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Glucagon-like peptide 1 receptor (GLP-1 receptor) (GLP-1-R) (GLP-1R)

 GLP1R_HUMAN             Reviewed;         463 AA.
P43220; Q2M229; Q99669;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 2.
12-SEP-2018, entry version 177.
RecName: Full=Glucagon-like peptide 1 receptor;
Short=GLP-1 receptor;
Short=GLP-1-R;
Short=GLP-1R;
Flags: Precursor;
Name=GLP1R;
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, SUBCELLULAR LOCATION, AND
VARIANT PHE-260.
TISSUE=Pancreatic islet;
PubMed=8405712; DOI=10.2337/diab.42.11.1678;
Thorens B., Porret A., Buehler L., Deng S., Morel P., Widmann C.;
"Cloning and functional expression of the human islet GLP-1 receptor.
Demonstration that exendin-4 is an agonist and exendin-(9-39) an
antagonist of the receptor.";
Diabetes 42:1678-1682(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-260.
TISSUE=Pancreas;
PubMed=8404634; DOI=10.1210/endo.133.4.8404634;
Dillon J.S., Tanizawa Y., Wheeler M.B., Leng X., Ligon B.B.,
Rabin D.U., Yoo-Warren H., Permutt M., Boyd A.E.;
"Cloning and functional expression of the human glucagon-like peptide-
1 (GLP-1) receptor.";
Endocrinology 133:1907-1910(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
VARIANT PHE-260.
TISSUE=Gastric carcinoma;
PubMed=8216285; DOI=10.1006/bbrc.1993.2226;
Graziano M.P., Hey P.J., Borkowski D., Chicchi G.C., Strader C.D.;
"Cloning and functional expression of a human glucagon-like peptide-1
receptor.";
Biochem. Biophys. Res. Commun. 196:141-146(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Insulinoma;
PubMed=7517895; DOI=10.1016/0014-5793(94)00553-2;
van Eyll B., Lankat-Buttgereit B., Bode H.P., Goeke R., Goeke B.;
"Signal transduction of the GLP-1-receptor cloned from a human
insulinoma.";
FEBS Lett. 348:7-13(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-260.
TISSUE=Pancreas;
PubMed=7843404; DOI=10.1016/0014-5793(94)01430-9;
Wei Y., Mojsov S.;
"Tissue-specific expression of the human receptor for glucagon-like
peptide-I: brain, heart and pancreatic forms have the same deduced
amino acid sequences.";
FEBS Lett. 358:219-224(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S.,
Tsutsumi S., Aburatani H., Asai K., Akiyama Y.;
"Genome-wide discovery and analysis of human seven transmembrane helix
receptor genes.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-7; LYS-20; HIS-44;
GLN-131; SER-168; PHE-260; THR-316; CYS-333 AND GLN-421.
NIEHS SNPs program;
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-260.
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).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
TISSUE=Placenta;
PubMed=9213353; DOI=10.1016/S0196-9781(97)00001-6;
Lankat-Buttgereit B., Goeke B.;
"Cloning and characterization of the 5' flanking sequences (promoter
region) of the human GLP-1 receptor gene.";
Peptides 18:617-624(1997).
[11]
DISULFIDE BOND.
PubMed=20869417; DOI=10.1016/j.peptides.2010.09.015;
Mann R.J., Al-Sabah S., de Maturana R.L., Sinfield J.K., Donnelly D.;
"Functional coupling of Cys-226 and Cys-296 in the glucagon-like
peptide-1 (GLP-1) receptor indicates a disulfide bond that is close to
the activation pocket.";
Peptides 31:2289-2293(2010).
[12]
ADP-RIBOSYLATION AT CYS-341 AND ARG-348.
PubMed=21901419; DOI=10.1007/s11033-011-1225-0;
Dezelak M., Bavec A.;
"Glucagon like-peptide-1 receptor is covalently modified by endogenous
mono-ADP-ribosyltransferase.";
Mol. Biol. Rep. 39:4375-4381(2012).
