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

 GLP1R_RAT               Reviewed;         463 AA.
P32301; Q64073; Q6LD83;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
20-DEC-2017, entry version 136.
RecName: Full=Glucagon-like peptide 1 receptor;
Short=GLP-1 receptor;
Short=GLP-1-R;
Short=GLP-1R;
Flags: Precursor;
Name=Glp1r; Synonyms=Glpr;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Pancreatic islet;
PubMed=1326760; DOI=10.1073/pnas.89.18.8641;
Thorens B.;
"Expression cloning of the pancreatic beta cell receptor for the
gluco-incretin hormone glucagon-like peptide 1.";
Proc. Natl. Acad. Sci. U.S.A. 89:8641-8645(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
TISSUE=Lung;
PubMed=7813606;
Lankat-Buttgereit B., Goke R., Fehmann H.C., Richter G., Goke B.;
"Molecular cloning of a cDNA encoding for the GLP-1 receptor expressed
in rat lung.";
Exp. Clin. Endocrinol. 102:341-347(1994).
-!- FUNCTION: G-protein coupled receptor for glucagon-like peptide 1
(GLP-1) (PubMed:1326760, PubMed:7813606). Ligand binding triggers
activation of a signaling cascade that leads to the activation of
adenylyl cyclase and increased intracellular cAMP levels
(PubMed:1326760, PubMed:7813606). Plays a role in regulating
insulin secretion in response to GLP-1 (By similarity).
{ECO:0000250|UniProtKB:O35659, ECO:0000269|PubMed:1326760,
ECO:0000269|PubMed:7813606}.
-!- SUBUNIT: May form homodimers and heterodimers with GIPR.
{ECO:0000250|UniProtKB:P43220}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1326760,
ECO:0000269|PubMed:7813606}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:P43220}.
-!- TISSUE SPECIFICITY: Pancreatic islets, stomach, lung, rat
insulinoma cell line. {ECO:0000269|PubMed:1326760}.
-!- PTM: N-glycosylation enhances cell surface expression and
lengthens receptor half-life by preventing degradation in the ER.
{ECO:0000250|UniProtKB:P43220}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
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EMBL; M97797; AAA73377.1; -; mRNA.
EMBL; S75952; AAP31860.1; -; mRNA.
PIR; A46172; A46172.
RefSeq; NP_036860.1; NM_012728.1.
UniGene; Rn.11408; -.
ProteinModelPortal; P32301; -.
SMR; P32301; -.
BioGrid; 247128; 1.
STRING; 10116.ENSRNOP00000001527; -.
BindingDB; P32301; -.
ChEMBL; CHEMBL5862; -.
GuidetoPHARMACOLOGY; 249; -.
iPTMnet; P32301; -.
PhosphoSitePlus; P32301; -.
SwissPalm; P32301; -.
PaxDb; P32301; -.
PRIDE; P32301; -.
GeneID; 25051; -.
KEGG; rno:25051; -.
CTD; 2740; -.
RGD; 2703; Glp1r.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
HOGENOM; HOG000008250; -.
HOVERGEN; HBG008318; -.
InParanoid; P32301; -.
KO; K04581; -.
PRO; PR:P32301; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008528; F:G-protein coupled peptide receptor activity; IPI:RGD.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:RGD.
GO; GO:0004967; F:glucagon receptor activity; IEA:InterPro.
GO; GO:0044508; F:glucagon-like peptide 1 receptor activity; ISS:UniProtKB.
GO; GO:0017046; F:peptide hormone binding; IDA:RGD.
GO; GO:0001653; F:peptide receptor activity; IDA:RGD.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IMP:RGD.
GO; GO:0008306; P:associative learning; IDA:RGD.
GO; GO:0019933; P:cAMP-mediated signaling; IMP:RGD.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0007631; P:feeding behavior; IMP:RGD.
GO; GO:0046879; P:hormone secretion; IDA:UniProtKB.
GO; GO:0030073; P:insulin secretion; IMP:UniProtKB.
GO; GO:0007611; P:learning or memory; IMP:UniProtKB.
GO; GO:0007613; P:memory; IDA:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD.
GO; GO:0007218; P:neuropeptide signaling pathway; TAS:RGD.
GO; GO:0045777; P:positive regulation of blood pressure; IDA:RGD.
GO; GO:0045597; P:positive regulation of cell differentiation; IMP:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:RGD.
GO; GO:0045823; P:positive regulation of heart contraction; IDA:RGD.
GO; GO:0032024; P:positive regulation of insulin secretion; IDA:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:RGD.
GO; GO:0051924; P:regulation of calcium ion transport; IMP:RGD.
GO; GO:0008016; P:regulation of heart contraction; ISO:RGD.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:RGD.
GO; GO:0009749; P:response to glucose; IMP:RGD.
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.
2: Evidence at transcript level;
ADP-ribosylation; Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 463 Glucagon-like peptide 1 receptor.
/FTId=PRO_0000012837.
TOPO_DOM 22 139 Extracellular. {ECO:0000305}.
TRANSMEM 140 164 Helical; Name=1.
{ECO:0000250|UniProtKB:P43220}.
TOPO_DOM 165 175 Cytoplasmic. {ECO:0000305}.
TRANSMEM 176 201 Helical; Name=2.
{ECO:0000250|UniProtKB:P43220}.
TOPO_DOM 202 227 Extracellular. {ECO:0000305}.
TRANSMEM 228 251 Helical; Name=3.
{ECO:0000250|UniProtKB:P43220}.
TOPO_DOM 252 265 Cytoplasmic. {ECO:0000305}.
TRANSMEM 266 290 Helical; Name=4.
{ECO:0000250|UniProtKB:P43220}.
TOPO_DOM 291 305 Extracellular. {ECO:0000305}.
TRANSMEM 306 328 Helical; Name=5.
{ECO:0000250|UniProtKB:P43220}.
TOPO_DOM 329 348 Cytoplasmic. {ECO:0000305}.
TRANSMEM 349 370 Helical; Name=6.
{ECO:0000250|UniProtKB:P43220}.
TOPO_DOM 371 383 Extracellular. {ECO:0000305}.
TRANSMEM 384 404 Helical; Name=7.
{ECO:0000250|UniProtKB:P43220}.
TOPO_DOM 405 463 Cytoplasmic. {ECO:0000305}.
REGION 352 355 Important for allosteric inhibitor
binding. {ECO:0000250|UniProtKB:P43220}.
SITE 121 121 Interaction with the endogenous ligand
GLP-1. {ECO:0000250|UniProtKB:P43220}.
SITE 128 128 Interaction with the endogenous ligand
GLP-1. {ECO:0000250|UniProtKB:P43220}.
MOD_RES 341 341 ADP-ribosylcysteine.
{ECO:0000250|UniProtKB:P43220}.
MOD_RES 348 348 ADP-ribosylarginine.
{ECO:0000250|UniProtKB:P43220}.
CARBOHYD 63 63 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 115 115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 46 71 {ECO:0000250|UniProtKB:P43220}.
DISULFID 62 104 {ECO:0000250|UniProtKB:P43220}.
DISULFID 85 126 {ECO:0000250|UniProtKB:P43220}.
DISULFID 226 296 {ECO:0000250|UniProtKB:P43220}.
CONFLICT 323 323 V -> I (in Ref. 2; AAP31860).
{ECO:0000305}.
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


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