ID GLP1R_HUMAN Reviewed; 463 AA. AC P43220; Q2M229; Q99669; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 2. DT 10-JUN-2026, entry version 220. 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 Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND VARIANT RP PHE-260. RC TISSUE=Pancreatic islet; RX PubMed=8405712; DOI=10.2337/diab.42.11.1678; RA Thorens B., Porret A., Buehler L., Deng S., Morel P., Widmann C.; RT "Cloning and functional expression of the human islet GLP-1 receptor. RT Demonstration that exendin-4 is an agonist and exendin-(9-39) an antagonist RT of the receptor."; RL Diabetes 42:1678-1682(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-260. RC TISSUE=Pancreas; RX PubMed=8404634; DOI=10.1210/endo.133.4.8404634; RA Dillon J.S., Tanizawa Y., Wheeler M.B., Leng X., Ligon B.B., Rabin D.U., RA Yoo-Warren H., Permutt M., Boyd A.E.; RT "Cloning and functional expression of the human glucagon-like peptide-1 RT (GLP-1) receptor."; RL Endocrinology 133:1907-1910(1993). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND VARIANT RP PHE-260. RC TISSUE=Gastric carcinoma; RX PubMed=8216285; DOI=10.1006/bbrc.1993.2226; RA Graziano M.P., Hey P.J., Borkowski D., Chicchi G.C., Strader C.D.; RT "Cloning and functional expression of a human glucagon-like peptide-1 RT receptor."; RL Biochem. Biophys. Res. Commun. 196:141-146(1993). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION. RC TISSUE=Insulinoma; RX PubMed=7517895; DOI=10.1016/0014-5793(94)00553-2; RA van Eyll B., Lankat-Buttgereit B., Bode H.P., Goeke R., Goeke B.; RT "Signal transduction of the GLP-1-receptor cloned from a human RT insulinoma."; RL FEBS Lett. 348:7-13(1994). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-260. RC TISSUE=Pancreas; RX PubMed=7843404; DOI=10.1016/0014-5793(94)01430-9; RA Wei Y., Mojsov S.; RT "Tissue-specific expression of the human receptor for glucagon-like RT peptide-I: brain, heart and pancreatic forms have the same deduced amino RT acid sequences."; RL FEBS Lett. 358:219-224(1995). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., RA Tsutsumi S., Aburatani H., Asai K., Akiyama Y.; RT "Genome-wide discovery and analysis of human seven transmembrane helix RT receptor genes."; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LEU-7; LYS-20; HIS-44; RP GLN-131; SER-168; PHE-260; THR-316; CYS-333 AND GLN-421. RG NIEHS SNPs program; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-260. 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). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26. RC TISSUE=Placenta; RX PubMed=9213353; DOI=10.1016/s0196-9781(97)00001-6; RA Lankat-Buttgereit B., Goeke B.; RT "Cloning and characterization of the 5' flanking sequences (promoter RT region) of the human GLP-1 receptor gene."; RL Peptides 18:617-624(1997). RN [11] RP DISULFIDE BOND. RX PubMed=20869417; DOI=10.1016/j.peptides.2010.09.015; RA Mann R.J., Al-Sabah S., de Maturana R.L., Sinfield J.K., Donnelly D.; RT "Functional coupling of Cys-226 and Cys-296 in the glucagon-like peptide-1 RT (GLP-1) receptor indicates a disulfide bond that is close to the activation RT pocket."; RL Peptides 31:2289-2293(2010). RN [12] RP ADP-RIBOSYLATION AT CYS-341 AND ARG-348. RX PubMed=21901419; DOI=10.1007/s11033-011-1225-0; RA Dezelak M., Bavec A.; RT "Glucagon like-peptide-1 receptor is covalently modified by endogenous RT mono-ADP-ribosyltransferase."; RL Mol. Biol. Rep. 39:4375-4381(2012). RN [13] RP GLYCOSYLATION AT ASN-63; ASN-82 AND ASN-115, AND SUBUNIT. RX PubMed=22412906; DOI=10.1371/journal.pone.0032675; RA Whitaker G.M., Lynn F.C., McIntosh C.H., Accili E.A.; RT "Regulation of GIP and GLP1 receptor cell surface expression by N- RT glycosylation and receptor heteromerization."; RL PLoS ONE 7:E32675-E32675(2012). RN [14] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 24-145 IN COMPLEX WITH ANTAGONIST RP EXENDIN-4, AND DISULFIDE BONDS. RX PubMed=18287102; DOI=10.1074/jbc.m708740200; RA Runge S., Thogersen H., Madsen K., Lau J., Rudolph R.; RT "Crystal structure of the ligand-bound glucagon-like peptide-1 receptor RT extracellular domain."; RL J. Biol. Chem. 283:11340-11347(2008). