GALR1_MOUSE
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 03-AUG-2022, entry version 156.
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 -!- SUBCELLULAR LOCATION: Cell membrane; 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}.
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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 GlyGen; P56479; 3 sites.
DR PhosphoSitePlus; P56479; -.
DR PaxDb; P56479; -.
DR PRIDE; P56479; -.
DR ProteomicsDB; 268838; -.
DR Antibodypedia; 10410; 368 antibodies from 35 providers.
DR DNASU; 14427; -.
DR Ensembl; ENSMUST00000065224; ENSMUSP00000066381; ENSMUSG00000024553.
DR GeneID; 14427; -.
DR KEGG; mmu:14427; -.
DR UCSC; uc008ftq.1; mouse.
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; LPHHIIH; -.
DR OrthoDB; 1294084at2759; -.
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 71 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 22 other tissues.
DR Genevisible; P56479; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0007194; P:negative regulation of adenylate cyclase activity; IEA:InterPro.
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 InterPro; IPR003906; GAL1_rcpt.
DR InterPro; IPR000405; Galanin_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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 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..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
