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NMUR2_RAT
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   03-AUG-2022, entry version 134.
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   GlyGen; Q9ESQ4; 3 sites.
DR   PhosphoSitePlus; Q9ESQ4; -.
DR   PaxDb; Q9ESQ4; -.
DR   GeneID; 64042; -.
DR   KEGG; rno:64042; -.
DR   UCSC; RGD:621155; rat.
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   OMA; YTVMTYV; -.
DR   OrthoDB; 890529at2759; -.
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 tissues.
DR   Genevisible; Q9ESQ4; RN.
DR   GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; 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:0006816; P:calcium ion transport; ISO:RGD.
DR   GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007625; P:grooming behavior; ISO:RGD.
DR   GO; GO:0048016; P:inositol phosphate-mediated signaling; 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:0007204; P:positive regulation of cytosolic calcium ion concentration; 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   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   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   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
 
 
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