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Sphingosine 1-phosphate receptor 1 (S1P receptor 1) (S1P1) (Endothelial differentiation G-protein coupled receptor 1) (Lysophospholipid receptor B1) (Sphingosine 1-phosphate receptor Edg-1) (S1P receptor Edg-1) (CD antigen CD363)

 S1PR1_MOUSE             Reviewed;         382 AA.
O08530; Q9DC35; Q9R235;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
25-OCT-2017, entry version 151.
RecName: Full=Sphingosine 1-phosphate receptor 1;
Short=S1P receptor 1;
Short=S1P1;
AltName: Full=Endothelial differentiation G-protein coupled receptor 1;
AltName: Full=Lysophospholipid receptor B1;
AltName: Full=Sphingosine 1-phosphate receptor Edg-1;
Short=S1P receptor Edg-1;
AltName: CD_antigen=CD363;
Name=S1pr1; Synonyms=Edg1, Lpb1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=9226368; DOI=10.1006/geno.1997.4759;
Liu C.H., Hla T.;
"The mouse gene for the inducible G-protein-coupled receptor edg-1.";
Genomics 43:15-24(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=129/SvJ;
PubMed=9931453; DOI=10.1016/S0378-1119(98)00589-7;
Zhang G., Contos J.J.A., Weiner J.A., Fukushima N., Chun J.;
"Comparative analysis of three murine G-protein coupled receptors
activated by sphingosine-1-phosphate.";
Gene 227:89-99(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Heart, and Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
DISRUPTION PHENOTYPE, FUNCTION IN VASCULAR MATURATION AND CHEMOTAXIS,
AND TISSUE SPECIFICITY.
PubMed=11032855; DOI=10.1172/JCI10905;
Liu Y., Wada R., Yamashita T., Mi Y., Deng C.X., Hobson J.P.,
Rosenfeldt H.M., Nava V.E., Chae S.S., Lee M.J., Liu C.H., Hla T.,
Spiegel S., Proia R.L.;
"Edg-1, the G protein-coupled receptor for sphingosine-1-phosphate, is
essential for vascular maturation.";
J. Clin. Invest. 106:951-961(2000).
[7]
FUNCTION IN FIBROBLAST CHEMOTAXIS, AND DISRUPTION PHENOTYPE.
PubMed=11726541; DOI=10.1096/fj.01-0523com;
Rosenfeldt H.M., Hobson J.P., Maceyka M., Olivera A., Nava V.E.,
Milstien S., Spiegel S.;
"EDG-1 links the PDGF receptor to Src and focal adhesion kinase
activation leading to lamellipodia formation and cell migration.";
FASEB J. 15:2649-2659(2001).
[8]
FUNCTION.
PubMed=11230698; DOI=10.1126/science.1057559;
Hobson J.P., Rosenfeldt H.M., Barak L.S., Olivera A., Poulton S.,
Caron M.G., Milstien S., Spiegel S.;
"Role of the sphingosine-1-phosphate receptor EDG-1 in PDGF-induced
cell motility.";
Science 291:1800-1803(2001).
[9]
DISRUPTION PHENOTYPE, AND FUNCTION IN VASCULAR MATURATION.
PubMed=12869509; DOI=10.1182/blood-2003-02-0460;
Allende M.L., Yamashita T., Proia R.L.;
"G-protein-coupled receptor S1P1 acts within endothelial cells to
regulate vascular maturation.";
Blood 102:3665-3667(2003).
[10]
DISRUPTION PHENOTYPE, AND FUNCTION IN T-CELL MIGRATION.
PubMed=14732704; DOI=10.1074/jbc.M314291200;
Allende M.L., Dreier J.L., Mandala S., Proia R.L.;
"Expression of the sphingosine 1-phosphate receptor, S1P1, on T-cells
controls thymic emigration.";
J. Biol. Chem. 279:15396-15401(2004).
[11]
DISRUPTION PHENOTYPE, AND FUNCTION IN T-CELL MIGRATION.
PubMed=14737169; DOI=10.1038/nature02284;
Matloubian M., Lo C.G., Cinamon G., Lesneski M.J., Xu Y.,
Brinkmann V., Allende M.L., Proia R.L., Cyster J.G.;
"Lymphocyte egress from thymus and peripheral lymphoid organs is
dependent on S1P receptor 1.";
Nature 427:355-360(2004).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[13]
FUNCTION.