[13]
GLYCOSYLATION AT ASN-63; ASN-82 AND ASN-115, AND SUBUNIT.
PubMed=22412906; DOI=10.1371/journal.pone.0032675;
Whitaker G.M., Lynn F.C., McIntosh C.H., Accili E.A.;
"Regulation of GIP and GLP1 receptor cell surface expression by N-
glycosylation and receptor heteromerization.";
PLoS ONE 7:E32675-E32675(2012).
[14]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 24-145 IN COMPLEX WITH
ANTAGONIST EXENDIN-4, AND DISULFIDE BONDS.
PubMed=18287102; DOI=10.1074/jbc.M708740200;
Runge S., Thogersen H., Madsen K., Lau J., Rudolph R.;
"Crystal structure of the ligand-bound glucagon-like peptide-1
receptor extracellular domain.";
J. Biol. Chem. 283:11340-11347(2008).
[15]
X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 24-145 IN COMPLEX WITH
GLUCAGON-LIKE PEPTIDE-1, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE
BONDS, AND MUTAGENESIS OF LEU-32; TYR-69; TYR-88; LEU-89; PRO-90;
ARG-121; GLU-127 AND GLU-128.
PubMed=19861722; DOI=10.1074/jbc.M109.033829;
Underwood C.R., Garibay P., Knudsen L.B., Hastrup S., Peters G.H.,
Rudolph R., Reedtz-Runge S.;
"Crystal structure of glucagon-like peptide-1 in complex with the
extracellular domain of the glucagon-like peptide-1 receptor.";
J. Biol. Chem. 285:723-730(2010).
[16]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 24-145, FUNCTION,
SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
PubMed=26308095; DOI=10.1021/acs.jmedchem.5b00726;
Lau J., Bloch P., Schaeffer L., Pettersson I., Spetzler J., Kofoed J.,
Madsen K., Knudsen L.B., McGuire J., Steensgaard D.B., Strauss H.M.,
Gram D.X., Knudsen S.M., Nielsen F.S., Thygesen P., Reedtz-Runge S.,
Kruse T.;
"Discovery of the Once-Weekly Glucagon-Like Peptide-1 (GLP-1) Analogue
Semaglutide.";
J. Med. Chem. 58:7370-7380(2015).
[17]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 24-145, FUNCTION,
SUBCELLULAR LOCATION, AND DISULFIDE BONDS.
PubMed=27196125; DOI=10.1038/srep26236;
Hennen S., Kodra J.T., Soroka V., Krogh B.O., Wu X., Kaastrup P.,
Oerskov C., Roenn S.G., Schluckebier G., Barbateskovic S.,
Gandhi P.S., Reedtz-Runge S.;
"Structural insight into antibody-mediated antagonism of the Glucagon-
like peptide-1 Receptor.";
Sci. Rep. 6:26236-26236(2016).
[18]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 128-431 IN COMPLEXES WITH
ALLOSTERIC MODULATORS, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
LOCATION, TOPOLOGY, DISULFIDE BOND, AND MUTAGENESIS OF ARG-176;
ILE-317; SER-352; THR-355 AND GLY-361.
PubMed=28514449; DOI=10.1038/nature22378;
Song G., Yang D., Wang Y., de Graaf C., Zhou Q., Jiang S., Liu K.,
Cai X., Dai A., Lin G., Liu D., Wu F., Wu Y., Zhao S., Ye L.,
Han G.W., Lau J., Wu B., Hanson M.A., Liu Z.J., Wang M.W.,
Stevens R.C.;
"Human GLP-1 receptor transmembrane domain structure in complex with
allosteric modulators.";
Nature 546:312-315(2017).
