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P32301 (GLP1R_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucagon-like peptide 1 receptor

Short name=GLP-1 receptor
Short name=GLP-1-R
Short name=GLP-1R
Gene names
Name:Glp1r
Synonyms:Glpr
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

This is a receptor for glucagon-like peptide 1. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.

Subunit structure

May form homodimers and heterodimers with GIPR By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Pancreatic islets, stomach, lung, rat insulinoma cell line.

Post-translational modification

N-glycosylation enhances cell surface expression and lengthens receptor half-life by preventing degradation in the ER By similarity.

Sequence similarities

Belongs to the G-protein coupled receptor 2 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMADP-ribosylation
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadenylate cyclase-activating G-protein coupled receptor signaling pathway

Inferred from mutant phenotype PubMed 8612565. Source: RGD

associative learning

Inferred from direct assay PubMed 12925848. Source: RGD

cAMP-mediated signaling

Inferred from mutant phenotype PubMed 10446905. Source: RGD

feeding behavior

Inferred from mutant phenotype PubMed 10933308. Source: RGD

hormone secretion

Inferred from direct assay PubMed 8828468. Source: UniProtKB

insulin secretion

Inferred from mutant phenotype PubMed 10362617. Source: UniProtKB

learning or memory

Inferred from mutant phenotype PubMed 12925848. Source: UniProtKB

memory

Inferred from direct assay PubMed 12925848. Source: RGD

negative regulation of apoptotic process

Inferred from direct assay PubMed 12409292. Source: RGD

negative regulation of neuron apoptotic process

Inferred from direct assay PubMed 12925848. Source: RGD

neuropeptide signaling pathway

Traceable author statement PubMed 12093887. Source: RGD

positive regulation of blood pressure

Inferred from direct assay PubMed 12093887. Source: RGD

positive regulation of cell differentiation

Inferred from mutant phenotype PubMed 10580413. Source: RGD

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 10580413. Source: RGD

positive regulation of heart contraction

Inferred from direct assay PubMed 12093887. Source: RGD

positive regulation of insulin secretion

Inferred from direct assay PubMed 12093887. Source: RGD

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 11845326. Source: RGD

regulation of calcium ion transport

Inferred from mutant phenotype PubMed 10446905. Source: RGD

release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 15789279. Source: RGD

response to glucose

Inferred from mutant phenotype PubMed 11845326. Source: RGD

   Cellular_componentintegral component of plasma membrane

Inferred from direct assay PubMed 16002551. Source: RGD

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionG-protein coupled peptide receptor activity

Inferred from physical interaction PubMed 8612565. Source: RGD

G-protein coupled receptor activity

Traceable author statement PubMed 12093887. Source: RGD

glucagon receptor activity

Inferred from electronic annotation. Source: InterPro

peptide hormone binding

Inferred from direct assay Ref.1. Source: RGD

peptide receptor activity

Inferred from direct assay PubMed 15789279. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 463442Glucagon-like peptide 1 receptor
PRO_0000012837

Regions

Topological domain22 – 139118Extracellular By similarity
Transmembrane140 – 16425Helical; Name=1; By similarity
Topological domain165 – 17612Cytoplasmic By similarity
Transmembrane177 – 20125Helical; Name=2; By similarity
Topological domain202 – 22726Extracellular By similarity
Transmembrane228 – 25124Helical; Name=3; By similarity
Topological domain252 – 26514Cytoplasmic By similarity
Transmembrane266 – 28722Helical; Name=4; By similarity
Topological domain288 – 30518Extracellular By similarity
Transmembrane306 – 32823Helical; Name=5; By similarity
Topological domain329 – 35224Cytoplasmic By similarity
Transmembrane353 – 37119Helical; Name=6; By similarity
Topological domain372 – 38312Extracellular By similarity
Transmembrane384 – 40421Helical; Name=7; By similarity
Topological domain405 – 46359Cytoplasmic By similarity