PubMed=19286607; DOI=10.1161/CIRCRESAHA.108.193367;
Singleton P.A., Chatchavalvanich S., Fu P., Xing J., Birukova A.A.,
Fortune J.A., Klibanov A.M., Garcia J.G., Birukov K.G.;
"Akt-mediated transactivation of the S1P1 receptor in caveolin-
enriched microdomains regulates endothelial barrier enhancement by
oxidized phospholipids.";
Circ. Res. 104:978-986(2009).
[14]
DISRUPTION PHENOTYPE, AND FUNCTION IN OSTEOCLAST MIGRATION AND BONE
HOMEOSTASIS.
PubMed=19204730; DOI=10.1038/nature07713;
Ishii M., Egen J.G., Klauschen F., Meier-Schellersheim M., Saeki Y.,
Vacher J., Proia R.L., Germain R.N.;
"Sphingosine-1-phosphate mobilizes osteoclast precursors and regulates
bone homeostasis.";
Nature 458:524-528(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
DISRUPTION PHENOTYPE, AND FUNCTION IN HEART MORPHOGENESIS AND
DEVELOPMENT.
PubMed=21668976; DOI=10.1186/1471-213X-11-37;
Poulsen R.R., McClaskey C.M., Rivkees S.A., Wendler C.C.;
"The Sphingosine-1-phospate receptor 1 mediates S1P action during
cardiac development.";
BMC Dev. Biol. 11:37-37(2011).
[17]
DISRUPTION PHENOTYPE, AND FUNCTION IN SPROUTING ANGIOGENESIS.
PubMed=22951644; DOI=10.1242/dev.078550;
Ben Shoham A., Malkinson G., Krief S., Shwartz Y., Ely Y., Ferrara N.,
Yaniv K., Zelzer E.;
"S1P1 inhibits sprouting angiogenesis during vascular development.";
Development 139:3859-3869(2012).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2 AND LYS-10, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- FUNCTION: G-protein coupled receptor for the bioactive
lysosphingolipid sphingosine 1-phosphate (S1P) that seems to be
coupled to the G(i) subclass of heteromeric G proteins. Signaling
leads to the activation of RAC1, SRC, PTK2/FAK1 and MAP kinases.
Plays an important role in cell migration, probably via its role
in the reorganization of the actin cytoskeleton and the formation
of lamellipodia in response to stimuli that increase the activity
of the sphingosine kinase SPHK1. Required for normal chemotaxis
toward sphingosine 1-phosphate. Required for normal embryonic
heart development and normal cardiac morphogenesis. Plays an
important role in the regulation of sprouting angiogenesis and
vascular maturation. Inhibits sprouting angiogenesis to prevent
excessive sprouting during blood vessel development. Required for
normal egress of mature T-cells from the thymus into the blood
stream and into peripheral lymphoid organs. Plays a role in the
migration of osteoclast precursor cells, the regulation of bone
mineralization and bone homeostasis. Plays a role in responses to
oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by
pulmonary endothelial cells and in the protection against
ventilator-induced lung injury. {ECO:0000269|PubMed:11032855,
ECO:0000269|PubMed:11230698, ECO:0000269|PubMed:11726541,
ECO:0000269|PubMed:12869509, ECO:0000269|PubMed:14732704,
ECO:0000269|PubMed:14737169, ECO:0000269|PubMed:19204730,
ECO:0000269|PubMed:19286607, ECO:0000269|PubMed:21668976,
ECO:0000269|PubMed:22951644}.
-!- SUBUNIT: Interacts with GNAI1 and GNAI3. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Endosome {ECO:0000250}. Membrane, caveola {ECO:0000250}.
Note=Recruited to caveolin-enriched plasma membrane microdomains
in response to oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-
phosphocholine. Ligand binding leads to receptor internalization
(By similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues with
highest levels in brain, heart and spleen. Lower levels found in
kidney, liver, lung, muscle, placenta, thymus, and uterus. Very
low levels in intestine, stomach and testis. According to
PubMed:9931453, expressed modestly in apparent endothelial cells
surrounding some blood vessels (e.g. aortic trunk).
{ECO:0000269|PubMed:11032855, ECO:0000269|PubMed:9931453}.
-!- DISRUPTION PHENOTYPE: Embryonic lethality, due to impaired
vascular maturation and defects in heart development. Embryos
appear normal up to 11.5 dpc, but after that they display massive
hemorrhage. They have a normally arborized vascular network, but
present excessive sprouting angiogenesis and severe aberrations in
vessel size. Their aorta and other arteries are not properly
enveloped by vascular smooth muscle cells, causing hemorrhage.
