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 27-MAR-2024, entry version 189. 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}. 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; 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 GlyCosmos; O08530; 1 site, No reported glycans. DR GlyGen; O08530; 1 site. DR iPTMnet; O08530; -. DR PhosphoSitePlus; O08530; -. DR SwissPalm; O08530; -. DR MaxQB; O08530; -. DR PaxDb; 10090-ENSMUSP00000050897; -. DR ProteomicsDB; 256817; -. DR Pumba; O08530; -. DR Antibodypedia; 4111; 816 antibodies from 45 providers. DR DNASU; 13609; -. DR Ensembl; ENSMUST00000055676.4; ENSMUSP00000050897.3; ENSMUSG00000045092.9. DR GeneID; 13609; -. DR KEGG; mmu:13609; -. DR UCSC; uc008rbo.2; mouse. DR AGR; MGI:1096355; -. 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; LSCCKCP; -. DR OrthoDB; 4607247at2759; -. DR PhylomeDB; O08530; -. DR TreeFam; TF330052; -. DR Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors. DR BioGRID-ORCS; 13609; 1 hit in 79 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 209 other cell types or tissues. 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:0043231; C:intracellular membrane-bounded organelle; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. 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:0030036; P:actin cytoskeleton organization; 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:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; ISO:MGI. 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: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 CDD; cd15346; 7tmA_S1PR1_Edg1; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000987; EDG1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR InterPro; IPR004061; S1P_rcpt. DR PANTHER; PTHR22750; G-PROTEIN COUPLED RECEPTOR; 1. DR PANTHER; PTHR22750:SF16; SPHINGOSINE 1-PHOSPHATE RECEPTOR 1; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00642; EDG1RECEPTOR. DR PRINTS; PR00237; GPCRRHODOPSN. DR PRINTS; PR01523; S1PRECEPTOR. DR SMART; SM01381; 7TM_GPCR_Srsx; 1. 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. DR Genevisible; O08530; MM. 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 //