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Glucagon receptor (GL-R)

 GLR_RAT                 Reviewed;         485 AA.
P30082;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
22-NOV-2017, entry version 133.
RecName: Full=Glucagon receptor;
Short=GL-R;
Flags: Precursor;
Name=Gcgr;
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, AND SUBCELLULAR LOCATION.
PubMed=8384375; DOI=10.1126/science.8384375;
Jelinek L.J., Lok S., Grant F.J., Rosenberg G.B., Smith R.A.,
Bensch P.A., Sheppard P.O., O'Hara P.J., Foster D.C., Kuijper J.L.,
Biggs S.H., Walker K.M., Chen L.H., McKernan P.A., Kindsvogel W.;
"Expression cloning and signaling properties of the rat glucagon
receptor.";
Science 259:1614-1616(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8384842; DOI=10.1006/bbrc.1993.1243;
Svoboda M., Ciccarelli E., Tastenoy M., Cauvin A., Stievenart M.,
Christophe J.;
"Small introns in a hepatic cDNA encoding a new glucagon-like peptide
1-type receptor.";
Biochem. Biophys. Res. Commun. 191:479-486(1993).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Wistar; TISSUE=Liver;
PubMed=8082779; DOI=10.1016/0014-5793(94)00875-2;
Maget B., Tastenoy M., Svoboda M.;
"Sequencing of eleven introns in genomic DNA encoding rat glucagon
receptor and multiple alternative splicing of its mRNA.";
FEBS Lett. 351:271-275(1994).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: G-protein coupled receptor for glucagon that plays a
central role in the regulation of blood glucose levels and glucose
homeostasis. Regulates the rate of hepatic glucose production by
promoting glycogen hydrolysis and gluconeogenesis. Plays an
important role in mediating the responses to fasting. Ligand
binding causes a conformation change that triggers signaling via
guanine nucleotide-binding proteins (G proteins) and modulates the
activity of down-stream effectors, such as adenylate cyclase.
Promotes activation of adenylate cyclase. Besides, plays a role in
signaling via a phosphatidylinositol-calcium second messenger
system. {ECO:0000269|PubMed:8384375}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8384375};
Multi-pass membrane protein {ECO:0000269|PubMed:8384375}. Note=Is
rapidly internalized after ligand-binding.
{ECO:0000250|UniProtKB:P47871}.
-!- PTM: Ligand-binding promotes phosphorylation of serine residues in
the C-terminal cytoplasmic domain. Phosphorylation is important
for receptor endocytosis after ligand-binding (By similarity).
{ECO:0000250|UniProtKB:P47871}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
{ECO:0000305}.
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EMBL; L04796; AAA16439.1; -; mRNA.
EMBL; X68692; CAA48651.1; -; mRNA.
EMBL; M96674; AAA02992.1; -; mRNA.
EMBL; U63021; AAB16800.1; -; Genomic_DNA.
PIR; JQ1957; JQ1957.
RefSeq; NP_742088.1; NM_172091.2.
RefSeq; NP_742089.1; NM_172092.2.
RefSeq; XP_006247938.1; XM_006247876.3.
UniGene; Rn.11225; -.
ProteinModelPortal; P30082; -.
SMR; P30082; -.
MINT; MINT-4996622; -.
STRING; 10116.ENSRNOP00000051845; -.
BindingDB; P30082; -.
ChEMBL; CHEMBL4720; -.
GuidetoPHARMACOLOGY; 251; -.
iPTMnet; P30082; -.
PhosphoSitePlus; P30082; -.
PaxDb; P30082; -.
PRIDE; P30082; -.
Ensembl; ENSRNOT00000054962; ENSRNOP00000051845; ENSRNOG00000036692.
Ensembl; ENSRNOT00000083601; ENSRNOP00000074929; ENSRNOG00000036692.
GeneID; 24953; -.
KEGG; rno:24953; -.
CTD; 2642; -.
RGD; 2669; Gcgr.
eggNOG; KOG4564; Eukaryota.
eggNOG; ENOG410XRS2; LUCA.
GeneTree; ENSGT00760000118800; -.
HOGENOM; HOG000008250; -.
HOVERGEN; HBG008318; -.
InParanoid; P30082; -.
KO; K04583; -.
OMA; TELVCNR; -.
PhylomeDB; P30082; -.
TreeFam; TF315710; -.
Reactome; R-RNO-163359; Glucagon signaling in metabolic regulation.
Reactome; R-RNO-416476; G alpha (q) signalling events.
Reactome; R-RNO-418555; G alpha (s) signalling events.
Reactome; R-RNO-420092; Glucagon-type ligand receptors.
PRO; PR:P30082; -.
Proteomes; UP000002494; Chromosome 10.
Bgee; ENSRNOG00000036692; -.
ExpressionAtlas; P30082; baseline and differential.
Genevisible; P30082; RN.
GO; GO:0005768; C:endosome; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; TAS:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0004967; F:glucagon receptor activity; IDA:RGD.
GO; GO:0017046; F:peptide hormone binding; IDA:RGD.
GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:RGD.
GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; IMP:RGD.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0071377; P:cellular response to glucagon stimulus; ISO:RGD.
GO; GO:0006887; P:exocytosis; IDA:RGD.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IDA:RGD.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0009755; P:hormone-mediated signaling pathway; IDA:RGD.
GO; GO:0070873; P:regulation of glycogen metabolic process; ISS:UniProtKB.
GO; GO:0042594; P:response to starvation; ISS:UniProtKB.
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; IPR003291; GPCR_2_glucagon_rcpt.
InterPro; IPR000832; GPCR_2_secretin-like.
InterPro; IPR017983; GPCR_2_secretin-like_CS.
Pfam; PF00002; 7tm_2; 1.
Pfam; PF02793; HRM; 1.
PRINTS; PR01353; GLUCAGNFAMLY.
PRINTS; PR01354; GLUCAGONR.
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.
1: Evidence at protein level;
Cell membrane; Complete proteome; Disulfide bond;
G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
Receptor; Reference proteome; Signal; Transducer; Transmembrane;
Transmembrane helix.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 485 Glucagon receptor.
/FTId=PRO_0000012834.
TOPO_DOM 27 137 Extracellular.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 138 162 Helical; Name=1.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 163 174 Cytoplasmic.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 175 199 Helical; Name=2.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 200 226 Extracellular.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 227 250 Helical; Name=3.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 251 264 Cytoplasmic.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 265 286 Helical; Name=4.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 287 304 Extracellular.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 305 327 Helical; Name=5.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 328 351 Cytoplasmic.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 352 370 Helical; Name=6.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 371 382 Extracellular.
{ECO:0000250|UniProtKB:P47871}.
TRANSMEM 383 403 Helical; Name=7.
{ECO:0000250|UniProtKB:P47871}.
TOPO_DOM 404 485 Cytoplasmic.
{ECO:0000250|UniProtKB:P47871}.
REGION 351 354 Allosteric inhibitor binding.
{ECO:0000250|UniProtKB:P47871}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000250|UniProtKB:P47871}.
MOD_RES 476 476 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 60 60 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 79 79 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 68 {ECO:0000250|UniProtKB:P47871}.
DISULFID 59 101 {ECO:0000250|UniProtKB:P47871}.
DISULFID 82 122 {ECO:0000250|UniProtKB:P47871}.
DISULFID 225 295 {ECO:0000250|UniProtKB:P47871}.
CONFLICT 216 216 W -> C (in Ref. 2). {ECO:0000305}.
CONFLICT 324 324 V -> A (in Ref. 2). {ECO:0000305}.
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


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