-!- FUNCTION: G-protein coupled receptor for glucagon-like peptide 1
(GLP-1) (PubMed:8405712, PubMed:8216285, PubMed:7517895,
PubMed:19861722, PubMed:26308095, PubMed:27196125,
PubMed:28514449). Ligand binding triggers activation of a
signaling cascade that leads to the activation of adenylyl cyclase
and increased intracellular cAMP levels (PubMed:8405712,
PubMed:8216285, PubMed:7517895, PubMed:19861722, PubMed:26308095,
PubMed:27196125, PubMed:28514449). 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}.
-!- 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}.
-!- SUBUNIT: May form homodimers and heterodimers with GIPR.
{ECO:0000269|PubMed:18287102, ECO:0000269|PubMed:22412906}.
-!- INTERACTION:
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-7466542, EBI-10172290;
P60410:KRTAP10-8; NbExp=3; IntAct=EBI-7466542, EBI-10171774;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-7466542, EBI-10172052;
Q7Z3S9:NOTCH2NL; NbExp=5; IntAct=EBI-7466542, EBI-945833;
-!- 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}.
-!- PTM: N-glycosylation enhances cell surface expression and
lengthens receptor half-life by preventing degradation in the ER.
{ECO:0000269|PubMed:22412906}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/glp1r/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Glucagon-like peptide 1 entry;
URL="https://en.wikipedia.org/wiki/Glucagon-like_peptide-1";
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EMBL; U01104; AAA03614.1; -; mRNA.
EMBL; U01157; AAA62471.1; -; mRNA.
EMBL; U01156; AAC50050.1; -; mRNA.
EMBL; L23503; AAA17021.1; -; mRNA.
EMBL; U10037; AAA63787.1; -; mRNA.
EMBL; AB065685; BAC05908.1; -; Genomic_DNA.
EMBL; AY439112; AAR05444.1; -; Genomic_DNA.
EMBL; AL035690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC112126; AAI12127.1; -; mRNA.
EMBL; BC113493; AAI13494.1; -; mRNA.
EMBL; U66062; AAB64013.1; -; Genomic_DNA.
CCDS; CCDS4839.1; -.
PIR; I84494; I84494.
PIR; S71624; S71624.
RefSeq; NP_002053.3; NM_002062.4.
UniGene; Hs.351883; -.
UniGene; Hs.389103; -.
PDB; 3C59; X-ray; 2.30 A; A=24-145.
PDB; 3C5T; X-ray; 2.10 A; A=24-145.
PDB; 3IOL; X-ray; 2.10 A; A=24-145.
PDB; 4ZGM; X-ray; 1.80 A; A=24-145.
PDB; 5E94; X-ray; 2.00 A; G/H=24-145.
PDB; 5NX2; X-ray; 3.70 A; A=24-432.
PDB; 5OTT; X-ray; 1.92 A; A=24-139.
PDB; 5OTU; X-ray; 1.80 A; A/C=24-139.
PDB; 5OTV; X-ray; 2.00 A; A/C=24-139.
PDB; 5OTW; X-ray; 2.10 A; A/C=24-139.
PDB; 5OTX; X-ray; 2.00 A; A/C=24-139.
PDB; 5VEW; X-ray; 2.70 A; A/B=128-257, A/B=261-431.
PDB; 5VEX; X-ray; 3.00 A; A/B=128-257, A/B=261-431.
PDB; 6B3J; EM; 3.30 A; R=24-463.
PDB; 6GB1; X-ray; 2.73 A; A=21-145.
PDBsum; 3C59; -.
PDBsum; 3C5T; -.
PDBsum; 3IOL; -.
PDBsum; 4ZGM; -.
PDBsum; 5E94; -.
PDBsum; 5NX2; -.
PDBsum; 5OTT; -.
PDBsum; 5OTU; -.
PDBsum; 5OTV; -.
PDBsum; 5OTW; -.
PDBsum; 5OTX; -.
PDBsum; 5VEW; -.
PDBsum; 5VEX; -.
PDBsum; 6B3J; -.
PDBsum; 6GB1; -.
ProteinModelPortal; P43220; -.
