ID GALR1_RAT Reviewed; 346 AA. AC Q62805; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 162. DE RecName: Full=Galanin receptor type 1; DE Short=GAL1-R; DE Short=GALR-1; GN Name=Galr1; Synonyms=Galnr, Galnr1; 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. RC TISSUE=Insulinoma; RX PubMed=8750821; DOI=10.1016/0169-328x(95)00159-p; RA Parker E.M., Izzarelli D.G., Nowak H.P., Mahle C.D., Iben L.G., Wang J., RA Goldstein M.E.; RT "Cloning and characterization of the rat GALR1 galanin receptor from Rin14B RT insulinoma cells."; RL Brain Res. Mol. Brain Res. 34:179-189(1995). CC -!- FUNCTION: Receptor for the hormone galanin. The activity of this CC receptor is mediated by G proteins that inhibit adenylate cyclase CC activity. {ECO:0000250|UniProtKB:P47211, ECO:0000269|PubMed:8750821}. CC -!- SUBUNIT: Interacts with GRP39 AND HTR1A. CC {ECO:0000250|UniProtKB:P47211}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P47211}; CC Multi-pass membrane protein. CC -!- TISSUE SPECIFICITY: Spinal cord, small intestine, Rin14B insulinoma CC cells and several brain regions, particularly ventral hippocampus, CC amygdala, supraoptic nucleus, hypothalamus, thalamus, lateral CC parabrachial nucleus and locus coeruleus. {ECO:0000269|PubMed:8750821}. CC -!- PTM: Three cysteine residues are found in the C-terminus, at least one CC of which may be palmitoylated. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U30290; AAC52438.1; -; mRNA. DR RefSeq; NP_037090.2; NM_012958.3. DR AlphaFoldDB; Q62805; -. DR SMR; Q62805; -. DR STRING; 10116.ENSRNOP00000022400; -. DR BindingDB; Q62805; -. DR ChEMBL; CHEMBL5504; -. DR GuidetoPHARMACOLOGY; 243; -. DR GlyCosmos; Q62805; 3 sites, No reported glycans. DR GlyGen; Q62805; 3 sites. DR PhosphoSitePlus; Q62805; -. DR PaxDb; 10116-ENSRNOP00000022400; -. DR Ensembl; ENSRNOT00000022401.3; ENSRNOP00000022400.1; ENSRNOG00000016654.6. DR Ensembl; ENSRNOT00055023247; ENSRNOP00055018876; ENSRNOG00055013560. DR Ensembl; ENSRNOT00060026112; ENSRNOP00060020905; ENSRNOG00060015234. DR Ensembl; ENSRNOT00065003850; ENSRNOP00065002709; ENSRNOG00065002805. DR GeneID; 50577; -. DR KEGG; rno:50577; -. DR AGR; RGD:2656; -. DR CTD; 2587; -. DR RGD; 2656; Galr1. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01050000244841; -. DR HOGENOM; CLU_009579_6_4_1; -. DR InParanoid; Q62805; -. DR OMA; VFKCHIR; -. DR OrthoDB; 2915794at2759; -. DR PhylomeDB; Q62805; -. DR TreeFam; TF315737; -. DR Reactome; R-RNO-375276; Peptide ligand-binding receptors. DR Reactome; R-RNO-418594; G alpha (i) signalling events. DR PRO; PR:Q62805; -. DR Proteomes; UP000002494; Chromosome 18. DR Bgee; ENSRNOG00000016654; Expressed in jejunum and 5 other cell types or tissues. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central. DR GO; GO:0004966; F:galanin receptor activity; IDA:RGD. DR GO; GO:0042923; F:neuropeptide binding; IDA:RGD. DR GO; GO:0017046; F:peptide hormone binding; ISS:UniProtKB. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:RGD. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD. DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central. DR GO; GO:0051464; P:positive regulation of cortisol secretion; ISO:RGD. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:InterPro. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR CDD; cd15098; 7tmA_Gal1_R; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR003906; GAL1_rcpt. DR InterPro; IPR000405; Galanin_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR45695:SF26; G PROTEIN-COUPLED RECEPTOR 15-LIKE; 1. DR PANTHER; PTHR45695; LEUCOKININ RECEPTOR-RELATED; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01418; GALANIN1R. DR PRINTS; PR00663; GALANINR. DR PRINTS; PR00237; GPCRRHODOPSN. 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; Q62805; RN. PE 2: Evidence at transcript level; KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer; KW Transmembrane; Transmembrane helix. FT CHAIN 1..346 FT /note="Galanin receptor type 1" FT /id="PRO_0000069465" FT TOPO_DOM 1..33 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 34..54 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 55..69 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 70..90 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 91..108 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 109..130 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 131..150 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 151..171 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 172..196 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 197..217 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 218..246 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 247..267 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 268..269 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 270..290 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 291..346 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 326..346 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT LIPID 318 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CARBOHYD 7 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 12 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 181 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 107..185 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" SQ SEQUENCE 346 AA; 38862 MW; 789FFBE40D1D3805 CRC64; MELAPVNLSE GNGSDPEPPA EPRPLFGIGV ENFITLVVFG LIFAMGVLGN SLVITVLARS KPGKPRSTTN LFILNLSIAD LAYLLFCIPF QATVYALPTW VLGAFICKFI HYFFTVSMLV SIFTLAAMSV DRYVAIVHSR RSSSLRVSRN ALLGVGFIWA LSIAMASPVA YYQRLFHRDS NQTFCWEHWP NQLHKKAYVV CTFVFGYLLP LLLICFCYAK VLNHLHKKLK NMSKKSEASK KKTAQTVLVV VVVFGISWLP HHVIHLWAEF GAFPLTPASF FFRITAHCLA YSNSSVNPII YAFLSENFRK AYKQVFKCRV CNESPHGDAK EKNRIDTPPS TNCTHV //