. 100:1438-1443(2003).
[7]
DISRUPTION PHENOTYPE.
PubMed=16627579; DOI=10.1210/en.2005-1410;
Vuguin P.M., Kedees M.H., Cui L., Guz Y., Gelling R.W., Nejathaim M.,
Charron M.J., Teitelman G.;
"Ablation of the glucagon receptor gene increases fetal lethality and
produces alterations in islet development and maturation.";
Endocrinology 147:3995-4006(2006).
[8]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=19046568; DOI=10.1016/j.cmet.2008.09.008;
Longuet C., Sinclair E.M., Maida A., Baggio L.L., Maziarz M.,
Charron M.J., Drucker D.J.;
"The glucagon receptor is required for the adaptive metabolic response
to fasting.";
Cell Metab. 8:359-371(2008).
-!- 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}.
-!- 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}.
-!- TISSUE SPECIFICITY: Expressed predominantly in liver, kidney,
adrenal, lung and stomach, while lower levels of expression are
detected in brown and white adipose tissue, cerebellum, duodenum
and heart. {ECO:0000269|PubMed:7590348}.
-!- 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}.
-!- DISRUPTION PHENOTYPE: Mice are born at the expected Mendelian
rate. They display pancreas islet and alpha-cell hyperplasia and
increased glucagon levels, but normal insulin levels. Mice display
low blood glucose levels combined with increased hepatic glycogen
levels. They develop severe hypoglycemia after prolonged fasting.
Mutant mice are fertile, but the females produce only few pups;
half of the embryos die before birth, and liveborn pups do not
survive more than one day. These pups are much smaller than their
littermates and exhibit severe hypoglycemia.
{ECO:0000269|PubMed:12552113, ECO:0000269|PubMed:16627579,
ECO:0000269|PubMed:19046568}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L38613; AAA88244.1; -; mRNA.
EMBL; AL669855; CAM27053.1; -; Genomic_DNA.
EMBL; CH466558; EDL34761.1; -; Genomic_DNA.
EMBL; BC031885; AAH31885.1; -; mRNA.
EMBL; BC057988; AAH57988.1; -; mRNA.
EMBL; S69384; AAB30529.2; -; mRNA.
CCDS; CCDS25739.1; -.
PIR; JC4363; JC4363.
RefSeq; NP_032127.2; NM_008101.2.
RefSeq; XP_017169755.1; XM_017314266.1.
UniGene; Mm.22329; -.
ProteinModelPortal; Q61606; -.
SMR; Q61606; -.
BioGrid; 199863; 1.
STRING; 10090.ENSMUSP00000026119; -.
BindingDB; Q61606; -.
ChEMBL; CHEMBL4773; -.
GuidetoPHARMACOLOGY; 251; -.
iPTMnet; Q61606; -.
PhosphoSitePlus; Q61606; -.
MaxQB; Q61606; -.
PaxDb; Q61606; -.
PRIDE; Q61606; -.
Ensembl; ENSMUST00000026119; ENSMUSP00000026119; ENSMUSG00000025127.
GeneID; 14527; -.
KEGG; mmu:14527; -.
UCSC; uc007mtc.2; mouse.
CTD; 2642; -.
MGI; MGI:99572; Gcgr.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
GeneTree; ENSGT00760000118800; -.
HOGENOM; HOG000008250; -.
HOVERGEN; HBG008318; -.
InParanoid; Q61606; -.
KO; K04583; -.
OMA; TELVCNR; -.
OrthoDB; EOG091G0NF8; -.
TreeFam; TF315710; -.
Reactome; R-MMU-163359; Glucagon signaling in metabolic regulation.
Reactome; R-MMU-416476; G alpha (q) signalling events.
Reactome; R-MMU-418555; G alpha (s) signalling events.
Reactome; R-MMU-420092; Glucagon-type ligand receptors.
ChiTaRS; Gcgr; mouse.
PRO; PR:Q61606; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000025127; Expressed in 111 organ(s), highest expression level in lobe of liver.
CleanEx; MM_GCGR; -.
Genevisible; Q61606; MM.
GO; GO:0005768; C:endosome; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0004967; F:glucagon receptor activity; IDA:UniProtKB.
