Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8SAI

Cryo-EM structure of GPR34-Gi complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004930	molecular_function	G protein-coupled receptor activity
A	0005506	molecular_function	iron ion binding
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0009055	molecular_function	electron transfer activity
A	0016020	cellular_component	membrane
A	0020037	molecular_function	heme binding
A	0022900	biological_process	electron transport chain
A	0042597	cellular_component	periplasmic space
C	0005515	molecular_function	protein binding
C	0005834	cellular_component	heterotrimeric G-protein complex
C	0005886	cellular_component	plasma membrane
C	0007165	biological_process	signal transduction
C	0007186	biological_process	G protein-coupled receptor signaling pathway
C	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
C	0016020	cellular_component	membrane
C	0031681	molecular_function	G-protein beta-subunit binding
C	0045202	cellular_component	synapse
C	0048144	biological_process	fibroblast proliferation
C	0070062	cellular_component	extracellular exosome
C	0071380	biological_process	cellular response to prostaglandin E stimulus
C	0071870	biological_process	cellular response to catecholamine stimulus
D	0000287	molecular_function	magnesium ion binding
D	0001664	molecular_function	G protein-coupled receptor binding
D	0003924	molecular_function	GTPase activity
D	0003925	molecular_function	G protein activity
D	0005515	molecular_function	protein binding
D	0005525	molecular_function	GTP binding
D	0005634	cellular_component	nucleus
D	0005654	cellular_component	nucleoplasm
D	0005730	cellular_component	nucleolus
D	0005737	cellular_component	cytoplasm
D	0005765	cellular_component	lysosomal membrane
D	0005813	cellular_component	centrosome
D	0005829	cellular_component	cytosol
D	0005834	cellular_component	heterotrimeric G-protein complex
D	0005856	cellular_component	cytoskeleton
D	0005886	cellular_component	plasma membrane
D	0005938	cellular_component	cell cortex
D	0007165	biological_process	signal transduction
D	0007186	biological_process	G protein-coupled receptor signaling pathway
D	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
D	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
D	0007198	biological_process	adenylate cyclase-inhibiting serotonin receptor signaling pathway
D	0010854	molecular_function	adenylate cyclase regulator activity
D	0016787	molecular_function	hydrolase activity
D	0019001	molecular_function	guanyl nucleotide binding
D	0019003	molecular_function	GDP binding
D	0030496	cellular_component	midbody
D	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
D	0031749	molecular_function	D2 dopamine receptor binding
D	0031821	molecular_function	G protein-coupled serotonin receptor binding
D	0034695	biological_process	response to prostaglandin E
D	0043434	biological_process	response to peptide hormone
D	0045542	biological_process	positive regulation of cholesterol biosynthetic process
D	0046872	molecular_function	metal ion binding
D	0051301	biological_process	cell division
D	0060236	biological_process	regulation of mitotic spindle organization
D	0070062	cellular_component	extracellular exosome
D	0072678	biological_process	T cell migration
D	1904322	biological_process	cellular response to forskolin
D	1904778	biological_process	positive regulation of protein localization to cell cortex
E	0001750	cellular_component	photoreceptor outer segment
E	0003924	molecular_function	GTPase activity
E	0005515	molecular_function	protein binding
E	0005737	cellular_component	cytoplasm
E	0005765	cellular_component	lysosomal membrane
E	0005829	cellular_component	cytosol
E	0005834	cellular_component	heterotrimeric G-protein complex
E	0005886	cellular_component	plasma membrane
E	0007165	biological_process	signal transduction
E	0007186	biological_process	G protein-coupled receptor signaling pathway
E	0007191	biological_process	adenylate cyclase-activating dopamine receptor signaling pathway
E	0007200	biological_process	phospholipase C-activating G protein-coupled receptor signaling pathway
E	0007213	biological_process	G protein-coupled acetylcholine receptor signaling pathway
E	0007265	biological_process	Ras protein signal transduction
E	0008283	biological_process	cell population proliferation
E	0016020	cellular_component	membrane
E	0030159	molecular_function	signaling receptor complex adaptor activity
E	0044877	molecular_function	protein-containing complex binding
E	0045202	cellular_component	synapse
E	0050909	biological_process	sensory perception of taste
E	0051020	molecular_function	GTPase binding
E	0060041	biological_process	retina development in camera-type eye
E	0070062	cellular_component	extracellular exosome
E	0071380	biological_process	cellular response to prostaglandin E stimulus
E	0071870	biological_process	cellular response to catecholamine stimulus
E	0097381	cellular_component	photoreceptor disc membrane
E	1903561	cellular_component	extracellular vesicle

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. ISIiLLGFISLDRYIkI

Chain	Residue	Details
A	ILE140-ILE156

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LVSAsqDgKLIIWDS

Chain	Residue	Details
E	LEU70-SER84
E	ILE157-ILE171
E	LEU285-ALA299

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
E	SER2
D	ASN269

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphohistidine => ECO:0000250\|UniProtKB:P62871

Chain	Residue	Details
E	HIS266
D	THR181
A	TYR238-PHE269

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744\|PDB:1KJY, ECO:0007744\|PDB:2OM2, ECO:0007744\|PDB:2XNS, ECO:0007744\|PDB:3ONW, ECO:0007744\|PDB:3QE0, ECO:0007744\|PDB:3QI2, ECO:0007744\|PDB:4G5Q

Chain	Residue	Details
D	SER151

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744\|PDB:1KJY, ECO:0007744\|PDB:1Y3A, ECO:0007744\|PDB:2G83, ECO:0007744\|PDB:2GTP, ECO:0007744\|PDB:2IK8, ECO:0007744\|PDB:2OM2, ECO:0007744\|PDB:2XNS, ECO:0007744\|PDB:3ONW, ECO:0007744\|PDB:3QE0, ECO:0007744\|PDB:3QI2, ECO:0007744\|PDB:3UMR, ECO:0007744\|PDB:3UMS, ECO:0007744\|PDB:4G5Q

Chain	Residue	Details
D	LEU175
A	THR193-GLU216
A	SER291-GLU310

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:21115486

Chain	Residue	Details
D	ASP200

site_id	SWS_FT_FI6
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744\|PDB:1Y3A, ECO:0007744\|PDB:2G83, ECO:0007744\|PDB:2GTP, ECO:0007744\|PDB:2IK8, ECO:0007744\|PDB:2OM2, ECO:0007744\|PDB:3ONW, ECO:0007744\|PDB:3QE0, ECO:0007744\|PDB:3QI2, ECO:0007744\|PDB:3UMR, ECO:0007744\|PDB:3UMS, ECO:0007744\|PDB:4G5Q

Chain	Residue	Details
D	ALA326

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250

Chain	Residue	Details
D	ARG178

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269\|PubMed:24141704

Chain	Residue	Details
D	GLN204

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: ADP-ribosylcysteine; by pertussis toxin => ECO:0000250

Chain	Residue	Details
D	CYS351

site_id	SWS_FT_FI10
Number of Residues	1
Details	LIPID: N-myristoyl glycine => ECO:0000269\|PubMed:20213681, ECO:0000269\|PubMed:25255805

Chain	Residue	Details
D	GLY2
A	ASN200
A	ASN295

site_id	SWS_FT_FI11
Number of Residues	1
Details	LIPID: S-palmitoyl cysteine => ECO:0000250\|UniProtKB:P10824

Chain	Residue	Details
D	CYS3

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