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 24-145 IN COMPLEX WITH RP GLUCAGON-LIKE PEPTIDE-1, FUNCTION, SUBCELLULAR LOCATION, DISULFIDE BONDS, RP AND MUTAGENESIS OF LEU-32; TYR-69; TYR-88; LEU-89; PRO-90; ARG-121; GLU-127 RP AND GLU-128. RX PubMed=19861722; DOI=10.1074/jbc.m109.033829; RA Underwood C.R., Garibay P., Knudsen L.B., Hastrup S., Peters G.H., RA Rudolph R., Reedtz-Runge S.; RT "Crystal structure of glucagon-like peptide-1 in complex with the RT extracellular domain of the glucagon-like peptide-1 receptor."; RL J. Biol. Chem. 285:723-730(2010). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 24-145, FUNCTION, SUBCELLULAR RP LOCATION, AND DISULFIDE BONDS. RX PubMed=26308095; DOI=10.1021/acs.jmedchem.5b00726; RA Lau J., Bloch P., Schaeffer L., Pettersson I., Spetzler J., Kofoed J., RA Madsen K., Knudsen L.B., McGuire J., Steensgaard D.B., Strauss H.M., RA Gram D.X., Knudsen S.M., Nielsen F.S., Thygesen P., Reedtz-Runge S., RA Kruse T.; RT "Discovery of the Once-Weekly Glucagon-Like Peptide-1 (GLP-1) Analogue RT Semaglutide."; RL J. Med. Chem. 58:7370-7380(2015). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 24-145, FUNCTION, SUBCELLULAR RP LOCATION, AND DISULFIDE BONDS. RX PubMed=27196125; DOI=10.1038/srep26236; RA Hennen S., Kodra J.T., Soroka V., Krogh B.O., Wu X., Kaastrup P., RA Oerskov C., Roenn S.G., Schluckebier G., Barbateskovic S., Gandhi P.S., RA Reedtz-Runge S.; RT "Structural insight into antibody-mediated antagonism of the Glucagon-like RT peptide-1 Receptor."; RL Sci. Rep. 6:26236-26236(2016). RN [18] RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 128-431 IN COMPLEXES WITH RP ALLOSTERIC MODULATORS, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RP TOPOLOGY, DISULFIDE BOND, AND MUTAGENESIS OF ARG-176; ILE-317; SER-352; RP THR-355 AND GLY-361. RX PubMed=28514449; DOI=10.1038/nature22378; RA Song G., Yang D., Wang Y., de Graaf C., Zhou Q., Jiang S., Liu K., Cai X., RA Dai A., Lin G., Liu D., Wu F., Wu Y., Zhao S., Ye L., Han G.W., Lau J., RA Wu B., Hanson M.A., Liu Z.J., Wang M.W., Stevens R.C.; RT "Human GLP-1 receptor transmembrane domain structure in complex with RT allosteric modulators."; RL Nature 546:312-315(2017). CC -!- FUNCTION: G protein-coupled receptor for glucagon-like peptide 1 (GLP- CC 1) (PubMed:19861722, PubMed:26308095, PubMed:27196125, PubMed:28514449, CC PubMed:7517895, PubMed:8216285, PubMed:8405712). Ligand binding CC triggers activation of a signaling cascade that leads to the activation CC of adenylyl cyclase and increased intracellular cAMP levels CC (PubMed:19861722, PubMed:26308095, PubMed:27196125, PubMed:28514449, CC PubMed:7517895, PubMed:8216285, PubMed:8405712). Plays a role in CC regulating insulin secretion in response to GLP-1 (By similarity). CC {ECO:0000250|UniProtKB:O35659, ECO:0000269|PubMed:19861722, CC ECO:0000269|PubMed:26308095, ECO:0000269|PubMed:27196125, CC ECO:0000269|PubMed:28514449, ECO:0000269|PubMed:7517895, CC ECO:0000269|PubMed:8216285, ECO:0000269|PubMed:8405712}. CC -!- ACTIVITY REGULATION: The allosteric modulators NNC0640, PF-06372222 and CC MK-0893 inhibit the increase of intracellular cAMP levels in response CC to GLP-1. {ECO:0000269|PubMed:28514449}. CC -!- SUBUNIT: May form homodimers and heterodimers with GIPR. CC {ECO:0000269|PubMed:18287102, ECO:0000269|PubMed:22412906}. CC -!