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Protein

Neurotensin receptor type 1

Gene

Ntsr1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

G-protein coupled receptor for the tridecapeptide neurotensin (NTS). Signaling is effected via G proteins that activate a phosphatidylinositol-calcium second messenger system. Signaling leads to the activation of downstream MAP kinases and protects cells against apoptosis.1 Publication

GO - Molecular functioni

  1. G-protein coupled neurotensin receptor activity Source: UniProtKB

GO - Biological processi

  1. adult locomotory behavior Source: Ensembl
  2. negative regulation of apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_250028. Peptide ligand-binding receptors.
REACT_263374. G alpha (q) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Neurotensin receptor type 1
Short name:
NT-R-1
Short name:
NTR1
Alternative name(s):
High-affinity levocabastine-insensitive neurotensin receptor
NTRH
Gene namesi
Name:Ntsr1
Synonyms:Ntsr
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi1306076. Ntsr1.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Membrane raft By similarity
Note: Palmitoylation is required for localization at CAV1-enriched membrane rafts.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6868Extracellular1 PublicationAdd
BLAST
Transmembranei69 – 8921Helical; Name=1Add
BLAST
Topological domaini90 – 10314Cytoplasmic1 PublicationAdd
BLAST
Transmembranei104 – 12320Helical; Name=2Add
BLAST
Topological domaini124 – 14320Extracellular1 PublicationAdd
BLAST
Transmembranei144 – 16522Helical; Name=3Add
BLAST
Topological domaini166 – 18823Cytoplasmic1 PublicationAdd
BLAST
Transmembranei189 – 21022Helical; Name=4Add
BLAST
Topological domaini211 – 23525Extracellular1 PublicationAdd
BLAST
Transmembranei236 – 26025Helical; Name=5Add
BLAST
Topological domaini261 – 30848Cytoplasmic1 PublicationAdd
BLAST
Transmembranei309 – 33022Helical; Name=6Add
BLAST
Topological domaini331 – 34818Extracellular1 PublicationAdd
BLAST
Transmembranei349 – 36921Helical; Name=7Add
BLAST
Topological domaini370 – 42455Cytoplasmic1 PublicationAdd
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: UniProtKB
  2. membrane raft Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 424424Neurotensin receptor type 1PRO_0000069948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi4 – 41N-linked (GlcNAc...)Sequence Analysis
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi42 – 421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi142 ↔ 225PROSITE-ProRule annotation2 Publications
Lipidationi386 – 3861S-palmitoyl cysteineBy similarity
Lipidationi388 – 3881S-palmitoyl cysteineBy similarity

Post-translational modificationi

N-gycosylated.By similarity
Palmitoylated; this is required for normal localization at membrane rafts and normal GNA11-mediated activation of down-stream signaling cascades. The palmitoylation level increases in response to neurotensin treatment (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

PTM databases

PhosphoSiteiP20789.

Expressioni

Gene expression databases

GenevestigatoriP20789.

Interactioni

Subunit structurei

Interacts (palmitoylated form) with GNA11.By similarity

Protein-protein interaction databases

DIPiDIP-59956N.
STRINGi10116.ENSRNOP00000035997.

Structurei

Secondary structure

1
424
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi53 – 553Combined sources
Helixi61 – 9030Combined sources
Helixi99 – 11820Combined sources
Helixi120 – 12910Combined sources
Helixi138 – 17235Combined sources
Helixi174 – 1785Combined sources
Helixi183 – 20119Combined sources
Helixi204 – 2074Combined sources
Beta strandi208 – 2125Combined sources
Beta strandi214 – 2174Combined sources
Helixi220 – 2223Combined sources
Beta strandi223 – 2275Combined sources
Helixi231 – 24515Combined sources
Helixi247 – 26923Combined sources
Helixi298 – 33336Combined sources
Turni336 – 3383Combined sources
Helixi341 – 37232Combined sources
Helixi374 – 38310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZEVX-ray3.00A/B50-390[»]
4BUOX-ray2.75A/B50-390[»]
4BV0X-ray3.10A/B50-390[»]
4BWBX-ray3.57A/B50-390[»]
4GRVX-ray2.80A43-268[»]
A300-396[»]
ProteinModelPortaliP20789.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni326 – 34924Neurotensin bindingAdd
BLAST

Domaini

The ligand binding pocket consists mainly of extracellular loops ECL2 and ECL3, as well as transmembranes TM6 and TM7.

