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   24-JAN-2024, entry version 119.
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).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=34871769; DOI=10.1016/j.mcn.2021.103691;
RA   Tanaka S., Shimada N., Shiraki H., Miyagi T., Harada K., Hide I., Sakai N.;
RT   "GPR3 accelerates neurite outgrowth and neuronal polarity formation via PI3
RT   kinase-mediating signaling pathway in cultured primary neurons.";
RL   Mol. Cell. Neurosci. 118:103691-103691(2022).
CC   -!- FUNCTION: Constitutively active G-protein coupled receptor that
CC       maintains high 3'-5'-cyclic adenosine monophosphate (cAMP) levels that
CC       a plays a role in serveral processes including meiotic arrest in
CC       oocytes or neuronal development via activation of numerous
CC       intracellular signaling pathways (PubMed:17284443). Acts as an
CC       essential activator of thermogenic adipocytes and drives thermogenesis
CC       via its intrinsic G(s)-coupling activity without the requirement of a
CC       ligand (By similarity). Has a potential role in modulating a number of
CC       brain functions, including behavioral responses to stress (By
CC       similarity), amyloid-beta peptide generation in neurons (By
CC       similarity). Stimulates neurite outgrowth in cerebellar granular
CC       neurons modulated via PKA, ERK, and most strongly PI3K-mediated
CC       signaling pathways (PubMed:34871769). {ECO:0000250|UniProtKB:P35413,
CC       ECO:0000269|PubMed:17284443, ECO:0000269|PubMed:34871769}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in granule neurons at all
CC       development stages. Enriched in the longest tips of neurites during
CC       differentiation of hippocampal neurons. {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   GlyCosmos; Q8K1Q3; 1 site, No reported glycans.
DR   GlyGen; Q8K1Q3; 1 site.
DR   PhosphoSitePlus; Q8K1Q3; -.
DR   PaxDb; 10116-ENSRNOP00000068107; -.
DR   Ensembl; ENSRNOT00000076866.2; ENSRNOP00000068417.2; ENSRNOG00000009540.6.
DR   Ensembl; ENSRNOT00055041858; ENSRNOP00055034096; ENSRNOG00055024360.
DR   Ensembl; ENSRNOT00060047693; ENSRNOP00060039670; ENSRNOG00060027503.
DR   Ensembl; ENSRNOT00065049906; ENSRNOP00065040988; ENSRNOG00065028905.
DR   GeneID; 266769; -.
DR   KEGG; rno:266769; -.
DR   UCSC; RGD:628686; rat.
DR   AGR; RGD:628686; -.
DR   CTD; 2827; -.
DR   RGD; 628686; Gpr3.
DR   eggNOG; KOG3656; Eukaryota.
DR   GeneTree; ENSGT01060000248564; -.
DR   InParanoid; Q8K1Q3; -.
DR   OMA; IQKVLWT; -.
DR   OrthoDB; 5397365at2759; -.
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: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   CDD; cd15963; 7tmA_GPR3; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR000984; GPR3.
DR   InterPro; IPR000723; GPR_3/6/12_orphan.
DR   PANTHER; PTHR22750; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR22750:SF39; G-PROTEIN COUPLED RECEPTOR 3; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR00648; GPR3ORPHANR.
DR   PRINTS; PR00644; GPRORPHANR.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 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; 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
//