- INTERACTION: CC P43220; Q4G176: ACSF3; NbExp=4; IntAct=EBI-7466542, EBI-10714818; CC P43220; Q96CW1: AP2M1; NbExp=4; IntAct=EBI-7466542, EBI-297683; CC P43220; Q96BI3: APH1A; NbExp=2; IntAct=EBI-7466542, EBI-2606935; CC P43220; P51693: APLP1; NbExp=4; IntAct=EBI-7466542, EBI-74648; CC P43220; Q9HD20: ATP13A1; NbExp=2; IntAct=EBI-7466542, EBI-3940599; CC P43220; Q99437: ATP6V0B; NbExp=2; IntAct=EBI-7466542, EBI-3904417; CC P43220; Q8TCD1: C18orf32; NbExp=2; IntAct=EBI-7466542, EBI-2954747; CC P43220; O75155: CAND2; NbExp=2; IntAct=EBI-7466542, EBI-5656182; CC P43220; P60033: CD81; NbExp=2; IntAct=EBI-7466542, EBI-712921; CC P43220; Q8N111: CEND1; NbExp=2; IntAct=EBI-7466542, EBI-946825; CC P43220; P05156: CFI; NbExp=2; IntAct=EBI-7466542, EBI-9352022; CC P43220; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-7466542, EBI-3867333; CC P43220; Q9H1C7: CYSTM1; NbExp=2; IntAct=EBI-7466542, EBI-12867082; CC P43220; Q9BW60: ELOVL1; NbExp=3; IntAct=EBI-7466542, EBI-1050331; CC P43220; P30040: ERP29; NbExp=2; IntAct=EBI-7466542, EBI-946830; CC P43220; P37268: FDFT1; NbExp=2; IntAct=EBI-7466542, EBI-714550; CC P43220; O75899: GABBR2; NbExp=2; IntAct=EBI-7466542, EBI-715469; CC P43220; O15354: GPR37; NbExp=4; IntAct=EBI-7466542, EBI-15639515; CC P43220; P05981: HPN; NbExp=4; IntAct=EBI-7466542, EBI-12816745; CC P43220; Q01628: IFITM3; NbExp=2; IntAct=EBI-7466542, EBI-7932862; CC P43220; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-7466542, EBI-11959885; CC P43220; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-7466542, EBI-11749135; CC P43220; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-7466542, EBI-10172290; CC P43220; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-7466542, EBI-10171774; CC P43220; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-7466542, EBI-10172052; CC P43220; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-7466542, EBI-11988175; CC P43220; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-7466542, EBI-3958099; CC P43220; Q6N075: MFSD5; NbExp=2; IntAct=EBI-7466542, EBI-3920969; CC P43220; Q9NWU5: MRPL22; NbExp=3; IntAct=EBI-7466542, EBI-5461867; CC P43220; P60660: MYL6; NbExp=2; IntAct=EBI-7466542, EBI-300817; CC P43220; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-7466542, EBI-945833; CC P43220; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-7466542, EBI-22310682; CC P43220; Q9H1E3: NUCKS1; NbExp=2; IntAct=EBI-7466542, EBI-1390111; CC P43220; Q9NXG6: P4HTM; NbExp=2; IntAct=EBI-7466542, EBI-2908337; CC P43220; Q6TCH4: PAQR6; NbExp=4; IntAct=EBI-7466542, EBI-17265310; CC P43220; Q5H8A4: PIGG; NbExp=2; IntAct=EBI-7466542, EBI-11724298; CC P43220; O60894: RAMP1; NbExp=2; IntAct=EBI-7466542, EBI-962893; CC P43220; O60895: RAMP2; NbExp=2; IntAct=EBI-7466542, EBI-9009040; CC P43220; O60896: RAMP3; NbExp=2; IntAct=EBI-7466542, EBI-720447; CC P43220; Q9Y224: RTRAF; NbExp=2; IntAct=EBI-7466542, EBI-1104547; CC P43220; Q8N697: SLC15A4; NbExp=4; IntAct=EBI-7466542, EBI-4319594; CC P43220; O15432: SLC31A2; NbExp=2; IntAct=EBI-7466542, EBI-17867220; CC P43220; Q9NZ72: STMN3; NbExp=2; IntAct=EBI-7466542, EBI-725557; CC P43220; Q9UJZ1: STOML2; NbExp=2; IntAct=EBI-7466542, EBI-1044428; CC P43220; Q8N4V2: SVOP; NbExp=4; IntAct=EBI-7466542, EBI-12883142; CC P43220; O43761: SYNGR3; NbExp=2; IntAct=EBI-7466542, EBI-11321949; CC P43220; Q9BVK8: TMEM147; NbExp=4; IntAct=EBI-7466542, EBI-348587; CC P43220; O95857: TSPAN13; NbExp=3; IntAct=EBI-7466542, EBI-61302419; CC PRO_0000012835; O60894: RAMP1; NbExp=2; IntAct=EBI-67110479, EBI-962893; CC PRO_0000012835; O60895: RAMP2; NbExp=4; IntAct=EBI-67110479, EBI-9009040; CC PRO_0000012835; O60896: RAMP3; NbExp=3; IntAct=EBI-67110479, EBI-720447; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19861722, CC ECO:0000269|PubMed:26308095, ECO:0000269|PubMed:27196125, CC ECO:0000269|PubMed:28514449, ECO:0000269|PubMed:7517895, CC ECO:0000269|PubMed:8216285, ECO:0000269|PubMed:8405712}; Multi-pass CC membrane protein {ECO:0000269|PubMed:28514449}. CC -!- PTM: N-glycosylation enhances cell surface expression and lengthens CC receptor half-life by preventing degradation in the ER. CC {ECO:0000269|PubMed:22412906}. CC -!