O08530 (S1PR1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sphingosine 1-phosphate receptor 1
Short name=S1P receptor 1
Short name=S1P1

Alternative name(s):
Endothelial differentiation G-protein coupled receptor 1
Lysophospholipid receptor B1
Sphingosine 1-phosphate receptor Edg-1
Short name=S1P receptor Edg-1
CD_antigen=CD363

Gene names

Name:	S1pr1
Synonyms:	Edg1, Lpb1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	382 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Receptor for the lysosphingolipid sphingosine 1-phosphate (S1P). S1P is a bioactive lysophospholipid that elicits diverse physiological effect on most types of cells and tissues. This inducible epithelial cell G-protein-coupled receptor may be involved in the processes that regulate the differentiation of endothelial cells. Seems to be coupled to the G(i) subclass of heteromeric G proteins By similarity. Ref.6
Subcellular location	Cell membrane; Multi-pass membrane protein.
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 Ref.2, expressed modestly in apparent endothelial cells surrounding some blood vessels (e.g. aortic trunk). Ref.2
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Glycoprotein Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Inferred from direct assay PubMed 11443127. Source: MGI angiogenesis Inferred from direct assay PubMed 15371328. Source: MGI brain development Inferred from mutant phenotype PubMed 16314531. Source: MGI elevation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathway Inferred from electronic annotation. Source: Compara endothelial cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of stress fiber assembly Inferred from electronic annotation. Source: Compara neuron differentiation Inferred from electronic annotation. Source: Compara positive regulation of Ras GTPase activity Inferred from electronic annotation. Source: Compara positive regulation of cell migration Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from mutant phenotype PubMed 16314531. Source: MGI positive regulation of positive chemotaxis Inferred from electronic annotation. Source: Compara positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara regulation of cell adhesion Inferred from direct assay PubMed 15371328. Source: MGI sphingosine-1-phosphate signaling pathway Inferred from electronic annotation. Source: GOC transmission of nerve impulse Inferred from electronic annotation. Source: Compara
Cellular_component	external side of plasma membrane Inferred from mutant phenotype PubMed 18836449. Source: MGI integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	sphingolipid binding Inferred from electronic annotation. Source: Compara sphingosine-1-phosphate receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 382	382	Sphingosine 1-phosphate receptor 1		PRO_0000069413
Regions
	Topological domain	1 – 46	46	Extracellular By similarity
	Transmembrane	47 – 71	25	Helical; Name=1; By similarity
	Topological domain	72 – 78	7	Cytoplasmic By similarity
	Transmembrane	79 – 107	29	Helical; Name=2; By similarity
	Topological domain	108 – 121	14	Extracellular By similarity
	Transmembrane	122 – 140	19	Helical; Name=3; By similarity
	Topological domain	141 – 159	19	Cytoplasmic By similarity
	Transmembrane	160 – 185	26	Helical; Name=4; By similarity
	Topological domain	186 – 201	16	Extracellular By similarity
	Transmembrane	202 – 222	21	Helical; Name=5; By similarity
	Topological domain	223 – 256	34	Cytoplasmic By similarity
	Transmembrane	257 – 278	22	Helical; Name=6; By similarity
	Topological domain	279 – 294	16	Extracellular By similarity
	Transmembrane	295 – 315	21	Helical; Name=7; By similarity
	Topological domain	316 – 382	67	Cytoplasmic By similarity
Amino acid modifications
