Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8JRU

Cryo-EM structure of the glucagon receptor bound to beta-arrestin 1 in ligand-free state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000822	molecular_function	inositol hexakisphosphate binding
A	0001664	molecular_function	G protein-coupled receptor binding
A	0001934	biological_process	positive regulation of protein phosphorylation
A	0002029	biological_process	desensitization of G protein-coupled receptor signaling pathway
A	0002031	biological_process	G protein-coupled receptor internalization
A	0002092	biological_process	positive regulation of receptor internalization
A	0005515	molecular_function	protein binding
A	0005547	molecular_function	phosphatidylinositol-3,4,5-trisphosphate binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005905	cellular_component	clathrin-coated pit
A	0006351	biological_process	DNA-templated transcription
A	0006511	biological_process	ubiquitin-dependent protein catabolic process
A	0006898	biological_process	receptor-mediated endocytosis
A	0007165	biological_process	signal transduction
A	0007600	biological_process	sensory perception
A	0008277	biological_process	regulation of G protein-coupled receptor signaling pathway
A	0009968	biological_process	negative regulation of signal transduction
A	0015031	biological_process	protein transport
A	0030132	cellular_component	clathrin coat of coated pit
A	0030276	molecular_function	clathrin binding
A	0031143	cellular_component	pseudopodium
A	0031410	cellular_component	cytoplasmic vesicle
A	0031623	biological_process	receptor internalization
A	0032050	molecular_function	clathrin heavy chain binding
A	0033130	molecular_function	acetylcholine receptor binding
A	0035612	molecular_function	AP-2 adaptor complex binding
A	0036094	molecular_function	small molecule binding
A	0045746	biological_process	negative regulation of Notch signaling pathway
A	0060090	molecular_function	molecular adaptor activity
A	0070374	biological_process	positive regulation of ERK1 and ERK2 cascade
A	0072583	biological_process	clathrin-dependent endocytosis
H	0000822	molecular_function	inositol hexakisphosphate binding
H	0001664	molecular_function	G protein-coupled receptor binding
H	0001934	biological_process	positive regulation of protein phosphorylation
H	0002029	biological_process	desensitization of G protein-coupled receptor signaling pathway
H	0002031	biological_process	G protein-coupled receptor internalization
H	0002092	biological_process	positive regulation of receptor internalization
H	0005515	molecular_function	protein binding
H	0005547	molecular_function	phosphatidylinositol-3,4,5-trisphosphate binding
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005829	cellular_component	cytosol
H	0005886	cellular_component	plasma membrane
H	0005905	cellular_component	clathrin-coated pit
H	0006351	biological_process	DNA-templated transcription
H	0006511	biological_process	ubiquitin-dependent protein catabolic process
H	0006898	biological_process	receptor-mediated endocytosis
H	0007165	biological_process	signal transduction
H	0007600	biological_process	sensory perception
H	0008277	biological_process	regulation of G protein-coupled receptor signaling pathway
H	0009968	biological_process	negative regulation of signal transduction
H	0015031	biological_process	protein transport
H	0030132	cellular_component	clathrin coat of coated pit
H	0030276	molecular_function	clathrin binding
H	0031143	cellular_component	pseudopodium
H	0031410	cellular_component	cytoplasmic vesicle
H	0031623	biological_process	receptor internalization
H	0032050	molecular_function	clathrin heavy chain binding
H	0033130	molecular_function	acetylcholine receptor binding
H	0035612	molecular_function	AP-2 adaptor complex binding
H	0036094	molecular_function	small molecule binding
H	0045746	biological_process	negative regulation of Notch signaling pathway
H	0060090	molecular_function	molecular adaptor activity
H	0070374	biological_process	positive regulation of ERK1 and ERK2 cascade
H	0072583	biological_process	clathrin-dependent endocytosis
L	0000822	molecular_function	inositol hexakisphosphate binding
L	0001664	molecular_function	G protein-coupled receptor binding
L	0001934	biological_process	positive regulation of protein phosphorylation