SMR; P43220; -.
BioGrid; 109002; 106.
DIP; DIP-29980N; -.
IntAct; P43220; 9.
MINT; P43220; -.
STRING; 9606.ENSP00000362353; -.
BindingDB; P43220; -.
ChEMBL; CHEMBL1784; -.
DrugBank; DB09043; Albiglutide.
DrugBank; DB09045; Dulaglutide.
DrugBank; DB01276; Exenatide.
DrugBank; DB00040; Glucagon recombinant.
DrugBank; DB05162; GSK716155.
DrugBank; DB06655; Liraglutide.
GuidetoPHARMACOLOGY; 249; -.
TCDB; 9.A.14.4.6; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P43220; -.
PhosphoSitePlus; P43220; -.
BioMuta; GLP1R; -.
DMDM; 311033387; -.
PaxDb; P43220; -.
PeptideAtlas; P43220; -.
PRIDE; P43220; -.
ProteomicsDB; 55596; -.
DNASU; 2740; -.
Ensembl; ENST00000373256; ENSP00000362353; ENSG00000112164.
GeneID; 2740; -.
KEGG; hsa:2740; -.
UCSC; uc003ooj.5; human.
CTD; 2740; -.
DisGeNET; 2740; -.
EuPathDB; HostDB:ENSG00000112164.5; -.
GeneCards; GLP1R; -.
H-InvDB; HIX0095000; -.
H-InvDB; HIX0200932; -.
HGNC; HGNC:4324; GLP1R.
MIM; 138032; gene.
neXtProt; NX_P43220; -.
OpenTargets; ENSG00000112164; -.
PharmGKB; PA28725; -.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
GeneTree; ENSGT00760000118800; -.
HOGENOM; HOG000008250; -.
HOVERGEN; HBG008318; -.
InParanoid; P43220; -.
KO; K04581; -.
OMA; RNSNMNY; -.
OrthoDB; EOG091G0NF8; -.
PhylomeDB; P43220; -.
TreeFam; TF315710; -.
Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
Reactome; R-HSA-418555; G alpha (s) signalling events.
Reactome; R-HSA-420092; Glucagon-type ligand receptors.
SIGNOR; P43220; -.
EvolutionaryTrace; P43220; -.
GeneWiki; Glucagon-like_peptide_1_receptor; -.
GenomeRNAi; 2740; -.
PRO; PR:P43220; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000112164; Expressed in 165 organ(s), highest expression level in myocardium.
CleanEx; HS_GLP1R; -.
Genevisible; P43220; HS.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004967; F:glucagon receptor activity; IEA:InterPro.
GO; GO:0044508; F:glucagon-like peptide 1 receptor activity; IDA:UniProtKB.
GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0007611; P:learning or memory; IEA:Ensembl.
GO; GO:0045777; P:positive regulation of blood pressure; IEA:Ensembl.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
GO; GO:0008016; P:regulation of heart contraction; IEA:Ensembl.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:1990911; P:response to psychosocial stress; IEA:Ensembl.
CDD; cd15268; 7tmB1_GLP1R; 1.
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; IPR003292; GPCR_2_GLP1_rcpt.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
PANTHER; PTHR12011:SF245; PTHR12011:SF245; 1.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF02793; HRM; 1.
PRINTS; PR01353; GLUCAGNFAMLY.
PRINTS; PR01355; GLUCAGNLIKER.
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; ADP-ribosylation; Cell membrane; Complete proteome;
Disulfide bond; G-protein coupled receptor; Glycoprotein; Membrane;
Polymorphism; Receptor; Reference proteome; Signal; Transducer;
Transmembrane; Transmembrane helix.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 463 Glucagon-like peptide 1 receptor.
/FTId=PRO_0000012835.
TOPO_DOM 24 139 Extracellular.
{ECO:0000269|PubMed:28514449}.
TRANSMEM 140 164 Helical; Name=1.
{ECO:0000269|PubMed:28514449}.