- MISCELLANEOUS: Selective recognition of glucagon-like peptide over CC glucagon is determined by residues located at the C-terminal end of the CC glucagon-like peptide. {ECO:0000250|UniProtKB:P32301}. CC -!- SIMILARITY: Belongs to the G protein-coupled receptor 2 family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Glucagon-like peptide 1 entry; CC URL="https://en.wikipedia.org/wiki/Glucagon-like_peptide-1"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U01104; AAA03614.1; -; mRNA. DR EMBL; U01157; AAA62471.1; -; mRNA. DR EMBL; U01156; AAC50050.1; -; mRNA. DR EMBL; L23503; AAA17021.1; -; mRNA. DR EMBL; U10037; AAA63787.1; -; mRNA. DR EMBL; AB065685; BAC05908.1; -; Genomic_DNA. DR EMBL; AY439112; AAR05444.1; -; Genomic_DNA. DR EMBL; AL035690; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC112126; AAI12127.1; -; mRNA. DR EMBL; BC113493; AAI13494.1; -; mRNA. DR EMBL; U66062; AAB64013.1; -; Genomic_DNA. DR CCDS; CCDS4839.1; -. DR PIR; I84494; I84494. DR PIR; S71624; S71624. DR RefSeq; NP_002053.3; NM_002062.4. DR PDB; 3C59; X-ray; 2.30 A; A=24-145. DR PDB; 3C5T; X-ray; 2.10 A; A=24-145. DR PDB; 3IOL; X-ray; 2.10 A; A=24-145. DR PDB; 4ZGM; X-ray; 1.80 A; A=24-145. DR PDB; 5E94; X-ray; 2.00 A; G/H=24-145. DR PDB; 5NX2; X-ray; 3.70 A; A=24-432. DR PDB; 5OTT; X-ray; 1.92 A; A=24-139. DR PDB; 5OTU; X-ray; 1.80 A; A/C=24-139. DR PDB; 5OTV; X-ray; 2.00 A; A/C=24-139. DR PDB; 5OTW; X-ray; 2.10 A; A/C=24-139. DR PDB; 5OTX; X-ray; 2.00 A; A/C=24-139. DR PDB; 5VEW; X-ray; 2.70 A; A/B=128-257, A/B=261-431. DR PDB; 5VEX; X-ray; 3.00 A; A/B=128-257, A/B=261-431. DR PDB; 6B3J; EM; 3.30 A; R=24-463. DR PDB; 6GB1; X-ray; 2.73 A; A=21-145. DR PDB; 6KJV; X-ray; 2.80 A; A/B=128-204, A/B=215-257, A/B=261-431. DR PDB; 6KK1; X-ray; 2.80 A; A/B=128-204, A/B=215-257, A/B=261-431. DR PDB; 6KK7; X-ray; 3.10 A; A/B=128-204, A/B=215-257, A/B=261-431. DR PDB; 6LN2; X-ray; 3.20 A; A=24-260, A=262-439. DR PDB; 6ORV; EM; 3.00 A; RP=24-463. DR PDB; 6VCB; EM; 3.30 A; R=24-422. DR PDB; 6X18; EM; 2.10 A; R=24-463. DR PDB; 6X19; EM; 2.10 A; R=24-463. DR PDB; 6X1A; EM; 2.50 A; R=24-463. DR PDB; 6XOX; EM; 3.10 A; R=24-422. DR PDB; 7C2E; EM; 4.20 A; R=24-463. DR PDB; 7DUQ; EM; 2.50 A; R=24-463. DR PDB; 7DUR; EM; 3.30 A; R=24-463. DR PDB; 7E14; EM; 2.90 A; R=24-463. DR PDB; 7EVM; EM; 2.50 A; R=24-463. DR PDB; 7FIM; EM; 3.40 A; R=24-463. DR PDB; 7KI0; EM; 2.50 A; R=24-463. DR PDB; 7KI1; EM; 2.50 A; R=24-463. DR PDB; 7LCI; EM; 2.90 A; R=24-463. DR PDB; 7LCJ; EM; 2.82 A; R=24-463. DR PDB; 7LCK; EM; 3.24 A; R=24-463. DR PDB; 7LLL; EM; 3.70 A; R=24-463. DR PDB; 7LLY; EM; 3.30 A; R=24-463. DR PDB; 7RG9; EM; 3.20 A; R=24-422. DR PDB; 7RGP; EM; 2.90 A; R=24-422. DR PDB; 7RTB; EM; 2.14 A; R=22-463. DR PDB; 7S15; EM; 3.80 A; R=24-422. DR PDB; 7S1M; EM; 2.41 A; R=24-463. DR PDB; 7S3I; EM; 2.51 A; R=24-463. DR PDB; 7VBH; EM; 3.00 A; R=24-463. DR PDB; 7VBI; EM; 3.00 A; R=24-463. DR PDB; 7X8R; EM; 2.61 A; R=24-463. DR PDB; 7X8S; EM; 3.09 A; R=24-463. DR PDB; 8JIP; EM; 2.85 A; R=24-463. DR PDB; 8JIR; EM; 2.57 A; R=24-463. DR PDB; 8JIS; EM; 2.46 A; R=30-423. DR PDB; 8WG7; EM; 2.54 A; R=24-463. DR PDB; 8YW3; EM; 2.68 A; R=24-463. DR PDB; 8YWF; EM; 2.74 A; R=24-463. DR PDB; 9BYO; EM; 2.31 A; R=24-463. DR PDB; 9C0K; EM; 2.72 A; R=24-463. DR PDB; 9EBN; EM; 3.44 A; R=24-463. DR PDB; 9EBO; EM; 3.13 A; R=24-463. DR PDB; 9EBQ; EM; 3.16 A; R=24-463. DR PDB; 9IVG; EM; 3.00 A; R=24-463. DR PDB; 9IVM; EM; 3.22 A; R=24-463. DR PDB; 9J1P; EM; 2.99 A; R=24-463. DR PDBsum; 3C59; -. DR PDBsum; 3C5T; -. DR PDBsum; 3IOL; -. DR PDBsum; 4ZGM; -. DR PDBsum; 5E94; -. DR PDBsum; 5NX2; -. DR PDBsum; 5OTT; -. DR PDBsum; 5OTU; -. DR PDBsum; 5OTV; -. DR PDBsum; 5OTW; -. DR PDBsum; 5OTX; -. DR PDBsum; 5VEW; -. DR PDBsum; 5VEX; -. DR PDBsum; 6B3J; -. DR PDBsum; 6GB1; -. DR PDBsum; 6KJV; -. DR PDBsum; 6KK1; -. DR PDBsum; 6KK7; -. DR PDBsum; 6LN2; -. DR PDBsum; 6ORV; -. DR PDBsum; 6VCB; -. DR PDBsum; 6X18; -. DR PDBsum; 6X19; -. DR PDBsum; 6X1A; -. DR PDBsum; 6XOX; -. DR PDBsum; 