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Glucagon receptor (GL-R)

 GLR_HUMAN               Reviewed;         477 AA.
P47871; Q2M3M5;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
12-SEP-2018, entry version 159.
RecName: Full=Glucagon receptor;
Short=GL-R;
Flags: Precursor;
Name=GCGR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Liver;
PubMed=7507321; DOI=10.1006/bbrc.1994.1046;
Macneil D.J., Occi J.L., Hey P.J., Strader C.D., Graziano M.P.;
"Cloning and expression of a human glucagon receptor.";
Biochem. Biophys. Res. Commun. 198:328-334(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8144028; DOI=10.1016/0378-1119(94)90545-2;
Lok S., Kuijper J.L., Jelinek L.J., Kramer J.M., Whitmore T.E.,
Sprecher C.A., Mathewes S., Grant F.J., Biggs S.H., Rosenberg G.B.;
"The human glucagon receptor encoding gene: structure, cDNA sequence
and chromosomal localization.";
Gene 140:203-209(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-54.
TISSUE=Placenta;
PubMed=8020989; DOI=10.1006/geno.1994.1179;
Menzel S., Stoffel M., Espinosa R. III, Fernald A.A., Le Beau M.M.,
Bell G.I.;
"Localization of the glucagon receptor gene to human chromosome band
17q25.";
Genomics 20:327-328(1994).
[5]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=9287038; DOI=10.2337/diab.46.9.1400;
Buggy J.J., Heurich R.O., MacDougall M., Kelley K.A., Livingston J.N.,
Yoo-Warren H., Rossomando A.J.;
"Role of the glucagon receptor COOH-terminal domain in glucagon-
mediated signaling and receptor internalization.";
Diabetes 46:1400-1405(1997).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456 AND SER-459, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[7]
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 412-420 IN COMPLEX WITH CLASS
I MHC.
PubMed=16221670; DOI=10.1074/jbc.M508528200;
Ruckert C., Fiorillo M.T., Loll B., Moretti R., Biesiadka J.,
Saenger W., Ziegler A., Sorrentino R., Uchanska-Ziegler B.;
"Conformational dimorphism of self-peptides and molecular mimicry in a
disease-associated HLA-B27 subtype.";
J. Biol. Chem. 281:2306-2316(2006).
[8]
X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 28-123, FUNCTION,
MUTAGENESIS OF TYR-65 AND GLN-113, DISULFIDE BONDS, AND GLYCOSYLATION
AT ASN-74 AND ASN-78.
PubMed=22908259; DOI=10.1073/pnas.1206734109;
Koth C.M., Murray J.M., Mukund S., Madjidi A., Minn A., Clarke H.J.,
Wong T., Chiang V., Luis E., Estevez A., Rondon J., Zhang Y.,
Hotzel I., Allan B.B.;
"Molecular basis for negative regulation of the glucagon receptor.";
Proc. Natl. Acad. Sci. U.S.A. 109:14393-14398(2012).
[9]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 123-432, FUNCTION,
SUBCELLULAR LOCATION, DISULFIDE BONDS, MEMBRANE TOPOLOGY, MUTAGENESIS
OF TRP-36; ASP-63; ALA-135; TYR-145; TYR-149; LEU-198; ARG-201;
TYR-202; ASP-208; TRP-215; GLN-232; TYR-233; LYS-286; GLU-290;
CYS-294; TRP-295; TRP-304; LEU-382 AND LEU-386, AND CHARACTERIZATION
OF VARIANT SER-86.
PubMed=23863937; DOI=10.1038/nature12393;
Siu F.Y., He M., de Graaf C., Han G.W., Yang D., Zhang Z., Zhou C.,
Xu Q., Wacker D., Joseph J.S., Liu W., Lau J., Cherezov V.,
Katritch V., Wang M.W., Stevens R.C.;
"Structure of the human glucagon class B G-protein-coupled receptor.";
Nature 499:444-449(2013).
