S1PR1_MOUSE
ID S1PR1_MOUSE Reviewed; 382 AA.
AC O08530; Q9DC35; Q9R235;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Sphingosine 1-phosphate receptor 1 {ECO:0000305};
DE Short=S1P receptor 1;
DE Short=S1P1 {ECO:0000303|PubMed:16314531};
DE AltName: Full=Endothelial differentiation G-protein coupled receptor 1;
DE AltName: Full=Lysophospholipid receptor B1;
DE AltName: Full=Sphingosine 1-phosphate receptor Edg-1;
DE Short=S1P receptor Edg-1;
DE AltName: CD_antigen=CD363;
GN Name=S1pr1 {ECO:0000312|MGI:MGI:1096355}; Synonyms=Edg1, Lpb1;
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=BALB/cJ; TISSUE=Liver;
RX PubMed=9226368; DOI=10.1006/geno.1997.4759;
RA Liu C.H., Hla T.;
RT "The mouse gene for the inducible G-protein-coupled receptor edg-1.";
RL Genomics 43:15-24(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Heart, and Lung;
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 [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 STRAIN=C57BL/6J; TISSUE=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).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION IN VASCULAR MATURATION AND CHEMOTAXIS, AND
RP TISSUE SPECIFICITY.
RX PubMed=11032855; DOI=10.1172/jci10905;
RA Liu Y., Wada R., Yamashita T., Mi Y., Deng C.X., Hobson J.P.,
RA Rosenfeldt H.M., Nava V.E., Chae S.S., Lee M.J., Liu C.H., Hla T.,
RA Spiegel S., Proia R.L.;
RT "Edg-1, the G protein-coupled receptor for sphingosine-1-phosphate, is
RT essential for vascular maturation.";
RL J. Clin. Invest. 106:951-961(2000).
RN [7]
RP FUNCTION IN FIBROBLAST CHEMOTAXIS, AND DISRUPTION PHENOTYPE.
RX PubMed=11726541; DOI=10.1096/fj.01-0523com;
RA Rosenfeldt H.M., Hobson J.P., Maceyka M., Olivera A., Nava V.E.,
RA Milstien S., Spiegel S.;
RT "EDG-1 links the PDGF receptor to Src and focal adhesion kinase activation
RT leading to lamellipodia formation and cell migration.";
RL FASEB J. 15:2649-2659(2001).
RN [8]
RP FUNCTION.
RX PubMed=11230698; DOI=10.1126/science.1057559;
RA Hobson J.P., Rosenfeldt H.M., Barak L.S., Olivera A., Poulton S.,
RA Caron M.G., Milstien S., Spiegel S.;
RT "Role of the sphingosine-1-phosphate receptor EDG-1 in PDGF-induced cell
RT motility.";
RL Science 291:1800-1803(2001).
RN [9]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN VASCULAR MATURATION.
RX PubMed=12869509; DOI=10.1182/blood-2003-02-0460;
RA Allende M.L., Yamashita T., Proia R.L.;
RT "G-protein-coupled receptor S1P1 acts within endothelial cells to regulate
RT vascular maturation.";
RL Blood 102:3665-3667(2003).
RN [10]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN T-CELL MIGRATION.
RX PubMed=14732704; DOI=10.1074/jbc.m314291200;
RA Allende M.L., Dreier J.L., Mandala S., Proia R.L.;
RT "Expression of the sphingosine 1-phosphate receptor, S1P1, on T-cells
RT controls thymic emigration.";
RL J. Biol. Chem. 279:15396-15401(2004).
RN [11]
RP DISRUPTION PHENOTYPE.
RX PubMed=16314531; DOI=10.1128/mcb.25.24.11113-11121.2005;
RA Mizugishi K., Yamashita T., Olivera A., Miller G.F., Spiegel S.,
RA Proia R.L.;
RT "Essential role for sphingosine kinases in neural and vascular
RT development.";
RL Mol. Cell. Biol. 25:11113-11121(2005).
RN [12]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN T-CELL MIGRATION.
