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GALR3_RAT
ID   GALR3_RAT               Reviewed;         370 AA.
AC   O88626; O54914; Q9QWZ2;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Galanin receptor type 3;
DE            Short=GAL3-R;
DE            Short=GALR-3;
GN   Name=Galr3; Synonyms=Galnr3;
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   STRAIN=Sprague-Dawley; TISSUE=Hypothalamus;
RX   PubMed=10619483; DOI=10.1016/s0306-4522(99)00407-8;
RA   Waters S.M., Krause J.E.;
RT   "Distribution of galanin-1, -2 and -3 receptor messenger RNAs in central
RT   and peripheral rat tissues.";
RL   Neuroscience 95:265-271(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Wang S., He C., Hashemi T., Bayne M.;
RT   "Molecular cloning of the rat galanin receptor type 3.";
RL   Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=Sprague-Dawley;
RX   PubMed=9722565; DOI=10.1074/jbc.273.36.23321;
RA   Smith K.E., Walker M.W., Artymyshyn R., Bard J., Borowsky B., Tamm J.A.,
RA   Yao W.-J., Vaysse P.J.-J., Branchek T.A., Gerald C., Jones K.A.;
RT   "Cloned human and rat galanin GALR3 receptors: pharmacology and activation
RT   of G-protein inwardly rectifying K+ channels.";
RL   J. Biol. Chem. 273:23321-23326(1998).
CC   -!- FUNCTION: Receptor for the hormone galanin and spexin-1.
CC       {ECO:0000250|UniProtKB:O60755, ECO:0000269|PubMed:9722565}.
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}.
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DR   EMBL; AF079844; AAC34590.1; -; mRNA.
DR   EMBL; AF031522; AAC26145.1; -; mRNA.
DR   EMBL; AF073798; AAC35943.1; -; mRNA.
DR   RefSeq; NP_062046.1; NM_019173.1.
DR   RefSeq; XP_006242034.1; XM_006241972.2.
DR   RefSeq; XP_017450186.1; XM_017594697.1.
DR   AlphaFoldDB; O88626; -.
DR   SMR; O88626; -.
DR   STRING; 10116.ENSRNOP00000014349; -.
DR   BindingDB; O88626; -.
DR   GuidetoPHARMACOLOGY; 245; -.
DR   GlyGen; O88626; 1 site.
DR   PhosphoSitePlus; O88626; -.
DR   PaxDb; O88626; -.
DR   GeneID; 29235; -.
DR   KEGG; rno:29235; -.
DR   UCSC; RGD:2658; rat.
DR   CTD; 8484; -.
DR   RGD; 2658; Galr3.
DR   eggNOG; KOG3656; Eukaryota.
DR   InParanoid; O88626; -.
DR   OrthoDB; 1294084at2759; -.
DR   PhylomeDB; O88626; -.
DR   Reactome; R-RNO-375276; Peptide ligand-binding receptors.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   PRO; PR:O88626; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005929; C:cilium; ISO:RGD.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0097730; C:non-motile cilium; ISO:RGD.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR   GO; GO:0004966; F:galanin receptor activity; IDA:MGI.
DR   GO; GO:0017046; F:peptide hormone binding; ISS:UniProtKB.
DR   GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007187; P:G protein-coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger; ISO:RGD.
DR   GO; GO:0090663; P:galanin-activated signaling pathway; ISO:RGD.
DR   GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IEA:InterPro.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IDA:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   InterPro; IPR000405; Galanin_rcpt.
DR   InterPro; IPR003908; Galnin_3_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01420; GALANIN3R.
DR   PRINTS; PR00663; GALANINR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
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   Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..370
FT                   /note="Galanin receptor type 3"
FT                   /id="PRO_0000069471"
FT   TOPO_DOM        1..20
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        21..41
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        42..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..96
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..118
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        119..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..184
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..236
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        258..259
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..370
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          317..370
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           308
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        6
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        95..172
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   CONFLICT        54
FT                   /note="R -> S (in Ref. 3; AAC35943)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        127
FT                   /note="P -> Q (in Ref. 2; AAC26145)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="A -> R (in Ref. 2; AAC26145)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        311
FT                   /note="R -> C (in Ref. 2; AAC26145)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   370 AA;  40410 MW;  CE5B39E6147AFAD4 CRC64;
     MADIQNISLD SPGSVGAVAV PVIFALIFLL GMVGNGLVLA VLLQPGPSAW QEPRSTTDLF
     ILNLAVADLC FILCCVPFQA AIYTLDAWLF GAFVCKTVHL LIYLTMYASS FTLAAVSLDR
     YLAVRHPLRS RALRTPRNAR AAVGLVWLLA ALFSAPYLSY YGTVRYGALE LCVPAWEDAR
     RRALDVATFA AGYLLPVAVV SLAYGRTLCF LWAAVGPAGA AAAEARRRAT GRAGRAMLAV
     AALYALCWGP HHALILCFWY GRFAFSPATY ACRLASHCLA YANSCLNPLV YSLASRHFRA
     RFRRLWPCGR RRHRHHHRAH RALRRVQPAS SGPAGYPGDA RPRGWSMEPR GDALRGGGET
     RLTLSPRGPQ
 
 
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