NTR1_MOUSE
ID NTR1_MOUSE Reviewed; 424 AA.
AC O88319;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Neurotensin receptor type 1;
DE Short=NT-R-1;
DE Short=NTR1;
GN Name=Ntsr1; Synonyms=Ntsr;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Snider J., Sano H., Ohta M.;
RT "Neurotensin receptor type 1.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: G-protein coupled receptor for the tridecapeptide neurotensin
CC (NTS). Signaling is effected via G proteins that activate a
CC phosphatidylinositol-calcium second messenger system. Signaling leads
CC to the activation of downstream MAP kinases and protects cells against
CC apoptosis. {ECO:0000250|UniProtKB:P30989}.
CC -!- SUBUNIT: Interacts (palmitoylated form) with GNA11.
CC {ECO:0000250|UniProtKB:P30989}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P30989};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P30989}. Membrane
CC raft {ECO:0000250|UniProtKB:P30989}. Note=Palmitoylation is required
CC for localization at CAV1-enriched membrane rafts.
CC {ECO:0000250|UniProtKB:P30989}.
CC -!- DOMAIN: The ligand binding pocket consists mainly of extracellular
CC loops ECL2 and ECL3, as well as transmembrane regions TM6 and TM7.
CC {ECO:0000250|UniProtKB:P20789}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P30989}.
CC -!- PTM: Palmitoylated; this is required for normal localization at
CC membrane rafts and normal GNA11-mediated activation of down-stream
CC signaling cascades. The palmitoylation level increases in response to
CC neurotensin treatment. {ECO:0000250|UniProtKB:P30989}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Neurotensin receptor subfamily. NTSR1 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB017027; BAA33013.1; -; mRNA.
DR CCDS; CCDS17177.1; -.
DR RefSeq; NP_061236.1; NM_018766.2.
DR AlphaFoldDB; O88319; -.
DR SMR; O88319; -.
DR STRING; 10090.ENSMUSP00000029084; -.
DR BindingDB; O88319; -.
DR ChEMBL; CHEMBL3570; -.
DR GuidetoPHARMACOLOGY; 309; -.
DR GlyGen; O88319; 4 sites.
DR iPTMnet; O88319; -.
DR PhosphoSitePlus; O88319; -.
DR PaxDb; O88319; -.
DR PRIDE; O88319; -.
DR ProteomicsDB; 291919; -.
DR Antibodypedia; 1519; 332 antibodies from 31 providers.
DR DNASU; 18216; -.
DR Ensembl; ENSMUST00000029084; ENSMUSP00000029084; ENSMUSG00000027568.
DR Ensembl; ENSMUST00000170448; ENSMUSP00000127548; ENSMUSG00000027568.
DR GeneID; 18216; -.
DR KEGG; mmu:18216; -.
DR UCSC; uc008ojg.1; mouse.
DR CTD; 4923; -.
DR MGI; MGI:97386; Ntsr1.
DR VEuPathDB; HostDB:ENSMUSG00000027568; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244813; -.
DR HOGENOM; CLU_009579_6_5_1; -.
DR InParanoid; O88319; -.
DR OMA; CLCPLWG; -.
DR OrthoDB; 890529at2759; -.
DR PhylomeDB; O88319; -.
DR TreeFam; TF337167; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-416476; G alpha (q) signalling events.
DR BioGRID-ORCS; 18216; 3 hits in 72 CRISPR screens.
DR PRO; PR:O88319; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; O88319; protein.
DR Bgee; ENSMUSG00000027568; Expressed in barrel cortex and 62 other tissues.
DR ExpressionAtlas; O88319; baseline and differential.
DR Genevisible; O88319; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0043679; C:axon terminus; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0044309; C:neuron spine; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032280; C:symmetric synapse; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; ISO:MGI.
DR GO; GO:0016492; F:G protein-coupled neurotensin receptor activity; ISS:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008188; F:neuropeptide receptor activity; TAS:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IGI:MGI.
DR GO; GO:0070779; P:D-aspartate import across plasma membrane; ISO:MGI.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0071545; P:inositol phosphate catabolic process; ISO:MGI.
DR GO; GO:0098712; P:L-glutamate import across plasma membrane; ISO:MGI.
DR GO; GO:0007612; P:learning; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISO:MGI.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
DR GO; GO:0090238; P:positive regulation of arachidonic acid secretion; ISO:MGI.
DR GO; GO:2001259; P:positive regulation of cation channel activity; ISO:MGI.
DR GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0014049; P:positive regulation of glutamate secretion; ISO:MGI.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; ISO:MGI.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
DR GO; GO:0098900; P:regulation of action potential; ISO:MGI.
DR GO; GO:0003254; P:regulation of membrane depolarization; ISO:MGI.
DR GO; GO:0043576; P:regulation of respiratory gaseous exchange; ISO:MGI.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISO:MGI.
DR GO; GO:0033993; P:response to lipid; ISO:MGI.
DR GO; GO:0001659; P:temperature homeostasis; ISO:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR003985; NT1_rcpt.
DR InterPro; IPR003984; NT_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01479; NEUROTENSINR.
DR PRINTS; PR01480; NEUROTENSN1R.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..424
FT /note="Neurotensin receptor type 1"
FT /id="PRO_0000069947"
FT TOPO_DOM 1..67
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 68..88
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 89..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 103..122
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 123..142
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 143..164
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 165..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 185..205
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 206..234
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 235..259
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 260..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 309..330
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 331..348
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TRANSMEM 349..369
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT TOPO_DOM 370..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P20789"
FT REGION 326..349
FT /note="Neurotensin binding"
FT /evidence="ECO:0000250"
FT REGION 398..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 386
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P30989"
FT LIPID 388
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P30989"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 141..224
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 424 AA; 47217 MW; 8E9A723171A48711 CRC64;
MHLNSSVQQG APSEPGAQPF PHPQFGLETM LLALSLSNGS GNSSESILEP NSNLDVNTDI
YSKVLVTAVY LALFVVGTVG NSVTAFTLAR KKSLQSLQST VHYHLGSLAL SDLLILLLAM
PVELYNFIWV HHPWAFGDAG CRGYYFLRDA CTYATALNVA SLSVERYLAI CHPFKAKTLM
SRSRTKKFIS AIWLASALLA VPMLFTMGLQ NRSADGQHPG GLVCTPTVDT ATVKVVIQVN
TFMSFLFPML IISILNTVIA NKLTVMVHQA AEQGRGVCTV GTHNSLEHST FNMSIEPGRV
QALRHGVLVL RAVVIAFVVC WLPYHVRRLM FCYISDEQWT TFLFDFYHYF YMLTNALFYV
SSAINPILYN LVSANFRQVF LSTLACLCPG WRRRRKKRPT FSRKPNSMSS NHAFSTSATR
ETLY
