GALR1_HUMAN
ID GALR1_HUMAN Reviewed; 349 AA.
AC P47211; Q4VBL7;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Galanin receptor type 1;
DE Short=GAL1-R;
DE Short=GALR-1;
GN Name=GALR1; Synonyms=GALNR, GALNR1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANTS CYS-15 AND ASN-334.
RC TISSUE=Melanoma;
RX PubMed=7524088; DOI=10.1073/pnas.91.21.9780;
RA Habert-Ortoli E., Amiranoff B., Loquet I., Laburthe M., Mayaux J.-F.;
RT "Molecular cloning of a functional human galanin receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:9780-9783(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS CYS-15 AND ASN-334.
RC TISSUE=Small intestine;
RX PubMed=9425310; DOI=10.1006/bbrc.1997.7838;
RA Lorimer D.D., Matkowskj K., Benya R.V.;
RT "Cloning, chromosomal location, and transcriptional regulation of the human
RT galanin-1 receptor gene (GALN1R).";
RL Biochem. Biophys. Res. Commun. 241:558-564(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASN-334.
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-334.
RC TISSUE=Brain;
RA Ross P.C.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-334.
RC TISSUE=Brain;
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "cDNA clones of human proteins involved in signal transduction sequenced by
RT the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-334.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-334.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP FUNCTION.
RX PubMed=25691535; DOI=10.1093/hmg/ddv060;
RA Guipponi M., Chentouf A., Webling K.E., Freimann K., Crespel A., Nobile C.,
RA Lemke J.R., Hansen J., Dorn T., Lesca G., Ryvlin P., Hirsch E., Rudolf G.,
RA Rosenberg D.S., Weber Y., Becker F., Helbig I., Muhle H., Salzmann A.,
RA Chaouch M., Oubaiche M.L., Ziglio S., Gehrig C., Santoni F., Pizzato M.,
RA Langel U., Antonarakis S.E.;
RT "Galanin pathogenic mutations in temporal lobe epilepsy.";
RL Hum. Mol. Genet. 24:3082-3091(2015).
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:0000269|PubMed:25691535, ECO:0000269|PubMed:7524088}.
CC -!- INTERACTION:
CC P47211; PRO_0000010449 [P22466]: GAL; NbExp=2; IntAct=EBI-6624741, EBI-6624800;
CC P47211; O75971-2: SNAPC5; NbExp=3; IntAct=EBI-6624741, EBI-12004298;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: Palmitoylated on at least one of the three cysteine residues
CC present in the C-terminal part.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; L34339; AAA50767.1; -; mRNA.
DR EMBL; U53511; AAC51936.1; -; mRNA.
DR EMBL; U90660; AAC95397.1; -; Genomic_DNA.
DR EMBL; U90658; AAC95397.1; JOINED; Genomic_DNA.
DR EMBL; U90659; AAC95397.1; JOINED; Genomic_DNA.
DR EMBL; U23854; AAB60356.1; -; mRNA.
DR EMBL; AY541036; AAS47032.1; -; mRNA.
DR EMBL; AC100863; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471117; EAW66603.1; -; Genomic_DNA.
DR EMBL; BC095530; AAH95530.1; -; mRNA.
DR CCDS; CCDS12012.1; -.
DR PIR; I59336; I59336.
DR RefSeq; NP_001471.2; NM_001480.3.
DR AlphaFoldDB; P47211; -.
DR SMR; P47211; -.
DR BioGRID; 108859; 2.
DR IntAct; P47211; 6.
DR STRING; 9606.ENSP00000299727; -.
DR BindingDB; P47211; -.
DR ChEMBL; CHEMBL4894; -.
DR GuidetoPHARMACOLOGY; 243; -.
DR GlyGen; P47211; 3 sites.
DR iPTMnet; P47211; -.
DR PhosphoSitePlus; P47211; -.
DR BioMuta; GALR1; -.
DR DMDM; 311033447; -.
DR PaxDb; P47211; -.
DR PeptideAtlas; P47211; -.
