S1PR3_MOUSE
ID S1PR3_MOUSE Reviewed; 378 AA.
AC Q9Z0U9; Q8BP20;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Sphingosine 1-phosphate receptor 3;
DE Short=S1P receptor 3;
DE Short=S1P3;
DE AltName: Full=Endothelial differentiation G-protein coupled receptor 3;
DE AltName: Full=Lysophospholipid receptor B3;
DE AltName: Full=Sphingosine 1-phosphate receptor Edg-3;
DE Short=S1P receptor Edg-3;
GN Name=S1pr3; Synonyms=Edg3, Lpb3;
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], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=9931453; DOI=10.1016/s0378-1119(98)00589-7;
RA Zhang G., Contos J.J.A., Weiner J.A., Fukushima N., Chun J.;
RT "Comparative analysis of three murine G-protein coupled receptors activated
RT by sphingosine-1-phosphate.";
RL Gene 227:89-99(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Head, Lung, Mesonephros, and Testis;
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 [MRNA].
RA Ohta K., Wada A., Igarashi Y.;
RT "Mus musculus sphingosine 1-phosphate receptor Edg3 gene, complete.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, and Eye;
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 lysosphingolipid sphingosine 1-phosphate
CC (S1P). S1P is a bioactive lysophospholipid that elicits diverse
CC physiological effect on most types of cells and tissues.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Most abundant in heart, lung, kidney and spleen;
CC low but detectable in brain, thymus, muscle and testis; and nearly
CC undetectable in liver, stomach, and intestine. Expressed in embryonic
CC lung from embryonic day 14-18. Also abundantly detected in embryonic
CC nasal cartilage, sphenoid bone, vena cava, Meckel's cartilage/incisor
CC teeth, genital tubercle and bladder. {ECO:0000269|PubMed:9931453}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF108021; AAD16977.1; -; Genomic_DNA.
DR EMBL; AK028043; BAC25715.1; -; mRNA.
DR EMBL; AK029852; BAC26645.1; -; mRNA.
DR EMBL; AK030134; BAC26800.1; -; mRNA.
DR EMBL; AK047268; BAC33008.1; -; mRNA.
DR EMBL; AK081919; BAC38373.1; -; mRNA.
DR EMBL; AK084944; BAC39316.1; -; mRNA.
DR EMBL; AK085180; BAC39383.1; -; mRNA.
DR EMBL; AK078443; BAC37277.1; -; mRNA.
DR EMBL; AB028143; BAA78207.1; -; mRNA.
DR EMBL; BC064007; AAH64007.1; -; mRNA.
DR EMBL; BC068176; AAH68176.1; -; mRNA.
DR CCDS; CCDS26512.1; -.
DR RefSeq; NP_034231.1; NM_010101.4.
DR AlphaFoldDB; Q9Z0U9; -.
DR SMR; Q9Z0U9; -.
DR STRING; 10090.ENSMUSP00000085293; -.
DR GuidetoPHARMACOLOGY; 277; -.
DR GlyGen; Q9Z0U9; 1 site.
DR iPTMnet; Q9Z0U9; -.
DR PhosphoSitePlus; Q9Z0U9; -.
DR MaxQB; Q9Z0U9; -.
DR PaxDb; Q9Z0U9; -.
DR PRIDE; Q9Z0U9; -.
DR ProteomicsDB; 256861; -.
DR Antibodypedia; 13485; 548 antibodies from 37 providers.
DR DNASU; 13610; -.
DR Ensembl; ENSMUST00000087978; ENSMUSP00000085293; ENSMUSG00000067586.
DR GeneID; 13610; -.
DR KEGG; mmu:13610; -.
DR UCSC; uc007qmf.2; mouse.
DR CTD; 1903; -.
DR MGI; MGI:1339365; S1pr3.
DR VEuPathDB; HostDB:ENSMUSG00000067586; -.
DR eggNOG; ENOG502R61K; Eukaryota.
DR GeneTree; ENSGT01050000244887; -.
DR HOGENOM; CLU_047979_1_0_1; -.
DR InParanoid; Q9Z0U9; -.
DR OMA; DVACRVK; -.
DR OrthoDB; 981486at2759; -.
DR PhylomeDB; Q9Z0U9; -.
DR TreeFam; TF330052; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors.
DR Reactome; R-MMU-9009391; Extra-nuclear estrogen signaling.
DR BioGRID-ORCS; 13610; 1 hit in 73 CRISPR screens.
DR ChiTaRS; S1pr3; mouse.
DR PRO; PR:Q9Z0U9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9Z0U9; protein.
DR Bgee; ENSMUSG00000067586; Expressed in internal carotid artery and 234 other tissues.
DR Genevisible; Q9Z0U9; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; IEA:InterPro.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:1903141; P:negative regulation of establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; IMP:MGI.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR InterPro; IPR004062; EDG3_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004061; S1P_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01524; EDG3RECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01523; S1PRECEPTOR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 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; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..378
FT /note="Sphingosine 1-phosphate receptor 3"
FT /id="PRO_0000069422"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 45..65
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 66..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 96..115
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 116..136
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 137..154
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 155..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 176..196
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 197..217
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 218..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 245..265
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 266..281
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 282..302
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 303..378
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 323..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99500"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 106
FT /note="S -> R (in Ref. 2; BAC37277)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 378 AA; 42270 MW; F466B25E77ECDCC8 CRC64;
MATTHAQGHQ PVLGNDTLRE HYDYVGKLAG RLRDPPEGGT LITTILFLVT CSFIVLENLM
VLIAIWKNNK FHNRMYFFIG NLALCDLLAG IAYKVNILMS GRKTFSLSPT VWFLREGSMF
VALGASTCSL LAIAIERHLT MIKMRPYDAN KKHRVFLLIG MCWLIAFSLG ALPILGWNCL
ENFPDCSTIL PLYSKKYIAF LISIFTAILV TIVILYARIY CLVKSSSRRV ANHNSERSMA
LLRTVVIVVS VFIACWSPLF ILFLIDVACR AKECSILFKS QWFIMLAVLN SAMNPVIYTL
ASKEMRRAFF RLVCGCLVKG KGTQASPMQP ALDPSRSKSS SSNNSSHSPK VKEDLPRVAT
SSCIIDKNRS FQNGVLCK