Likewise, small blood vessels show a marked reduction in the
number of vascular pericytes. In addition, mutants display defects
in heart morphogenesis, with reduced myocardial tissue and altered
morphology of the heart wall and the trabeculae. Conditional
knockout in endothelial cells leads to the same vascular
maturation defect as that seen in homozygous knockout mice.
Conditional knockout in fibroblasts leads to defects in
chemotaxis, probably due to defects in the activation of SRC and
PTK2/FAK1, resulting in defects in the reorganization of the actin
cytoskeleton and lamellipodia formation. A T-cell-specific
knockout leads to a defect in the egress of mature T-cells from
the thymus into the periphery. Conditional knockout in osteoclast
precursors leads to osteoporosis, due to impaired migration of
osteoclast precursors and increased osteoclast attachment to the
bone. {ECO:0000269|PubMed:11032855, ECO:0000269|PubMed:11726541,
ECO:0000269|PubMed:12869509, ECO:0000269|PubMed:14732704,
ECO:0000269|PubMed:14737169, ECO:0000269|PubMed:19204730,
ECO:0000269|PubMed:21668976, ECO:0000269|PubMed:22951644}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; U40811; AAC53294.1; -; Genomic_DNA.
EMBL; AF108019; AAD16975.1; -; Genomic_DNA.
EMBL; AK004591; BAB23393.1; -; mRNA.
EMBL; AK146501; BAE27216.1; -; mRNA.
EMBL; CH466532; EDL12402.1; -; Genomic_DNA.
EMBL; BC049094; AAH49094.1; -; mRNA.
EMBL; BC051023; AAH51023.1; -; mRNA.
CCDS; CCDS17781.1; -.
RefSeq; NP_031927.2; NM_007901.5.
UniGene; Mm.982; -.
ProteinModelPortal; O08530; -.
SMR; O08530; -.
BioGrid; 199373; 2.
DIP; DIP-32248N; -.
IntAct; O08530; 2.
STRING; 10090.ENSMUSP00000050897; -.
BindingDB; O08530; -.
ChEMBL; CHEMBL1914262; -.
GuidetoPHARMACOLOGY; 275; -.
iPTMnet; O08530; -.
PhosphoSitePlus; O08530; -.
MaxQB; O08530; -.
PaxDb; O08530; -.
PRIDE; O08530; -.
Ensembl; ENSMUST00000055676; ENSMUSP00000050897; ENSMUSG00000045092.
GeneID; 13609; -.
KEGG; mmu:13609; -.
UCSC; uc008rbo.2; mouse.
CTD; 1901; -.
MGI; MGI:1096355; S1pr1.
eggNOG; ENOG410IIA7; Eukaryota.
eggNOG; ENOG410XQD3; LUCA.
GeneTree; ENSGT00760000118804; -.
HOGENOM; HOG000233501; -.
HOVERGEN; HBG103071; -.
InParanoid; O08530; -.
KO; K04288; -.
OMA; CFIACWA; -.
OrthoDB; EOG091G0DD4; -.
TreeFam; TF330052; -.
Reactome; R-MMU-418594; G alpha (i) signalling events.
Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors.
PRO; PR:O08530; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000045092; -.
Genevisible; O08530; MM.
GO; GO:0005901; C:caveola; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0009897; C:external side of plasma membrane; IMP:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0001664; F:G-protein coupled receptor binding; ISO:MGI.
GO; GO:0046625; F:sphingolipid binding; IEA:Ensembl.
GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; IMP:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IDA:MGI.
GO; GO:0001525; P:angiogenesis; IDA:MGI.
GO; GO:0001955; P:blood vessel maturation; IMP:UniProtKB.
GO; GO:0007420; P:brain development; IMP:MGI.
GO; GO:0003245; P:cardiac muscle tissue growth involved in heart morphogenesis; IMP:UniProtKB.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0006935; P:chemotaxis; IMP:UniProtKB.
GO; GO:0045446; P:endothelial cell differentiation; IEA:Ensembl.
GO; GO:0061384; P:heart trabecula morphogenesis; IMP:UniProtKB.
GO; GO:0030032; P:lamellipodium assembly; IMP:UniProtKB.
GO; GO:0030595; P:leukocyte chemotaxis; IDA:MGI.
GO; GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl.
GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway; IEA:Ensembl.
GO; GO:0043547; P:positive regulation of GTPase activity; IEA:Ensembl.
GO; GO:0050927; P:positive regulation of positive chemotaxis; IEA:Ensembl.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0030500; P:regulation of bone mineralization; IMP:UniProtKB.
GO; GO:0045124; P:regulation of bone resorption; IMP:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IDA:MGI.
GO; GO:0003376; P:sphingosine-1-phosphate signaling pathway; IMP:UniProtKB.