7C2E; -. DR PDBsum; 7DUQ; -. DR PDBsum; 7DUR; -. DR PDBsum; 7E14; -. DR PDBsum; 7EVM; -. DR PDBsum; 7FIM; -. DR PDBsum; 7KI0; -. DR PDBsum; 7KI1; -. DR PDBsum; 7LCI; -. DR PDBsum; 7LCJ; -. DR PDBsum; 7LCK; -. DR PDBsum; 7LLL; -. DR PDBsum; 7LLY; -. DR PDBsum; 7RG9; -. DR PDBsum; 7RGP; -. DR PDBsum; 7RTB; -. DR PDBsum; 7S15; -. DR PDBsum; 7S1M; -. DR PDBsum; 7S3I; -. DR PDBsum; 7VBH; -. DR PDBsum; 7VBI; -. DR PDBsum; 7X8R; -. DR PDBsum; 7X8S; -. DR PDBsum; 8JIP; -. DR PDBsum; 8JIR; -. DR PDBsum; 8JIS; -. DR PDBsum; 8WG7; -. DR PDBsum; 8YW3; -. DR PDBsum; 8YWF; -. DR PDBsum; 9BYO; -. DR PDBsum; 9C0K; -. DR PDBsum; 9EBN; -. DR PDBsum; 9EBO; -. DR PDBsum; 9EBQ; -. DR PDBsum; 9IVG; -. DR PDBsum; 9IVM; -. DR PDBsum; 9J1P; -. DR AlphaFoldDB; P43220; -. DR EMDB; EMD-20179; -. DR EMDB; EMD-21147; -. DR EMDB; EMD-21992; -. DR EMDB; EMD-21993; -. DR EMDB; EMD-21994; -. DR EMDB; EMD-22283; -. DR EMDB; EMD-22882; -. DR EMDB; EMD-22883; -. DR EMDB; EMD-23274; -. DR EMDB; EMD-23275; -. DR EMDB; EMD-23276; -. DR EMDB; EMD-23425; -. DR EMDB; EMD-23436; -. DR EMDB; EMD-24445; -. DR EMDB; EMD-24453; -. DR EMDB; EMD-24680; -. DR EMDB; EMD-24794; -. DR EMDB; EMD-24805; -. DR EMDB; EMD-24825; -. DR EMDB; EMD-30274; -. DR EMDB; EMD-30866; -. DR EMDB; EMD-30867; -. DR EMDB; EMD-31329; -. DR EMDB; EMD-31603; -. DR EMDB; EMD-31879; -. DR EMDB; EMD-31880; -. DR EMDB; EMD-33057; -. DR EMDB; EMD-33058; -. DR EMDB; EMD-36323; -. DR EMDB; EMD-36325; -. DR EMDB; EMD-36326; -. DR EMDB; EMD-37504; -. DR EMDB; EMD-39621; -. DR EMDB; EMD-39631; -. DR EMDB; EMD-45040; -. DR EMDB; EMD-45087; -. DR EMDB; EMD-47447; -. DR EMDB; EMD-47882; -. DR EMDB; EMD-47883; -. DR EMDB; EMD-47884; -. DR EMDB; EMD-60927; -. DR EMDB; EMD-60930; -. DR EMDB; EMD-61077; -. DR EMDB; EMD-7039; -. DR SMR; P43220; -. DR BioGRID; 109002; 262. DR CORUM; P43220; -. DR DIP; DIP-29980N; -. DR FunCoup; P43220; 887. DR IntAct; P43220; 55. DR MINT; P43220; -. DR NDEx; IQUERY-CP-GLP1R; 5 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000362353; -. DR BindingDB; P43220; -. DR ChEMBL; CHEMBL1784; -. DR DrugBank; DB09043; Albiglutide. DR DrugBank; DB14806; Avexitide. DR DrugBank; DB09045; Dulaglutide. DR DrugBank; DB15650; Efpeglenatide. DR DrugBank; DB01276; Exenatide. DR DrugBank; DB00040; Glucagon. DR DrugBank; DB16697; Glutazumab. DR DrugBank; DB06655; Liraglutide. DR DrugBank; DB09265; Lixisenatide. DR DrugBank; DB21631; Lotiglipron. DR DrugBank; DB18964; Orforglipron. DR DrugBank; DB14817; Pegapamodutide. DR DrugBank; DB18998; Pemvidutide. DR DrugBank; DB16043; PF-06882961. DR DrugBank; DB01278; Pramlintide. DR DrugBank; DB13928; Semaglutide. DR DrugBank; DB14027; Taspoglutide. DR DrugBank; DB15171; Tirzepatide. DR DrugCentral; P43220; -. DR GuidetoPHARMACOLOGY; 249; -. DR TCDB; 9.A.14.4.6; the g-protein-coupled receptor (gpcr) family. DR GlyCosmos; P43220; 3 sites, No reported glycans. DR GlyGen; P43220; 3 sites. DR iPTMnet; P43220; -. DR PhosphoSitePlus; P43220; -. DR BioMuta; GLP1R; -. DR DMDM; 311033387; -. DR MassIVE; P43220; -. DR PaxDb; 9606-ENSP00000362353; -. DR ProteomicsDB; 55596; -. DR ABCD; P43220; 339 sequenced antibodies. DR Antibodypedia; 15682; 564 antibodies from 35 providers. DR DNASU; 2740; -. DR Ensembl; ENST00000373256.5; ENSP00000362353.4; ENSG00000112164.6. DR GeneID; 2740; -. DR KEGG; hsa:2740; -. DR MANE-Select; ENST00000373256.5; ENSP00000362353.4; NM_002062.5; NP_002053.3. DR UCSC; uc003ooj.5; human. DR AGR; HGNC:4324; -. DR ClinPGx; PA28725; -. DR CTD; 2740; -. DR DisGeNET; 2740; -. DR GeneCards; GLP1R; -. DR HGNC; HGNC:4324; GLP1R. DR HPA; ENSG00000112164; Tissue enhanced (heart muscle, pancreas). DR MIM; 138032; gene. DR OpenTargets; ENSG00000112164; -. DR VEuPathDB; HostDB:ENSG00000112164; -. DR eggNOG; KOG4564; Eukaryota. DR GeneTree; ENSGT00940000161009; -. DR HOGENOM; CLU_002753_4_0_1; -. DR InParanoid; P43220; -. DR OMA; CFVNNEK; -. DR OrthoDB; 5967113at2759; -. DR PAN-GO; P43220; 