ID   GALR2_RAT               Reviewed;         372 AA.
AC   O08726;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 156.
DE   RecName: Full=Galanin receptor type 2;
DE            Short=GAL2-R;
DE            Short=GALR-2;
GN   Name=Galr2; Synonyms=Galnr2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hypothalamus;
RX   PubMed=9108306; DOI=10.1016/s0014-5793(97)00196-8;
RA   Howard A.D., Tan C., Shiao L.L., Palyha O.C., McKee K.K., Weinberg D.H.,
RA   Feighner S.D., Cascieri M.A., Smith R.G., van der Ploeg L.H.T.,
RA   Sullivan K.A.;
RT   "Molecular cloning and characterization of a new receptor for galanin.";
RL   FEBS Lett. 405:285-290(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9305929; DOI=10.1074/jbc.272.39.24612;
RA   Smith K.E., Forray C., Walker M.W., Jones K.A., Tamm J.A., Bard J.,
RA   Branchek T.A., Linemeyer D.L., Gerald C.;
RT   "Expression cloning of a rat hypothalamic galanin receptor coupled to
RT   phosphoinositide turnover.";
RL   J. Biol. Chem. 272:24612-24616(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Hypothalamus;
RX   PubMed=9281594; DOI=10.1124/mol.52.3.337;
RA   Wang S., Hashemi T., He C., Strader C., Bayne M.;
RT   "Molecular cloning and pharmacological characterization of a new galanin
RT   receptor subtype.";
RL   Mol. Pharmacol. 52:337-343(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=9427506; DOI=10.1016/s0169-328x(97)00210-6;
RA   Fathi Z., Cunningham A.M., Iben L.G., Battaglino P.B., Ward S.A.,
RA   Nichol K.A., Pine K.A., Wang J., Goldstein M.E., Iismaa T.P., Zimanyi I.A.;
RT   "Cloning, pharmacological characterization and distribution of a novel
RT   galanin receptor.";
RL   Brain Res. Mol. Brain Res. 51:49-59(1997).
RN   [5]
RP   ERRATUM OF PUBMED:9427506.
RX   PubMed=9473722; DOI=10.1016/s0169-328x(97)00359-8;
RA   Fathi Z., Cunningham A.M., Iben L.G., Battaglino P.B., Ward S.A.,
RA   Nichol K.A., Pine K.A., Wang J., Goldstein M.E., Iismaa T.P., Zimanyi I.A.;
RL   Brain Res. Mol. Brain Res. 53:348-348(1998).
CC   -!- FUNCTION: Receptor for the hormone galanin, GALP and spexin-1. The
CC       activity of this receptor is mediated by G proteins that activate the
CC       phospholipase C/protein kinase C pathway (via G(q)) and that inhibit
CC       adenylyl cyclase (via G(i)).
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U94322; AAB53220.1; -; mRNA.
DR   EMBL; AF010318; AAC53358.1; -; mRNA.
DR   EMBL; Y15248; CAA75532.1; -; mRNA.
DR   EMBL; AF008548; AAB62573.1; -; mRNA.
DR   RefSeq; NP_062045.1; NM_019172.5.
DR   RefSeq; XP_008766654.1; XM_008768432.2.
DR   RefSeq; XP_017459673.1; XM_017604184.1.
DR   AlphaFoldDB; O08726; -.
DR   SMR; O08726; -.
DR   BioGRID; 247911; 1.
DR   IntAct; O08726; 1.
DR   STRING; 10116.ENSRNOP00000012523; -.
DR   BindingDB; O08726; -.
DR   ChEMBL; CHEMBL5577; -.
DR   GuidetoPHARMACOLOGY; 244; -.
DR   GlyGen; O08726; 2 sites.
DR   PhosphoSitePlus; O08726; -.
DR   PaxDb; O08726; -.
DR   Ensembl; ENSRNOT00000086288; ENSRNOP00000073780; ENSRNOG00000061733.
DR   GeneID; 29234; -.
DR   KEGG; rno:29234; -.
DR   CTD; 8811; -.
DR   RGD; 2657; Galr2.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01050000244983; -.
DR   InParanoid; O08726; -.
DR   OMA; DICTFVF; -.
DR   OrthoDB; 1294084at2759; -.
DR   PhylomeDB; O08726; -.
DR   TreeFam; TF315737; -.
DR   Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   PRO; PR:O08726; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000061733; Expressed in esophagus and 19 other tissues.
DR   Genevisible; O08726; RN.
DR   GO; GO:0005929; C:cilium; ISO:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004966; F:galanin receptor activity; IDA:RGD.
DR   GO; GO:0042923; F:neuropeptide binding; IDA:RGD.
DR   GO; GO:0017046; F:peptide hormone binding; ISS:UniProtKB.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:RGD.
DR   GO; GO:0090663; P:galanin-activated signaling pathway; ISO:RGD.
DR   GO; GO:0043647; P:inositol phosphate metabolic process; IDA:RGD.
DR   GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IEA:InterPro.
DR   GO; GO:0031175; P:neuron projection development; ISO:RGD.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR   GO; GO:0046488; P:phosphatidylinositol metabolic process; IDA:RGD.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:RGD.
DR   GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:RGD.
DR   GO; GO:1902608; P:positive regulation of large conductance calcium-activated potassium channel activity; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS: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   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..372
FT                   /note="Galanin receptor type 2"
FT                   /id="PRO_0000069468"
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..372
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          353..372
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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   372 AA;  40676 MW;  5E7B67B35A54AB6E CRC64;
     MNGSGSQGAE NTSQEGGSGG WQPEAVLVPL FFALIFLVGT VGNALVLAVL LRGGQAVSTT
     NLFILNLGVA DLCFILCCVP FQATIYTLDD WVFGSLLCKA VHFLIFLTMH ASSFTLAAVS
     LDRYLAIRYP LHSRELRTPR NALAAIGLIW GLALLFSGPY LSYYRQSQLA NLTVCHPAWS
     APRRRAMDLC TFVFSYLLPV LVLSLTYART LRYLWRTVDP VTAGSGSQRA KRKVTRMIII
     VAVLFCLCWM PHHALILCVW FGRFPLTRAT YALRILSHLV SYANSCVNPI VYALVSKHFR
     KGFRKICAGL LRPAPRRASG RVSILAPGNH SGSMLEQEST DLTQVSEAAG PLVPPPALPN
     CTASSRTLDP AC