GPR3_MOUSE
ID GPR3_MOUSE Reviewed; 330 AA.
AC P35413; Q3USD4;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=G-protein coupled receptor 3;
DE AltName: Full=GPCR21;
GN Name=Gpr3; Synonyms=Gpcr3;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8262253; DOI=10.1016/0014-5793(93)80828-i;
RA Saeki Y., Ueno S., Mizuno R., Nishimura T., Fujimura H., Nagai Y.,
RA Yanagihara T.;
RT "Molecular cloning of a novel putative G protein-coupled receptor (GPCR21)
RT which is expressed predominantly in mouse central nervous system.";
RL FEBS Lett. 336:317-322(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Corpora quadrigemina, Medulla oblongata, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
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).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=15956199; DOI=10.1073/pnas.0503840102;
RA Ledent C., Demeestere I., Blum D., Petermans J., Hamalainen T., Smits G.,
RA Vassart G.;
RT "Premature ovarian aging in mice deficient for Gpr3.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:8922-8926(2005).
RN [7]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19259266; DOI=10.1371/journal.pone.0004704;
RA Valverde O., Celerier E., Baranyi M., Vanderhaeghen P., Maldonado R.,
RA Sperlagh B., Vassart G., Ledent C.;
RT "GPR3 receptor, a novel actor in the emotional-like responses.";
RL PLoS ONE 4:E4704-E4704(2009).
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, amyloid-
CC beta peptide generation in neurons (By similarity) and neurite
CC outgrowth (By similarity). Maintains also meiotic arrest in oocytes.
CC {ECO:0000250, ECO:0000269|PubMed:15956199,
CC ECO:0000269|PubMed:19259266}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in both the forebrain and hindbrain, with
CC the highest level in habenula. Lower level expression in the testis.
CC Highly expressed in regions. {ECO:0000269|PubMed:19259266,
CC ECO:0000269|PubMed:8262253}.
CC -!- DISRUPTION PHENOTYPE: Mice are fertile but display progressive
CC reduction in litter size despite a stable age-independent alteration of
CC the meiotic pause, characterized by premature resumption of meiosis in
CC about one-third of antral follicles in mutant females regardless of
CC age. Aging mutant mice had severe reduction of fertility, manifested by
CC an increasing number of nondeveloping early embryos upon spontaneous
CC ovulation and massive amounts of fragmented oocytes after
CC superovulation. {ECO:0000269|PubMed:15956199}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; D21062; BAA04641.1; -; mRNA.
DR EMBL; AK140302; BAE24325.1; -; mRNA.
DR EMBL; AK140464; BAE24399.1; -; mRNA.
DR EMBL; AK158917; BAE34727.1; -; mRNA.
DR EMBL; AL671858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30077.1; -; Genomic_DNA.
DR EMBL; BC138248; AAI38249.1; -; mRNA.
DR EMBL; BC138250; AAI38251.1; -; mRNA.
DR CCDS; CCDS18743.1; -.
DR PIR; S40454; S40454.
DR RefSeq; NP_032180.1; NM_008154.3.
DR AlphaFoldDB; P35413; -.
DR SMR; P35413; -.
DR STRING; 10090.ENSMUSP00000101531; -.
DR GlyGen; P35413; 1 site.
DR PhosphoSitePlus; P35413; -.
DR PaxDb; P35413; -.
DR PRIDE; P35413; -.
DR Antibodypedia; 3339; 371 antibodies from 39 providers.
DR DNASU; 14748; -.
DR Ensembl; ENSMUST00000052090; ENSMUSP00000062083; ENSMUSG00000049649.
DR Ensembl; ENSMUST00000105911; ENSMUSP00000101531; ENSMUSG00000049649.
DR GeneID; 14748; -.
DR KEGG; mmu:14748; -.
DR UCSC; uc008vci.1; mouse.
DR CTD; 2827; -.
DR MGI; MGI:101908; Gpr3.
DR VEuPathDB; HostDB:ENSMUSG00000049649; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01000000214392; -.
DR HOGENOM; CLU_065071_0_0_1; -.
DR InParanoid; P35413; -.
DR OMA; GTFASCW; -.
DR OrthoDB; 903801at2759; -.
DR PhylomeDB; P35413; -.
DR TreeFam; TF330052; -.
DR BioGRID-ORCS; 14748; 2 hits in 75 CRISPR screens.
DR PRO; PR:P35413; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P35413; protein.
DR Bgee; ENSMUSG00000049649; Expressed in animal zygote and 46 other tissues.
DR ExpressionAtlas; P35413; baseline and differential.
DR Genevisible; P35413; MM.
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; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0040020; P:regulation of meiotic nuclear division; IMP:MGI.
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..330
FT /note="G-protein coupled receptor 3"
FT /id="PRO_0000069511"
FT TOPO_DOM 1..42
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 43..62
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..272
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..277
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..299
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT LIPID 313
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 330 AA; 35453 MW; 89122C57945482B3 CRC64;
MMWGAGSSMA WFSAGSGSVN VSSVDPVEEP TGPATLLPSP RAWDVVLCIS GTLVSCENAL
VVAIIVGTPA FRAPMFLLVG SLAVADLLAG LGLVLHFAAD FCIGSPEMSL MLVGVLAMAF
TASIGSLLAI TVDRYLSLYN ALTYYSETTV TRTYVMLALV WVGALGLGLV PVLAWNCRDG
LTTCGVVYPL SKNHLVVLAI AFFMVFGIML QLYAQICRIV CRHAQQIALQ RHLLPASHYV
ATRKGIATLA VVLGAFAACW LPFTVYCLLG DADSPRLYTY LTLLPATYNS MINPVIYAFR
NQDVQKVLWA ICCCCSTSKI PFRSRSPSDV