TOPO_DOM 165 175 Cytoplasmic.
{ECO:0000269|PubMed:28514449}.
TRANSMEM 176 201 Helical; Name=2.
{ECO:0000269|PubMed:28514449}.
TOPO_DOM 202 227 Extracellular.
{ECO:0000269|PubMed:28514449}.
TRANSMEM 228 251 Helical; Name=3.
{ECO:0000269|PubMed:28514449}.
TOPO_DOM 252 265 Cytoplasmic.
{ECO:0000269|PubMed:28514449}.
TRANSMEM 266 290 Helical; Name=4.
{ECO:0000269|PubMed:28514449}.
TOPO_DOM 291 305 Extracellular.
{ECO:0000269|PubMed:28514449}.
TRANSMEM 306 328 Helical; Name=5.
{ECO:0000269|PubMed:28514449}.
TOPO_DOM 329 348 Cytoplasmic.
{ECO:0000269|PubMed:28514449}.
TRANSMEM 349 370 Helical; Name=6.
{ECO:0000269|PubMed:28514449}.
TOPO_DOM 371 383 Extracellular.
{ECO:0000269|PubMed:28514449}.
TRANSMEM 384 404 Helical; Name=7.
{ECO:0000269|PubMed:28514449}.
TOPO_DOM 405 463 Cytoplasmic.
{ECO:0000269|PubMed:28514449}.
REGION 352 355 Important for allosteric inhibitor
binding. {ECO:0000269|PubMed:28514449}.
SITE 121 121 Interaction with the endogenous ligand
GLP-1. {ECO:0000269|PubMed:19861722}.
SITE 128 128 Interaction with the endogenous ligand
GLP-1. {ECO:0000269|PubMed:19861722}.
MOD_RES 341 341 ADP-ribosylcysteine.
{ECO:0000269|PubMed:21901419}.
MOD_RES 348 348 ADP-ribosylarginine.
{ECO:0000269|PubMed:21901419}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22412906}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22412906}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22412906}.
DISULFID 46 71 {ECO:0000244|PDB:3C59,
ECO:0000244|PDB:3C5T,
ECO:0000244|PDB:3IOL,
ECO:0000244|PDB:4ZGM,
ECO:0000244|PDB:5E94,
ECO:0000269|PubMed:19861722,
ECO:0000269|PubMed:26308095,
ECO:0000269|PubMed:27196125}.
DISULFID 62 104 {ECO:0000244|PDB:3C59,
ECO:0000244|PDB:3C5T,
ECO:0000244|PDB:3IOL,
ECO:0000244|PDB:4ZGM,
ECO:0000244|PDB:5E94,
ECO:0000269|PubMed:19861722,
ECO:0000269|PubMed:26308095,
ECO:0000269|PubMed:27196125}.
DISULFID 85 126 {ECO:0000244|PDB:3C59,
ECO:0000244|PDB:3C5T,
ECO:0000244|PDB:3IOL,
ECO:0000244|PDB:4ZGM,
ECO:0000244|PDB:5E94,
ECO:0000269|PubMed:19861722,
ECO:0000269|PubMed:26308095,
ECO:0000269|PubMed:27196125}.
DISULFID 226 296 {ECO:0000244|PDB:3C59,
ECO:0000244|PDB:3C5T,
ECO:0000244|PDB:3IOL,
ECO:0000244|PDB:4ZGM,
ECO:0000244|PDB:5E94,
ECO:0000244|PDB:5VEW,
ECO:0000244|PDB:5VEX,
ECO:0000269|PubMed:19861722,
ECO:0000269|PubMed:26308095,
ECO:0000269|PubMed:27196125,
ECO:0000269|PubMed:28514449}.
VARIANT 7 7 P -> L (in dbSNP:rs10305420).
{ECO:0000269|Ref.7}.
/FTId=VAR_018924.
VARIANT 20 20 R -> K (in dbSNP:rs10305421).
