GLP1R_MOUSE
ID GLP1R_MOUSE Reviewed; 463 AA.
AC O35659; Q1JQR8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 154.
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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=9568699; DOI=10.2337/diabetes.47.4.646;
RA Flamez D., van Breusegem A., Scrocchi L.A., Quartier E., Pipeleers D.,
RA Drucker D.J., Schuit F.;
RT "Mouse pancreatic beta-cells exhibit preserved glucose competence after
RT disruption of the glucagon-like peptide-1 receptor gene.";
RL Diabetes 47:646-652(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Intestine;
RX PubMed=16946080; DOI=10.1152/ajpregu.00491.2006;
RA Kumar K.G., Poole A.C., York B., Volaufova J., Zuberi A., Richards B.K.;
RT "Quantitative trait loci for carbohydrate and total energy intake on mouse
RT chromosome 17: congenic strain confirmation and candidate gene analyses
RT (Glo1, Glp1r).";
RL Am. J. Physiol. 292:R207-R216(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=LAF1; TISSUE=Pituitary;
RA Watanabe K., Doran A.C., Tibaduiza E.C., Chen C., Beinborn M.;
RT "Identification and characterization of glucagon-like peptide-1 receptors
RT in a pituitary ACTH-secreting cell line.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: G-protein coupled receptor for glucagon-like peptide 1 (GLP-
CC 1) (PubMed:9568699). Ligand binding triggers activation of a signaling
CC cascade that leads to the activation of adenylyl cyclase and increased
CC intracellular cAMP levels (By similarity). Plays a role in regulating
CC insulin secretion in response to GLP-1 (PubMed:9568699).
CC {ECO:0000250|UniProtKB:P43220, ECO:0000269|PubMed:9568699}.
CC -!- SUBUNIT: May form homodimers and heterodimers with GIPR.
CC {ECO:0000250|UniProtKB:P43220}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:9568699};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P43220}.
CC -!- TISSUE SPECIFICITY: Detected in pancreatic islets (at protein level).
CC Detected in pancreatic islets and lungs. {ECO:0000269|PubMed:9568699}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA04930.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ001692; CAA04930.1; ALT_FRAME; mRNA.
DR EMBL; DQ093397; AAZ83365.1; -; mRNA.
DR EMBL; AY293742; AAQ54583.1; -; mRNA.
DR EMBL; AC165951; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC139464; AAI39465.1; -; mRNA.
DR EMBL; BC139466; AAI39467.1; -; mRNA.
DR CCDS; CCDS37542.1; -.
DR RefSeq; NP_067307.2; NM_021332.2.
DR AlphaFoldDB; O35659; -.
DR SMR; O35659; -.
DR BioGRID; 199950; 1.
DR STRING; 10090.ENSMUSP00000110221; -.
DR BindingDB; O35659; -.
DR ChEMBL; CHEMBL1075290; -.
DR GlyGen; O35659; 3 sites.
DR iPTMnet; O35659; -.
DR PhosphoSitePlus; O35659; -.
DR PaxDb; O35659; -.
DR PRIDE; O35659; -.
DR ProteomicsDB; 270995; -.
DR Antibodypedia; 15682; 543 antibodies from 35 providers.
DR DNASU; 14652; -.
DR Ensembl; ENSMUST00000114574; ENSMUSP00000110221; ENSMUSG00000024027.
DR Ensembl; ENSMUST00000236038; ENSMUSP00000157572; ENSMUSG00000024027.
DR GeneID; 14652; -.
DR KEGG; mmu:14652; -.
DR UCSC; uc008bud.1; mouse.
DR CTD; 2740; -.
DR MGI; MGI:99571; Glp1r.
DR VEuPathDB; HostDB:ENSMUSG00000024027; -.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000161009; -.
DR HOGENOM; CLU_002753_4_0_1; -.
DR InParanoid; O35659; -.
DR OMA; CFVNNEK; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; O35659; -.
DR TreeFam; TF315710; -.
DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-MMU-418555; G alpha (s) signalling events.
DR Reactome; R-MMU-420092; Glucagon-type ligand receptors.
DR BioGRID-ORCS; 14652; 7 hits in 76 CRISPR screens.
DR PRO; PR:O35659; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; O35659; protein.
DR Bgee; ENSMUSG00000024027; Expressed in islet of Langerhans and 56 other tissues.
DR Genevisible; O35659; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0001653; F:peptide receptor activity; ISO:MGI.
DR GO; GO:0038023; F:signaling receptor activity; TAS:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0008306; P:associative learning; ISO:MGI.
DR GO; GO:0019933; P:cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0007631; P:feeding behavior; ISO:MGI.
DR GO; GO:0046879; P:hormone secretion; IMP:MGI.
DR GO; GO:0030073; P:insulin secretion; ISO:MGI.
DR GO; GO:0007611; P:learning or memory; IMP:UniProtKB.
DR GO; GO:0007613; P:memory; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; TAS:MGI.
DR GO; GO:0045777; P:positive regulation of blood pressure; IDA:CACAO.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0045823; P:positive regulation of heart contraction; ISO:MGI.
DR GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0031204; P:post-translational protein targeting to membrane, translocation; IMP:MGI.
DR GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:UniProtKB.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0009749; P:response to glucose; ISO:MGI.
DR GO; GO:1990911; P:response to psychosocial stress; IMP:UniProtKB.
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 1: Evidence at protein 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_0000012836"
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"
SQ SEQUENCE 463 AA; 53028 MW; FBA3D9D79A30E9C3 CRC64;
MASTPSLLRL ALLLLGAVGR AGPRPQGTTV SLSETVQKWR EYRRQCQRFL TEAPLLATGL
FCNRTFDDYA CWPDGPPGSF VNVSCPWYLP WASSVLQGHV YRFCTAEGLW LHKDNSSLPW
RDLSECEESK RGERNFPEEQ LLSLYIIYTV GYALSFSALV IASAILVGFR HLHCTRNYIH
LNLFASFILR ALSVFIKDAA LKWMYSTAAQ QHQWDGLLSY QDSLGCRLVF LLMQYCVAAN
YYWLLVEGVY LYTLLAFSVF SEQRIFKLYL SIGWGVPLLF VIPWGIVKYL YEDEGCWTRN
SNMNYWLIIR LPILFAIGVN FLIFIRVICI VVSKLKANLM CKTDIKCRLA KSTLTLIPLL
GTHEVIFAFV MDEHARGTLR FIKLFTELSF TSFQGLMVAI LYCFVNNEVQ MEFRKCWERW
RLEHLNIQRD CSMKPLKCPT SSVSSGATVG SSVYAATCQS SYS