6 GO annotations based on evolutionary models. DR PhylomeDB; P43220; -. DR PathwayCommons; P43220; -. DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion. DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR Reactome; R-HSA-420092; Glucagon-type ligand receptors. DR SignaLink; P43220; -. DR SIGNOR; P43220; -. DR Agora; ENSG00000112164; -. DR BioGRID-ORCS; 2740; 10 hits in 1156 CRISPR screens. DR EvolutionaryTrace; P43220; -. DR GeneWiki; Glucagon-like_peptide_1_receptor; -. DR GenomeRNAi; 2740; -. DR Pharos; P43220; Tclin. DR PRO; PR:P43220; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; P43220; protein. DR Bgee; ENSG00000112164; Expressed in islet of Langerhans and 106 other cell types or tissues. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0004967; F:glucagon receptor activity; IBA:GO_Central. DR GO; GO:0044508; F:glucagon-like peptide 1 receptor activity; IDA:UniProtKB. DR GO; GO:0017046; F:peptide hormone binding; IBA:GO_Central. DR GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc. DR GO; GO:0007190; P:activation of adenylate cyclase activity; TAS:ProtInc. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB. DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro. DR GO; GO:0007611; P:learning or memory; IEA:Ensembl. DR GO; GO:0045777; P:positive regulation of blood pressure; IBA:GO_Central. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB. DR GO; GO:0008016; P:regulation of heart contraction; IEA:Ensembl. DR GO; GO:1990911; P:response to psychosocial stress; IEA:Ensembl. DR CDD; cd15268; 7tmB1_GLP1R; 1. DR FunFam; 1.20.1070.10:FF:000105; Glucagon like peptide 1 receptor; 1. DR FunFam; 4.10.1240.10:FF:000013; Glucagon like peptide 1 receptor; 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; IPR050332; GPCR_2. 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. PE 1: Evidence at protein level; KW 3D-structure; 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..23 FT /evidence="ECO:0000255" FT CHAIN 24..463 FT /note="Glucagon-like peptide 1 receptor" FT /id="PRO_0000012835" FT TOPO_DOM 24..139 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:28514449" FT TRANSMEM 140..164 FT /note="Helical; Name=1" FT /evidence="ECO:0000269|PubMed:28514449" FT TOPO_DOM 165..175 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:28514449" FT TRANSMEM 176..201 FT /note="Helical; Name=2" FT /evidence="ECO:0000269|PubMed:28514449" FT TOPO_DOM 202..227 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:28514449" FT TRANSMEM 228..251 FT /note="Helical; Name=3" FT /evidence="ECO:0000269|PubMed:28514449" FT TOPO_DOM 252..265 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:28514449" FT TRANSMEM 266..290 FT /note="Helical; Name=4" FT /evidence="ECO:0000269|PubMed:28514449" FT TOPO_DOM 291..305 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:28514449" FT TRANSMEM 306..328 FT /note="Helical; Name=5" FT /evidence="ECO:0000269|PubMed:28514449" FT TOPO_DOM 329..348 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:28514449" FT TRANSMEM 349..370 FT /note="Helical; Name=6" FT /evidence="ECO:0000269|PubMed:28514449" FT TOPO_DOM 371..383 FT /note="Extracellular" FT /evidence="ECO:0000269|PubMed:28514449" FT TRANSMEM 384..404 FT /note="Helical; Name=7" FT /evidence="ECO:0000269|PubMed:28514449" FT TOPO_DOM 405..463 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:28514449" FT REGION 352..355 FT /note="Important for allosteric inhibitor binding" FT /evidence="ECO:0000269|PubMed:28514449" FT SITE 121 FT /note="Interaction with the endogenous ligand GLP-1" FT /evidence="ECO:0000269|PubMed:19861722" FT SITE 128 FT /note="Interaction with the endogenous ligand GLP-1" FT /evidence="ECO:0000269|PubMed:19861722" FT MOD_RES 341 FT /note="ADP-ribosylcysteine" FT /evidence="ECO:0000269|PubMed:21901419" FT MOD_RES 348 FT /note="ADP-ribosylarginine" FT /evidence="ECO:0000269|PubMed:21901419" FT CARBOHYD 63 