Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P30989 (NTR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neurotensin receptor type 1

Short name=NT-R-1
Short name=NTR1
Alternative name(s):
High-affinity levocabastine-insensitive neurotensin receptor
NTRH
Gene names
Name:NTSR1
Synonyms:NTRR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for the tridecapeptide neurotensin. It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. Ref.1 Ref.5

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.1.

Tissue specificity

Expressed in prostate (at protein level). Detected in colon and peripheral blood mononuclear cells. Detected at very low levels in brain. Ref.1 Ref.4

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Neurotensin receptor type 1
PRO_0000069946

Regions

Topological domain1 – 6363Extracellular Potential
Transmembrane64 – 8623Helical; Name=1; Potential
Topological domain87 – 959Cytoplasmic Potential
Transmembrane96 – 12025Helical; Name=2; Potential
Topological domain121 – 14222Extracellular Potential
Transmembrane143 – 16422Helical; Name=3; Potential
Topological domain165 – 18723Cytoplasmic Potential
Transmembrane188 – 20922Helical; Name=4; Potential
Topological domain210 – 23425Extracellular Potential
Transmembrane235 – 25925Helical; Name=5; Potential
Topological domain260 – 30344Cytoplasmic Potential
Transmembrane304 – 32522Helical; Name=6; Potential
Topological domain326 – 34318Extracellular Potential
Transmembrane344 – 36724Helical; Name=7; Potential
Topological domain368 – 41851Cytoplasmic Potential

Amino acid modifications

Lipidation3831S-palmitoyl cysteine Potential
Glycosylation41N-linked (GlcNAc...) Potential
Glycosylation371N-linked (GlcNAc...) Potential
Glycosylation411N-linked (GlcNAc...) Potential
Disulfide bond141 ↔ 224 By similarity

Natural variations

Natural variant721A → V.
Corresponds to variant rs11698783 [ dbSNP | Ensembl ].
VAR_059328
Natural variant2751Q → H.
Corresponds to variant rs35373650 [ dbSNP | Ensembl ].
VAR_049424
Natural variant3041V → I.
Corresponds to variant rs2273075 [ dbSNP | Ensembl ].
VAR_020071

Experimental info

Sequence conflict2001A → T in CAA49675. Ref.1

Secondary structure

..... 418
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P30989 [UniParc].

Last modified March 29, 2005. Version 2.
Checksum: 471AD1C49D29C2C8

FASTA41846,259
        10         20         30         40         50         60 
MRLNSSAPGT PGTPAADPFQ RAQAGLEEAL LAPGFGNASG NASERVLAAP SSELDVNTDI 

        70         80         90        100        110        120 
YSKVLVTAVY LALFVVGTVG NTVTAFTLAR KKSLQSLQST VHYHLGSLAL SDLLTLLLAM 

       130        140        150        160        170        180 
PVELYNFIWV HHPWAFGDAG CRGYYFLRDA CTYATALNVA SLSVERYLAI CHPFKAKTLM 

       190        200        210        220        230        240 
SRSRTKKFIS AIWLASALLA VPMLFTMGEQ NRSADGQHAG GLVCTPTIHT ATVKVVIQVN 

       250        260        270        280        290        300 
TFMSFIFPMV VISVLNTIIA NKLTVMVRQA AEQGQVCTVG GEHSTFSMAI EPGRVQALRH 

       310        320        330        340        350        360 
GVRVLRAVVI AFVVCWLPYH VRRLMFCYIS DEQWTPFLYD FYHYFYMVTN ALFYVSSTIN 

       370        380        390        400        410 
PILYNLVSAN FRHIFLATLA CLCPVWRRRR KRPAFSRKAD SVSSNHTLSS NATRETLY 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a complementary DNA encoding a high affinity human neurotensin receptor."
Vita N., Laurent P., Lefort S., Chalon P., Dumont X., Kaghad M., Gully D., le Fur G., Ferrara P., Caput D.
FEBS Lett. 317:139-142(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Kopatz S.A., Aronstam R.S., Sharma S.V.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Altered expression of neurotensin receptors is associated with the differentiation state of prostate cancer."
Swift S.L., Burns J.E., Maitland N.J.
Cancer Res. 70:347-356(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[5]"Intermolecular interactions between the neurotensin and the third extracellular loop of human neurotensin 1 receptor."
Da Costa G., Bondon A., Coutant J., Curmi P., Monti J.P.
J. Biomol. Struct. Dyn. 31:1381-1392(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 321-344 IN COMPLEX WITH NTS, FUNCTION.
+Additional computationally mapped references.

Web resources

Wikipedia

Neurotensin receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X70070 mRNA. Translation: CAA49675.1.
AY429106 mRNA. Translation: AAR07901.1.
AL035669, AL357033 Genomic DNA. Translation: CAC12747.2.
AL357033 Genomic DNA. Translation: CAC14923.2.
PIRS29506.
RefSeqNP_002522.2. NM_002531.2.
UniGeneHs.590869.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LYWNMR-A321-344[»]
ProteinModelPortalP30989.
SMRP30989. Positions 51-267, 293-374.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110977. 2 interactions.
IntActP30989. 1 interaction.
STRING9606.ENSP00000359532.

Chemistry

BindingDBP30989.
ChEMBLCHEMBL2111438.
GuidetoPHARMACOLOGY309.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP30989.

Polymorphism databases

DMDM62297312.

Proteomic databases

PaxDbP30989.
PeptideAtlasP30989.
PRIDEP30989.

Protocols and materials databases

DNASU4923.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370501; ENSP00000359532; ENSG00000101188.
GeneID4923.
KEGGhsa:4923.
UCSCuc002ydf.3. human.

Organism-specific databases

CTD4923.
GeneCardsGC20P061340.
HGNCHGNC:8039. NTSR1.
HPAHPA050299.
MIM162651. gene.
neXtProtNX_P30989.
PharmGKBPA31821.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303702.
HOGENOMHOG000231271.
HOVERGENHBG098285.
InParanoidP30989.
KOK04211.
OMATVMVRQA.
OrthoDBEOG75F4DR.
PhylomeDBP30989.
TreeFamTF337167.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP30989.
CleanExHS_NTSR1.
GenevestigatorP30989.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR003985. NT1_rcpt.
IPR003984. NT_rcpt.
[Graphical view]
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR01479. NEUROTENSINR.
PR01480. NEUROTENSN1R.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiNeurotensin_receptor_1.
GenomeRNAi4923.
NextBio18959.
PROP30989.
SOURCESearch...

Entry information

Entry nameNTR1_HUMAN
AccessionPrimary (citable) accession number: P30989
Secondary accession number(s): Q9H4H1, Q9H4T5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: March 29, 2005
Last modified: April 16, 2014
This is version 135 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries