Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9IJS

Cryo-EM structure of the orphan GPR52 bound to beta-arrestin 1 in ligand-free state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004930	molecular_function	G protein-coupled receptor activity
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0007165	biological_process	signal transduction
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0007602	biological_process	phototransduction
A	0007626	biological_process	locomotory behavior
A	0008020	molecular_function	G protein-coupled photoreceptor activity
A	0009410	biological_process	response to xenobiotic stimulus
A	0009584	biological_process	detection of visible light
A	0071482	biological_process	cellular response to light stimulus
C	0000139	cellular_component	Golgi membrane
C	0000785	cellular_component	chromatin
C	0001664	molecular_function	G protein-coupled receptor binding
C	0001678	biological_process	intracellular glucose homeostasis
C	0001934	biological_process	positive regulation of protein phosphorylation
C	0002029	biological_process	desensitization of G protein-coupled receptor signaling pathway
C	0002031	biological_process	G protein-coupled receptor internalization
C	0002092	biological_process	positive regulation of receptor internalization
C	0003713	molecular_function	transcription coactivator activity
C	0004402	molecular_function	histone acetyltransferase activity
C	0004857	molecular_function	enzyme inhibitor activity
C	0005096	molecular_function	GTPase activator activity
C	0005159	molecular_function	insulin-like growth factor receptor binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005654	cellular_component	nucleoplasm
C	0005737	cellular_component	cytoplasm
C	0005765	cellular_component	lysosomal membrane
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0005905	cellular_component	clathrin-coated pit
C	0006357	biological_process	regulation of transcription by RNA polymerase II
C	0006511	biological_process	ubiquitin-dependent protein catabolic process
C	0007166	biological_process	cell surface receptor signaling pathway
C	0007600	biological_process	sensory perception
C	0009968	biological_process	negative regulation of signal transduction
C	0010613	biological_process	positive regulation of cardiac muscle hypertrophy
C	0015031	biological_process	protein transport
C	0016567	biological_process	protein ubiquitination
C	0016604	cellular_component	nuclear body
C	0019899	molecular_function	enzyme binding
C	0030659	cellular_component	cytoplasmic vesicle membrane
C	0030666	cellular_component	endocytic vesicle membrane
C	0031143	cellular_component	pseudopodium
C	0031397	biological_process	negative regulation of protein ubiquitination
C	0031410	cellular_component	cytoplasmic vesicle
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0031701	molecular_function	angiotensin receptor binding
C	0032088	biological_process	negative regulation of NF-kappaB transcription factor activity
C	0032715	biological_process	negative regulation of interleukin-6 production
C	0032717	biological_process	negative regulation of interleukin-8 production
C	0035025	biological_process	positive regulation of Rho protein signal transduction
C	0043149	biological_process	stress fiber assembly
C	0043161	biological_process	proteasome-mediated ubiquitin-dependent protein catabolic process
C	0045746	biological_process	negative regulation of Notch signaling pathway
C	0045944	biological_process	positive regulation of transcription by RNA polymerase II
C	0060090	molecular_function	molecular adaptor activity
C	0070374	biological_process	positive regulation of ERK1 and ERK2 cascade
C	1902533	biological_process	positive regulation of intracellular signal transduction
C	1990763	molecular_function	arrestin family protein binding

Functional Information from PROSITE/UniProt

site_id	PS00237
Number of Residues	17
Details	G_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. VSMwCLACISVDRYLaI

Chain	Residue	Details
A	VAL127-ILE143

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

Chain	Residue	Details
C	PHE61-LEU79

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	42
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	38
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	41
Details	Region: {"description":"Interaction with CHRM2","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
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)