Amino acid modifications

Modified residue3411ADP-ribosylcysteine By similarity
Modified residue3481ADP-ribosylarginine By similarity
Glycosylation631N-linked (GlcNAc...) Potential
Glycosylation821N-linked (GlcNAc...) Potential
Glycosylation1151N-linked (GlcNAc...) Potential
Disulfide bond46 ↔ 71 By similarity
Disulfide bond62 ↔ 104 By similarity
Disulfide bond85 ↔ 126 By similarity
Disulfide bond226 ↔ 296 By similarity

Experimental info

Sequence conflict3231V → I in AAP31860. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P32301 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: ABE2183E8EBE621F

FASTA46352,877
        10         20         30         40         50         60 
MAVTPSLLRL ALLLLGAVGR AGPRPQGATV SLSETVQKWR EYRHQCQRFL TEAPLLATGL 

        70         80         90        100        110        120 
FCNRTFDDYA CWPDGPPGSF VNVSCPWYLP WASSVLQGHV YRFCTAEGIW LHKDNSSLPW 

       130        140        150        160        170        180 
RDLSECEESK QGERNSPEEQ LLSLYIIYTV GYALSFSALV IASAILVSFR HLHCTRNYIH 

       190        200        210        220        230        240 
LNLFASFILR ALSVFIKDAA LKWMYSTAAQ QHQWDGLLSY QDSLGCRLVF LLMQYCVAAN 

       250        260        270        280        290        300 
YYWLLVEGVY LYTLLAFSVF SEQRIFKLYL SIGWGVPLLF VIPWGIVKYL YEDEGCWTRN 

       310        320        330        340        350        360 
SNMNYWLIIR LPILFAIGVN FLVFIRVICI VIAKLKANLM CKTDIKCRLA KSTLTLIPLL 

       370        380        390        400        410        420 
GTHEVIFAFV MDEHARGTLR FVKLFTELSF TSFQGFMVAV LYCFVNNEVQ MEFRKSWERW 

       430        440        450        460 
RLERLNIQRD SSMKPLKCPT SSVSSGATVG SSVYAATCQN SCS 

« Hide

References

[1]"Expression cloning of the pancreatic beta cell receptor for the gluco-incretin hormone glucagon-like peptide 1."
Thorens B.
Proc. Natl. Acad. Sci. U.S.A. 89:8641-8645(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Pancreatic islet.
[2]"Molecular cloning of a cDNA encoding for the GLP-1 receptor expressed in rat lung."
Lankat-Buttgereit B., Goke R., Fehmann H.C., Richter G., Goke B.
Exp. Clin. Endocrinol. 102:341-347(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lung.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97797 mRNA. Translation: AAA73377.1.
S75952 mRNA. Translation: AAP31860.1.
PIRA46172.
RefSeqNP_036860.1. NM_012728.1.
UniGeneRn.11408.

3D structure databases

ProteinModelPortalP32301.
SMRP32301. Positions 28-131.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247128. 1 interaction.

Chemistry

BindingDBP32301.
ChEMBLCHEMBL5862.
GuidetoPHARMACOLOGY249.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP32301.

Proteomic databases

PRIDEP32301.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25051.
KEGGrno:25051.

Organism-specific databases

CTD2740.
RGD2703. Glp1r.

Phylogenomic databases

eggNOGNOG263329.
HOGENOMHOG000008250.
HOVERGENHBG008318.
InParanoidP32301.
KOK04581.

Gene expression databases

GenevestigatorP32301.

Family and domain databases

InterProIPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR003290. GPCR_2_GLP1/glucagon_rcpt.
IPR003292. GPCR_2_GLP1_rcpt.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view]
PANTHERPTHR12011:SF20. PTHR12011:SF20. 1 hit.
PfamPF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]
PRINTSPR01353. GLUCAGNFAMLY.
PR01355. GLUCAGNLIKER.
PR00249. GPCRSECRETIN.
SMARTSM00008. HormR. 1 hit.
[Graphical view]
PROSITEPS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio605244.
PROP32301.

Entry information

Entry nameGLP1R_RAT
AccessionPrimary (citable) accession number: P32301
Secondary accession number(s): Q64073, Q6LD83
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: April 16, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries