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

 S1PR1_HUMAN             Reviewed;         382 AA.
P21453; D3DT66; Q9BYY4; Q9NYN8;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
02-SEP-2008, sequence version 2.
22-NOV-2017, entry version 177.
RecName: Full=Sphingosine 1-phosphate receptor 1;
Short=S1P receptor 1;
Short=S1P1;
AltName: Full=Endothelial differentiation G-protein coupled receptor 1;
AltName: Full=Sphingosine 1-phosphate receptor Edg-1;
Short=S1P receptor Edg-1;
AltName: CD_antigen=CD363;
Name=S1PR1; Synonyms=CHEDG1, EDG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Umbilical vein endothelial cell;
PubMed=2160972;
Hla T., Maciag T.;
"An abundant transcript induced in differentiating human endothelial
cells encodes a polypeptide with structural similarities to G-protein-
coupled receptors.";
J. Biol. Chem. 265:9308-9313(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=9409733; DOI=10.1016/S0014-5793(97)01301-X;
An S., Bleu T., Huang W., Hallmark O.G., Coughlin S.R., Goetzl E.J.;
"Identification of cDNAs encoding two G protein-coupled receptors for
lysosphingolipids.";
FEBS Lett. 417:279-282(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF ARG-120; GLU-121 AND ARG-292.
PubMed=10982820; DOI=10.1074/jbc.M007680200;
Parrill A.L., Wang D., Bautista D.L., Van Brocklyn J.R., Lorincz Z.,
Fischer D.J., Baker D.L., Liliom K., Spiegel S., Tigyi G.;
"Identification of Edg1 receptor residues that recognize sphingosine
1-phosphate.";
J. Biol. Chem. 275:39379-39384(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Substantia nigra;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[9]
FUNCTION, AND INTERACTION WITH GNAI1 AND GNAI3.
PubMed=8626678; DOI=10.1074/jbc.271.19.11272;
Lee M.-J., Evans M., Hla T.;
"The inducible G protein-coupled receptor edg-1 signals via the
G(i)/mitogen-activated protein kinase pathway.";
J. Biol. Chem. 271:11272-11279(1996).
[10]
FUNCTION.
PubMed=9488656; DOI=10.1126/science.279.5356.1552;
Lee M.-J., Van Brocklyn J.R., Thangada S., Liu C.H., Hand A.R.,
Menzeleev R., Spiegel S., Hla T.;
"Sphingosine-1-phosphate as a ligand for the G protein-coupled
receptor EDG-1.";
Science 279:1552-1555(1998).
[11]
PHARMACOLOGICAL CHARACTERIZATION.
PubMed=10383399; DOI=10.1074/jbc.274.27.18997;
Ancellin N., Hla T.;
"Differential pharmacological properties and signal transduction of
the sphingosine 1-phosphate receptors EDG-1, EDG-3, and EDG-5.";
J. Biol. Chem. 274:18997-19002(1999).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11604399; DOI=10.1074/jbc.M107301200;
Wang D.A., Lorincz Z., Bautista D.L., Liliom K., Tigyi G.,
Parrill A.L.;
"A single amino acid determines lysophospholipid specificity of the
S1P1 (EDG1) and LPA1 (EDG2) phospholipid growth factor receptors.";
J. Biol. Chem. 276:49213-49220(2001).
[13]
FUNCTION IN CHEMOTAXIS, PHOSPHORYLATION AT THR-236, AND MUTAGENESIS OF
THR-236.
PubMed=11583630; DOI=10.1016/S1097-2765(01)00324-0;
Lee M.-J., Thangada S., Paik J.-H., Sapkota G.P., Ancellin N.,
Chae S.-S., Wu M., Morales-Ruiz M., Sessa W.C., Alessi D.R., Hla T.;
"Akt-mediated phosphorylation of the G protein-coupled receptor EDG-1
is required for endothelial cell chemotaxis.";
Mol. Cell 8:693-704(2001).
[14]
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).
[15]
SUBCELLULAR LOCATION, TOPOLOGY, AND GLYCOSYLATION AT ASN-30.
PubMed=15750791; DOI=10.1007/s10719-004-5540-8;
Kohno T., Igarashi Y.;
"Roles for N-glycosylation in the dynamics of Edg-1/S1P1 in
sphingosine 1-phosphate-stimulated cells.";
Glycoconj. J. 21:497-501(2004).
