NTR2_MOUSE
ID NTR2_MOUSE Reviewed; 416 AA.
AC P70310; Q8VIF5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-OCT-2013, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Neurotensin receptor type 2;
DE Short=NT-R-2;
DE Short=NTR2;
DE AltName: Full=Low-affinity levocabastine-sensitive neurotensin receptor;
DE AltName: Full=NTRL;
GN Name=Ntsr2;
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 STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8795617; DOI=10.1523/jneurosci.16-18-05613.1996;
RA Mazella J., Botto J.-M., Guillemare E., Coppola T., Sarret P.,
RA Vincent J.-P.;
RT "Structure, functional expression, and cerebral localization of the
RT levocabastine-sensitive neurotensin/neuromedin N receptor from mouse
RT brain.";
RL J. Neurosci. 16:5613-5620(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=11687289; DOI=10.1016/s0169-328x(01)00220-0;
RA Sun Y.J., Maeno H., Aoki S., Wada K.;
RT "Mouse neurotensin receptor 2 gene (Ntsr2): genomic organization,
RT transcriptional regulation and genetic mapping on chromosome 12.";
RL Brain Res. Mol. Brain Res. 95:167-171(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Receptor for the tridecapeptide neurotensin. It is associated
CC with G proteins that activate a phosphatidylinositol-calcium second
CC messenger system.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed maximally in the cerebellum, hippocampus,
CC piriform cortex and neocortex of adult brain.
CC -!- DEVELOPMENTAL STAGE: Expressed poorly in 7-day-old brain. Expression
CC increases at day 15 to reach a maximal level in 35-day-old brain.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC Neurotensin receptor subfamily. NTSR2 sub-subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB17285.1; Type=Frameshift; Evidence={ECO:0000305};
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; U51908; AAB17285.1; ALT_FRAME; mRNA.
DR EMBL; AB041827; BAB79257.1; -; mRNA.
DR EMBL; AK158943; BAE34736.1; -; mRNA.
DR EMBL; AC122228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141019; AAI41020.1; -; mRNA.
DR CCDS; CCDS36407.1; -.
DR RefSeq; NP_032773.2; NM_008747.2.
DR AlphaFoldDB; P70310; -.
DR SMR; P70310; -.
DR STRING; 10090.ENSMUSP00000106693; -.
DR BindingDB; P70310; -.
DR DrugCentral; P70310; -.
DR GuidetoPHARMACOLOGY; 310; -.
DR iPTMnet; P70310; -.
DR PhosphoSitePlus; P70310; -.
DR SwissPalm; P70310; -.
DR PaxDb; P70310; -.
DR PRIDE; P70310; -.
DR ProteomicsDB; 293771; -.
DR Antibodypedia; 12728; 303 antibodies from 29 providers.
DR DNASU; 18217; -.
DR Ensembl; ENSMUST00000111064; ENSMUSP00000106693; ENSMUSG00000020591.
DR GeneID; 18217; -.
DR KEGG; mmu:18217; -.
DR UCSC; uc007nbw.1; mouse.
DR CTD; 23620; -.
DR MGI; MGI:108018; Ntsr2.
DR VEuPathDB; HostDB:ENSMUSG00000020591; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244813; -.
DR HOGENOM; CLU_009579_6_5_1; -.
DR InParanoid; P70310; -.
DR OMA; YSFRLWG; -.
DR OrthoDB; 890529at2759; -.
DR PhylomeDB; P70310; -.
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; 18217; 1 hit in 73 CRISPR screens.
DR PRO; PR:P70310; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P70310; protein.
DR Bgee; ENSMUSG00000020591; Expressed in globus pallidus and 87 other tissues.
DR ExpressionAtlas; P70310; baseline and differential.
DR Genevisible; P70310; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0043198; C:dendritic shaft; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0016492; F:G protein-coupled neurotensin receptor activity; IDA:MGI.
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:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR003986; NT2_rcpt.
DR InterPro; IPR003984; NT_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01479; NEUROTENSINR.
DR PRINTS; PR01481; NEUROTENSN2R.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..416
FT /note="Neurotensin receptor type 2"
FT /id="PRO_0000069950"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..55
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..87
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 88..109
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..176
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..217
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..237
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..416
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63384"
FT LIPID 377
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT DISULFID 108..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 62
FT /note="A -> T (in Ref. 1; AAB17285)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="R -> C (in Ref. 1; AAB17285)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="F -> I (in Ref. 1; AAB17285)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 416 AA; 46376 MW; 290F8CCB726694B4 CRC64;
METSSLWPPR PSPSAGLSLE ARLGVDTRLW AKVLFTALYS LIFALGTAGN ALSVHVVLKA
RAGRPGRLRY HVLSLALSAL LLLLISVPME LYNFVWSHYP WVFGDLGCRG YYFVRELCAY
ATVLSVASLS AERCLAVCQP LRARRLLTPR RTRRLLSLVW VASLGLALPM AVIMGQKHEM
ERADGEPEPA SRVCTVLVSR ATLQVFIQVN VLVSFVLPLA LTAFLNGITV NHLVALYSQV
PSASAQVNSI PSRLELLSEE GLLGFITWRK TLSLGVQASL VRHKDASQIR SLQHSAQVLR
AIVAVYVICW LPYHARRLMY CYIPDDGWTD ELYDFYHYFY MVTNTLFYVS SAVTPVLYNA
VSSSFRKLFL ESLSSLCGEQ RSVVPLPQEA PESTTSTYSF RLWGSPRNPS LGEIQV