RX PubMed=14737169; DOI=10.1038/nature02284;
RA Matloubian M., Lo C.G., Cinamon G., Lesneski M.J., Xu Y., Brinkmann V.,
RA Allende M.L., Proia R.L., Cyster J.G.;
RT "Lymphocyte egress from thymus and peripheral lymphoid organs is dependent
RT on S1P receptor 1.";
RL Nature 427:355-360(2004).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [14]
RP FUNCTION.
RX PubMed=19286607; DOI=10.1161/circresaha.108.193367;
RA Singleton P.A., Chatchavalvanich S., Fu P., Xing J., Birukova A.A.,
RA Fortune J.A., Klibanov A.M., Garcia J.G., Birukov K.G.;
RT "Akt-mediated transactivation of the S1P1 receptor in caveolin-enriched
RT microdomains regulates endothelial barrier enhancement by oxidized
RT phospholipids.";
RL Circ. Res. 104:978-986(2009).
RN [15]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN OSTEOCLAST MIGRATION AND BONE
RP HOMEOSTASIS.
RX PubMed=19204730; DOI=10.1038/nature07713;
RA Ishii M., Egen J.G., Klauschen F., Meier-Schellersheim M., Saeki Y.,
RA Vacher J., Proia R.L., Germain R.N.;
RT "Sphingosine-1-phosphate mobilizes osteoclast precursors and regulates bone
RT homeostasis.";
RL Nature 458:524-528(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [17]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN HEART MORPHOGENESIS AND DEVELOPMENT.
RX PubMed=21668976; DOI=10.1186/1471-213x-11-37;
RA Poulsen R.R., McClaskey C.M., Rivkees S.A., Wendler C.C.;
RT "The Sphingosine-1-phosphate receptor 1 mediates S1P action during cardiac
RT development.";
RL BMC Dev. Biol. 11:37-37(2011).
RN [18]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN SPROUTING ANGIOGENESIS.
RX PubMed=22951644; DOI=10.1242/dev.078550;
RA Ben Shoham A., Malkinson G., Krief S., Shwartz Y., Ely Y., Ferrara N.,
RA Yaniv K., Zelzer E.;
RT "S1P1 inhibits sprouting angiogenesis during vascular development.";
RL Development 139:3859-3869(2012).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2 AND LYS-10, CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: G-protein coupled receptor for the bioactive lysosphingolipid
CC sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i)
CC subclass of heteromeric G proteins. Signaling leads to the activation
CC of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in
CC cell migration, probably via its role in the reorganization of the
CC actin cytoskeleton and the formation of lamellipodia in response to
CC stimuli that increase the activity of the sphingosine kinase SPHK1.
CC Required for normal chemotaxis toward sphingosine 1-phosphate. Required
CC for normal embryonic heart development and normal cardiac
CC morphogenesis. Plays an important role in the regulation of sprouting
CC angiogenesis and vascular maturation. Inhibits sprouting angiogenesis
CC to prevent excessive sprouting during blood vessel development.
CC Required for normal egress of mature T-cells from the thymus into the
CC blood stream and into peripheral lymphoid organs. Plays a role in the
CC migration of osteoclast precursor cells, the regulation of bone
CC mineralization and bone homeostasis. Plays a role in responses to
CC oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by
CC pulmonary endothelial cells and in the protection against ventilator-
CC induced lung injury. {ECO:0000269|PubMed:11032855,
CC ECO:0000269|PubMed:11230698, ECO:0000269|PubMed:11726541,
CC ECO:0000269|PubMed:12869509, ECO:0000269|PubMed:14732704,
CC ECO:0000269|PubMed:14737169, ECO:0000269|PubMed:19204730,
CC ECO:0000269|PubMed:19286607, ECO:0000269|PubMed:21668976,
CC ECO:0000269|PubMed:22951644}.
CC -!- SUBUNIT: Interacts with GNAI1 and GNAI3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endosome {ECO:0000250}. Membrane, caveola {ECO:0000250}. Note=Recruited
CC to caveolin-enriched plasma membrane microdomains in response to
CC oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine. Ligand
CC binding leads to receptor internalization (By similarity).