[16]
FUNCTION, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
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).
[17]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-326 IN COMPLEX WITH
SPHINGOLIPID ANALOG, FUNCTION, SUBCELLULAR LOCATION, MEMBRANE
TOPOLOGY, MUTAGENESIS OF PHE-210; PHE-265 AND TRP-269, GLYCOSYLATION
AT ASN-30, AND DISULFIDE BONDS.
PubMed=22344443; DOI=10.1126/science.1215904;
Hanson M.A., Roth C.B., Jo E., Griffith M.T., Scott F.L., Reinhart G.,
Desale H., Clemons B., Cahalan S.M., Schuerer S.C., Sanna M.G.,
Han G.W., Kuhn P., Rosen H., Stevens R.C.;
"Crystal structure of a lipid G protein-coupled receptor.";
Science 335:851-855(2012).
-!- 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 (By similarity). 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:0000250,
ECO:0000269|PubMed:10982820, ECO:0000269|PubMed:11230698,
ECO:0000269|PubMed:11583630, ECO:0000269|PubMed:11604399,
ECO:0000269|PubMed:19286607, ECO:0000269|PubMed:22344443,
ECO:0000269|PubMed:8626678, ECO:0000269|PubMed:9488656}.
-!- SUBUNIT: Interacts with GNAI1 and GNAI3.
{ECO:0000269|PubMed:22344443, ECO:0000269|PubMed:8626678}.
-!- INTERACTION:
Q07108:CD69; NbExp=2; IntAct=EBI-2681920, EBI-2836595;
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Endosome. Membrane raft. 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.
-!- TISSUE SPECIFICITY: Endothelial cells, and to a lesser extent, in
vascular smooth muscle cells, fibroblasts, melanocytes, and cells
of epithelioid origin.
-!- INDUCTION: By the tumor promoter phorbol 12-myristate 13-acetate
(PMA) in the presence of cycloheximide.
-!- PTM: S1P-induced endothelial cell migration requires the PKB/AKT1-
mediated phosphorylation of the third intracellular loop at the
Thr-236 residue. {ECO:0000269|PubMed:11583630,
ECO:0000269|PubMed:19286607}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; M31210; AAA52336.1; -; mRNA.
EMBL; AF022137; AAC51905.1; -; mRNA.
EMBL; AF233365; AAF43420.1; -; mRNA.
EMBL; AK312493; BAG35395.1; -; mRNA.
EMBL; CR541786; CAG46585.1; -; mRNA.
EMBL; CR542269; CAG47065.1; -; mRNA.
EMBL; AL109741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471097; EAW72927.1; -; Genomic_DNA.
EMBL; CH471097; EAW72928.1; -; Genomic_DNA.
EMBL; BC018650; AAH18650.1; -; mRNA.
CCDS; CCDS777.1; -.
PIR; A35300; A35300.
RefSeq; NP_001307659.1; NM_001320730.1.
RefSeq; NP_001391.2; NM_001400.4.
UniGene; Hs.154210; -.
PDB; 3V2W; X-ray; 3.35 A; A=2-231, A=244-326.
PDB; 3V2Y; X-ray; 2.80 A; A=2-231, A=244-326.
PDBsum; 3V2W; -.
PDBsum; 3V2Y; -.
ProteinModelPortal; P21453; -.
SMR; P21453; -.
BioGrid; 108225; 30.
CORUM; P21453; -.
DIP; DIP-60427N; -.
IntAct; P21453; 4.
STRING; 9606.ENSP00000305416; -.
BindingDB; P21453; -.
ChEMBL; CHEMBL4333; -.
DrugBank; DB09105; Asfotase Alfa.
GuidetoPHARMACOLOGY; 275; -.
TCDB; 9.A.14.2.1; the g-protein-coupled receptor (gpcr) family.
iPTMnet; P21453; -.
PhosphoSitePlus; P21453; -.
SwissPalm; P21453; -.
BioMuta; S1PR1; -.
DMDM; 205371820; -.
EPD; P21453; -.
PaxDb; P21453; -.
PeptideAtlas; P21453; -.
PRIDE; P21453; -.
DNASU; 1901; -.
Ensembl; ENST00000305352; ENSP00000305416; ENSG00000170989.
GeneID; 1901; -.
KEGG; hsa:1901; -.
UCSC; uc001dud.3; human.
CTD; 1901; -.
