8JPF

Focused refiment structure of NTSR1 in NTSR1-GRK2-Galpha(q) complexes

Functional Information from GO Data

Chain	GOid	namespace	contents
R	0001659	biological_process	temperature homeostasis
R	0003085	biological_process	negative regulation of systemic arterial blood pressure
R	0003254	biological_process	regulation of membrane depolarization
R	0004930	molecular_function	G protein-coupled receptor activity
R	0005515	molecular_function	protein binding
R	0005783	cellular_component	endoplasmic reticulum
R	0005794	cellular_component	Golgi apparatus
R	0005886	cellular_component	plasma membrane
R	0006171	biological_process	cAMP biosynthetic process
R	0006950	biological_process	response to stress
R	0007165	biological_process	signal transduction
R	0007186	biological_process	G protein-coupled receptor signaling pathway
R	0007218	biological_process	neuropeptide signaling pathway
R	0007268	biological_process	chemical synaptic transmission
R	0007612	biological_process	learning
R	0008306	biological_process	associative learning
R	0009898	cellular_component	cytoplasmic side of plasma membrane
R	0009986	cellular_component	cell surface
R	0010628	biological_process	positive regulation of gene expression
R	0014049	biological_process	positive regulation of glutamate secretion
R	0014054	biological_process	positive regulation of gamma-aminobutyric acid secretion
R	0016020	cellular_component	membrane
R	0016492	molecular_function	G protein-coupled neurotensin receptor activity
R	0030424	cellular_component	axon
R	0030425	cellular_component	dendrite
R	0032094	biological_process	response to food
R	0032280	cellular_component	symmetric synapse
R	0032960	biological_process	regulation of inositol trisphosphate biosynthetic process
R	0033993	biological_process	response to lipid
R	0040017	biological_process	positive regulation of locomotion
R	0042802	molecular_function	identical protein binding
R	0043025	cellular_component	neuronal cell body
R	0043065	biological_process	positive regulation of apoptotic process
R	0043066	biological_process	negative regulation of apoptotic process
R	0043195	cellular_component	terminal bouton
R	0043197	cellular_component	dendritic spine
R	0043198	cellular_component	dendritic shaft
R	0043204	cellular_component	perikaryon
R	0043576	biological_process	regulation of respiratory gaseous exchange
R	0043679	cellular_component	axon terminus
R	0044309	cellular_component	neuron spine
R	0044877	molecular_function	protein-containing complex binding
R	0045121	cellular_component	membrane raft
R	0050965	biological_process	detection of temperature stimulus involved in sensory perception of pain
R	0051280	biological_process	negative regulation of release of sequestered calcium ion into cytosol
R	0051281	biological_process	positive regulation of release of sequestered calcium ion into cytosol
R	0060732	biological_process	positive regulation of inositol phosphate biosynthetic process
R	0070779	biological_process	D-aspartate import across plasma membrane
R	0071545	biological_process	inositol phosphate catabolic process
R	0071625	biological_process	vocalization behavior
R	0090238	biological_process	positive regulation of arachidonate secretion
R	0097151	biological_process	positive regulation of inhibitory postsynaptic potential
R	0098712	biological_process	L-glutamate import across plasma membrane
R	1990708	biological_process	conditioned place preference
R	2000822	biological_process	regulation of behavioral fear response

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. ATAlNVASLSVERYLaI

Chain	Residue	Details
R	ALA154-ILE170

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	19
Details	Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	64
Details	Topological domain: {"description":"Extracellular","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	19
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	24
Details	Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	21
Details	Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	20
Details	Transmembrane: {"description":"Helical; Name=7","evidences":[{"source":"UniProtKB","id":"P20789","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	23
Details	Region: {"description":"Neurotensin binding","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---