GRPR_RAT
ID GRPR_RAT Reviewed; 384 AA.
AC P52500; G3V6I7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Gastrin-releasing peptide receptor;
DE Short=GRP-R;
DE AltName: Full=GRP-preferring bombesin receptor;
GN Name=Grpr;
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].
RC TISSUE=Pancreatic acinar cell;
RA Wada E., Way J., Shapira H., Battey J.F.;
RT "Two distinct bombesin receptor subtype subtypes in ppostnatal rat central
RT nervous system.";
RL Mol. Cell. Neurosci. 3:446-460(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8391296; DOI=10.1007/bf02736689;
RA Giladi E., Nagalla S.R., Spindel E.R.;
RT "Molecular cloning and characterization of receptors for the mammalian
RT bombesin-like peptides.";
RL J. Mol. Neurosci. 4:41-54(1993).
RN [5]
RP FUNCTION.
RX PubMed=26855425; DOI=10.1038/nature16964;
RA Li P., Janczewski W.A., Yackle K., Kam K., Pagliardini S., Krasnow M.A.,
RA Feldman J.L.;
RT "The peptidergic control circuit for sighing.";
RL Nature 530:293-297(2016).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=33059246; DOI=10.1016/j.npep.2020.102080;
RA Yang J., Yang X., Xiao X., Ming D.;
RT "The effects of gastrin-releasing peptide on the voltage-gated channels in
RT rat hippocampal neurons.";
RL Neuropeptides 84:102080-102080(2020).
CC -!- FUNCTION: Receptor for gastrin-releasing peptide (GRP)
CC (PubMed:8391296). Signals via association with G proteins that activate
CC a phosphatidylinositol-calcium second messenger system, resulting in
CC Akt phosphorylation. Contributes to the regulation of food intake.
CC Contributes to the perception of prurient stimuli and transmission of
CC itch signals in the spinal cord that promote scratching behavior, but
CC does not play a role in the perception of pain. Contributes primarily
CC to nonhistaminergic itch sensation. In one study, shown to act in the
CC amygdala as part of an inhibitory network which inhibits memory
CC specifically related to learned fear (By similarity). In another study,
CC shown to contribute to disinhibition of glutamatergic cells in the
CC auditory cortex via signaling on vasoactive intestinal peptide-
CC expressing cells which leads to enhanced auditory fear memories (By
CC similarity). Contributes to the induction of sighing through signaling
CC in the pre-Botzinger complex, a cluster of several thousand neurons in
CC the ventrolateral medulla responsible for inspiration during
CC respiratory activity (PubMed:26855425). {ECO:0000250|UniProtKB:P21729,
CC ECO:0000269|PubMed:26855425, ECO:0000269|PubMed:8391296}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8391296};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in the hippocampal CA1 region (at protein
CC level). {ECO:0000269|PubMed:33059246}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; X56661; CAA39988.1; -; mRNA.
DR EMBL; AABR07037836; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474014; EDL90503.1; -; Genomic_DNA.
DR PIR; I57682; I57682.
DR RefSeq; NP_036838.1; NM_012706.2.
DR AlphaFoldDB; P52500; -.
DR SMR; P52500; -.
DR STRING; 10116.ENSRNOP00000005559; -.
DR BindingDB; P52500; -.
DR ChEMBL; CHEMBL4280; -.
DR GuidetoPHARMACOLOGY; 39; -.
DR GlyGen; P52500; 3 sites.
DR PhosphoSitePlus; P52500; -.
DR PaxDb; P52500; -.
DR Ensembl; ENSRNOT00000005559; ENSRNOP00000005559; ENSRNOG00000004124.
DR GeneID; 24938; -.
DR KEGG; rno:24938; -.
DR UCSC; RGD:2750; rat.
DR CTD; 2925; -.
DR RGD; 2750; Grpr.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244862; -.
DR InParanoid; P52500; -.
DR OMA; IWIASML; -.
DR OrthoDB; 1153238at2759; -.
DR PhylomeDB; P52500; -.
DR TreeFam; TF331292; -.
DR Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR Reactome; R-RNO-416476; G alpha (q) signalling events.
DR PRO; PR:P52500; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome x.
DR Bgee; ENSRNOG00000004124; Expressed in pancreas and 7 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0004946; F:bombesin receptor activity; TAS:RGD.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; ISO:RGD.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IDA:RGD.
DR GO; GO:0042923; F:neuropeptide binding; IDA:RGD.
DR GO; GO:0008188; F:neuropeptide receptor activity; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR GO; GO:0007611; P:learning or memory; IMP:RGD.
DR GO; GO:0061744; P:motor behavior; ISS:UniProtKB.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:2000987; P:positive regulation of behavioral fear response; ISS:UniProtKB.
DR GO; GO:1903942; P:positive regulation of respiratory gaseous exchange; ISS:UniProtKB.
DR GO; GO:0036343; P:psychomotor behavior; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0043207; P:response to external biotic stimulus; ISO:RGD.
DR GO; GO:0035176; P:social behavior; IMP:RGD.
DR InterPro; IPR001556; Bombsn_rcpt-like.
DR InterPro; IPR001966; Gastrin_pep_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00358; BOMBESINR.
DR PRINTS; PR00640; GASTRINRELPR.
DR PRINTS; PR00237; GPCRRHODOPSN.
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 Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..384
FT /note="Gastrin-releasing peptide receptor"
FT /id="PRO_0000069664"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..97
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..137
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..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..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..326
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..384
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54799"
FT LIPID 340
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 114..197
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 28
FT /note="N -> S (in Ref. 1; CAA39988)"
SQ SEQUENCE 384 AA; 43236 MW; 86C0671671812EEB CRC64;
MDPNNCSHLN LEVDPFLSCN NTFNQTLNPP KMDNWFHPGI IYVIPAVYGL IIVIGLIGNI
TLIKIFCTVK SMRNVPNLFI SSLALGDLLL LVTCAPVDAS KYLADRWLFG RIGCKLIPFI
QLTSVGVSVF TLTALSADRY KAIVRPMDIQ ASHALMKICL KAALIWIVSM LLAIPEAVFS
DLHPFHVKDT NQTFISCAPY PHSNELHPKI HSMASFLVFY IIPLSIISVY YYFIARNLIQ
SAYNLPVEGN IHVKKQIESR KRLAKTVLVF VGLFAFCWLP NHVIYLYRSY HYSEVDTSML
HFITSICARL LAFTNSCVNP FALYLLSKSF RKQFNTQLLC CQPSLLNRSH STGRSTTCMT
SFKSTNPSAT FSLINGNICH EGYV