L	0002029	biological_process	desensitization of G protein-coupled receptor signaling pathway
L	0002031	biological_process	G protein-coupled receptor internalization
L	0002092	biological_process	positive regulation of receptor internalization
L	0005515	molecular_function	protein binding
L	0005547	molecular_function	phosphatidylinositol-3,4,5-trisphosphate binding
L	0005634	cellular_component	nucleus
L	0005737	cellular_component	cytoplasm
L	0005829	cellular_component	cytosol
L	0005886	cellular_component	plasma membrane
L	0005905	cellular_component	clathrin-coated pit
L	0006351	biological_process	DNA-templated transcription
L	0006511	biological_process	ubiquitin-dependent protein catabolic process
L	0006898	biological_process	receptor-mediated endocytosis
L	0007165	biological_process	signal transduction
L	0007600	biological_process	sensory perception
L	0008277	biological_process	regulation of G protein-coupled receptor signaling pathway
L	0009968	biological_process	negative regulation of signal transduction
L	0015031	biological_process	protein transport
L	0030132	cellular_component	clathrin coat of coated pit
L	0030276	molecular_function	clathrin binding
L	0031143	cellular_component	pseudopodium
L	0031410	cellular_component	cytoplasmic vesicle
L	0031623	biological_process	receptor internalization
L	0032050	molecular_function	clathrin heavy chain binding
L	0033130	molecular_function	acetylcholine receptor binding
L	0035612	molecular_function	AP-2 adaptor complex binding
L	0036094	molecular_function	small molecule binding
L	0045746	biological_process	negative regulation of Notch signaling pathway
L	0060090	molecular_function	molecular adaptor activity
L	0070374	biological_process	positive regulation of ERK1 and ERK2 cascade
L	0072583	biological_process	clathrin-dependent endocytosis
R	0004888	molecular_function	transmembrane signaling receptor activity
R	0004930	molecular_function	G protein-coupled receptor activity
R	0004967	molecular_function	glucagon receptor activity
R	0005085	molecular_function	guanyl-nucleotide exchange factor activity
R	0005886	cellular_component	plasma membrane
R	0006091	biological_process	generation of precursor metabolites and energy
R	0007165	biological_process	signal transduction
R	0007166	biological_process	cell surface receptor signaling pathway
R	0007186	biological_process	G protein-coupled receptor signaling pathway
R	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
R	0007189	biological_process	adenylate cyclase-activating G protein-coupled receptor signaling pathway
R	0007584	biological_process	response to nutrient
R	0008217	biological_process	regulation of blood pressure
R	0009267	biological_process	cellular response to starvation
R	0010628	biological_process	positive regulation of gene expression
R	0016020	cellular_component	membrane
R	0017046	molecular_function	peptide hormone binding
R	0042593	biological_process	glucose homeostasis
R	0042594	biological_process	response to starvation
R	0071377	biological_process	cellular response to glucagon stimulus

Functional Information from PROSITE/UniProt

site_id	PS00295
Number of Residues	19
Details	ARRESTINS Arrestins signature. FRYGrEDlDVLGLtFrKDL

Chain	Residue	Details
A	PHE61-LEU79

site_id	PS00649
Number of Residues	25
Details	G_PROTEIN_RECEP_F2_1 G-protein coupled receptors family 2 signature 1. CnrtFDkys.CWpdTpanttanisCP

Chain	Residue	Details
R	CYS58-PRO82

site_id	PS00650
Number of Residues	16
Details	G_PROTEIN_RECEP_F2_2 G-protein coupled receptors family 2 signature 2. QGLLVaVLYCFlNkeV

Chain	Residue	Details
R	GLN392-VAL407

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	34
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	23
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	17
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	22
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"PubMed","id":"23863937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	3
Details	Region: {"description":"Important for allosteric inhibitor binding","evidences":[{"source":"PubMed","id":"27111510","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28514451","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BWG8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)