ID   NMUR2_HUMAN             Reviewed;         415 AA.
AC   Q9GZQ4; Q7LC54; Q96AM5; Q9NRA6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 2.
DT   28-JUN-2023, entry version 166.
DE   RecName: Full=Neuromedin-U receptor 2;
DE            Short=NMU-R2;
DE   AltName: Full=G-protein coupled receptor FM-4;
DE   AltName: Full=G-protein coupled receptor TGR-1;
GN   Name=NMUR2; Synonyms=NMU2R, TGR1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT THR-395.
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, TISSUE SPECIFICITY, AND VARIANT
RP   THR-395.
RX   PubMed=10899166; DOI=10.1074/jbc.m004613200;
RA   Raddatz R., Wilson A.E., Artymyshyn R., Bonini J.A., Borowsky B.,
RA   Boteju L.W., Zhou S., Kouranova E.V., Nagorny R., Guevarra M.S., Dai M.,
RA   Lerman G.S., Vaysse P.J., Branchek T.A., Gerald C., Forray C., Adham N.;
RT   "Identification and characterization of two neuromedin U receptors
RT   differentially expressed in peripheral tissues and the central nervous
RT   system.";
RL   J. Biol. Chem. 275:32452-32459(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT THR-395.
RX   PubMed=11010960; DOI=10.1074/jbc.c000522200;
RA   Shan L., Qiao X., Crona J.H., Behan J., Wang S., Laz T., Bayne M.,
RA   Gustafson E.L., Monsma F.J. Jr., Hedrick J.A.;
RT   "Identification of a novel neuromedin U receptor subtype expressed in the
RT   central nervous system.";
RL   J. Biol. Chem. 275:39482-39486(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-395.
RC   TISSUE=Colon, and Placenta;
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).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 4-415, TISSUE SPECIFICITY, AND VARIANT
RP   THR-395.
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).
CC   -!- FUNCTION: Receptor for the neuromedin-U and neuromedin-S neuropeptides.
CC       {ECO:0000250, ECO:0000269|PubMed:10899166}.
CC   -!- INTERACTION:
CC       Q9GZQ4; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-10303844, EBI-10173507;
CC       Q9GZQ4; P15884: TCF4; NbExp=3; IntAct=EBI-10303844, EBI-533224;
CC       Q9GZQ4; Q12933: TRAF2; NbExp=3; IntAct=EBI-10303844, EBI-355744;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Predominantly expressed in the CNS, particularly in
CC       the medulla oblongata, pontine reticular formation, spinal cord, and
CC       thalamus. High level in testis whereas lower levels are present in a
CC       variety of peripheral tissues including the gastrointestinal tract,
CC       genitourinary tract, liver, pancreas, adrenal gland, thyroid gland,
CC       lung, trachea, spleen and thymus. {ECO:0000269|PubMed:10887190,
CC       ECO:0000269|PubMed:10894543, ECO:0000269|PubMed:10899166,
CC       ECO:0000269|PubMed:11010960}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB13721.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB041228; BAB13721.1; ALT_INIT; mRNA.
DR   EMBL; AF272363; AAG24794.1; -; mRNA.
DR   EMBL; AF292402; AAG03064.1; -; mRNA.
DR   EMBL; AC008571; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC016938; AAH16938.1; -; mRNA.
DR   EMBL; BC067776; AAH67776.1; -; mRNA.
DR   EMBL; AF242874; AAF82755.1; -; mRNA.
DR   CCDS; CCDS4321.1; -.
DR   RefSeq; NP_064552.3; NM_020167.4.
DR   PDB; 7W55; EM; 2.80 A; R=1-415.
DR   PDB; 7W57; EM; 3.20 A; R=1-415.
DR   PDB; 7XK8; EM; 3.30 A; R=1-345.
DR   PDBsum; 7W55; -.
DR   PDBsum; 7W57; -.
DR   PDBsum; 7XK8; -.
DR   AlphaFoldDB; Q9GZQ4; -.
DR   SMR; Q9GZQ4; -.
DR   BioGRID; 121250; 30.
DR   IntAct; Q9GZQ4; 22.
DR   STRING; 9606.ENSP00000255262; -.
DR   BindingDB; Q9GZQ4; -.
DR   ChEMBL; CHEMBL1075144; -.
DR   DrugCentral; Q9GZQ4; -.
DR   GuidetoPHARMACOLOGY; 299; -.
DR   GlyCosmos; Q9GZQ4; 3 sites, No reported glycans.
DR   GlyGen; Q9GZQ4; 3 sites.
DR   iPTMnet; Q9GZQ4; -.
DR   PhosphoSitePlus; Q9GZQ4; -.
DR   BioMuta; NMUR2; -.
DR   DMDM; 311033403; -.
DR   MassIVE; Q9GZQ4; -.
DR   PaxDb; Q9GZQ4; -.
DR   PeptideAtlas; Q9GZQ4; -.
DR   Antibodypedia; 16394; 219 antibodies from 29 providers.
DR   DNASU; 56923; -.
DR   Ensembl; ENST00000255262.4; ENSP00000255262.4; ENSG00000132911.5.
DR   GeneID; 56923; -.
DR   KEGG; hsa:56923; -.
DR   MANE-Select; ENST00000255262.4; ENSP00000255262.4; NM_020167.5; NP_064552.3.
DR   UCSC; uc003luv.3; human.
DR   AGR; HGNC:16454; -.
DR   CTD; 56923; -.
DR   DisGeNET; 56923; -.
DR   GeneCards; NMUR2; -.
DR   HGNC; HGNC:16454; NMUR2.