[10] {ECO:0000244|PDB:5EE7}
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 136-254; 256-256 AND 259-417
IN COMPLEX WITH SYNTHETIC ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION,
AND DISULFIDE BONDS.
PubMed=27111510; DOI=10.1038/nature17414;
Jazayeri A., Dore A.S., Lamb D., Krishnamurthy H., Southall S.M.,
Baig A.H., Bortolato A., Koglin M., Robertson N.J., Errey J.C.,
Andrews S.P., Teobald I., Brown A.J., Cooke R.M., Weir M.,
Marshall F.H.;
"Extra-helical binding site of a glucagon receptor antagonist.";
Nature 533:274-277(2016).
[11]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 27-432 IN COMPLEX WITH THE
SYNTHETIC ANTAGONIST NNC0640, FUNCTION, SUBCELLULAR LOCATION,
TOPOLOGY, GLYCOSYLATION AT ASN-46; ASN-59; ASN-74 AND ASN-78,
MUTAGENESIS OF GLN-113; VAL-130; ASP-209; LEU-210; SER-350 AND
THR-353, AND DISULFIDE BONDS.
PubMed=28514451; DOI=10.1038/nature22363;
Zhang H., Qiao A., Yang D., Yang L., Dai A., de Graaf C.,
Reedtz-Runge S., Dharmarajan V., Zhang H., Han G.W., Grant T.D.,
Sierra R.G., Weierstall U., Nelson G., Liu W., Wu Y., Ma L., Cai X.,
Lin G., Wu X., Geng Z., Dong Y., Song G., Griffin P.R., Lau J.,
Cherezov V., Yang H., Hanson M.A., Stevens R.C., Zhao Q., Jiang H.,
Wang M.W., Wu B.;
"Structure of the full-length glucagon class B G-protein-coupled
receptor.";
Nature 546:259-264(2017).
[12]
VARIANT SER-40.
PubMed=7589886; DOI=10.1007/BF00400589;
Fujisawa T., Ikegami H., Yamato E., Takekawa K., Nakagawa Y.,
Hamada Y., Ueda H., Fukuda M., Ogihara T.;
"A mutation in the glucagon receptor gene (Gly40Ser): heterogeneity in
the association with diabetes mellitus.";
Diabetologia 38:983-985(1995).
[13]
VARIANT SER-86, FUNCTION, SUBCELLULAR LOCATION, AND CHARACTERIZATION
OF VARIANT SER-86.
PubMed=19657311; DOI=10.1097/MPA.0b013e3181b2bb03;
Zhou C., Dhall D., Nissen N.N., Chen C.R., Yu R.;
"Homozygous P86S mutation of the human glucagon receptor is associated
with hyperglucagonemia, alpha cell hyperplasia, and islet cell
tumor.";
Pancreas 38:941-946(2009).
-!- 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:19657311, ECO:0000269|PubMed:22908259,
ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451, ECO:0000269|PubMed:7507321,
ECO:0000269|PubMed:9287038}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19657311,
ECO:0000269|PubMed:23863937, ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451, 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}.
-!- 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}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
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EMBL; U03469; AAC52063.1; -; mRNA.
EMBL; L20316; AAA53628.1; -; mRNA.
EMBL; BC104854; AAI04855.1; -; mRNA.
EMBL; BC112041; AAI12042.1; -; mRNA.
EMBL; L24751; AAA35897.1; -; Genomic_DNA.
CCDS; CCDS54177.1; -.
PIR; JC2041; JC2041.
RefSeq; NP_000151.1; NM_000160.4.
RefSeq; XP_006722340.1; XM_006722277.1.
UniGene; Hs.208; -.
PDB; 2A83; X-ray; 1.40 A; C=412-420.
PDB; 3CZF; X-ray; 1.20 A; C=412-420.
PDB; 4ERS; X-ray; 2.64 A; A=28-123.