DisGeNET; 1901; -.
EuPathDB; HostDB:ENSG00000170989.8; -.
GeneCards; S1PR1; -.
HGNC; HGNC:3165; S1PR1.
HPA; CAB010104; -.
HPA; HPA075568; -.
MIM; 601974; gene.
neXtProt; NX_P21453; -.
OpenTargets; ENSG00000170989; -.
PharmGKB; PA162402344; -.
eggNOG; ENOG410IIA7; Eukaryota.
eggNOG; ENOG410XQD3; LUCA.
GeneTree; ENSGT00760000118804; -.
HOGENOM; HOG000233501; -.
HOVERGEN; HBG103071; -.
InParanoid; P21453; -.
KO; K04288; -.
OMA; CFIACWA; -.
OrthoDB; EOG091G0DD4; -.
PhylomeDB; P21453; -.
TreeFam; TF330052; -.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-419408; Lysosphingolipid and LPA receptors.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SignaLink; P21453; -.
SIGNOR; P21453; -.
GeneWiki; S1PR1; -.
GenomeRNAi; 1901; -.
PRO; PR:P21453; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000170989; -.
CleanEx; HS_S1PR1; -.
Genevisible; P21453; HS.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc.
GO; GO:0001664; F:G-protein coupled receptor binding; IPI:UniProtKB.
GO; GO:0046625; F:sphingolipid binding; IEA:Ensembl.
GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0001955; P:blood vessel maturation; ISS:UniProtKB.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0003245; P:cardiac muscle tissue growth involved in heart morphogenesis; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0006935; P:chemotaxis; ISS:UniProtKB.
GO; GO:0045446; P:endothelial cell differentiation; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc.
GO; GO:0061384; P:heart trabecula morphogenesis; ISS:UniProtKB.
GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
GO; GO:0030595; P:leukocyte chemotaxis; IEA:Ensembl.
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: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; ISS:UniProtKB.
GO; GO:0045124; P:regulation of bone resorption; ISS:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
GO; GO:0003376; P:sphingosine-1-phosphate signaling pathway; IDA:UniProtKB.
GO; GO:0072678; P:T cell migration; ISS: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;
3D-structure; Acetylation; Angiogenesis; Cell membrane; Chemotaxis;
Complete proteome; Disulfide bond; Endosome;
G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 382 Sphingosine 1-phosphate receptor 1.
/FTId=PRO_0000069412.
TOPO_DOM 1 46 Extracellular.
{ECO:0000269|PubMed:15750791}.
TRANSMEM 47 68 Helical; Name=1.
TOPO_DOM 69 82 Cytoplasmic.
{ECO:0000269|PubMed:15750791}.
TRANSMEM 83 104 Helical; Name=2.
TOPO_DOM 105 116 Extracellular.
{ECO:0000269|PubMed:15750791}.
TRANSMEM 117 138 Helical; Name=3.
TOPO_DOM 139 160 Cytoplasmic.
{ECO:0000269|PubMed:15750791}.
TRANSMEM 161 182 Helical; Name=4.
TOPO_DOM 183 196 Extracellular.
{ECO:0000269|PubMed:15750791}.
TRANSMEM 197 224 Helical; Name=5.
TOPO_DOM 225 257 Cytoplasmic.
{ECO:0000269|PubMed:15750791}.
TRANSMEM 258 278 Helical; Name=6.
TOPO_DOM 279 289 Extracellular.
{ECO:0000269|PubMed:15750791}.
TRANSMEM 290 310 Helical; Name=7.
TOPO_DOM 311 382 Cytoplasmic.
{ECO:0000269|PubMed:15750791}.
REGION 120 121 Sphingosine 1-phosphate binding.
REGION 265 269 Sphingosine 1-phosphate binding.
MOD_RES 10 10 N6-acetyllysine.
{ECO:0000250|UniProtKB:O08530}.
MOD_RES 236 236 Phosphothreonine; by PKB/AKT1.
{ECO:0000269|PubMed:11583630}.
MOD_RES 351 351 Phosphoserine.
{ECO:0000250|UniProtKB:O08530}.
MOD_RES 353 353 Phosphoserine. {ECO:0000255}.
LIPID 328 328 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15750791,
ECO:0000269|PubMed:22344443}.
CARBOHYD 36 36 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 184 191 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:22344443}.
DISULFID 282 287 {ECO:0000255|PROSITE-ProRule:PRU00521,
ECO:0000269|PubMed:22344443}.
VARIANT 15 15 S -> L (in dbSNP:rs4987250).
/FTId=VAR_046158.
VARIANT 115 115 A -> T (in dbSNP:rs11542632).
/FTId=VAR_046159.
VARIANT 332 332 P -> R (in dbSNP:rs7549921).
/FTId=VAR_046160.
MUTAGEN 120 120 R->A: Drastically reduced affinity for
sphingosine 1-phosphate.
{ECO:0000269|PubMed:10982820}.
MUTAGEN 121 121 E->A: Drastically reduced affinity for
sphingosine 1-phosphate.
{ECO:0000269|PubMed:10982820}.
MUTAGEN 121 121 E->Q: Slight activation of the receptor
at maximal ligand concentration.
{ECO:0000269|PubMed:10982820}.
MUTAGEN 210 210 F->L: Impairs sphingosine 1-phosphate
binding and signaling.
{ECO:0000269|PubMed:22344443}.
MUTAGEN 236 236 T->A: Acts as a dominant negative GPCR
and inhibits S1P-induced Rac activation,
chemotaxis, and angiogenesis.
{ECO:0000269|PubMed:11583630}.
MUTAGEN 265 265 F->L: Impairs sphingosine 1-phosphate
binding and signaling.
{ECO:0000269|PubMed:22344443}.
MUTAGEN 269 269 W->F,L: Impairs sphingosine 1-phosphate
binding and signaling.
{ECO:0000269|PubMed:22344443}.
MUTAGEN 292 292 R->A,V: Drastically reduced affinity for
sphingosine 1-phosphate.
{ECO:0000269|PubMed:10982820}.
CONFLICT 250 252 KSL -> NV (in Ref. 1; AAA52336 and 2;
AAC51905). {ECO:0000305}.
HELIX 23 31 {ECO:0000244|PDB:3V2Y}.
HELIX 36 39 {ECO:0000244|PDB:3V2Y}.
HELIX 42 72 {ECO:0000244|PDB:3V2Y}.
HELIX 74 76 {ECO:0000244|PDB:3V2W}.
HELIX 79 104 {ECO:0000244|PDB:3V2Y}.
HELIX 106 109 {ECO:0000244|PDB:3V2Y}.
HELIX 114 146 {ECO:0000244|PDB:3V2Y}.
HELIX 158 176 {ECO:0000244|PDB:3V2Y}.
TURN 177 181 {ECO:0000244|PDB:3V2Y}.
HELIX 188 190 {ECO:0000244|PDB:3V2Y}.
STRAND 193 195 {ECO:0000244|PDB:3V2Y}.
HELIX 200 231 {ECO:0000244|PDB:3V2Y}.
TURN 247 249 {ECO:0000244|PDB:3V2Y}.
HELIX 251 280 {ECO:0000244|PDB:3V2Y}.
TURN 284 286 {ECO:0000244|PDB:3V2Y}.
TURN 289 291 {ECO:0000244|PDB:3V2Y}.
HELIX 294 302 {ECO:0000244|PDB:3V2Y}.
HELIX 303 305 {ECO:0000244|PDB:3V2Y}.
HELIX 307 314 {ECO:0000244|PDB:3V2Y}.
HELIX 316 323 {ECO:0000244|PDB:3V2Y}.
SEQUENCE 382 AA; 42811 MW; 0CCE8685A5E1BAD2 CRC64;
MGPTSVPLVK AHRSSVSDYV NYDIIVRHYN YTGKLNISAD KENSIKLTSV VFILICCFII
LENIFVLLTI WKTKKFHRPM YYFIGNLALS DLLAGVAYTA NLLLSGATTY KLTPAQWFLR
EGSMFVALSA SVFSLLAIAI ERYITMLKMK LHNGSNNFRL FLLISACWVI SLILGGLPIM
GWNCISALSS CSTVLPLYHK HYILFCTTVF TLLLLSIVIL YCRIYSLVRT RSRRLTFRKN
ISKASRSSEK SLALLKTVII VLSVFIACWA PLFILLLLDV GCKVKTCDIL FRAEYFLVLA
VLNSGTNPII YTLTNKEMRR AFIRIMSCCK CPSGDSAGKF KRPIIAGMEF SRSKSDNSSH
PQKDEGDNPE TIMSSGNVNS SS


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