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P52592 (S1PR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sphingosine 1-phosphate receptor 2

Short name=S1P receptor 2
Short name=S1P2
Alternative name(s):
Endothelial differentiation G-protein coupled receptor 5
Lysophospholipid receptor B2
Sphingosine 1-phosphate receptor Edg-5
Short name=S1P receptor Edg-5
Gene names
Name:S1pr2
Synonyms:Edg5, Gpcr13, Lpb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Tissue specificity

Most abundant in heart and lung; low, but clearly observed in kidney, liver and thymus; much lower but detectable in brain, testis, stomach and intestine. Not significantly detected in any of the sections of embryonic day (E) 14-18, except in embryonic brain. Ref.1

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352Sphingosine 1-phosphate receptor 2
PRO_0000069428

Regions

Topological domain1 – 3434Extracellular By similarity
Transmembrane35 – 5925Helical; Name=1; By similarity
Topological domain60 – 667Cytoplasmic By similarity
Transmembrane67 – 9529Helical; Name=2; By similarity
Topological domain96 – 10914Extracellular By similarity
Transmembrane110 – 12819Helical; Name=3; By similarity
Topological domain129 – 14719Cytoplasmic By similarity
Transmembrane148 – 17326Helical; Name=4; By similarity
Topological domain174 – 18916Extracellular By similarity
Transmembrane190 – 21021Helical; Name=5; By similarity
Topological domain211 – 23323Cytoplasmic By similarity
Transmembrane234 – 25522Helical; Name=6; By similarity
Topological domain256 – 27116Extracellular By similarity
Transmembrane272 – 29221Helical; Name=7; By similarity
Topological domain293 – 35260Cytoplasmic By similarity

Amino acid modifications

Lipidation3051S-palmitoyl cysteine By similarity
Glycosylation191N-linked (GlcNAc...) Ref.7 Ref.8

Experimental info

Sequence conflict1101G → V in AAD16976. Ref.1
Sequence conflict1101G → V in AAA16846. Ref.5
Sequence conflict1661P → S in AAA16846. Ref.5
Sequence conflict1751Q → K in AAA16846. Ref.5
Sequence conflict1891H → R in AAA16846. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P52592 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 6A3E426B0FE54406

FASTA35238,829
        10         20         30         40         50         60 
MGGLYSEYLN PEKVLEHYNY TKETLDMQET TSRKVASAFI IILCCAIVVE NLLVLIAVAR 

        70         80         90        100        110        120 
NSKFHSAMYL FLGNLAASDL LAGVAFVANT LLSGHVTLSL TPVQWFAREG SAFITLSASV 

       130        140        150        160        170        180 
FSLLAIAIER QVALAKVKLY GSDKSCRMLM LIGASWLISL ILGGLPILGW NCLNQLEACS 

       190        200        210        220        230        240 
TVLPLYAKHY VLCVVTIFSV ILLAIVALYV RIYFVVRSSH ADVAGPQTLA LLKTVTIVLG 

       250        260        270        280        290        300 
VFIICWLPAF SILLLDSTCP VRACPVLYKA HYFFAFATLN SLLNPVIYTW RSRDLRREVL 

       310        320        330        340        350 
RPLQCWRRGK GVTGRRGGNP GHRLLPLRSS SSLERGMHMP TSPTFLEGNT VV 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"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. expand/collapse author list , 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 and NOD.
Tissue: Bone marrow, Forelimb and Lung.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
[5]"Identification, chromosomal location, and genome organization of mammalian G-protein-coupled receptors."
Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I., Copeland N.G., Jenkins N.A.
Genomics 18:175-184(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 62-241.
Tissue: Testis.
[6]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-19.
Tissue: Myoblast.
[8]"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-19.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF108020 Genomic DNA. Translation: AAD16976.1.
AK085114 mRNA. Translation: BAC39368.1.
AK134275 mRNA. Translation: BAE22078.1.
AK151062 mRNA. Translation: BAE30079.1.
AK159605 mRNA. Translation: BAE35224.1.
AK170436 mRNA. Translation: BAE41795.1.
CH466522 Genomic DNA. Translation: EDL25146.1.
BC096760 mRNA. Translation: AAH96760.1.
L20334 mRNA. Translation: AAA16846.1.
PIRE48909.
RefSeqNP_034463.2. NM_010333.4.
XP_006510082.1. XM_006510019.1.
UniGeneMm.46493.

3D structure databases

ProteinModelPortalP52592.
SMRP52592. Positions 6-304.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000053394.

Chemistry

GuidetoPHARMACOLOGY276.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP52592.

Proteomic databases

PaxDbP52592.
PRIDEP52592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000054197; ENSMUSP00000053394; ENSMUSG00000043895.
GeneID14739.
KEGGmmu:14739.
UCSCuc009ojt.2. mouse.

Organism-specific databases

CTD9294.
MGIMGI:99569. S1pr2.

Phylogenomic databases

eggNOGNOG149362.
GeneTreeENSGT00750000117544.
HOGENOMHOG000233501.
HOVERGENHBG103071.
InParanoidQ8C3Q7.
KOK04292.
OMADKSCRML.
OrthoDBEOG708W0B.
TreeFamTF330052.

Gene expression databases

BgeeP52592.
GenevestigatorP52592.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR004063. EDG5_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
IPR004061. S1P_rcpt.
[Graphical view]
PANTHERPTHR22750:SF17. PTHR22750:SF17. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR01525. EDG5RECEPTOR.
PR00237. GPCRRHODOPSN.
PR01523. S1PRECEPTOR.
PROSITEPS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSS1PR2. mouse.
NextBio286795.
PROP52592.
SOURCESearch...

Entry information

Entry nameS1PR2_MOUSE
AccessionPrimary (citable) accession number: P52592
Secondary accession number(s): Q8C3Q7, Q9R236
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries