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   02-JUN-2021, entry version 170.
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   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   PaxDb; O43603; -.
DR   PeptideAtlas; O43603; -.
DR   PRIDE; O43603; -.
DR   ProteomicsDB; 49077; -.
DR   Antibodypedia; 19663; 290 antibodies.
DR   DNASU; 8811; -.
DR   Ensembl; ENST00000329003; ENSP00000329684; ENSG00000182687.
DR   GeneID; 8811; -.
DR   KEGG; hsa:8811; -.
DR   UCSC; uc002jqm.3; human.
DR   CTD; 8811; -.
DR   DisGeNET; 8811; -.
DR   GeneCards; GALR2; -.
DR   HGNC; HGNC:4133; GALR2.
DR   HPA; ENSG00000182687; Group enriched (bone marrow, intestine, lymphoid tissue, smooth muscle).
DR   MIM; 603691; gene.
DR   neXtProt; NX_O43603; -.
DR   OpenTargets; ENSG00000182687; -.
DR   PharmGKB; PA28546; -.
DR   VEuPathDB; HostDB:ENSG00000182687.3; -.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01030000234678; -.
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   SIGNOR; O43603; -.
DR   BioGRID-ORCS; 8811; 10 hits in 984 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 60 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:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
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:0007275; P:multicellular organism development; 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
//