GO; GO:0017046; F:peptide hormone binding; ISO:MGI.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0071377; P:cellular response to glucagon stimulus; IDA:UniProtKB.
GO; GO:0006887; P:exocytosis; ISO:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:MGI.
GO; GO:0070873; P:regulation of glycogen metabolic process; IMP:UniProtKB.
GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
Gene3D; 4.10.1240.10; -; 1.
InterPro; IPR017981; GPCR_2-like.
InterPro; IPR036445; GPCR_2_extracell_dom_sf.
InterPro; IPR001879; GPCR_2_extracellular_dom.
InterPro; IPR003290; GPCR_2_GLP1/glucagon_rcpt.
InterPro; IPR003291; GPCR_2_glucagon_rcpt.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF02793; HRM; 1.
PRINTS; PR01353; GLUCAGNFAMLY.
PRINTS; PR01354; GLUCAGONR.
PRINTS; PR00249; GPCRSECRETIN.
SMART; SM00008; HormR; 1.
SUPFAM; SSF111418; SSF111418; 1.
PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
2: Evidence at transcript level;
Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 485 Glucagon receptor.
/FTId=PRO_0000012833.
TOPO_DOM 27 137 Extracellular.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 138 162 Helical; Name=1.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 163 174 Cytoplasmic.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 175 199 Helical; Name=2.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 200 226 Extracellular.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 227 250 Helical; Name=3.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 251 264 Cytoplasmic.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 265 286 Helical; Name=4.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 287 304 Extracellular.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 305 327 Helical; Name=5.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 328 351 Cytoplasmic.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 352 370 Helical; Name=6.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 371 382 Extracellular.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 383 403 Helical; Name=7.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 404 485 Cytoplasmic.
{ECO:0000250|UniProtKB:P47871}.
REGION 351 354 Allosteric inhibitor binding.
{ECO:0000250|UniProtKB:P47871}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000250|UniProtKB:P47871}.
MOD_RES 476 476 Phosphoserine.
{ECO:0000250|UniProtKB:P30082}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 118 118 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 68 {ECO:0000250|UniProtKB:P47871}.
DISULFID 59 101 {ECO:0000250|UniProtKB:P47871}.
DISULFID 82 122 {ECO:0000250|UniProtKB:P47871}.
DISULFID 225 295 {ECO:0000250|UniProtKB:P47871}.
CONFLICT 65 65 K -> N (in Ref. 1; AAA88244).
{ECO:0000305}.
CONFLICT 89 89 Y -> C (in Ref. 1; AAA88244).
{ECO:0000305}.
CONFLICT 238 238 A -> P (in Ref. 1; AAA88244).
{ECO:0000305}.
CONFLICT 325 325 H -> R (in Ref. 3; AAB30529).
{ECO:0000305}.
CONFLICT 328 328 H -> Q (in Ref. 1; AAA88244).
{ECO:0000305}.
SEQUENCE 485 AA; 54929 MW; 578EB30BF281E67A CRC64;
MPLTQLHCPH LLLLLLVLSC LPEAPSAQVM DFLFEKWKLY SDQCHHNLSL LPPPTELVCN
RTFDKYSCWP DTPPNTTANI SCPWYLPWYH KVQHRLVFKR CGPDGQWVRG PRGQPWRNAS
QCQLDDEEIE VQKGVAKMYS SQQVMYTVGY SLSLGALLLA LVILLGLRKL HCTRNYIHGN
LFASFVLKAG SVLVIDWLLK TRYSQKIGDD LSVSVWLSDG AMAGCRVATV IMQYGIIANY
CWLLVEGVYL YSLLSLATFS ERSFFSLYLG IGWGAPLLFV IPWVVVKCLF ENVQCWTSND
NMGFWWILRI PVFLALLINF FIFVHIIHLL VAKLRAHQMH YADYKFRLAR STLTLIPLLG
VHEVVFAFVT DEHAQGTLRS TKLFFDLFLS SFQGLLVAVL YCFLNKEVQA ELMRRWRQWQ
EGKALQEERL ASSHGSHMAP AGPCHGDPCE KLQLMSAGSS SGTGCVPSME TSLASSLPRL
ADSPT


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