Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00653
Entry Name
UniProt Accession
Theoretical PI
9.59
Molecular Weight
42810.79
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Sphingosine 1-phosphate receptor 1
Protein Synonyms/Alias
S1P receptor 1; S1P1; Endothelial differentiation G-protein coupled receptor 1; Sphingosine 1-phosphate receptor Edg-1; S1P receptor Edg-1; CD363;
Gene Name
S1PR1
Gene Synonyms/Alias
CHEDG1; EDG1;
Created Date
01-MAY-1991
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
328
Canonical
AFIRIMSCCKCPSGD
[1]
S-Palmitoylation
329
Canonical
FIRIMSCCKCPSGDS
[1]
S-Palmitoylation
331
Canonical
RIMSCCKCPSGDSAG
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Ohno Y, Ito A, Ogata R, Hiraga Y, Igarashi Y, Kihara A. Palmitoylation of the sphingosine 1-phosphate receptor S1P is involved in its signaling functions andinternalization. Genes Cells. 2009 Aug;14(8):911-23. doi:10.1111/j.1365-2443.2009.01319.x. Epub 2009 Jul 10.[PMID:19619245]
Functional Description
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.
Sequence Annotation
Topological domain: 2 46 Extracellular.
Transmembrane: 47 68 Helical; Name=1.
Topological domain: 69 82 Cytoplasmic.
Transmembrane: 83 104 Helical; Name=2.
Topological domain: 105 116 Extracellular.
Transmembrane: 117 138 Helical; Name=3.
Topological domain: 139 160 Cytoplasmic.
Transmembrane: 161 182 Helical; Name=4.
Topological domain: 183 196 Extracellular.
Transmembrane: 197 224 Helical; Name=5.
Topological domain: 225 257 Cytoplasmic.
Transmembrane: 258 278 Helical; Name=6.
Topological domain: 279 289 Extracellular.
Transmembrane: 290 310 Helical; Name=7.
Topological domain: 311 382 Cytoplasmic.
Region: 120 121 Sphingosine 1-phosphate binding.
Region: 265 269 Sphingosine 1-phosphate binding.
Modified residue: 10 10 N6-acetyllysine.
Modified residue: 236 236 Phosphothreonine; by PKB/AKT1.
Modified residue: 353 353 Phosphoserine.
Protein Length
382 AA.
Protein Sequence
(Canonical)
MGPTSVPLVK AHRSSVSDYV NYDIIVRHYN YTGKLNISAD KENSIKLTSV VFILICCFII  60
LENIFVLLTI WKTKKFHRPM YYFIGNLALS DLLAGVAYTA NLLLSGATTY KLTPAQWFLR  120
EGSMFVALSA SVFSLLAIAI ERYITMLKMK LHNGSNNFRL FLLISACWVI SLILGGLPIM  180
GWNCISALSS CSTVLPLYHK HYILFCTTVF TLLLLSIVIL YCRIYSLVRT RSRRLTFRKN  240
ISKASRSSEK SLALLKTVII VLSVFIACWA PLFILLLLDV GCKVKTCDIL FRAEYFLVLA  300
VLNSGTNPII YTLTNKEMRR AFIRIMSCCK CPSGDSAGKF KRPIIAGMEF SRSKSDNSSH  360
PQKDEGDNPE TIMSSGNVNS SS                                           382
FASTA
(Canonical)
>LipidDB-9606-00653|P21453
MGPTSVPLVKAHRSSVSDYVNYDIIVRHYNYTGKLNISADKENSIKLTSVVFILICCFII
LENIFVLLTIWKTKKFHRPMYYFIGNLALSDLLAGVAYTANLLLSGATTYKLTPAQWFLR
EGSMFVALSASVFSLLAIAIERYITMLKMKLHNGSNNFRLFLLISACWVISLILGGLPIM
GWNCISALSSCSTVLPLYHKHYILFCTTVFTLLLLSIVILYCRIYSLVRTRSRRLTFRKN
ISKASRSSEKSLALLKTVIIVLSVFIACWAPLFILLLLDVGCKVKTCDILFRAEYFLVLA
VLNSGTNPIIYTLTNKEMRRAFIRIMSCCKCPSGDSAGKFKRPIIAGMEFSRSKSDNSSH
PQKDEGDNPETIMSSGNVNSSS
Gene Ontology
GO:0005768; C:endosome; IEA:UniProtKB-KW
GO:0009897; C:external side of plasma membrane; IEA:Ensembl
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0004930; F:G-protein coupled receptor activity; TAS:ProtInc
GO:0001664; F:G-protein coupled receptor binding; IPI:UniProtKB
GO:0046625; F:sphingolipid binding; IEA:Ensembl
GO:0038036; F:sphingosine-1-phosphate receptor activity; IDA:UniProtKB
GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB
GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; IEA:Ensembl
GO:0001525; P:angiogenesis; IEA:UniProtKB-KW
GO:0001955; P:blood vessel maturation; ISS:UniProtKB
GO:0007420; P:brain development; IEA:Ensembl
GO:0003245; P:cardiac muscle tissue growth involved in heart morphogenesis; ISS:UniProtKB
GO:0007155; P:cell adhesion; TAS:ProtInc
GO:0016477; P:cell migration; ISS:UniProtKB
GO:0006935; P:chemotaxis; ISS:UniProtKB
GO:0045446; P:endothelial cell differentiation; IEA:Ensembl
GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:ProtInc
GO:0061384; P:heart trabecula morphogenesis; ISS:UniProtKB
GO:0030032; P:lamellipodium assembly; ISS:UniProtKB
GO:0051497; P:negative regulation of stress fiber assembly; IEA:Ensembl
GO:0030182; P:neuron differentiation; IEA:Ensembl
GO:0030335; P:positive regulation of cell migration; IEA:Ensembl
GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway; IEA:Ensembl
GO:0050927; P:positive regulation of positive chemotaxis; IEA:Ensembl
GO:0032320; P:positive regulation of Ras GTPase activity; IEA:Ensembl
GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl
GO:0030500; P:regulation of bone mineralization; ISS:UniProtKB
GO:0045124; P:regulation of bone resorption; ISS:UniProtKB
GO:0030155; P:regulation of cell adhesion; IEA:Ensembl
GO:0003376; P:sphingosine-1-phosphate signaling pathway; IDA:UniProtKB
GO:0072678; P:T cell migration; ISS:UniProtKB
GO:0019226; P:transmission of nerve impulse; IEA:Ensembl
Interpro
InterPro; IPR000987; EDG1_rcpt
InterPro; IPR000276; GPCR_Rhodpsn
InterPro; IPR017452; GPCR_Rhodpsn_7TM
InterPro; IPR004061; S1P_rcpt
Pfam
Pfam; PF00001; 7tm_1;
SMART
PROSITE
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1;
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2;
PRINTS
PRINTS; PR00642; EDG1RECEPTOR;
PRINTS; PR00237; GPCRRHODOPSN;
PRINTS; PR01523; S1PRECEPTOR;