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. Neurotensin receptor subfamily. NTSR1 sub-subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG303702.
GeneTreeiENSGT00700000104070.
HOGENOMiHOG000231271.
HOVERGENiHBG098285.
InParanoidiP20789.
KOiK04211.
OMAiTVMVRQA.
OrthoDBiEOG75F4DR.
PhylomeDBiP20789.
TreeFamiTF337167.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003985. NT1_rcpt.
IPR003984. NT_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01479. NEUROTENSINR.
PR01480. NEUROTENSN1R.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20789-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHLNSSVPQG TPGEPDAQPF SGPQSEMEAT FLALSLSNGS GNTSESDTAG
60 70 80 90 100
PNSDLDVNTD IYSKVLVTAI YLALFVVGTV GNSVTAFTLA RKKSLQSLQS
110 120 130 140 150
TVHYHLGSLA LSDLLILLLA MPVELYNFIW VHHPWAFGDA GCRGYYFLRD
160 170 180 190 200
ACTYATALNV ASLSVERYLA ICHPFKAKTL MSRSRTKKFI SAIWLASALL
210 220 230 240 250
AIPMLFTMGL QNRSGDGTHP GGLVCTPIVD TATVKVVIQV NTFMSFLFPM
260 270 280 290 300
LVISILNTVI ANKLTVMVHQ AAEQGRVCTV GTHNGLEHST FNMTIEPGRV
310 320 330 340 350
QALRHGVLVL RAVVIAFVVC WLPYHVRRLM FCYISDEQWT TFLFDFYHYF
360 370 380 390 400
YMLTNALFYV SSAINPILYN LVSANFRQVF LSTLACLCPG WRHRRKKRPT
410 420
FSRKPNSMSS NHAFSTSATR ETLY
Length:424
Mass (Da):47,055
Last modified:February 1, 1991 - v1
Checksum:iA9C2F7EAF8D9BCD3
GO

Sequence databases

PIRiJH0164.
RefSeqiNP_001102437.1. NM_001108967.1.
XP_006235850.1. XM_006235788.1.
UniGeneiRn.200149.

Genome annotation databases

EnsembliENSRNOT00000039780; ENSRNOP00000035997; ENSRNOG00000028708.
GeneIDi366274.
KEGGirno:366274.
UCSCiRGD:1306076. rat.

Cross-referencesi

Sequence databases

PIRiJH0164.
RefSeqiNP_001102437.1. NM_001108967.1.
XP_006235850.1. XM_006235788.1.
UniGeneiRn.200149.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3ZEVX-ray3.00A/B50-390[»]
4BUOX-ray2.75A/B50-390[»]
4BV0X-ray3.10A/B50-390[»]
4BWBX-ray3.57A/B50-390[»]
4GRVX-ray2.80A43-268[»]
A300-396[»]
ProteinModelPortaliP20789.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59956N.
STRINGi10116.ENSRNOP00000035997.

Chemistry

BindingDBiP20789.
ChEMBLiCHEMBL3027.
GuidetoPHARMACOLOGYi309.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP20789.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000039780; ENSRNOP00000035997; ENSRNOG00000028708.
GeneIDi366274.
KEGGirno:366274.
UCSCiRGD:1306076. rat.

Organism-specific databases

CTDi4923.
RGDi1306076. Ntsr1.

Phylogenomic databases

eggNOGiNOG303702.
GeneTreeiENSGT00700000104070.
HOGENOMiHOG000231271.
HOVERGENiHBG098285.
InParanoidiP20789.
KOiK04211.
OMAiTVMVRQA.
OrthoDBiEOG75F4DR.
PhylomeDBiP20789.
TreeFamiTF337167.

Enzyme and pathway databases

ReactomeiREACT_250028. Peptide ligand-binding receptors.
REACT_263374. G alpha (q) signalling events.

Miscellaneous databases

NextBioi689103.
PROiP20789.

Gene expression databases

GenevestigatoriP20789.

Family and domain databases

InterProiIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003985. NT1_rcpt.
IPR003984. NT_rcpt.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00237. GPCRRHODOPSN.
PR01479. NEUROTENSINR.
PR01480. NEUROTENSN1R.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Structure and functional expression of the cloned rat neurotensin receptor."
    Tanaka K., Masu M., Nakanishi S.
    Neuron 4:847-854(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: Brain.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 43-396 IN COMPLEX WITH NEUROTENSIN FRAGMENT, LIGAND BINDING DOMAIN, DISULFIDE BOND.
  3. "Structure of signaling-competent neurotensin receptor 1 obtained by directed evolution in Escherichia coli."
    Egloff P., Hillenbrand M., Klenk C., Batyuk A., Heine P., Balada S., Schlinkmann K.M., Scott D.J., Schutz M., Pluckthun A.
    Proc. Natl. Acad. Sci. U.S.A. 111:E655-E662(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 50-390 IN COMPLEX WITH NEUROTENSIN FRAGMENT, DISULFIDE BOND, SUBCELLULAR LOCATION, TOPOLOGY, FUNCTION.

Entry informationi

Entry nameiNTR1_RAT
AccessioniPrimary (citable) accession number: P20789
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: March 4, 2015
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.