PDB; 4L6R; X-ray; 3.30 A; A=123-432.
PDB; 4LF3; X-ray; 2.74 A; C/F=29-123.
PDB; 5EE7; X-ray; 2.50 A; A=136-254, A=259-417.
PDB; 5XEZ; X-ray; 3.00 A; A/B=27-432.
PDBsum; 2A83; -.
PDBsum; 3CZF; -.
PDBsum; 4ERS; -.
PDBsum; 4L6R; -.
PDBsum; 4LF3; -.
PDBsum; 5EE7; -.
PDBsum; 5XEZ; -.
ProteinModelPortal; P47871; -.
SMR; P47871; -.
BioGrid; 108912; 3.
IntAct; P47871; 4.
STRING; 9606.ENSP00000383558; -.
BindingDB; P47871; -.
ChEMBL; CHEMBL1985; -.
DrugBank; DB00040; Glucagon recombinant.
GuidetoPHARMACOLOGY; 251; -.
iPTMnet; P47871; -.
PhosphoSitePlus; P47871; -.
BioMuta; GCGR; -.
DMDM; 1346144; -.
PaxDb; P47871; -.
PeptideAtlas; P47871; -.
PRIDE; P47871; -.
ProteomicsDB; 55805; -.
Ensembl; ENST00000400723; ENSP00000383558; ENSG00000215644.
GeneID; 2642; -.
KEGG; hsa:2642; -.
UCSC; uc010wuw.2; human.
CTD; 2642; -.
DisGeNET; 2642; -.
EuPathDB; HostDB:ENSG00000215644.9; -.
GeneCards; GCGR; -.
HGNC; HGNC:4192; GCGR.
HPA; HPA071228; -.
MalaCards; GCGR; -.
MIM; 138033; gene.
neXtProt; NX_P47871; -.
OpenTargets; ENSG00000215644; -.
PharmGKB; PA28607; -.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
GeneTree; ENSGT00760000118800; -.
HOGENOM; HOG000008250; -.
HOVERGEN; HBG008318; -.
InParanoid; P47871; -.
KO; K04583; -.
PhylomeDB; P47871; -.
TreeFam; TF315710; -.
Reactome; R-HSA-163359; Glucagon signaling in metabolic regulation.
Reactome; R-HSA-416476; G alpha (q) signalling events.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-420092; Glucagon-type ligand receptors.
SIGNOR; P47871; -.
EvolutionaryTrace; P47871; -.
GeneWiki; Glucagon_receptor; -.
GenomeRNAi; 2642; -.
PRO; PR:P47871; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000215644; Expressed in 69 organ(s), highest expression level in right lobe of liver.
CleanEx; HS_GCGR; -.
ExpressionAtlas; P47871; baseline and differential.
Genevisible; P47871; HS.
GO; GO:0005768; C:endosome; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004967; F:glucagon receptor activity; IDA:UniProtKB.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0017046; F:peptide hormone binding; IEA:Ensembl.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IMP: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; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:Ensembl.
GO; GO:0008217; P:regulation of blood pressure; TAS:ProtInc.
GO; GO:0070873; P:regulation of glycogen metabolic process; ISS:UniProtKB.
GO; GO:0007584; P:response to nutrient; TAS:ProtInc.
GO; GO:0042594; P:response to starvation; ISS: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.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Diabetes mellitus;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Signal;
Transducer; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 477 Glucagon receptor.
/FTId=PRO_0000012832.
TOPO_DOM 26 136 Extracellular.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TRANSMEM 137 161 Helical; Name=1.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TOPO_DOM 162 173 Cytoplasmic.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TRANSMEM 174 198 Helical; Name=2.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TOPO_DOM 199 225 Extracellular.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TRANSMEM 226 249 Helical; Name=3.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TOPO_DOM 250 263 Cytoplasmic.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TRANSMEM 264 285 Helical; Name=4.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TOPO_DOM 286 303 Extracellular.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TRANSMEM 304 326 Helical; Name=5.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TOPO_DOM 327 350 Cytoplasmic.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TRANSMEM 351 369 Helical; Name=6.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TOPO_DOM 370 381 Extracellular.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TRANSMEM 382 402 Helical; Name=7.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
TOPO_DOM 403 477 Cytoplasmic.
{ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
REGION 350 353 Allosteric inhibitor binding.
{ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
MOD_RES 456 456 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 459 459 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 46 46 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:28514451}.
CARBOHYD 59 59 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:28514451}.
CARBOHYD 74 74 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4ERS,
ECO:0000269|PubMed:22908259,
ECO:0000269|PubMed:28514451}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:4ERS,
ECO:0000269|PubMed:22908259,
ECO:0000269|PubMed:28514451}.
DISULFID 43 67 {ECO:0000244|PDB:4ERS,
ECO:0000244|PDB:4LF3,
ECO:0000269|PubMed:22908259,
ECO:0000269|PubMed:28514451}.
DISULFID 58 100 {ECO:0000244|PDB:4ERS,
ECO:0000244|PDB:4LF3,
ECO:0000269|PubMed:22908259,
ECO:0000269|PubMed:28514451}.
DISULFID 81 121 {ECO:0000244|PDB:4ERS,
ECO:0000244|PDB:4LF3,
ECO:0000269|PubMed:22908259,
ECO:0000269|PubMed:28514451}.
DISULFID 224 294 {ECO:0000244|PDB:4L6R,
ECO:0000244|PDB:5EE7,
ECO:0000269|PubMed:23863937,
ECO:0000269|PubMed:27111510,
ECO:0000269|PubMed:28514451}.
VARIANT 40 40 G -> S (in dbSNP:rs1801483).
{ECO:0000269|PubMed:7589886}.
/FTId=VAR_003581.
VARIANT 86 86 P -> S (abolishes glucagon binding).
{ECO:0000269|PubMed:19657311,
ECO:0000269|PubMed:23863937}.
/FTId=VAR_069815.
VARIANT 114 114 P -> A (in dbSNP:rs5385).
/FTId=VAR_014837.
VARIANT 303 303 F -> C (in dbSNP:rs5387).
/FTId=VAR_033966.
MUTAGEN 36 36 W->A: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 63 63 D->A: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 65 65 Y->A: Strongly reduced affinity for
glucagon. Increased constitutive
signaling via G-proteins.
{ECO:0000269|PubMed:22908259}.
MUTAGEN 113 113 Q->A,N: No effect on affinity for
glucagon. {ECO:0000269|PubMed:22908259}.
MUTAGEN 113 113 Q->C: Causes the formation of an
artifactual disulfide bond that abolishes
glucagon binding; when associated with C-
209. {ECO:0000269|PubMed:28514451}.
MUTAGEN 113 113 Q->E: Strongly reduced affinity for
glucagon. {ECO:0000269|PubMed:22908259}.
MUTAGEN 130 130 V->C: Causes the formation of an
artifactual disulfide bond that
interferes with glucagon binding; when
associated with C-210.
{ECO:0000269|PubMed:28514451}.
MUTAGEN 135 135 A->P: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 145 145 Y->A: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 149 149 Y->A: Abolishes expression at cell
surface and glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 198 198 L->A: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 201 201 R->D: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 202 202 Y->A: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 208 208 D->Q: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 209 209 D->C: Causes the formation of an
artifactual disulfide bond that abolishes
glucagon binding; when associated with C-
113. {ECO:0000269|PubMed:28514451}.
MUTAGEN 210 210 L->C: Causes the formation of an
artifactual disulfide bond that
interferes with glucagon binding; when
associated with C-130.
{ECO:0000269|PubMed:28514451}.