GO; GO:0072678; P:T cell migration; IMP:UniProtKB.
GO; GO:0019226; P:transmission of nerve impulse; IEA:Ensembl.
InterPro; IPR000987; EDG1_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR004061; S1P_rcpt.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00642; EDG1RECEPTOR.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR01523; S1PRECEPTOR.
SMART; SM01381; 7TM_GPCR_Srsx; 1.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Acetylation; Angiogenesis; Cell membrane; Chemotaxis;
Complete proteome; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Receptor; Reference proteome; Transducer;
Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:23806337}.
CHAIN 2 382 Sphingosine 1-phosphate receptor 1.
/FTId=PRO_0000069413.
TOPO_DOM 2 46 Extracellular. {ECO:0000250}.
TRANSMEM 47 68 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 69 82 Cytoplasmic. {ECO:0000250}.
TRANSMEM 83 104 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 105 116 Extracellular. {ECO:0000250}.
TRANSMEM 117 138 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 139 160 Cytoplasmic. {ECO:0000250}.
TRANSMEM 161 182 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 183 196 Extracellular. {ECO:0000250}.
TRANSMEM 197 224 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 225 257 Cytoplasmic. {ECO:0000250}.
TRANSMEM 258 278 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 279 289 Extracellular. {ECO:0000250}.
TRANSMEM 290 310 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 311 382 Cytoplasmic. {ECO:0000250}.
REGION 120 121 Sphingosine 1-phosphate binding.
{ECO:0000250}.
REGION 265 269 Sphingosine 1-phosphate binding.
{ECO:0000250}.
MOD_RES 2 2 N-acetylvaline.
{ECO:0000244|PubMed:23806337}.
MOD_RES 10 10 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 236 236 Phosphothreonine.
{ECO:0000250|UniProtKB:P21453}.
MOD_RES 351 351 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 353 353 Phosphoserine. {ECO:0000255}.
LIPID 328 328 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 184 191 {ECO:0000255|PROSITE-ProRule:PRU00521}.
DISULFID 282 287 {ECO:0000255|PROSITE-ProRule:PRU00521}.
CONFLICT 179 179 I -> S (in Ref. 1; AAC53294 and 2;
AAD16975). {ECO:0000305}.
CONFLICT 218 218 V -> A (in Ref. 1; AAC53294).
{ECO:0000305}.
CONFLICT 244 244 A -> G (in Ref. 1; AAC53294).
{ECO:0000305}.
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


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EIAAB36669 Edg1,Endothelial differentiation G-protein coupled receptor 1,Lpb1,Lysophospholipid receptor B1,Mouse,Mus musculus,S1P receptor 1,S1P receptor Edg-1,S1P1,S1pr1,Sphingosine 1-phosphate receptor 1,Sphin
EIAAB36671 CHEDG1,EDG1,Endothelial differentiation G-protein coupled receptor 1,Homo sapiens,Human,S1P receptor 1,S1P receptor Edg-1,S1P1,S1PR1,Sphingosine 1-phosphate receptor 1,Sphingosine 1-phosphate receptor
EIAAB36672 Edg1,Endothelial differentiation G-protein coupled receptor 1,Rat,Rattus norvegicus,S1P receptor 1,S1P receptor Edg-1,S1P1,S1pr1,Sphingosine 1-phosphate receptor 1,Sphingosine 1-phosphate receptor Edg
EIAAB36670 Bos taurus,Bovine,EDG1,Endothelial differentiation G-protein coupled receptor 1,S1P receptor 1,S1P receptor Edg-1,S1P1,S1PR1,Sphingosine 1-phosphate receptor 1,Sphingosine 1-phosphate receptor Edg-1
EIAAB36673 Edg5,Endothelial differentiation G-protein coupled receptor 5,Gpcr13,Lpb2,Lysophospholipid receptor B2,Mouse,Mus musculus,S1P receptor 2,S1P receptor Edg-5,S1P2,S1pr2,Sphingosine 1-phosphate receptor
EIAAB36681 Edg8,Endothelial differentiation G-protein-coupled receptor 8,Lpb4,Lysophospholipid receptor B4,Mouse,Mus musculus,S1P receptor 5,S1P receptor Edg-8,S1P5,S1pr5,Sphingosine 1-phosphate receptor 5,Sphin
