ID   NMUR1_HUMAN             Reviewed;         426 AA.
AC   Q9HB89; O43664; Q7LDP6; Q8NE20;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Neuromedin-U receptor 1;
DE            Short=NMU-R1;
DE   AltName: Full=G-protein coupled receptor 66;
DE   AltName: Full=G-protein coupled receptor FM-3;
GN   Name=NMUR1; Synonyms=GPR66;
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], FUNCTION, AND TISSUE SPECIFICITY.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=PNS, and Testis;
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-426, AND TISSUE SPECIFICITY.
RX   PubMed=9782091; DOI=10.1006/geno.1998.5441;
RA   Tan C.P., McKee K.K., Liu Q., Palyha O.C., Feighner S.D., Hreniuk D.L.,
RA   Smith R.G., Howard A.D.;
RT   "Cloning and characterization of a human and murine T-cell orphan G-
RT   protein-coupled receptor similar to the growth hormone secretagogue and
RT   neurotensin receptors.";
RL   Genomics 52:223-229(1998).
CC   -!- FUNCTION: Receptor for the neuromedin-U and neuromedin-S neuropeptides.
CC       {ECO:0000250, ECO:0000269|PubMed:10899166}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in greatest abundance in peripheral
CC       organs, particularly in elements of the gastrointestinal and urogenital
CC       systems with highest levels in testes. In central nervous system
CC       structures express levels are much lower than those seen in peripheral
CC       organs. Within the CNS, has been detected in highest abundance in the
CC       cerebellum, dorsal root ganglia, hippocampus, and spinal cord.
CC       {ECO:0000269|PubMed:10899166, ECO:0000269|PubMed:9782091}.
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-24 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AF272362; AAG24793.1; -; mRNA.
DR   EMBL; AC017104; AAY24249.1; -; Genomic_DNA.
DR   EMBL; BC036543; AAH36543.1; -; mRNA.
DR   EMBL; BC051914; AAH51914.1; -; mRNA.
DR   EMBL; AF044601; AAC02680.1; -; Genomic_DNA.
DR   EMBL; AF044600; AAC02680.1; JOINED; Genomic_DNA.
DR   CCDS; CCDS2486.1; -.
DR   RefSeq; NP_006047.3; NM_006056.4.
DR   RefSeq; XP_011508789.1; XM_011510487.2.
DR   PDB; 7W53; EM; 3.20 A; R=1-426.
DR   PDB; 7W56; EM; 2.90 A; R=1-426.
DR   PDBsum; 7W53; -.
DR   PDBsum; 7W56; -.
DR   AlphaFoldDB; Q9HB89; -.
DR   EMDB; EMD-32313; -.
DR   EMDB; EMD-32315; -.
DR   SMR; Q9HB89; -.
DR   BioGRID; 115600; 407.
DR   STRING; 9606.ENSP00000305877; -.
DR   BindingDB; Q9HB89; -.
DR   ChEMBL; CHEMBL1075178; -.
DR   GuidetoPHARMACOLOGY; 298; -.
DR   TCDB; 9.A.14.1.13; the g-protein-coupled receptor (gpcr) family.
DR   GlyCosmos; Q9HB89; 3 sites, No reported glycans.
DR   GlyGen; Q9HB89; 3 sites.
DR   iPTMnet; Q9HB89; -.
DR   PhosphoSitePlus; Q9HB89; -.
DR   BioMuta; NMUR1; -.
DR   DMDM; 74761608; -.
DR   PaxDb; 9606-ENSP00000305877; -.
DR   PeptideAtlas; Q9HB89; -.
DR   Antibodypedia; 20210; 277 antibodies from 29 providers.
DR   DNASU; 10316; -.
DR   Ensembl; ENST00000305141.5; ENSP00000305877.4; ENSG00000171596.7.
DR   GeneID; 10316; -.
DR   KEGG; hsa:10316; -.
DR   MANE-Select; ENST00000305141.5; ENSP00000305877.4; NM_006056.5; NP_006047.3.
DR   UCSC; uc002vry.5; human.
DR   AGR; HGNC:4518; -.
DR   CTD; 10316; -.
DR   DisGeNET; 10316; -.
DR   GeneCards; NMUR1; -.
DR   HGNC; HGNC:4518; NMUR1.
DR   HPA; ENSG00000171596; Tissue enhanced (retina).
