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   27-MAR-2024, entry version 191.
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).
RN   [10]
RP   SUBCELLULAR LOCATION, AND INTERACTION WITH GRP39 AND HTR1A.
RX   PubMed=26365466; DOI=10.1016/j.bbadis.2015.09.003;
RA   Tena-Campos M., Ramon E., Borroto-Escuela D.O., Fuxe K., Garriga P.;
RT   "The zinc binding receptor GPR39 interacts with 5-HT1A and GalR1 to form
RT   dynamic heteroreceptor complexes with signaling diversity.";
RL   Biochim. Biophys. Acta 1852:2585-2592(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   -!- SUBUNIT: Interacts with GRP39 AND HTR1A. {ECO:0000269|PubMed:26365466}.
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 {ECO:0000269|PubMed:26365466};
CC       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   PDB; 7WQ3; EM; 2.70 A; R=1-349.
DR   PDB; 7XJJ; EM; 3.30 A; E=1-322.
DR   PDBsum; 7WQ3; -.
DR   PDBsum; 7XJJ; -.
DR   AlphaFoldDB; P47211; -.
DR   EMDB; EMD-32698; -.
DR   EMDB; EMD-33229; -.
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   GlyCosmos; P47211; 3 sites, No reported glycans.
DR   GlyGen; P47211; 3 sites.
DR   iPTMnet; P47211; -.
DR   PhosphoSitePlus; P47211; -.
DR   BioMuta; GALR1; -.
DR   DMDM; 311033447; -.
DR   PaxDb; 9606-ENSP00000299727; -.
DR   PeptideAtlas; P47211; -.
DR   Antibodypedia; 10410; 399 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   AGR; HGNC:4132; -.
DR   CTD; 2587; -.
DR   DisGeNET; 2587; -.
DR   GeneCards; GALR1; -.
DR   HGNC; HGNC:4132; GALR1.
DR   HPA; ENSG00000166573; Tissue enhanced (adrenal gland, 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; VFKCHIR; -.
DR   OrthoDB; 2915794at2759; -.
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; 9 hits in 1147 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 cell types or tissues.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
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   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; P47211; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW   Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor;
KW   Reference proteome; Transducer; 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"
FT   HELIX           33..60
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   HELIX           69..97
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   STRAND          98..100
FT                   /evidence="ECO:0007829|PDB:7XJJ"
FT   HELIX           104..138
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   TURN            139..142
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   HELIX           143..146
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   HELIX           149..166
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   HELIX           168..173
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   STRAND          175..177
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   HELIX           194..208
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   HELIX           210..230
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   HELIX           236..259
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   HELIX           261..271
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   HELIX           279..302
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   STRAND          303..307
FT                   /evidence="ECO:0007829|PDB:7WQ3"
FT   HELIX           308..317
FT                   /evidence="ECO:0007829|PDB:7WQ3"
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
//