DR PRIDE; P47211; -.
DR Antibodypedia; 10410; 368 antibodies from 35 providers.
DR DNASU; 2587; -.
DR Ensembl; ENST00000299727.5; ENSP00000299727.3; ENSG00000166573.6.
DR GeneID; 2587; -.
DR KEGG; hsa:2587; -.
DR MANE-Select; ENST00000299727.5; ENSP00000299727.3; NM_001480.4; NP_001471.2.
DR UCSC; uc002lms.5; human.
DR CTD; 2587; -.
DR DisGeNET; 2587; -.
DR GeneCards; GALR1; -.
DR HGNC; HGNC:4132; GALR1.
DR HPA; ENSG00000166573; Tissue enhanced (adrenal gland, brain, pituitary gland).
DR MIM; 600377; gene.
DR neXtProt; NX_P47211; -.
DR OpenTargets; ENSG00000166573; -.
DR PharmGKB; PA28545; -.
DR VEuPathDB; HostDB:ENSG00000166573; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244841; -.
DR HOGENOM; CLU_009579_6_4_1; -.
DR InParanoid; P47211; -.
DR OMA; LPHHIIH; -.
DR OrthoDB; 1294084at2759; -.
DR PhylomeDB; P47211; -.
DR TreeFam; TF315737; -.
DR PathwayCommons; P47211; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P47211; -.
DR SIGNOR; P47211; -.
DR BioGRID-ORCS; 2587; 8 hits in 1061 CRISPR screens.
DR ChiTaRS; GALR1; human.
DR GeneWiki; Galanin_receptor_1; -.
DR GenomeRNAi; 2587; -.
DR Pharos; P47211; Tchem.
DR PRO; PR:P47211; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P47211; protein.
DR Bgee; ENSG00000166573; Expressed in pituitary gland and 82 other tissues.
DR Genevisible; P47211; HS.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004966; F:galanin receptor activity; IDA:UniProtKB.
DR GO; GO:0042923; F:neuropeptide binding; IEA:Ensembl.
DR GO; GO:0017046; F:peptide hormone binding; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0051464; P:positive regulation of cortisol secretion; IMP:UniProtKB.
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; IDA: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 1: Evidence at protein 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..349
FT /note="Galanin receptor type 1"
FT /id="PRO_0000069463"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..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..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..271
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT LIPID 320
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 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 108..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VARIANT 15
FT /note="W -> C (in dbSNP:rs1143093)"
FT /evidence="ECO:0000269|PubMed:7524088,
FT ECO:0000269|PubMed:9425310"
FT /id="VAR_003514"
FT VARIANT 334
FT /note="S -> N (in dbSNP:rs5376)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:7524088, ECO:0000269|PubMed:9367674,
FT ECO:0000269|PubMed:9425310, ECO:0000269|Ref.4,
FT ECO:0000269|Ref.5, ECO:0000269|Ref.7"
FT /id="VAR_014682"
FT VARIANT 342
FT /note="P -> L (in dbSNP:rs5377)"
FT /id="VAR_014683"
SQ SEQUENCE 349 AA; 38953 MW; A0664227157B3410 CRC64;
MELAVGNLSE GNASWPEPPA PEPGPLFGIG VENFVTLVVF GLIFALGVLG NSLVITVLAR
SKPGKPRSTT NLFILNLSIA DLAYLLFCIP FQATVYALPT WVLGAFICKF IHYFFTVSML
VSIFTLAAMS VDRYVAIVHS RRSSSLRVSR NALLGVGCIW ALSIAMASPV AYHQGLFHPR
ASNQTFCWEQ WPDPRHKKAY VVCTFVFGYL LPLLLICFCY AKVLNHLHKK LKNMSKKSEA
SKKKTAQTVL VVVVVFGISW LPHHIIHLWA EFGVFPLTPA SFLFRITAHC LAYSNSSVNP
IIYAFLSENF RKAYKQVFKC HIRKDSHLSD TKESKSRIDT PPSTNCTHV