DR   MIM; 604153; gene.
DR   neXtProt; NX_Q9HB89; -.
DR   OpenTargets; ENSG00000171596; -.
DR   PharmGKB; PA28910; -.
DR   VEuPathDB; HostDB:ENSG00000171596; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01100000263484; -.
DR   HOGENOM; CLU_009579_6_5_1; -.
DR   InParanoid; Q9HB89; -.
DR   OMA; HKAMHTP; -.
DR   OrthoDB; 3471593at2759; -.
DR   PhylomeDB; Q9HB89; -.
DR   TreeFam; TF318522; -.
DR   PathwayCommons; Q9HB89; -.
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; Q9HB89; -.
DR   SIGNOR; Q9HB89; -.
DR   BioGRID-ORCS; 10316; 14 hits in 1147 CRISPR screens.
DR   ChiTaRS; NMUR1; human.
DR   GeneWiki; Neuromedin_U_receptor_1; -.
DR   GenomeRNAi; 10316; -.
DR   Pharos; Q9HB89; Tchem.
DR   PRO; PR:Q9HB89; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9HB89; Protein.
DR   Bgee; ENSG00000171596; Expressed in granulocyte and 88 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; TAS: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:0008188; F:neuropeptide receptor activity; IBA:GO_Central.
DR   GO; GO:0019722; P:calcium-mediated signaling; IDA:UniProtKB.
DR   GO; GO:0006821; P:chloride transport; IDA:UniProtKB.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
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:UniProtKB.
DR   GO; GO:0050850; P:positive regulation of calcium-mediated signaling; IDA:UniProtKB.
DR   GO; GO:0006939; P:smooth muscle contraction; IEP:UniProtKB.
DR   CDD; cd15358; 7tmA_NMU-R1; 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; IPR005391; NeuromedU_rcpt_1.
DR   PANTHER; PTHR24243; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR24243:SF109; NEUROMEDIN-U RECEPTOR 1; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01565; NEUROMEDINUR.
DR   PRINTS; PR01566; NEUROMEDNU1R.
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.
DR   Genevisible; Q9HB89; HS.
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..426
FT                   /note="Neuromedin-U receptor 1"
FT                   /id="PRO_0000069906"
FT   TOPO_DOM        1..65
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        66..86
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        87..97
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..138
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..161
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        162..181
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        203..235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..294
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..315
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        316..338
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        360..426
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        7
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        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        134..219
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        203
FT                   /note="R -> Q (in Ref. 3; AAH36543)"
FT                   /evidence="ECO:0000305"
FT   HELIX           61..87
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   HELIX           89..91
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   HELIX           94..122
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   HELIX           130..159
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   HELIX           160..162
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   HELIX           167..171
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   HELIX           175..197
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:7W53"
FT   STRAND          219..223
FT                   /evidence="ECO:0007829|PDB:7W53"
FT   HELIX           225..239
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   HELIX           241..259
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   HELIX           293..322
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   HELIX           331..356
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   TURN            357..359
FT                   /evidence="ECO:0007829|PDB:7W56"
FT   HELIX           361..364
FT                   /evidence="ECO:0007829|PDB:7W56"
SQ   SEQUENCE   426 AA;  47351 MW;  F8DD781C020F04AA CRC64;
     MTPLCLNCSV LPGDLYPGGA RNPMACNGSA ARGHFDPEDL NLTDEALRLK YLGPQQTELF
     MPICATYLLI FVVGAVGNGL TCLVILRHKA MRTPTNYYLF SLAVSDLLVL LVGLPLELYE
     MWHNYPFLLG VGGCYFRTLL FEMVCLASVL NVTALSVERY VAVVHPLQAR SMVTRAHVRR
     VLGAVWGLAM LCSLPNTSLH GIRQLHVPCR GPVPDSAVCM LVRPRALYNM VVQTTALLFF
     CLPMAIMSVL YLLIGLRLRR ERLLLMQEAK GRGSAAARSR YTCRLQQHDR GRRQVTKMLF
     VLVVVFGICW APFHADRVMW SVVSQWTDGL HLAFQHVHVI SGIFFYLGSA ANPVLYSLMS
     SRFRETFQEA LCLGACCHRL RPRHSSHSLS RMTTGSTLCD VGSLGSWVHP LAGNDGPEAQ
     QETDPS
//