GPR3_RAT
ID GPR3_RAT Reviewed; 329 AA.
AC Q8K1Q3; Q63230;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=G-protein coupled receptor 3;
DE AltName: Full=G-protein-coupled receptor R4;
GN Name=Gpr3;
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 [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-117.
RC STRAIN=New England Deaconess Hospital; TISSUE=Pancreas;
RX PubMed=7698767; DOI=10.1006/geno.1994.1635;
RA Iismaa T.P., Kiefer J., Liu M.L., Baker E., Sutherland G.R., Shine J.;
RT "Isolation and chromosomal localization of a novel human G-protein-coupled
RT receptor (GPR3) expressed predominantly in the central nervous system.";
RL Genomics 24:391-394(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-329.
RX PubMed=12220620; DOI=10.1016/s0898-6568(02)00041-4;
RA Uhlenbrock K., Gassenhuber J., Kostenis E.;
RT "Sphingosine 1-phosphate is a ligand of the human gpr3, gpr6 and gpr12
RT family of constitutively active G protein-coupled receptors.";
RL Cell. Signal. 14:941-953(2002).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17284443; DOI=10.1074/jbc.m700911200;
RA Tanaka S., Ishii K., Kasai K., Yoon S.O., Saeki Y.;
RT "Neural expression of G protein-coupled receptors GPR3, GPR6, and GPR12 up-
RT regulates cyclic AMP levels and promotes neurite outgrowth.";
RL J. Biol. Chem. 282:10506-10515(2007).
CC -!- FUNCTION: Orphan receptor with constitutive G(s) signaling activity
CC that activate cyclic AMP. Has a potential role in modulating a number
CC of brain functions, including behavioral responses to stress (By
CC similarity), amyloid-beta peptide generation in neurons (By similarity)
CC and neurite outgrowth. Maintains also meiotic arrest in oocytes (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:17284443}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in granule neurons at all
CC development stages. {ECO:0000269|PubMed:17284443}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD20634.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; CH473968; EDL80660.1; -; Genomic_DNA.
DR EMBL; L32829; AAA73559.1; -; mRNA.
DR EMBL; AJ427482; CAD20634.1; ALT_FRAME; mRNA.
DR RefSeq; NP_714949.1; NM_153727.1.
DR RefSeq; XP_006239068.1; XM_006239006.3.
DR AlphaFoldDB; Q8K1Q3; -.
DR SMR; Q8K1Q3; -.
DR STRING; 10116.ENSRNOP00000068107; -.
DR GlyGen; Q8K1Q3; 1 site.
DR PhosphoSitePlus; Q8K1Q3; -.
DR Ensembl; ENSRNOT00000076866; ENSRNOP00000068417; ENSRNOG00000009540.
DR GeneID; 266769; -.
DR KEGG; rno:266769; -.
DR UCSC; RGD:628686; rat.
DR CTD; 2827; -.
DR RGD; 628686; Gpr3.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01000000214392; -.
DR InParanoid; Q8K1Q3; -.
DR OrthoDB; 903801at2759; -.
DR PhylomeDB; Q8K1Q3; -.
DR TreeFam; TF330052; -.
DR PRO; PR:Q8K1Q3; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Proteomes; UP000234681; Chromosome 5.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IDA:RGD.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; ISO:RGD.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR000984; GPR3.
DR InterPro; IPR000723; GPR_3/6/12_orphan.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00648; GPR3ORPHANR.
DR PRINTS; PR00644; GPRORPHANR.
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; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Receptor; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..329
FT /note="G-protein coupled receptor 3"
FT /id="PRO_0000379597"
FT TOPO_DOM 1..43
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..108
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT LIPID 312
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 61
FT /note="V -> M (in Ref. 2; AAA73559)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="T -> M (in Ref. 2; AAA73559)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 329 AA; 35327 MW; 96E347B2059BD85A CRC64;
MMWGAGRSMA WFSAGSGSVN VSIDPAEEPT GPATLLPSPR AWDVVLCISG TLVSCENALV
VAIIVGTPAF RAPMFLLVGS LAVADLLAGL GLVLHFAADF CIGSPEMSLV LVGVLATAFT
ASIGSLLAIT VDRYLSLYNA LTYYSETTVT RTYVMLALVW VGALGLGLVP VLAWNCRDGL
TTCGVVYPLS KNHLVVLAIV FFMVFGIMLQ LYAQICRIVC RHAQQIALQR HLLPASHYVA
TRKGIATLAV VLGAFAACWL PFTVYCLLGD ANSPPLYTYL TLLPATYNSM INPVIYAFRN
QDVQKVLWAI CCCCSTSKIP FRSRSPSDV
