ID GALR3_RAT Reviewed; 370 AA. AC O88626; O54914; Q9QWZ2; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 24-JAN-2024, entry version 137. DE RecName: Full=Galanin receptor type 3; DE Short=GAL3-R; DE Short=GALR-3; GN Name=Galr3; Synonyms=Galnr3; 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 STRAIN=Sprague-Dawley; TISSUE=Hypothalamus; RX PubMed=10619483; DOI=10.1016/s0306-4522(99)00407-8; RA Waters S.M., Krause J.E.; RT "Distribution of galanin-1, -2 and -3 receptor messenger RNAs in central RT and peripheral rat tissues."; RL Neuroscience 95:265-271(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Wang S., He C., Hashemi T., Bayne M.; RT "Molecular cloning of the rat galanin receptor type 3."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION. RC STRAIN=Sprague-Dawley; RX PubMed=9722565; DOI=10.1074/jbc.273.36.23321; RA Smith K.E., Walker M.W., Artymyshyn R., Bard J., Borowsky B., Tamm J.A., RA Yao W.-J., Vaysse P.J.-J., Branchek T.A., Gerald C., Jones K.A.; RT "Cloned human and rat galanin GALR3 receptors: pharmacology and activation RT of G-protein inwardly rectifying K+ channels."; RL J. Biol. Chem. 273:23321-23326(1998). CC -!- FUNCTION: Receptor for the hormone galanin and spexin-1. CC {ECO:0000250|UniProtKB:O60755, ECO:0000269|PubMed:9722565}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. 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; AF079844; AAC34590.1; -; mRNA. DR EMBL; AF031522; AAC26145.1; -; mRNA. DR EMBL; AF073798; AAC35943.1; -; mRNA. DR RefSeq; NP_062046.1; NM_019173.1. DR RefSeq; XP_006242034.1; XM_006241972.2. DR RefSeq; XP_017450186.1; XM_017594697.1. DR AlphaFoldDB; O88626; -. DR SMR; O88626; -. DR STRING; 10116.ENSRNOP00000014349; -. DR BindingDB; O88626; -. DR GuidetoPHARMACOLOGY; 245; -. DR GlyCosmos; O88626; 1 site, No reported glycans. DR GlyGen; O88626; 1 site. DR PhosphoSitePlus; O88626; -. DR PaxDb; 10116-ENSRNOP00000014349; -. DR Ensembl; ENSRNOT00055051521; ENSRNOP00055042465; ENSRNOG00055029749. DR Ensembl; ENSRNOT00060042638; ENSRNOP00060035320; ENSRNOG00060024647. DR GeneID; 29235; -. DR KEGG; rno:29235; -. DR UCSC; RGD:2658; rat. DR AGR; RGD:2658; -. DR CTD; 8484; -. DR RGD; 2658; Galr3. DR eggNOG; KOG3656; Eukaryota. DR InParanoid; O88626; -. DR OrthoDB; 2915794at2759; -. DR PhylomeDB; O88626; -. DR Reactome; R-RNO-375276; Peptide ligand-binding receptors. DR Reactome; R-RNO-418594; G alpha (i) signalling events. DR PRO; PR:O88626; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005929; C:cilium; ISO:RGD. DR GO; GO:0097730; C:non-motile cilium; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004966; F:galanin receptor activity; IDA:MGI. DR GO; GO:0017046; F:peptide hormone binding; ISS:UniProtKB. DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central. DR GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; ISO:RGD. DR GO; GO:0090663; P:galanin-activated signaling pathway; ISO:RGD. DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:RGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000405; Galanin_rcpt. DR InterPro; IPR003908; Galnin_3_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR24230; G-PROTEIN COUPLED RECEPTOR; 1. DR PANTHER; PTHR24230:SF17; GALANIN RECEPTOR TYPE 3; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR01420; GALANIN3R. DR PRINTS; PR00663; GALANINR. DR PRINTS; PR00237; GPCRRHODOPSN. 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 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..370 FT /note="Galanin receptor type 3" FT /id="PRO_0000069471" FT TOPO_DOM 1..20 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 21..41 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 42..57 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 58..78 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 79..96 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 97..118 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 119..138 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 139..159 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 160..184 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 185..205 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 206..236 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 237..257 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 258..259 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 260..280 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 281..370 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 317..370 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT LIPID 308 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CARBOHYD 6 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 95..172 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT CONFLICT 54 FT /note="R -> S (in Ref. 3; AAC35943)" FT /evidence="ECO:0000305" FT CONFLICT 127 FT /note="P -> Q (in Ref. 2; AAC26145)" FT /evidence="ECO:0000305" FT CONFLICT 183 FT /note="A -> R (in Ref. 2; AAC26145)" FT /evidence="ECO:0000305" FT CONFLICT 311 FT /note="R -> C (in Ref. 2; AAC26145)" FT /evidence="ECO:0000305" SQ SEQUENCE 370 AA; 40410 MW; CE5B39E6147AFAD4 CRC64; MADIQNISLD SPGSVGAVAV PVIFALIFLL GMVGNGLVLA VLLQPGPSAW QEPRSTTDLF ILNLAVADLC FILCCVPFQA AIYTLDAWLF GAFVCKTVHL LIYLTMYASS FTLAAVSLDR YLAVRHPLRS RALRTPRNAR AAVGLVWLLA ALFSAPYLSY YGTVRYGALE LCVPAWEDAR RRALDVATFA AGYLLPVAVV SLAYGRTLCF LWAAVGPAGA AAAEARRRAT GRAGRAMLAV AALYALCWGP HHALILCFWY GRFAFSPATY ACRLASHCLA YANSCLNPLV YSLASRHFRA RFRRLWPCGR RRHRHHHRAH RALRRVQPAS SGPAGYPGDA RPRGWSMEPR GDALRGGGET RLTLSPRGPQ //