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues with highest
CC levels in brain, heart and spleen. Lower levels found in kidney, liver,
CC lung, muscle, placenta, thymus, and uterus. Very low levels in
CC intestine, stomach and testis. According to PubMed:9931453, expressed
CC modestly in apparent endothelial cells surrounding some blood vessels
CC (e.g. aortic trunk). {ECO:0000269|PubMed:11032855,
CC ECO:0000269|PubMed:9931453}.
CC -!- PTM: Palmitoylated by ZDHHC5. Palmitoylation is required for targeting
CC to plasma membrane, enabling G(i) coupling.
CC {ECO:0000250|UniProtKB:P21453}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality, due to impaired vascular
CC maturation and defects in heart development. Embryos appear normal up
CC to 11.5 dpc, but after that they display massive hemorrhage. They have
CC a normally arborized vascular network, but present excessive sprouting
CC angiogenesis and severe aberrations in vessel size. Their aorta and
CC other arteries are not properly enveloped by vascular smooth muscle
CC cells, causing hemorrhage. Likewise, small blood vessels show a marked
CC reduction in the number of vascular pericytes. In addition, mutants
CC display defects in heart morphogenesis, with reduced myocardial tissue
CC and altered morphology of the heart wall and the trabeculae
CC (PubMed:11032855, PubMed:14732704, PubMed:21668976, PubMed:22951644).
CC At 12.5 dpc, mutant embryos also show a massive cell loss in the
CC forebrain (PubMed:16314531). Conditional knockout in endothelial cells
CC leads to the same vascular maturation defect as that seen in homozygous
CC knockout mice (PubMed:12869509). Conditional knockout in fibroblasts
CC leads to defects in chemotaxis, probably due to defects in the
CC activation of SRC and PTK2/FAK1, resulting in defects in the
CC reorganization of the actin cytoskeleton and lamellipodia formation
CC (PubMed:11726541). A T-cell-specific knockout leads to a defect in the
CC egress of mature T-cells from the thymus into the periphery
CC (PubMed:14737169). Conditional knockout in osteoclast precursors leads
CC to osteoporosis, due to impaired migration of osteoclast precursors and
CC increased osteoclast attachment to the bone (PubMed:19204730).
CC {ECO:0000269|PubMed:11032855, ECO:0000269|PubMed:11726541,
CC ECO:0000269|PubMed:12869509, ECO:0000269|PubMed:14732704,
CC ECO:0000269|PubMed:14737169, ECO:0000269|PubMed:16314531,
CC ECO:0000269|PubMed:19204730, ECO:0000269|PubMed:21668976,
CC ECO:0000269|PubMed:22951644}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U40811; AAC53294.1; -; Genomic_DNA.
DR EMBL; AF108019; AAD16975.1; -; Genomic_DNA.
DR EMBL; AK004591; BAB23393.1; -; mRNA.
DR EMBL; AK146501; BAE27216.1; -; mRNA.
DR EMBL; CH466532; EDL12402.1; -; Genomic_DNA.
DR EMBL; BC049094; AAH49094.1; -; mRNA.
DR EMBL; BC051023; AAH51023.1; -; mRNA.
DR CCDS; CCDS17781.1; -.
DR RefSeq; NP_031927.2; NM_007901.5.
DR AlphaFoldDB; O08530; -.
DR SMR; O08530; -.
DR BioGRID; 199373; 2.
DR DIP; DIP-32248N; -.
DR IntAct; O08530; 1.
DR STRING; 10090.ENSMUSP00000050897; -.
DR BindingDB; O08530; -.
DR ChEMBL; CHEMBL1914262; -.
DR GuidetoPHARMACOLOGY; 275; -.
DR GlyGen; O08530; 1 site.
DR iPTMnet; O08530; -.
DR PhosphoSitePlus; O08530; -.
DR SwissPalm; O08530; -.
DR MaxQB; O08530; -.
DR PaxDb; O08530; -.
DR PRIDE; O08530; -.
DR ProteomicsDB; 256817; -.
DR Antibodypedia; 4111; 768 antibodies from 45 providers.
DR DNASU; 13609; -.
DR Ensembl; ENSMUST00000055676; ENSMUSP00000050897; ENSMUSG00000045092.
DR GeneID; 13609; -.