MUTAGEN 215 215 W->L: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 232 232 Q->L: Abolishes expression at cell
surface and glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 233 233 Y->A: Abolishes glucagon binding.
Strongly reduces expression at the cell
surface. {ECO:0000269|PubMed:23863937}.
MUTAGEN 286 286 K->L: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 290 290 E->A: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 294 294 C->A,S: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 295 295 W->A,H: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 304 304 W->Q: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 350 350 S->A: Strongly decreases affinity for
synthetic antagonist.
{ECO:0000269|PubMed:28514451}.
MUTAGEN 353 353 T->A: Loss of synthetic antagonist
binding. {ECO:0000269|PubMed:28514451}.
MUTAGEN 382 382 L->A: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
MUTAGEN 386 386 L->F: Abolishes glucagon binding.
{ECO:0000269|PubMed:23863937}.
HELIX 31 49 {ECO:0000244|PDB:4ERS}.
STRAND 54 58 {ECO:0000244|PDB:4ERS}.
STRAND 64 68 {ECO:0000244|PDB:4LF3}.
STRAND 75 80 {ECO:0000244|PDB:4ERS}.
TURN 86 90 {ECO:0000244|PDB:4ERS}.
STRAND 95 100 {ECO:0000244|PDB:4ERS}.
STRAND 104 106 {ECO:0000244|PDB:4LF3}.
HELIX 119 121 {ECO:0000244|PDB:4ERS}.
STRAND 127 130 {ECO:0000244|PDB:5XEZ}.
HELIX 139 165 {ECO:0000244|PDB:5EE7}.
HELIX 167 169 {ECO:0000244|PDB:5EE7}.
HELIX 172 198 {ECO:0000244|PDB:5EE7}.
STRAND 203 206 {ECO:0000244|PDB:5XEZ}.
HELIX 213 215 {ECO:0000244|PDB:5EE7}.
HELIX 218 253 {ECO:0000244|PDB:5EE7}.
HELIX 264 271 {ECO:0000244|PDB:5EE7}.
HELIX 273 289 {ECO:0000244|PDB:5EE7}.
STRAND 293 295 {ECO:0000244|PDB:4L6R}.
HELIX 305 307 {ECO:0000244|PDB:5EE7}.
HELIX 308 334 {ECO:0000244|PDB:5EE7}.
HELIX 343 369 {ECO:0000244|PDB:5EE7}.
HELIX 379 389 {ECO:0000244|PDB:5EE7}.
HELIX 392 400 {ECO:0000244|PDB:5EE7}.
TURN 401 403 {ECO:0000244|PDB:5EE7}.
HELIX 405 417 {ECO:0000244|PDB:5EE7}.
SEQUENCE 477 AA; 54009 MW; ADBB477C6267AE6E CRC64;
MPPCQPQRPL LLLLLLLACQ PQVPSAQVMD FLFEKWKLYG DQCHHNLSLL PPPTELVCNR
TFDKYSCWPD TPANTTANIS CPWYLPWHHK VQHRFVFKRC GPDGQWVRGP RGQPWRDASQ
CQMDGEEIEV QKEVAKMYSS FQVMYTVGYS LSLGALLLAL AILGGLSKLH CTRNAIHANL
FASFVLKASS VLVIDGLLRT RYSQKIGDDL SVSTWLSDGA VAGCRVAAVF MQYGIVANYC
WLLVEGLYLH NLLGLATLPE RSFFSLYLGI GWGAPMLFVV PWAVVKCLFE NVQCWTSNDN
MGFWWILRFP VFLAILINFF IFVRIVQLLV AKLRARQMHH TDYKFRLAKS TLTLIPLLGV
HEVVFAFVTD EHAQGTLRSA KLFFDLFLSS FQGLLVAVLY CFLNKEVQSE LRRRWHRWRL
GKVLWEERNT SNHRASSSPG HGPPSKELQF GRGGGSQDSS AETPLAGGLP RLAESPF


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