GALR3_MOUSE
ID GALR3_MOUSE Reviewed; 370 AA.
AC O88853; A2RS28; E9QPX7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Galanin receptor type 3;
DE Short=GAL3-R;
DE Short=GALR-3;
GN Name=Galr3; Synonyms=Galnr3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
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.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Receptor for the hormone galanin and spexin-1.
CC {ECO:0000250|UniProtKB:O60755}.
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; AF042783; AAC36588.1; -; Genomic_DNA.
DR EMBL; AL589670; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC131950; AAI31951.1; -; mRNA.
DR EMBL; BC131952; AAI31953.1; -; mRNA.
DR CCDS; CCDS27631.1; -.
DR RefSeq; NP_056553.2; NM_015738.2.
DR AlphaFoldDB; O88853; -.
DR SMR; O88853; -.
DR GlyGen; O88853; 1 site.
DR iPTMnet; O88853; -.
DR PhosphoSitePlus; O88853; -.
DR PRIDE; O88853; -.
DR Antibodypedia; 12147; 245 antibodies from 32 providers.
DR DNASU; 14429; -.
DR Ensembl; ENSMUST00000058004; ENSMUSP00000060517; ENSMUSG00000114755.
DR GeneID; 14429; -.
DR KEGG; mmu:14429; -.
DR UCSC; uc007wsg.2; mouse.
DR CTD; 8484; -.
DR MGI; MGI:1329003; Galr3.
DR VEuPathDB; HostDB:ENSMUSG00000114755; -.
DR GeneTree; ENSGT01050000244841; -.
DR HOGENOM; CLU_009579_6_4_1; -.
DR OMA; GCPGDAR; -.
DR OrthoDB; 1294084at2759; -.
DR Reactome; R-MMU-375276; Peptide ligand-binding receptors.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 14429; 2 hits in 23 CRISPR screens.
DR ChiTaRS; Galr3; mouse.
DR PRO; PR:O88853; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; O88853; protein.
DR Bgee; ENSMUSG00000114755; Expressed in CA3 field of hippocampus and 11 other tissues.
DR Genevisible; O88853; MM.
DR GO; GO:0005929; C:cilium; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0097730; C:non-motile cilium; IDA:MGI.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; IBA:GO_Central.
DR GO; GO:0004966; F:galanin receptor activity; ISS:UniProtKB.
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:MGI.
DR GO; GO:0090663; P:galanin-activated signaling pathway; ISO:MGI.
DR GO; GO:0007194; P:negative regulation of adenylate cyclase activity; IEA:InterPro.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:MGI.
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_0000069470"
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 328..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 239
FT /note="T -> A (in Ref. 1; AAC36588 and 3; AAI31951/
FT AAI31953)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 370 AA; 40420 MW; D397A3F0C7CEFB18 CRC64;
MADIQNISLD SPGSVGAVAV PVVFALIFLL GMVGNGLVLA VLLQPGPSAW QEPGSTTDLF
ILNLAVADLC FILCCVPFQA AIYTLDAWLF GAFVCKTVHL LIYLTMYASS FTLAAVSVDR
YLAVRHPLRS RALRTPRNAR AAVGLVWLLA ALFSAPYLSY YGTVRYGALE LCVPAWEDAR
RRALDVATFA AGYLLPVTVV SLAYGRTLCF LWAAVGPAGA AAAEARRRAT GRAGRAMLTV
AALYALCWGP HHALILCFWY GRFAFSPATY ACRLASHCLA YANSCLNPLV YSLASRHFRA
RFRRLWPCGH RRHRHHHHRL HRALRRVQPA SSGPAGYPGD ARPRGWSMEP RGDALRGGET
RLTLSARGPQ