EIAAB36677 Edg3,Endothelial differentiation G-protein coupled receptor 3,Lpb3,Lysophospholipid receptor B3,Mouse,Mus musculus,S1P receptor 3,S1P receptor Edg-3,S1P3,S1pr3,Sphingosine 1-phosphate receptor 3,Sphin
EIAAB36676 EDG3,Endothelial differentiation G-protein coupled receptor 3,Homo sapiens,Human,S1P receptor 3,S1P receptor Edg-3,S1P3,S1PR3,Sphingosine 1-phosphate receptor 3,Sphingosine 1-phosphate receptor Edg-3
EIAAB36683 EDG8,Endothelial differentiation G-protein-coupled receptor 8,Homo sapiens,Human,S1P receptor 5,S1P receptor Edg-8,S1P5,S1PR5,Sphingosine 1-phosphate receptor 5,Sphingosine 1-phosphate receptor Edg-8
EIAAB36678 EDG6,Endothelial differentiation G-protein coupled receptor 6,Homo sapiens,Human,S1P receptor 4,S1P receptor Edg-6,S1P4,S1PR4,Sphingosine 1-phosphate receptor 4,Sphingosine 1-phosphate receptor Edg-6
EIAAB36675 EDG5,Endothelial differentiation G-protein coupled receptor 5,Homo sapiens,Human,S1P receptor 2,S1P receptor Edg-5,S1P2,S1PR2,Sphingosine 1-phosphate receptor 2,Sphingosine 1-phosphate receptor Edg-5
EIAAB36680 EDG8,Endothelial differentiation G-protein-coupled receptor 8,Pig,S1P receptor 5,S1P receptor Edg-8,S1P5,S1PR5,Sphingosine 1-phosphate receptor 5,Sphingosine 1-phosphate receptor Edg-8,Sus scrofa
EIAAB36679 Edg6,Endothelial differentiation G-protein coupled receptor 6,Lpc1,Lysophospholipid receptor C1,Mouse,Mus musculus,S1P receptor 4,S1P receptor Edg-6,S1P4,S1p4,S1pr4,Sphingosine 1-phosphate receptor 4,
18-461-10002 Sphingosine 1-phosphate receptor Edg-5 - S1P receptor Edg-5; Endothelial differentiation G-protein coupled receptor 5; Sphingosine 1-phosphate receptor 2; S1P2 Polyclonal 0.05 ml
18-461-10815 Sphingosine 1-phosphate receptor Edg-6 - S1P receptor Edg-6; Endothelial differentiation G-protein coupled receptor 6; Sphingosine 1-phosphate receptor 4; S1P4 Polyclonal 0.05 ml
18-461-10003 Sphingosine 1-phosphate receptor Edg-5 - S1P receptor Edg-5; Endothelial differentiation G-protein coupled receptor 5; Sphingosine 1-phosphate receptor 2; S1P2 Polyclonal 0.05 ml
18-461-10108 Sphingosine 1-phosphate receptor Edg-6 - S1P receptor Edg-6; Endothelial differentiation G-protein coupled receptor 6; Sphingosine 1-phosphate receptor 4; S1P4 Polyclonal 0.05 ml
18-461-10109 Sphingosine 1-phosphate receptor Edg-6 - S1P receptor Edg-6; Endothelial differentiation G-protein coupled receptor 6; Sphingosine 1-phosphate receptor 4; S1P4 Polyclonal 0.05 ml
18-461-10316 Sphingosine 1-phosphate receptor Edg-5 - S1P receptor Edg-5; Endothelial differentiation G-protein coupled receptor 5; Sphingosine 1-phosphate receptor 2; S1P2 Polyclonal 0.05 ml
EIAAB36674 AGR16,Edg5,Endothelial differentiation G-protein coupled receptor 5,G-protein coupled receptor H218,Rat,Rattus norvegicus,S1P receptor 2,S1P receptor Edg-5,S1P2,S1pr2,Sphingosine 1-phosphate receptor
25-749 GPR6 belongs to the G-protein coupled receptor 1 family.It is a receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological 0.05 mg
20-272-190766 EDG3 - Mouse monoclonal [AS61] to EDG3; S1P receptor Edg-3; Endothelial differentiation G-protein coupled receptor 3; Sphingosine 1-phosphate receptor 3; S1P3 Monoclonal 0.025 mg
18-461-10276 Sphingosine 1-phosphate receptor Edg-1 - Sphingosine 1-phosphate receptor 1; S1P1 Polyclonal 0.05 ml
18-461-10122 Sphingosine 1-phosphate receptor Edg-1 - Sphingosine 1-phosphate receptor 1; S1P1 Polyclonal 0.05 ml
18-461-10389 Sphingosine 1-phosphate receptor GPR6 - G-protein coupled receptor 6 Polyclonal 0.05 ml


 

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