{ECO:0000269|Ref.7}.
/FTId=VAR_018925.
VARIANT 44 44 R -> H (in dbSNP:rs2295006).
{ECO:0000269|Ref.7}.
/FTId=VAR_018926.
VARIANT 131 131 R -> Q (in dbSNP:rs3765467).
{ECO:0000269|Ref.7}.
/FTId=VAR_018927.
VARIANT 168 168 G -> S (in dbSNP:rs6923761).
{ECO:0000269|Ref.7}.
/FTId=VAR_018928.
VARIANT 260 260 L -> F (in dbSNP:rs1042044).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:7843404,
ECO:0000269|PubMed:8216285,
ECO:0000269|PubMed:8404634,
ECO:0000269|PubMed:8405712,
ECO:0000269|Ref.7}.
/FTId=VAR_015098.
VARIANT 316 316 A -> T (in dbSNP:rs10305492).
{ECO:0000269|Ref.7}.
/FTId=VAR_018929.
VARIANT 333 333 S -> C (in dbSNP:rs10305493).
{ECO:0000269|Ref.7}.
/FTId=VAR_018930.
VARIANT 421 421 R -> Q (in dbSNP:rs10305510).
{ECO:0000269|Ref.7}.
/FTId=VAR_018931.
MUTAGEN 32 32 L->A: No effect on stimulation of cAMP
accumulation and on GLP-1 binding.
{ECO:0000269|PubMed:19861722}.
MUTAGEN 69 69 Y->A: Abolishes stimulation of cAMP
accumulation in response to GLP-1.
{ECO:0000269|PubMed:19861722}.
MUTAGEN 88 88 Y->A: Abolishes stimulation of cAMP
accumulation in response to GLP-1.
{ECO:0000269|PubMed:19861722}.
MUTAGEN 89 89 L->A: Abolishes stimulation of cAMP
accumulation in response to GLP-1.
{ECO:0000269|PubMed:19861722}.
MUTAGEN 90 90 P->A: Strongly decreased stimulation of
cAMP accumulation in response to GLP-1.
{ECO:0000269|PubMed:19861722}.
MUTAGEN 121 121 R->A: Strongly decreased stimulation of
cAMP accumulation in response to GLP-1.
{ECO:0000269|PubMed:19861722}.
MUTAGEN 127 127 E->A: No effect on stimulation of cAMP
accumulation in response to GLP-1.
{ECO:0000269|PubMed:19861722}.
MUTAGEN 128 128 E->A: Slightly decreases stimulation of
cAMP accumulation in response to GLP-1.
{ECO:0000269|PubMed:19861722}.
MUTAGEN 128 128 E->Q: No effect on stimulation of cAMP
accumulation in response to GLP-1.
{ECO:0000269|PubMed:19861722}.
MUTAGEN 176 176 R->Q: Decreases sensitivity to GLP-1.
{ECO:0000269|PubMed:28514449}.
MUTAGEN 317 317 I->C: Causes the formation of an
artifactual disulfide bond that abolishes
signaling in response to GLP-1 binding;
when associated with C-361.
{ECO:0000269|PubMed:28514449}.
MUTAGEN 352 352 S->A: Abolishes inhibition by negative
allosteric modulators.
{ECO:0000269|PubMed:28514449}.
MUTAGEN 355 355 T->A: Abolishes inhibition by the
negative allosteric modulators NNC0640
and PF-06372222, but does not abolish
inhibition by MK-0893.
{ECO:0000269|PubMed:28514449}.
MUTAGEN 361 361 G->C: Causes the formation of an
artifactual disulfide bond that abolishes
signaling in response to GLP-1 binding;
when associated with C-317.
{ECO:0000269|PubMed:28514449}.
CONFLICT 12 12 L -> V (in Ref. 1; AAA03614, 4; no
nucleotide entry and 10; AAB64013).
{ECO:0000305}.