DR KEGG; mmu:13609; -.
DR UCSC; uc008rbo.2; mouse.
DR CTD; 1901; -.
DR MGI; MGI:1096355; S1pr1.
DR VEuPathDB; HostDB:ENSMUSG00000045092; -.
DR eggNOG; ENOG502QSFG; Eukaryota.
DR GeneTree; ENSGT01050000244887; -.
DR HOGENOM; CLU_047979_1_0_1; -.
DR InParanoid; O08530; -.
DR OMA; HPNKEEV; -.
DR OrthoDB; 981486at2759; -.
DR PhylomeDB; O08530; -.
DR TreeFam; TF330052; -.
DR Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors.
DR BioGRID-ORCS; 13609; 1 hit in 74 CRISPR screens.
DR ChiTaRS; S1pr1; mouse.
DR PRO; PR:O08530; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O08530; protein.
DR Bgee; ENSMUSG00000045092; Expressed in right lung lobe and 206 other tissues.
DR Genevisible; O08530; MM.
DR GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IMP:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0046625; F:sphingolipid binding; ISO:MGI.
DR GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; IMP:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
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:0001525; P:angiogenesis; IDA:MGI.
DR GO; GO:0001955; P:blood vessel maturation; IMP:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0003245; P:cardiac muscle tissue growth involved in heart morphogenesis; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006935; P:chemotaxis; IMP:UniProtKB.
DR GO; GO:0045446; P:endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0061384; P:heart trabecula morphogenesis; IMP:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
DR GO; GO:0030595; P:leukocyte chemotaxis; IDA:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; ISO:MGI.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0050927; P:positive regulation of positive chemotaxis; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0030500; P:regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:0045124; P:regulation of bone resorption; IMP:UniProtKB.
DR GO; GO:0030155; P:regulation of cell adhesion; IDA:MGI.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0072678; P:T cell migration; IMP:UniProtKB.
DR GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
DR InterPro; IPR000987; EDG1_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004061; S1P_rcpt.
DR PANTHER; PTHR22750:SF16; PTHR22750:SF16; 1.
DR Pfam; PF00001; 7tm_1; 1.
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 1: Evidence at protein level;
KW Acetylation; Angiogenesis; Cell membrane; Chemotaxis; Disulfide bond;
KW Endosome; G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW Palmitate; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CHAIN 2..382
FT /note="Sphingosine 1-phosphate receptor 1"
FT /id="PRO_0000069413"
FT TOPO_DOM 2..46
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 47..68
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 69..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 83..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 105..116
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 117..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 139..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 161..182
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 183..196
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 197..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 225..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 258..278
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 279..289
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 290..310
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 311..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 348..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120..121
FT /ligand="sphing-4-enine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:60119"
FT /evidence="ECO:0000250"
FT BINDING 265..269
FT /ligand="sphing-4-enine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:60119"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylvaline"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 236
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P21453"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT LIPID 328
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 184..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 282..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 179
FT /note="I -> S (in Ref. 1; AAC53294 and 2; AAD16975)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="V -> A (in Ref. 1; AAC53294)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="A -> G (in Ref. 1; AAC53294)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 42639 MW; 5FE4C9A2BD65CB2A CRC64;
MVSTSIPEVK ALRSSVSDYG NYDIIVRHYN YTGKLNIGAE KDHGIKLTSV VFILICCFII
LENIFVLLTI WKTKKFHRPM YYFIGNLALS DLLAGVAYTA NLLLSGATTY KLTPAQWFLR
EGSMFVALSA SVFSLLAIAI ERYITMLKMK LHNGSNSSRS FLLISACWVI SLILGGLPIM
GWNCISSLSS CSTVLPLYHK HYILFCTTVF TLLLLSIVIL YCRIYSLVRT RSRRLTFRKN
ISKASRSSEK SLALLKTVII VLSVFIACWA PLFILLLLDV GCKAKTCDIL YKAEYFLVLA
VLNSGTNPII YTLTNKEMRR AFIRIVSCCK CPNGDSAGKF KRPIIPGMEF SRSKSDNSSH
PQKDDGDNPE TIMSSGNVNS SS
