ID NMUR2_RAT Reviewed; 395 AA.
AC Q9ESQ4; Q9JIB1;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 27-MAR-2024, entry version 141.
DE RecName: Full=Neuromedin-U receptor 2;
DE Short=NMU-R2;
DE AltName: Full=G-protein coupled receptor TGR-1;
DE AltName: Full=G-protein-coupled receptor FM-4;
GN Name=Nmur2; Synonyms=Tgr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=10887190; DOI=10.1074/jbc.m004261200;
RA Hosoya M., Moriya T., Kawamata Y., Ohkubo S., Fujii R., Matsui H.,
RA Shintani Y., Fukusumi S., Habata Y., Hinuma S., Onda H., Nishimura O.,
RA Fujino M.;
RT "Identification and functional characterization of a novel subtype of
RT neuromedin U receptor.";
RL J. Biol. Chem. 275:29528-29532(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=10894543; DOI=10.1038/35017610;
RA Howard A.D., Wang R., Pong S.-S., Mellin T.N., Strack A., Guan X.-M.,
RA Zeng Z., Williams D.L., Feighner S.D., Nunes C.N., Murphy B., Stair J.N.,
RA Yu H., Jiang Q., Clements M.K., Tan C.P., Mckee K.K., Hreniuk D.L.,
RA Mcdonald T.P., Lynch K.R., Evans J.F., Austin C.P., Caskey T.,
RA van der Ploeg L.H.T., Liu Q.;
RT "Identification of receptors for neuromedin U and its role in feeding.";
RL Nature 406:70-74(2000).
RN [3]
RP FUNCTION AS A NEUROMEDIN-S RECEPTOR, AND TISSUE SPECIFICITY.
RX PubMed=15635449; DOI=10.1038/sj.emboj.7600526;
RA Mori K., Miyazato M., Ida T., Murakami N., Serino R., Ueta Y., Kojima M.,
RA Kangawa K.;
RT "Identification of neuromedin S and its possible role in the mammalian
RT circadian oscillator system.";
RL EMBO J. 24:325-335(2005).
CC -!- FUNCTION: Receptor for the neuromedin-U and neuromedin-S neuropeptides.
CC {ECO:0000269|PubMed:10887190, ECO:0000269|PubMed:10894543,
CC ECO:0000269|PubMed:15635449}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: The highest level is detected in the uterus. In the
CC central nervous system, high expression levels were found in the
CC hypothalamus and moderate levels in both the medulla oblongata and
CC spinal cord. Expressed in the hypothalamic paraventricular nucleus
CC (PVN) and suprachiasmatic nuclei (SCN) of the hypothalamus. Expression
CC is low in the gastrointestinal tract. In other peripheral tissues,
CC moderate expression was observed in the lung and ovary.
CC {ECO:0000269|PubMed:10887190, ECO:0000269|PubMed:10894543,
CC ECO:0000269|PubMed:15635449}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB041229; BAB13722.1; -; mRNA.
DR EMBL; AF242875; AAF82756.1; -; mRNA.
DR RefSeq; NP_071611.3; NM_022275.3.
DR AlphaFoldDB; Q9ESQ4; -.
DR SMR; Q9ESQ4; -.
DR STRING; 10116.ENSRNOP00000018967; -.
DR GlyCosmos; Q9ESQ4; 3 sites, No reported glycans.
DR GlyGen; Q9ESQ4; 3 sites.
DR PhosphoSitePlus; Q9ESQ4; -.
DR PaxDb; 10116-ENSRNOP00000018967; -.
DR GeneID; 64042; -.
DR KEGG; rno:64042; -.
DR UCSC; RGD:621155; rat.
DR AGR; RGD:621155; -.
DR CTD; 56923; -.
DR RGD; 621155; Nmur2.
DR VEuPathDB; HostDB:ENSRNOG00000014081; -.
DR eggNOG; KOG3656; Eukaryota.
DR HOGENOM; CLU_009579_6_5_1; -.
DR InParanoid; Q9ESQ4; -.
DR OrthoDB; 3471593at2759; -.
DR PhylomeDB; Q9ESQ4; -.
DR TreeFam; TF318522; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:Q9ESQ4; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000014081; Expressed in ovary and 2 other cell types or tissues.
DR Genevisible; Q9ESQ4; RN.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISO:RGD.
DR GO; GO:0005229; F:intracellular calcium activated chloride channel activity; ISO:RGD.
DR GO; GO:0042924; F:neuromedin U binding; ISO:RGD.
DR GO; GO:0001607; F:neuromedin U receptor activity; ISO:RGD.
DR GO; GO:0008188; F:neuropeptide receptor activity; IDA:RGD.
DR GO; GO:0050482; P:arachidonic acid secretion; ISO:RGD.
DR GO; GO:0007625; P:grooming behavior; ISO:RGD.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:RGD.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0002023; P:reduction of food intake in response to dietary excess; ISO:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IDA:UniProtKB.
DR GO; GO:0048265; P:response to pain; ISO:RGD.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR005390; NeuromedU_rcpt.
DR InterPro; IPR005392; NeuromedU_rcpt_2.
DR InterPro; IPR045561; NMU-R2_C.
DR PANTHER; PTHR24243; G-PROTEIN COUPLED RECEPTOR; 1.
DR PANTHER; PTHR24243:SF14; NEUROMEDIN-U RECEPTOR 2; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF19285; NmU-R2_C_term; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01565; NEUROMEDINUR.
DR PRINTS; PR01567; NEUROMEDNU2R.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
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 Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..395
FT /note="Neuromedin-U receptor 2"
FT /id="PRO_0000069912"
FT TOPO_DOM 1..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 139..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..293
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..395
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 374..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 111..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 346
FT /note="R -> Q (in Ref. 1; BAB13722)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="V -> M (in Ref. 1; BAB13722)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="T -> M (in Ref. 1; BAB13722)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 44723 MW; 01D3765B5D5355C0 CRC64;
MGKLENASWI HDPLMKYLNS TEEYLAHLCG PKRSDLSLPV SVAYALIFLV GVMGNLLVCM
VIVRHQTLKT PTNYYLFSLA VSDLLVLLLG MPLEIYEMWH NYPFLFGPVG CYFKTALFET
VCFASILSVT TVSVERYVAI VHPFRAKLES TRRRALRILS LVWSFSVVFS LPNTSIHGIK
FQHFPNGSSV PGSATCTVTK PMWVYNLIIQ ATSFLFYILP MTLISVLYYL MGLRLKRDES
LEANKVAVNI HRPSRKSVTK MLFVLVLVFA ICWTPFHVDR LFFSFVEEWT ESLAAVFNLI
HVVSGVFFYL SSAVNPIIYN LLSRRFRAAF RNVVSPTCKW CHPRHRPQGP PAQKIIFLTE
CHLVELTEDA GPQFPGQSSI HNTNLTTAPC AGEVP
//