CONFLICT 136 137 SP -> WG (in Ref. 1; AAA03614).
{ECO:0000305}.
CONFLICT 137 137 P -> R (in Ref. 4; no nucleotide entry).
{ECO:0000305}.
CONFLICT 151 151 G -> A (in Ref. 1; AAA03614).
{ECO:0000305}.
CONFLICT 221 221 Q -> L (in Ref. 5; AAA63787).
{ECO:0000305}.
CONFLICT 289 289 Y -> I (in Ref. 1; AAA03614).
{ECO:0000305}.
CONFLICT 316 316 A -> G (in Ref. 2; AAA62471/AAC50050).
{ECO:0000305}.
HELIX 32 52 {ECO:0000244|PDB:4ZGM}.
STRAND 57 59 {ECO:0000244|PDB:5E94}.
STRAND 68 71 {ECO:0000244|PDB:6B3J}.
STRAND 79 84 {ECO:0000244|PDB:4ZGM}.
HELIX 92 94 {ECO:0000244|PDB:4ZGM}.
STRAND 99 104 {ECO:0000244|PDB:4ZGM}.
STRAND 108 110 {ECO:0000244|PDB:4ZGM}.
STRAND 116 119 {ECO:0000244|PDB:4ZGM}.
HELIX 124 126 {ECO:0000244|PDB:4ZGM}.
HELIX 137 142 {ECO:0000244|PDB:5E94}.
HELIX 170 172 {ECO:0000244|PDB:5VEW}.
HELIX 175 199 {ECO:0000244|PDB:5VEW}.
HELIX 206 210 {ECO:0000244|PDB:6B3J}.
TURN 220 222 {ECO:0000244|PDB:5VEW}.
HELIX 224 256 {ECO:0000244|PDB:5VEW}.
HELIX 263 273 {ECO:0000244|PDB:5VEW}.
HELIX 275 291 {ECO:0000244|PDB:5VEW}.
TURN 295 298 {ECO:0000244|PDB:5VEW}.
TURN 304 306 {ECO:0000244|PDB:5VEW}.
HELIX 307 336 {ECO:0000244|PDB:5VEW}.
HELIX 345 366 {ECO:0000244|PDB:5VEW}.
TURN 367 369 {ECO:0000244|PDB:5VEW}.
TURN 370 372 {ECO:0000244|PDB:6B3J}.
HELIX 373 375 {ECO:0000244|PDB:6B3J}.
HELIX 381 384 {ECO:0000244|PDB:5VEW}.
HELIX 387 402 {ECO:0000244|PDB:5VEW}.
TURN 403 405 {ECO:0000244|PDB:5VEW}.
HELIX 407 421 {ECO:0000244|PDB:5VEW}.
SEQUENCE 463 AA; 53026 MW; EE7C0EAE29931F5D CRC64;
MAGAPGPLRL ALLLLGMVGR AGPRPQGATV SLWETVQKWR EYRRQCQRSL TEDPPPATDL
FCNRTFDEYA CWPDGEPGSF VNVSCPWYLP WASSVPQGHV YRFCTAEGLW LQKDNSSLPW
RDLSECEESK RGERSSPEEQ LLFLYIIYTV GYALSFSALV IASAILLGFR HLHCTRNYIH
LNLFASFILR ALSVFIKDAA LKWMYSTAAQ QHQWDGLLSY QDSLSCRLVF LLMQYCVAAN
YYWLLVEGVY LYTLLAFSVL SEQWIFRLYV SIGWGVPLLF VVPWGIVKYL YEDEGCWTRN
SNMNYWLIIR LPILFAIGVN FLIFVRVICI VVSKLKANLM CKTDIKCRLA KSTLTLIPLL
GTHEVIFAFV MDEHARGTLR FIKLFTELSF TSFQGLMVAI LYCFVNNEVQ LEFRKSWERW
RLEHLHIQRD SSMKPLKCPT SSLSSGATAG SSMYTATCQA SCS


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