ID GALR1_MOUSE Reviewed; 348 AA. AC P56479; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 27-MAR-2024, entry version 165. DE RecName: Full=Galanin receptor type 1; DE Short=GAL1-R; DE Short=GALR-1; GN Name=Galr1; Synonyms=Galnr, Galnr1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=9271210; DOI=10.1016/s0014-5793(97)00695-9; RA Wang S., He C., Maguire M.T., Clemmons A.L., Burrier R.E., Guzzi M.F., RA Strader C.D., Parker E.M., Bayne M.L.; RT "Genomic organization and functional characterization of the mouse GalR1 RT galanin receptor."; RL FEBS Lett. 411:225-230(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129; RX PubMed=9367674; DOI=10.1006/geno.1997.4960; RA Jacoby A.S., Webb G.C., Liu M.L., Kofler B., Hort Y.J., Fathi Z., RA Bottema C.D.K., Shine J., Iismaa T.P.; RT "Structural organization of the mouse and human GALR1 galanin receptor RT genes (Galnr and GALNR) and chromosomal localization of the mouse gene."; RL Genomics 45:496-508(1997). 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:9271210}. 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: Expression is detected in brain, spinal cord, heart CC and skeletal muscle. {ECO:0000269|PubMed:9271210}. CC -!- PTM: Three cysteine residues are found in the C-terminus, at least one CC of which may be palmitoylated. {ECO:0000250}. 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; Y15004; CAA75237.1; -; mRNA. DR EMBL; U90657; AAB87748.1; -; Genomic_DNA. DR EMBL; U90655; AAB87748.1; JOINED; Genomic_DNA. DR EMBL; U90656; AAB87748.1; JOINED; Genomic_DNA. DR CCDS; CCDS29372.1; -. DR RefSeq; NP_032108.1; NM_008082.2. DR AlphaFoldDB; P56479; -. DR SMR; P56479; -. DR STRING; 10090.ENSMUSP00000066381; -. DR GuidetoPHARMACOLOGY; 243; -. DR GlyCosmos; P56479; 3 sites, No reported glycans. DR GlyGen; P56479; 3 sites. DR PhosphoSitePlus; P56479; -. DR PaxDb; 10090-ENSMUSP00000066381; -. DR ProteomicsDB; 268838; -. DR Antibodypedia; 10410; 399 antibodies from 35 providers. DR DNASU; 14427; -. DR Ensembl; ENSMUST00000065224.8; ENSMUSP00000066381.7; ENSMUSG00000024553.9. DR GeneID; 14427; -. DR KEGG; mmu:14427; -. DR UCSC; uc008ftq.1; mouse. DR AGR; MGI:1096364; -. DR CTD; 2587; -. DR MGI; MGI:1096364; Galr1. DR VEuPathDB; HostDB:ENSMUSG00000024553; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01050000244841; -. DR HOGENOM; CLU_009579_6_4_1; -. DR InParanoid; P56479; -. DR OMA; VFKCHIR; -. DR OrthoDB; 2915794at2759; -. DR PhylomeDB; P56479; -. DR TreeFam; TF315737; -. DR Reactome; R-MMU-375276; Peptide ligand-binding receptors. DR Reactome; R-MMU-418594; G alpha (i) signalling events. DR BioGRID-ORCS; 14427; 4 hits in 76 CRISPR screens. DR ChiTaRS; Galr1; mouse. DR PRO; PR:P56479; -. DR Proteomes; UP000000589; Chromosome 18. DR RNAct; P56479; Protein. DR Bgee; ENSMUSG00000024553; Expressed in lumbar dorsal root ganglion and 23 other cell types or tissues. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central. DR GO; GO:0004966; F:galanin receptor activity; ISS:UniProtKB. DR GO; GO:0042923; F:neuropeptide binding; ISO:MGI. DR GO; GO:0017046; F:peptide hormone binding; ISS:UniProtKB. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISO:MGI. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI. DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central. DR GO; GO:0051464; P:positive regulation of cortisol secretion; ISO:MGI. 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; P56479; MM. 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..348 FT /note="Galanin receptor type 1" FT /id="PRO_0000069464" FT TOPO_DOM 1..34 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 35..55 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 56..70 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 71..91 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 92..109 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 110..131 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 132..151 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 152..172 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 173..197 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 198..218 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 219..247 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 248..268 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 269..270 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 271..291 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 292..348 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 328..348 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT LIPID 319 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 182 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 108..186 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" SQ SEQUENCE 348 AA; 39114 MW; 6F52D752BAA19F9A CRC64; MELAMVNLSE GNGSDPEPPA PESRPLFGIG VENFITLVVF GLIFAMGVLG NSLVITVLAR SKPGKPRSTT NLFILNLSIA DLAYLLFCIP FQATVYALPT WVLGAFICKF IHYFFTVSML VSIFTLAAMS VDRYVAIVHS RRSSSLRVSR NALLGVGFIW ALSIAMASPV AYHQRLFHRD SNQTFCWEQW PNKLHKKAYV VCTFVFGYLL PLLLICFCYA KVLNHLHKKL KNMSKKSEAS KKKTAQTVLV VVVVFGISWL PHHVVHLWAE FGAFPLTPAS FFFRITAHCL AYSNSSVNPI IYAFLSENFR KAYKQVFKCH VCDESPRSET KENKSRMDTP PSTNCTHV //