GLR_RAT
ID GLR_RAT Reviewed; 485 AA.
AC P30082;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Glucagon receptor;
DE Short=GL-R;
DE Flags: Precursor;
GN Name=Gcgr;
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, AND SUBCELLULAR LOCATION.
RX PubMed=8384375; DOI=10.1126/science.8384375;
RA Jelinek L.J., Lok S., Grant F.J., Rosenberg G.B., Smith R.A., Bensch P.A.,
RA Sheppard P.O., O'Hara P.J., Foster D.C., Kuijper J.L., Biggs S.H.,
RA Walker K.M., Chen L.H., McKernan P.A., Kindsvogel W.;
RT "Expression cloning and signaling properties of the rat glucagon
RT receptor.";
RL Science 259:1614-1616(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8384842; DOI=10.1006/bbrc.1993.1243;
RA Svoboda M., Ciccarelli E., Tastenoy M., Cauvin A., Stievenart M.,
RA Christophe J.;
RT "Small introns in a hepatic cDNA encoding a new glucagon-like peptide 1-
RT type receptor.";
RL Biochem. Biophys. Res. Commun. 191:479-486(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=8082779; DOI=10.1016/0014-5793(94)00875-2;
RA Maget B., Tastenoy M., Svoboda M.;
RT "Sequencing of eleven introns in genomic DNA encoding rat glucagon receptor
RT and multiple alternative splicing of its mRNA.";
RL FEBS Lett. 351:271-275(1994).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: G-protein coupled receptor for glucagon that plays a central
CC role in the regulation of blood glucose levels and glucose homeostasis.
CC Regulates the rate of hepatic glucose production by promoting glycogen
CC hydrolysis and gluconeogenesis. Plays an important role in mediating
CC the responses to fasting. Ligand binding causes a conformation change
CC that triggers signaling via guanine nucleotide-binding proteins (G
CC proteins) and modulates the activity of down-stream effectors, such as
CC adenylate cyclase. Promotes activation of adenylate cyclase. Besides,
CC plays a role in signaling via a phosphatidylinositol-calcium second
CC messenger system. {ECO:0000269|PubMed:8384375}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8384375};
CC Multi-pass membrane protein {ECO:0000269|PubMed:8384375}. Note=Is
CC rapidly internalized after ligand-binding.
CC {ECO:0000250|UniProtKB:P47871}.
CC -!- PTM: Ligand-binding promotes phosphorylation of serine residues in the
CC C-terminal cytoplasmic domain. Phosphorylation is important for
CC receptor endocytosis after ligand-binding (By similarity).
CC {ECO:0000250|UniProtKB:P47871}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; L04796; AAA16439.1; -; mRNA.
DR EMBL; X68692; CAA48651.1; -; mRNA.
DR EMBL; M96674; AAA02992.1; -; mRNA.
DR EMBL; U63021; AAB16800.1; -; Genomic_DNA.
DR PIR; JQ1957; JQ1957.
DR RefSeq; NP_742088.1; NM_172091.2.
DR RefSeq; NP_742089.1; NM_172092.2.
DR RefSeq; XP_006247938.1; XM_006247876.3.
DR AlphaFoldDB; P30082; -.
DR SMR; P30082; -.
DR STRING; 10116.ENSRNOP00000051845; -.
DR BindingDB; P30082; -.
DR ChEMBL; CHEMBL4720; -.
DR DrugCentral; P30082; -.
DR GuidetoPHARMACOLOGY; 251; -.
DR GlyGen; P30082; 4 sites.
DR iPTMnet; P30082; -.
DR PhosphoSitePlus; P30082; -.
DR PaxDb; P30082; -.
DR Ensembl; ENSRNOT00000054962; ENSRNOP00000051845; ENSRNOG00000036692.
DR GeneID; 24953; -.
DR KEGG; rno:24953; -.
DR CTD; 2642; -.
DR RGD; 2669; Gcgr.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000157969; -.
DR HOGENOM; CLU_002753_4_0_1; -.
DR InParanoid; P30082; -.
DR OMA; ARQMHYA; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P30082; -.
DR TreeFam; TF315710; -.
DR PRO; PR:P30082; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000036692; Expressed in liver and 18 other tissues.
DR ExpressionAtlas; P30082; baseline and differential.
DR Genevisible; P30082; RN.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004967; F:glucagon receptor activity; IDA:RGD.
DR GO; GO:0017046; F:peptide hormone binding; IDA:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; ISO:RGD.
DR GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
DR GO; GO:0006887; P:exocytosis; IDA:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0070873; P:regulation of glycogen metabolic process; ISS:UniProtKB.
DR GO; GO:0042594; P:response to starvation; ISS: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; IPR003291; GPCR_2_glucagon_rcpt.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
DR PRINTS; PR01353; GLUCAGNFAMLY.
DR PRINTS; PR01354; GLUCAGONR.
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 Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Signal; Transducer;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..485
FT /note="Glucagon receptor"
FT /id="PRO_0000012834"
FT TOPO_DOM 27..137
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TRANSMEM 138..162
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TOPO_DOM 163..174
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TRANSMEM 175..199
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TOPO_DOM 200..226
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TRANSMEM 227..250
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TOPO_DOM 251..264
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TRANSMEM 265..286
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TOPO_DOM 287..304
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TRANSMEM 305..327
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TOPO_DOM 328..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TRANSMEM 352..370
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TOPO_DOM 371..382
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TRANSMEM 383..403
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT TOPO_DOM 404..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT REGION 351..354
FT /note="Important for allosteric inhibitor binding"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT REGION 455..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 44..68
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT DISULFID 59..101
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT DISULFID 82..122
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT DISULFID 225..295
FT /evidence="ECO:0000250|UniProtKB:P47871"
FT CONFLICT 216
FT /note="W -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="V -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 55038 MW; 91AC67D7A4F5090E CRC64;
MLLTQLHCPY LLLLLVVLSC LPKAPSAQVM DFLFEKWKLY SDQCHHNLSL LPPPTELVCN
RTFDKYSCWP DTPPNTTANI SCPWYLPWYH KVQHRLVFKR CGPDGQWVRG PRGQSWRDAS
QCQMDDDEIE VQKGVAKMYS SYQVMYTVGY SLSLGALLLA LVILLGLRKL HCTRNYIHGN
LFASFVLKAG SVLVIDWLLK TRYSQKIGDD LSVSVWLSDG AVAGCRVATV IMQYGIIANY
CWLLVEGVYL YSLLSITTFS EKSFFSLYLC IGWGSPLLFV IPWVVVKCLF ENVQCWTSND
NMGFWWILRI PVLLAILINF FIFVRIIHLL VAKLRAHQMH YADYKFRLAR STLTLIPLLG
VHEVVFAFVT DEHAQGTLRS TKLFFDLFFS SFQGLLVAVL YCFLNKEVQA ELLRRWRRWQ
EGKALQEERM ASSHGSHMAP AGTCHGDPCE KLQLMSAGSS SGTGCEPSAK TSLASSLPRL
ADSPT