DR   HPA; ENSG00000132911; Tissue enriched (brain).
DR   MIM; 605108; gene.
DR   neXtProt; NX_Q9GZQ4; -.
DR   OpenTargets; ENSG00000132911; -.
DR   PharmGKB; PA31664; -.
DR   VEuPathDB; HostDB:ENSG00000132911; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01080000257331; -.
DR   HOGENOM; CLU_009579_6_5_1; -.
DR   InParanoid; Q9GZQ4; -.
DR   OMA; QEVWFIW; -.
DR   OrthoDB; 3471593at2759; -.
DR   PhylomeDB; Q9GZQ4; -.
DR   TreeFam; TF318522; -.
DR   PathwayCommons; Q9GZQ4; -.
DR   Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; Q9GZQ4; -.
DR   SIGNOR; Q9GZQ4; -.
DR   BioGRID-ORCS; 56923; 10 hits in 1134 CRISPR screens.
DR   GeneWiki; Neuromedin_U_receptor_2; -.
DR   GenomeRNAi; 56923; -.
DR   Pharos; Q9GZQ4; Tchem.
DR   PRO; PR:Q9GZQ4; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9GZQ4; protein.
DR   Bgee; ENSG00000132911; Expressed in tibialis anterior and 56 other tissues.
DR   Genevisible; Q9GZQ4; HS.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR   GO; GO:0005229; F:intracellular calcium activated chloride channel activity; IDA:UniProtKB.
DR   GO; GO:0042924; F:neuromedin U binding; IDA:UniProtKB.
DR   GO; GO:0001607; F:neuromedin U receptor activity; IDA:UniProtKB.
DR   GO; GO:0050482; P:arachidonic acid secretion; IDA:UniProtKB.
DR   GO; GO:0006816; P:calcium ion transport; IDA:UniProtKB.
DR   GO; GO:0019722; P:calcium-mediated signaling; NAS:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0007417; P:central nervous system development; IEP:UniProtKB.
DR   GO; GO:0007631; P:feeding behavior; TAS:ProtInc.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007625; P:grooming behavior; IEA:Ensembl.
DR   GO; GO:0048016; P:inositol phosphate-mediated signaling; IDA:UniProtKB.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
DR   GO; GO:0002023; P:reduction of food intake in response to dietary excess; IEA:Ensembl.
DR   GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
DR   GO; GO:0006940; P:regulation of smooth muscle contraction; NAS:UniProtKB.
DR   GO; GO:0048265; P:response to pain; IEA:Ensembl.
DR   CDD; cd15357; 7tmA_NMU-R2; 1.
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   3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..415
FT                   /note="Neuromedin-U receptor 2"
FT                   /id="PRO_0000069910"
FT   TOPO_DOM        1..49
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..82
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        83..103
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        104..123
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..146
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        147..165
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..214
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236..265
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        266..286
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        287..301
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        323..415
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        9
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        194
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        119..204
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   VARIANT         298
FT                   /note="S -> T (in dbSNP:rs4958535)"
FT                   /id="VAR_023941"
FT   VARIANT         315
FT                   /note="F -> L (in dbSNP:rs1895245)"
FT                   /id="VAR_023942"
FT   VARIANT         383
FT                   /note="P -> L (in dbSNP:rs4958532)"
FT                   /id="VAR_032770"
FT   VARIANT         388
FT                   /note="M -> V (in dbSNP:rs4958531)"
FT                   /id="VAR_023943"
FT   VARIANT         395
FT                   /note="A -> T (in dbSNP:rs1363422)"
FT                   /evidence="ECO:0000269|PubMed:10887190,
FT                   ECO:0000269|PubMed:10894543, ECO:0000269|PubMed:10899166,
FT                   ECO:0000269|PubMed:11010960, ECO:0000269|PubMed:15489334"
FT                   /id="VAR_023944"
FT   CONFLICT        204
FT                   /note="C -> F (in Ref. 5; AAH16938)"
FT                   /evidence="ECO:0000305"
FT   HELIX           45..72
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   HELIX           74..76
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   HELIX           79..107
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   HELIX           116..149
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   HELIX           151..157
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   HELIX           160..183
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   STRAND          185..187
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   STRAND          204..206
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   HELIX           210..224
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   HELIX           226..244
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   TURN            256..258
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   HELIX           259..293
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   HELIX           299..327
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   STRAND          329..331
FT                   /evidence="ECO:0007829|PDB:7W55"
FT   HELIX           332..345
FT                   /evidence="ECO:0007829|PDB:7W55"
SQ   SEQUENCE   415 AA;  47696 MW;  C2BACD84A812890F CRC64;
     MSGMEKLQNA SWIYQQKLED PFQKHLNSTE EYLAFLCGPR RSHFFLPVSV VYVPIFVVGV
     IGNVLVCLVI LQHQAMKTPT NYYLFSLAVS DLLVLLLGMP LEVYEMWRNY PFLFGPVGCY
     FKTALFETVC FASILSITTV SVERYVAILH PFRAKLQSTR RRALRILGIV WGFSVLFSLP
     NTSIHGIKFH YFPNGSLVPG SATCTVIKPM WIYNFIIQVT SFLFYLLPMT VISVLYYLMA
     LRLKKDKSLE ADEGNANIQR PCRKSVNKML FVLVLVFAIC WAPFHIDRLF FSFVEEWSES
     LAAVFNLVHV VSGVFFYLSS AVNPIIYNLL SRRFQAAFQN VISSFHKQWH SQHDPQLPPA
     QRNIFLTECH FVELTEDIGP QFPCQSSMHN SHLPAALSSE QMSRTNYQSF HFNKT
//