GALR2_HUMAN
ID GALR2_HUMAN Reviewed; 387 AA.
AC O43603; A5JUU4; Q32MN8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Galanin receptor type 2;
DE Short=GAL2-R;
DE Short=GALR-2;
GN Name=GALR2; Synonyms=GALNR2;
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], AND FUNCTION.
RX PubMed=9480833; DOI=10.1006/bbrc.1998.8133;
RA Bloomquist B.T., Beauchamp M.R., Zhelnin L., Brown S.-E., Gore-Willse A.R.,
RA Gregor P., Cornfield L.J.;
RT "Cloning and expression of the human galanin receptor GalR2.";
RL Biochem. Biophys. Res. Commun. 243:474-479(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=9880084; DOI=10.1016/s0196-9781(98)00133-8;
RA Borowsky B., Walker M.W., Huang L.-Y., Jones K.A., Smith K.E., Bard J.,
RA Branchek T.A., Gerald C.;
RT "Cloning and characterization of the human galanin GALR2 receptor.";
RL Peptides 19:1771-1781(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9685625; DOI=10.1016/s0169-328x(98)00116-8;
RA Fathi Z., Battaglino P.M., Iben L.G., Li H., Baker E., Zhang D.,
RA McGovern R., Mahle C.D., Sutherland G.R., Iismaa T.P., Dickinson K.E.J.,
RA Zimanyi I.A.;
RT "Molecular characterization, pharmacological properties and chromosomal
RT localization of the human GALR2 galanin receptor.";
RL Brain Res. Mol. Brain Res. 58:156-169(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=9832121; DOI=10.1046/j.1471-4159.1998.71062239.x;
RA Kolakowski L.F. Jr., O'Neill G.P., Howard A.D., Broussard S.R.,
RA Sullivan K.A., Feighner S.D., Sawzdargo M., Nguyen T., Kargman S.,
RA Shiao L.-L., Hreniuk D.L., Tan C.P., Evans J., Abramovitz M.,
RA Chateauneuf A., Coulombe N., Ng G., Johnson M.P., Tharian A.,
RA Khoshbouei H., George S.R., Smith R.G., O'Dowd B.F.;
RT "Molecular characterization and expression of cloned human galanin
RT receptors GALR2 and GALR3.";
RL J. Neurochem. 71:2239-2251(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hippocampus;
RA Martin A.L., Kaighin V.A., Aronstam R.S.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [8]
RP FUNCTION AS A RECEPTOR FOR SPEXIN-1, AND PHYLOGENY.
RX PubMed=24517231; DOI=10.1210/en.2013-2106;
RA Kim D.K., Yun S., Son G.H., Hwang J.I., Park C.R., Kim J.I., Kim K.,
RA Vaudry H., Seong J.Y.;
RT "Coevolution of the spexin/galanin/kisspeptin family: Spexin activates
RT galanin receptor type II and III.";
RL Endocrinology 155:1864-1873(2014).
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 and GALP. Receptor for the
CC hormone spexin-1 (PubMed:24517231). The activity of this receptor is
CC mediated by G proteins that activate the phospholipase C/protein kinase
CC C pathway (via G(q)) and that inhibit adenylyl cyclase (via G(i)).
CC {ECO:0000269|PubMed:24517231, ECO:0000269|PubMed:25691535,
CC ECO:0000269|PubMed:9480833, ECO:0000269|PubMed:9685625,
CC ECO:0000269|PubMed:9832121, ECO:0000269|PubMed:9880084}.
CC -!- INTERACTION:
CC O43603; PRO_0000010449 [P22466]: GAL; NbExp=2; IntAct=EBI-6624855, EBI-6624800;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed abundantly within the central nervous
CC system in both hypothalamus and hippocampus. In peripheral tissues, the
CC strongest expression was observed in heart, kidney, liver, and small
CC intestine.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF040630; AAC39634.1; -; mRNA.
DR EMBL; AF080586; AAD08671.1; -; mRNA.
DR EMBL; AF058762; AAC18118.1; -; Genomic_DNA.
DR EMBL; AF042782; AAC36587.1; -; Genomic_DNA.
DR EMBL; EF577401; ABQ52421.1; -; mRNA.
DR EMBL; CH471099; EAW89364.1; -; Genomic_DNA.
DR EMBL; BC069130; AAH69130.1; -; mRNA.
DR EMBL; BC074914; AAH74914.1; -; mRNA.
DR EMBL; BC074915; AAH74915.1; -; mRNA.
DR EMBL; BC109051; AAI09052.1; -; mRNA.
DR EMBL; BC109052; AAI09053.1; -; mRNA.
DR CCDS; CCDS11739.1; -.
DR PIR; JC5949; JC5949.
DR RefSeq; NP_003848.1; NM_003857.3.
DR AlphaFoldDB; O43603; -.
DR SMR; O43603; -.
DR IntAct; O43603; 2.
DR STRING; 9606.ENSP00000329684; -.
DR BindingDB; O43603; -.
DR ChEMBL; CHEMBL3176; -.
DR GuidetoPHARMACOLOGY; 244; -.
DR GlyGen; O43603; 2 sites.
DR iPTMnet; O43603; -.
DR PhosphoSitePlus; O43603; -.
DR BioMuta; GALR2; -.
DR MassIVE; O43603; -.
DR PaxDb; O43603; -.
DR PeptideAtlas; O43603; -.
DR PRIDE; O43603; -.
DR Antibodypedia; 19663; 297 antibodies from 37 providers.
DR DNASU; 8811; -.
DR Ensembl; ENST00000329003.4; ENSP00000329684.3; ENSG00000182687.4.
DR GeneID; 8811; -.
DR KEGG; hsa:8811; -.
DR MANE-Select; ENST00000329003.4; ENSP00000329684.3; NM_003857.4; NP_003848.1.
DR UCSC; uc002jqm.3; human.
DR CTD; 8811; -.
DR DisGeNET; 8811; -.
DR GeneCards; GALR2; -.
DR HGNC; HGNC:4133; GALR2.
DR HPA; ENSG00000182687; Group enriched (intestine, smooth muscle).
DR MIM; 603691; gene.
DR neXtProt; NX_O43603; -.
DR OpenTargets; ENSG00000182687; -.
DR PharmGKB; PA28546; -.
DR VEuPathDB; HostDB:ENSG00000182687; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244983; -.
DR HOGENOM; CLU_009579_6_4_1; -.
DR InParanoid; O43603; -.
DR OMA; DICTFVF; -.
DR OrthoDB; 1294084at2759; -.
DR PhylomeDB; O43603; -.
DR TreeFam; TF315737; -.
DR PathwayCommons; O43603; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; O43603; -.
DR SIGNOR; O43603; -.
DR BioGRID-ORCS; 8811; 18 hits in 1066 CRISPR screens.
DR GeneWiki; Galanin_receptor_2; -.
DR GenomeRNAi; 8811; -.
DR Pharos; O43603; Tchem.
DR PRO; PR:O43603; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; O43603; protein.
DR Bgee; ENSG00000182687; Expressed in muscle layer of sigmoid colon and 62 other tissues.
DR Genevisible; O43603; HS.
DR GO; GO:0005929; C:cilium; IDA:MGI.
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; TAS:Reactome.
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:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0007631; P:feeding behavior; TAS:ProtInc.
DR GO; GO:0090663; P:galanin-activated signaling pathway; IDA:GO_Central.
DR GO; GO:0043647; P:inositol phosphate metabolic process; IEA:Ensembl.
DR GO; GO:0007611; P:learning or memory; TAS:ProtInc.
DR GO; GO:0006936; P:muscle contraction; TAS:ProtInc.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IEA:InterPro.
DR GO; GO:0031175; P:neuron projection development; IEA:Ensembl.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:Ensembl.
DR GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IDA:GO_Central.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; TAS:ProtInc.
DR GO; GO:1902608; P:positive regulation of large conductance calcium-activated potassium channel activity; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR InterPro; IPR003907; GAL2_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; PR01419; GALANIN2R.
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 Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..387
FT /note="Galanin receptor type 2"
FT /id="PRO_0000069466"
FT TOPO_DOM 1..28
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..60
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..99
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..260
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 2
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 11
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 98..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 387 AA; 41700 MW; C2D2FCB93E53C47E CRC64;
MNVSGCPGAG NASQAGGGGG WHPEAVIVPL LFALIFLVGT VGNTLVLAVL LRGGQAVSTT
NLFILNLGVA DLCFILCCVP FQATIYTLDG WVFGSLLCKA VHFLIFLTMH ASSFTLAAVS
LDRYLAIRYP LHSRELRTPR NALAAIGLIW GLSLLFSGPY LSYYRQSQLA NLTVCHPAWS
APRRRAMDIC TFVFSYLLPV LVLGLTYART LRYLWRAVDP VAAGSGARRA KRKVTRMILI
VAALFCLCWM PHHALILCVW FGQFPLTRAT YALRILSHLV SYANSCVNPI VYALVSKHFR
KGFRTICAGL LGRAPGRASG RVCAAARGTH SGSVLERESS DLLHMSEAAG ALRPCPGASQ
PCILEPCPGP SWQGPKAGDS ILTVDVA