	Modified residue	236	1	Phosphothreonine By similarity
	Modified residue	353	1	Phosphoserine Potential
	Lipidation	328	1	S-palmitoyl cysteine By similarity
	Glycosylation	30	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	179	1	I → S in AAC53294. Ref.1
	Sequence conflict	179	1	I → S in AAD16975. Ref.2
	Sequence conflict	218	1	V → A in AAC53294. Ref.1
	Sequence conflict	244	1	A → G in AAC53294. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O08530 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 5FE4C9A2BD65CB2A	FASTA	382	42,639
	10 20 30 40 50 60 MVSTSIPEVK ALRSSVSDYG NYDIIVRHYN YTGKLNIGAE KDHGIKLTSV VFILICCFII 70 80 90 100 110 120 LENIFVLLTI WKTKKFHRPM YYFIGNLALS DLLAGVAYTA NLLLSGATTY KLTPAQWFLR 130 140 150 160 170 180 EGSMFVALSA SVFSLLAIAI ERYITMLKMK LHNGSNSSRS FLLISACWVI SLILGGLPIM 190 200 210 220 230 240 GWNCISSLSS CSTVLPLYHK HYILFCTTVF TLLLLSIVIL YCRIYSLVRT RSRRLTFRKN 250 260 270 280 290 300 ISKASRSSEK SLALLKTVII VLSVFIACWA PLFILLLLDV GCKAKTCDIL YKAEYFLVLA 310 320 330 340 350 360 VLNSGTNPII YTLTNKEMRR AFIRIVSCCK CPNGDSAGKF KRPIIPGMEF SRSKSDNSSH 370 380 PQKDDGDNPE TIMSSGNVNS SS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The mouse gene for the inducible G-protein-coupled receptor edg-1." Liu C.H., Hla T. Genomics 43:15-24(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: BALB/c. Tissue: Liver.
[2]	"Comparative analysis of three murine G-protein coupled receptors activated by sphingosine-1-phosphate." Zhang G., Contos J.J.A., Weiner J.A., Fukushima N., Chun J. Gene 227:89-99(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY. Strain: 129/SvJ.
[3]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Heart and Lung.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Eye.
[6]	"Role of the sphingosine-1-phosphate receptor EDG-1 in PDGF-induced cell motility." Hobson J.P., Rosenfeldt H.M., Barak L.S., Olivera A., Poulton S., Caron M.G., Milstien S., Spiegel S. Science 291:1800-1803(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U40811 Genomic DNA. Translation: AAC53294.1. AF108019 Genomic DNA. Translation: AAD16975.1. AK004591 mRNA. Translation: BAB23393.1. AK146501 mRNA. Translation: BAE27216.1. CH466532 Genomic DNA. Translation: EDL12402.1. BC049094 mRNA. Translation: AAH49094.1. BC051023 mRNA. Translation: AAH51023.1.
IPI	IPI00308940.
RefSeq	NP_031927.2. NM_007901.5.
UniGene	Mm.982.
3D structure databases
ProteinModelPortal	O08530.
SMR	O08530. Positions 16-326.
ModBase	Search...
Protein-protein interaction databases
IntAct	O08530. 1 interaction.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	O08530.
Proteomic databases
PaxDb	O08530.
PRIDE	O08530.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000055676; ENSMUSP00000050897; ENSMUSG00000045092.
GeneID	13609.
KEGG	mmu:13609.
Organism-specific databases
CTD	1901.
MGI	MGI:1096355. S1pr1.
Phylogenomic databases
eggNOG	NOG148018.
GeneTree	ENSGT00700000104088.
HOGENOM	HOG000233501.
HOVERGEN	HBG103071.
InParanoid	Q9DC35.
KO	K04288.
OMA	SAFIACW.
OrthoDB	EOG418BNR.
Gene expression databases
ArrayExpress	O08530.
Bgee	O08530.
Genevestigator	O08530.
GermOnline	ENSMUSG00000045092. Mus musculus.
Family and domain databases
InterPro	IPR000987. EDG1_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. IPR004061. S1P_rcpt. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00642. EDG1RECEPTOR. PR00237. GPCRRHODOPSN. PR01523. S1PRECEPTOR.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	O08530.
ChEMBL	CHEMBL1914262.
NextBio	284254.
SOURCE	Search...

Entry information

Entry name

S1PR1_MOUSE

Accession

Primary (citable) accession number: O08530
Secondary accession number(s): Q9DC35, Q9R235

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 113 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program