GLP2R_RAT
ID GLP2R_RAT Reviewed; 550 AA.
AC Q9Z0W0;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Glucagon-like peptide 2 receptor;
DE Short=GLP-2 receptor;
DE Short=GLP-2-R;
DE Short=GLP-2R;
GN Name=Glp2r;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Hypothalamus;
RX PubMed=9990065; DOI=10.1073/pnas.96.4.1569;
RA Munroe D.G., Gupta A.K., Kooshesh F., Vyas T.B., Rizkalla G., Wang H.,
RA Demchyshyn L., Yang Z.-H., Kamboj R.K., Chen H., McCallum K.,
RA Sumner-Smith M., Drucker D.J., Crivici A.;
RT "Prototypic G protein-coupled receptor for the intestinotrophic factor
RT glucagon-like peptide 2.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1569-1573(1999).
CC -!- FUNCTION: This is a receptor for glucagon-like peptide 2. The activity
CC of this receptor is mediated by G proteins which activate adenylyl
CC cyclase.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family.
CC {ECO:0000305}.
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DR EMBL; AF105368; AAD16896.1; -; mRNA.
DR RefSeq; NP_068620.1; NM_021848.1.
DR AlphaFoldDB; Q9Z0W0; -.
DR SMR; Q9Z0W0; -.
DR BioGRID; 248832; 1.
DR STRING; 10116.ENSRNOP00000004946; -.
DR BindingDB; Q9Z0W0; -.
DR ChEMBL; CHEMBL3822349; -.
DR GuidetoPHARMACOLOGY; 250; -.
DR GlyGen; Q9Z0W0; 4 sites.
DR PhosphoSitePlus; Q9Z0W0; -.
DR PaxDb; Q9Z0W0; -.
DR PRIDE; Q9Z0W0; -.
DR Ensembl; ENSRNOT00000004946; ENSRNOP00000004946; ENSRNOG00000003683.
DR GeneID; 60432; -.
DR KEGG; rno:60432; -.
DR UCSC; RGD:620270; rat.
DR CTD; 9340; -.
DR RGD; 620270; Glp2r.
DR eggNOG; KOG4564; Eukaryota.
DR GeneTree; ENSGT00940000158127; -.
DR HOGENOM; CLU_002753_4_0_1; -.
DR InParanoid; Q9Z0W0; -.
DR OMA; STDIWRD; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; Q9Z0W0; -.
DR TreeFam; TF315710; -.
DR Reactome; R-RNO-420092; Glucagon-type ligand receptors.
DR PRO; PR:Q9Z0W0; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000003683; Expressed in jejunum and 4 other tissues.
DR Genevisible; Q9Z0W0; RN.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0042592; P:homeostatic process; TAS:RGD.
DR Gene3D; 4.10.1240.10; -; 1.
DR InterPro; IPR039125; GLP2R.
DR InterPro; IPR017981; GPCR_2-like.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR PANTHER; PTHR45620:SF23; PTHR45620:SF23; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF02793; HRM; 1.
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; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..550
FT /note="Glucagon-like peptide 2 receptor"
FT /id="PRO_0000012839"
FT TOPO_DOM 1..173
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 174..198
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 199..210
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 211..235
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 236..261
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 262..285
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 286..299
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 300..321
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 322..339
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 340..362
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 363..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 387..405
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 406..417
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 418..438
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 439..550
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 83..105
FT /evidence="ECO:0000250"
FT DISULFID 96..137
FT /evidence="ECO:0000250"
FT DISULFID 118..159
FT /evidence="ECO:0000250"
SQ SEQUENCE 550 AA; 63102 MW; 22E269F811E25226 CRC64;
MRPQPSPAVP SRCREAPVPR VRAQPVGIPE AQGPVPLHSQ QMRLLWGPGR PFLALLLLVS
IKQVTGSLLK ETTQKWANYK EKCLEDLHNR LSGIFCNGTF DRYVCWPHSY PGNVSVPCPS
YLPWWNAESP GRAYRHCLAQ GTWQTRENTT DIWQDESECS ENHSFRQNVD HYALLYTLQL
MYTVGYSVSL ISLFLALTLF LFLRKLHCTR NYIHMNLFAS FILKVLAVLV KDMVSHNSYS
KRPDDESGWM SYLSETSVSC RSVQVLLHYF VGTNHLWLLV EGLYLHTLLE PTVFPERRLW
PKYLVVGWAF PMLFVIPWGF ARAHLENTRC WATNGNLKIW WIIRGPMLLC VTVNFFIFLK
ILKLLISKLK AHQMCFRDYK YRLAKSTLLL IPLLGVHEVL FTFFPDDQVQ GFSKRIRLFI
QLTLSSVHGF LVALQYGFAN GEVKAELRKS WGRFLLARHW GCRTCVLGKN FRFLGKCSKK
LSEGDGSETL QKLRFSTCSS HLASETLGDV GVQPHRGRGA WPRGSSLSES SEGDFTLANT
MEEILEESEI