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:22412906" FT CARBOHYD 82 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:22412906" FT CARBOHYD 115 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:22412906" FT DISULFID 46..71 FT /evidence="ECO:0000269|PubMed:19861722, FT ECO:0000269|PubMed:26308095, ECO:0000269|PubMed:27196125, FT ECO:0007744|PDB:3C59, ECO:0007744|PDB:3C5T, FT ECO:0007744|PDB:3IOL, ECO:0007744|PDB:4ZGM, FT ECO:0007744|PDB:5E94" FT DISULFID 62..104 FT /evidence="ECO:0000269|PubMed:19861722, FT ECO:0000269|PubMed:26308095, ECO:0000269|PubMed:27196125, FT ECO:0007744|PDB:3C59, ECO:0007744|PDB:3C5T, FT ECO:0007744|PDB:3IOL, ECO:0007744|PDB:4ZGM, FT ECO:0007744|PDB:5E94" FT DISULFID 85..126 FT /evidence="ECO:0000269|PubMed:19861722, FT ECO:0000269|PubMed:26308095, ECO:0000269|PubMed:27196125, FT ECO:0007744|PDB:3C59, ECO:0007744|PDB:3C5T, FT ECO:0007744|PDB:3IOL, ECO:0007744|PDB:4ZGM, FT ECO:0007744|PDB:5E94" FT DISULFID 226..296 FT /evidence="ECO:0000269|PubMed:19861722, FT ECO:0000269|PubMed:26308095, ECO:0000269|PubMed:27196125, FT ECO:0000269|PubMed:28514449, ECO:0007744|PDB:3C59, FT ECO:0007744|PDB:3C5T, ECO:0007744|PDB:3IOL, FT ECO:0007744|PDB:4ZGM, ECO:0007744|PDB:5E94, FT ECO:0007744|PDB:5VEW, ECO:0007744|PDB:5VEX" FT VARIANT 7 FT /note="P -> L (in dbSNP:rs10305420)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_018924" FT VARIANT 20 FT /note="R -> K (in dbSNP:rs10305421)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_018925" FT VARIANT 44 FT /note="R -> H (in dbSNP:rs2295006)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_018926" FT VARIANT 131 FT /note="R -> Q (in dbSNP:rs3765467)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_018927" FT VARIANT 168 FT /note="G -> S (in dbSNP:rs6923761)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_018928" FT VARIANT 260 FT /note="L -> F (in dbSNP:rs1042044)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:7843404, ECO:0000269|PubMed:8216285, FT ECO:0000269|PubMed:8404634, ECO:0000269|PubMed:8405712, FT ECO:0000269|Ref.7" FT /id="VAR_015098" FT VARIANT 316 FT /note="A -> T (in dbSNP:rs10305492)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_018929" FT VARIANT 333 FT /note="S -> C (in dbSNP:rs10305493)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_018930" FT VARIANT 421 FT /note="R -> Q (in dbSNP:rs10305510)" FT /evidence="ECO:0000269|Ref.7" FT /id="VAR_018931" FT MUTAGEN 32 FT /note="L->A: No effect on stimulation of cAMP accumulation FT and on GLP-1 binding." FT /evidence="ECO:0000269|PubMed:19861722" FT MUTAGEN 69 FT /note="Y->A: Abolishes stimulation of cAMP accumulation in FT response to GLP-1." FT /evidence="ECO:0000269|PubMed:19861722" FT MUTAGEN 88 FT /note="Y->A: Abolishes stimulation of cAMP accumulation in FT response to GLP-1." FT /evidence="ECO:0000269|PubMed:19861722" FT MUTAGEN 89 FT /note="L->A: Abolishes stimulation of cAMP accumulation in FT response to GLP-1." FT /evidence="ECO:0000269|PubMed:19861722" FT MUTAGEN 90 FT /note="P->A: Strongly decreased stimulation of cAMP FT accumulation in response to GLP-1." FT /evidence="ECO:0000269|PubMed:19861722" FT MUTAGEN 121 FT /note="R->A: Strongly decreased stimulation of cAMP FT accumulation in response to GLP-1." FT /evidence="ECO:0000269|PubMed:19861722" FT MUTAGEN 127 FT /note="E->A: No effect on stimulation of cAMP accumulation FT in response to GLP-1." FT /evidence="ECO:0000269|PubMed:19861722" FT MUTAGEN 128 FT /note="E->A: Slightly decreases stimulation of cAMP FT accumulation in response to GLP-1." FT /evidence="ECO:0000269|PubMed:19861722" FT MUTAGEN 128 FT /note="E->Q: No effect on stimulation of cAMP accumulation FT in response to GLP-1." FT /evidence="ECO:0000269|PubMed:19861722" FT MUTAGEN 176 FT /note="R->Q: Decreases sensitivity to GLP-1." FT /evidence="ECO:0000269|PubMed:28514449" FT MUTAGEN 317 FT /note="I->C: Causes the formation of an artifactual FT disulfide