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   24-JAN-2024, entry version 162.
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   GlyCosmos; O35659; 3 sites, No reported glycans.
DR   GlyGen; O35659; 3 sites.
DR   iPTMnet; O35659; -.
DR   PhosphoSitePlus; O35659; -.
DR   PaxDb; 10090-ENSMUSP00000110221; -.
DR   ProteomicsDB; 270995; -.
DR   Antibodypedia; 15682; 609 antibodies from 35 providers.
DR   DNASU; 14652; -.
DR   Ensembl; ENSMUST00000114574.3; ENSMUSP00000110221.2; ENSMUSG00000024027.9.
DR   Ensembl; ENSMUST00000236038.2; ENSMUSP00000157572.2; ENSMUSG00000024027.9.
DR   GeneID; 14652; -.
DR   KEGG; mmu:14652; -.
DR   UCSC; uc008bud.1; mouse.
DR   AGR; MGI:99571; -.
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; 4209404at2759; -.
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; 8 hits in 81 CRISPR screens.
DR   PRO; PR:O35659; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; O35659; Protein.
DR   Bgee; ENSMUSG00000024027; Expressed in islet of Langerhans and 58 other cell types or tissues.
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; IBA:GO_Central.
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: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: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   CDD; cd15268; 7tmB1_GLP1R; 1.
DR   Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR047033; GLP1R_7TM.
DR   InterPro; IPR017981; GPCR_2-like_7TM.
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; GLUCAGON-LIKE PEPTIDE 1 RECEPTOR; 1.
DR   PANTHER; PTHR45620; PDF RECEPTOR-LIKE PROTEIN-RELATED; 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; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   SUPFAM; SSF111418; Hormone receptor domain; 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.
DR   Genevisible; O35659; MM.
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
//