GLP1R_RAT
ID GLP1R_RAT Reviewed; 463 AA.
AC P32301; Q64073; Q6LD83;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Glucagon-like peptide 1 receptor;
DE Short=GLP-1 receptor;
DE Short=GLP-1-R;
DE Short=GLP-1R;
DE Flags: Precursor;
GN Name=Glp1r; Synonyms=Glpr;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Pancreatic islet;
RX PubMed=1326760; DOI=10.1073/pnas.89.18.8641;
RA Thorens B.;
RT "Expression cloning of the pancreatic beta cell receptor for the gluco-
RT incretin hormone glucagon-like peptide 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:8641-8645(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Lung;
RX PubMed=7813606; DOI=10.1055/s-0029-1211301;
RA Lankat-Buttgereit B., Goke R., Fehmann H.C., Richter G., Goke B.;
RT "Molecular cloning of a cDNA encoding for the GLP-1 receptor expressed in
RT rat lung.";
RL Exp. Clin. Endocrinol. 102:341-347(1994).
CC -!- FUNCTION: G-protein coupled receptor for glucagon-like peptide 1 (GLP-
CC 1) (PubMed:1326760, PubMed:7813606). Ligand binding triggers activation
CC of a signaling cascade that leads to the activation of adenylyl cyclase
CC and increased intracellular cAMP levels (PubMed:1326760,
CC PubMed:7813606). Plays a role in regulating insulin secretion in
CC response to GLP-1 (By similarity). {ECO:0000250|UniProtKB:O35659,
CC ECO:0000269|PubMed:1326760, ECO:0000269|PubMed:7813606}.
CC -!- SUBUNIT: May form homodimers and heterodimers with GIPR.
CC {ECO:0000250|UniProtKB:P43220}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1326760,
CC ECO:0000269|PubMed:7813606}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P43220}.
CC -!- TISSUE SPECIFICITY: Pancreatic islets, stomach, lung, rat insulinoma
CC cell line. {ECO:0000269|PubMed:1326760}.
CC -!- PTM: N-glycosylation enhances cell surface expression and lengthens
CC receptor half-life by preventing degradation in the ER.
CC {ECO:0000250|UniProtKB:P43220}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; M97797; AAA73377.1; -; mRNA.
DR EMBL; S75952; AAP31860.1; -; mRNA.
DR PIR; A46172; A46172.
DR RefSeq; NP_036860.1; NM_012728.1.
DR AlphaFoldDB; P32301; -.
DR SMR; P32301; -.
DR BioGRID; 247128; 1.
DR STRING; 10116.ENSRNOP00000001527; -.
DR BindingDB; P32301; -.
DR ChEMBL; CHEMBL5862; -.
DR DrugCentral; P32301; -.
DR GuidetoPHARMACOLOGY; 249; -.
DR GlyGen; P32301; 3 sites.
DR iPTMnet; P32301; -.
DR PhosphoSitePlus; P32301; -.
DR SwissPalm; P32301; -.
DR PaxDb; P32301; -.
DR GeneID; 25051; -.
DR KEGG; rno:25051; -.
DR CTD; 2740; -.
DR RGD; 2703; Glp1r.
DR eggNOG; KOG4564; Eukaryota.
DR InParanoid; P32301; -.
DR OrthoDB; 651627at2759; -.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR PRO; PR:P32301; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IPI:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:RGD.
DR GO; GO:0004967; F:glucagon receptor activity; IEA:InterPro.
DR GO; GO:0044508; F:glucagon-like peptide 1 receptor activity; ISS:UniProtKB.
DR GO; GO:0017046; F:peptide hormone binding; IDA:RGD.
DR GO; GO:0001653; F:peptide receptor activity; IDA:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0008306; P:associative learning; IDA:RGD.
DR GO; GO:0019933; P:cAMP-mediated signaling; IMP:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007631; P:feeding behavior; IMP:RGD.
DR GO; GO:0046879; P:hormone secretion; IDA:UniProtKB.
DR GO; GO:0030073; P:insulin secretion; IMP:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IMP:UniProtKB.
DR GO; GO:0007613; P:memory; IDA:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; TAS:RGD.
DR GO; GO:0045777; P:positive regulation of blood pressure; IDA:RGD.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:RGD.
DR GO; GO:0045823; P:positive regulation of heart contraction; IDA:RGD.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IDA:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; ISO:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0008016; P:regulation of heart contraction; ISO:RGD.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:RGD.
DR GO; GO:0009749; P:response to glucose; IMP:RGD.
DR GO; GO:1990911; P:response to psychosocial stress; ISO:RGD.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR003290; GPCR_2_GLP1/glucagon_rcpt.
DR InterPro; IPR003292; GPCR_2_GLP1_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR PANTHER; PTHR45620:SF25; PTHR45620:SF25; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR01353; GLUCAGNFAMLY.
DR PRINTS; PR01355; GLUCAGNLIKER.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00008; HormR; 1.
DR SUPFAM; SSF111418; SSF111418; 1.
DR PROSITE; PS00649; G_PROTEIN_RECEP_F2_1; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Signal; Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..463
FT /note="Glucagon-like peptide 1 receptor"
FT /id="PRO_0000012837"
FT TOPO_DOM 22..139
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 140..164
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT TOPO_DOM 165..175
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 176..201
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT TOPO_DOM 202..227
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 228..251
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT TOPO_DOM 252..265
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 266..290
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT TOPO_DOM 291..305
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 306..328
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT TOPO_DOM 329..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 349..370
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT TOPO_DOM 371..383
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 384..404
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT TOPO_DOM 405..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 352..355
FT /note="Important for allosteric inhibitor binding"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT SITE 121
FT /note="Interaction with the endogenous ligand GLP-1"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT SITE 128
FT /note="Interaction with the endogenous ligand GLP-1"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT MOD_RES 341
FT /note="ADP-ribosylcysteine"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT MOD_RES 348
FT /note="ADP-ribosylarginine"
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..71
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT DISULFID 62..104
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT DISULFID 85..126
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT DISULFID 226..296
FT /evidence="ECO:0000250|UniProtKB:P43220"
FT CONFLICT 323
FT /note="V -> I (in Ref. 2; AAP31860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 52877 MW; ABE2183E8EBE621F CRC64;
MAVTPSLLRL ALLLLGAVGR AGPRPQGATV SLSETVQKWR EYRHQCQRFL TEAPLLATGL
FCNRTFDDYA CWPDGPPGSF VNVSCPWYLP WASSVLQGHV YRFCTAEGIW LHKDNSSLPW
RDLSECEESK QGERNSPEEQ LLSLYIIYTV GYALSFSALV IASAILVSFR HLHCTRNYIH
LNLFASFILR ALSVFIKDAA LKWMYSTAAQ QHQWDGLLSY QDSLGCRLVF LLMQYCVAAN
YYWLLVEGVY LYTLLAFSVF SEQRIFKLYL SIGWGVPLLF VIPWGIVKYL YEDEGCWTRN
SNMNYWLIIR LPILFAIGVN FLVFIRVICI VIAKLKANLM CKTDIKCRLA KSTLTLIPLL
GTHEVIFAFV MDEHARGTLR FVKLFTELSF TSFQGFMVAV LYCFVNNEVQ MEFRKSWERW
RLERLNIQRD SSMKPLKCPT SSVSSGATVG SSVYAATCQN SCS