bond that abolishes signaling in response to FT GLP-1 binding; when associated with C-361." FT /evidence="ECO:0000269|PubMed:28514449" FT MUTAGEN 352 FT /note="S->A: Abolishes inhibition by negative allosteric FT modulators." FT /evidence="ECO:0000269|PubMed:28514449" FT MUTAGEN 355 FT /note="T->A: Abolishes inhibition by the negative FT allosteric modulators NNC0640 and PF-06372222, but does not FT abolish inhibition by MK-0893." FT /evidence="ECO:0000269|PubMed:28514449" FT MUTAGEN 361 FT /note="G->C: Causes the formation of an artifactual FT disulfide bond that abolishes signaling in response to FT GLP-1 binding; when associated with C-317." FT /evidence="ECO:0000269|PubMed:28514449" FT CONFLICT 12 FT /note="L -> V (in Ref. 1; AAA03614, 4; no nucleotide entry FT and 10; AAB64013)" FT /evidence="ECO:0000305" FT CONFLICT 136..137 FT /note="SP -> WG (in Ref. 1; AAA03614)" FT /evidence="ECO:0000305" FT CONFLICT 137 FT /note="P -> R (in Ref. 4; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 151 FT /note="G -> A (in Ref. 1; AAA03614)" FT /evidence="ECO:0000305" FT CONFLICT 221 FT /note="Q -> L (in Ref. 5; AAA63787)" FT /evidence="ECO:0000305" FT CONFLICT 289 FT /note="Y -> I (in Ref. 1; AAA03614)" FT /evidence="ECO:0000305" FT CONFLICT 316 FT /note="A -> G (in Ref. 2; AAA62471/AAC50050)" FT /evidence="ECO:0000305" FT HELIX 32..52 FT /evidence="ECO:0007829|PDB:4ZGM" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:4ZGM" FT STRAND 57..59 FT /evidence="ECO:0007829|PDB:5E94" FT HELIX 62..64 FT /evidence="ECO:0007829|PDB:7RTB" FT STRAND 68..72 FT /evidence="ECO:0007829|PDB:7RTB" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:7E14" FT STRAND 79..84 FT /evidence="ECO:0007829|PDB:4ZGM" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:7VBH" FT HELIX 92..94 FT /evidence="ECO:0007829|PDB:4ZGM" FT STRAND 95..97 FT /evidence="ECO:0007829|PDB:6X19" FT STRAND 99..104 FT /evidence="ECO:0007829|PDB:4ZGM" FT TURN 105..107 FT /evidence="ECO:0007829|PDB:7KI0" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:4ZGM" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:8JIS" FT STRAND 116..119 FT /evidence="ECO:0007829|PDB:4ZGM" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:4ZGM" FT HELIX 137..142 FT /evidence="ECO:0007829|PDB:5E94" FT HELIX 145..168 FT /evidence="ECO:0007829|PDB:7EVM" FT HELIX 170..172 FT /evidence="ECO:0007829|PDB:6X18" FT HELIX 175..204 FT /evidence="ECO:0007829|PDB:6X18" FT HELIX 207..215 FT /evidence="ECO:0007829|PDB:6X18" FT HELIX 216..219 FT /evidence="ECO:0007829|PDB:9IVG" FT TURN 220..222 FT /evidence="ECO:0007829|PDB:7S1M" FT HELIX 224..255 FT /evidence="ECO:0007829|PDB:6X18" FT STRAND 256..258 FT /evidence="ECO:0007829|PDB:8JIS" FT HELIX 264..291 FT /evidence="ECO:0007829|PDB:6X18" FT TURN 294..298 FT /evidence="ECO:0007829|PDB:6X19" FT HELIX 303..337 FT /evidence="ECO:0007829|PDB:6X18" FT HELIX 345..360 FT /evidence="ECO:0007829|PDB:6X18" FT HELIX 362..365 FT /evidence="ECO:0007829|PDB:6X18" FT TURN 366..369 FT /evidence="ECO:0007829|PDB:6X18" FT TURN 372..374 FT /evidence="ECO:0007829|PDB:6X18" FT HELIX 378..392 FT /evidence="ECO:0007829|PDB:6X18" FT HELIX 394..399 FT /evidence="ECO:0007829|PDB:6X18" FT HELIX 400..404 FT /evidence="ECO:0007829|PDB:6X18" FT HELIX 407..418 FT /evidence="ECO:0007829|PDB:6X18" FT TURN 419..422 FT /evidence="ECO:0007829|PDB:6X18" SQ SEQUENCE 463 AA; 53026 MW; EE7C0EAE29931F5D CRC64; MAGAPGPLRL ALLLLGMVGR AGPRPQGATV SLWETVQKWR EYRRQCQRSL TEDPPPATDL FCNRTFDEYA CWPDGEPGSF VNVSCPWYLP WASSVPQGHV YRFCTAEGLW LQKDNSSLPW RDLSECEESK RGERSSPEEQ LLFLYIIYTV GYALSFSALV IASAILLGFR HLHCTRNYIH LNLFASFILR ALSVFIKDAA LKWMYSTAAQ QHQWDGLLSY QDSLSCRLVF LLMQYCVAAN YYWLLVEGVY LYTLLAFSVL SEQWIFRLYV SIGWGVPLLF VVPWGIVKYL YEDEGCWTRN SNMNYWLIIR LPILFAIGVN FLIFVRVICI VVSKLKANLM CKTDIKCRLA KSTLTLIPLL GTHEVIFAFV MDEHARGTLR FIKLFTELSF TSFQGLMVAI LYCFVNNEVQ LEFRKSWERW RLEHLHIQRD SSMKPLKCPT SSLSSGATAG SSMYTATCQA SCS //