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Sphingosine 1-phosphate receptor 2 (S1P receptor 2) (S1P2) (Endothelial differentiation G-protein coupled receptor 5) (Lysophospholipid receptor B2) (Sphingosine 1-phosphate receptor Edg-5) (S1P receptor Edg-5)

 S1PR2_MOUSE             Reviewed;         352 AA.
P52592; Q8C3Q7; Q9R236;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
25-OCT-2017, entry version 139.
RecName: Full=Sphingosine 1-phosphate receptor 2;
Short=S1P receptor 2;
Short=S1P2;
AltName: Full=Endothelial differentiation G-protein coupled receptor 5;
AltName: Full=Lysophospholipid receptor B2;
AltName: Full=Sphingosine 1-phosphate receptor Edg-5;
Short=S1P receptor Edg-5;
Name=S1pr2; Synonyms=Edg5, Gpcr13, Lpb2;
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], 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Forelimb, 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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 62-241.
TISSUE=Testis;
PubMed=8288218; DOI=10.1006/geno.1993.1452;
Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I.,
Copeland N.G., Jenkins N.A.;
"Identification, chromosomal location, and genome organization of
mammalian G-protein-coupled receptors.";
Genomics 18:175-184(1993).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-19.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[8]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-19.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
-!- 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.
-!- INTERACTION:
Q99P72:Rtn4; NbExp=2; IntAct=EBI-16091339, EBI-3869532;
Q9JK11-1:Rtn4 (xeno); NbExp=3; IntAct=EBI-16091339, EBI-919989;
-!- 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. {ECO:0000269|PubMed:9931453}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
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EMBL; AF108020; AAD16976.1; -; Genomic_DNA.
EMBL; AK085114; BAC39368.1; -; mRNA.
EMBL; AK134275; BAE22078.1; -; mRNA.
EMBL; AK151062; BAE30079.1; -; mRNA.
EMBL; AK159605; BAE35224.1; -; mRNA.
EMBL; AK170436; BAE41795.1; -; mRNA.
EMBL; CH466522; EDL25146.1; -; Genomic_DNA.
EMBL; BC096760; AAH96760.1; -; mRNA.
EMBL; L20334; AAA16846.1; -; mRNA.
CCDS; CCDS22888.1; -.
PIR; E48909; E48909.
RefSeq; NP_034463.2; NM_010333.4.
RefSeq; XP_006510082.1; XM_006510019.3.
UniGene; Mm.46493; -.
ProteinModelPortal; P52592; -.
SMR; P52592; -.
DIP; DIP-60681N; -.
IntAct; P52592; 3.
STRING; 10090.ENSMUSP00000053394; -.
GuidetoPHARMACOLOGY; 276; -.
iPTMnet; P52592; -.
PhosphoSitePlus; P52592; -.
MaxQB; P52592; -.
PaxDb; P52592; -.
PeptideAtlas; P52592; -.
PRIDE; P52592; -.
Ensembl; ENSMUST00000054197; ENSMUSP00000053394; ENSMUSG00000043895.
GeneID; 14739; -.
KEGG; mmu:14739; -.
UCSC; uc009ojt.2; mouse.
CTD; 9294; -.
MGI; MGI:99569; S1pr2.
eggNOG; ENOG410IHTX; Eukaryota.
eggNOG; ENOG41100F8; LUCA.
GeneTree; ENSGT00760000118804; -.
HOGENOM; HOG000233501; -.
HOVERGEN; HBG103071; -.
InParanoid; P52592; -.
KO; K04292; -.
OMA; DYACPVR; -.
OrthoDB; EOG091G0DD4; -.
TreeFam; TF330052; -.
Reactome; R-MMU-418594; G alpha (i) signalling events.
Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors.
ChiTaRS; S1pr2; mouse.
PRO; PR:P52592; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000043895; -.
ExpressionAtlas; P52592; baseline and differential.
Genevisible; P52592; MM.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0001664; F:G-protein coupled receptor binding; ISO:MGI.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; ISO:MGI.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
GO; GO:0046847; P:filopodium assembly; ISO:MGI.
GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IMP:MGI.
GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; ISO:MGI.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:UniProtKB.
GO; GO:0003376; P:sphingosine-1-phosphate signaling pathway; IMP:UniProtKB.
CDD; cd15347; 7tmA_S1PR2_Edg5; 1.
InterPro; IPR004063; EDG5_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
InterPro; IPR004061; S1P_rcpt.
PANTHER; PTHR22750:SF17; PTHR22750:SF17; 1.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR01525; EDG5RECEPTOR.
PRINTS; PR00237; GPCRRHODOPSN.
PRINTS; PR01523; S1PRECEPTOR.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; G-protein coupled receptor;
Glycoprotein; Lipoprotein; Membrane; Palmitate; Receptor;
Reference proteome; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 352 Sphingosine 1-phosphate receptor 2.
/FTId=PRO_0000069428.
TOPO_DOM 1 34 Extracellular. {ECO:0000250}.
TRANSMEM 35 59 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 60 66 Cytoplasmic. {ECO:0000250}.
TRANSMEM 67 95 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 96 109 Extracellular. {ECO:0000250}.
TRANSMEM 110 128 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 129 147 Cytoplasmic. {ECO:0000250}.
TRANSMEM 148 173 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 174 189 Extracellular. {ECO:0000250}.
TRANSMEM 190 210 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 211 233 Cytoplasmic. {ECO:0000250}.
TRANSMEM 234 255 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 256 271 Extracellular. {ECO:0000250}.
TRANSMEM 272 292 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 293 352 Cytoplasmic. {ECO:0000250}.
LIPID 305 305 S-palmitoyl cysteine. {ECO:0000250}.
CARBOHYD 19 19 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:19656770}.
CONFLICT 110 110 G -> V (in Ref. 1; AAD16976 and 5;
AAA16846). {ECO:0000305}.
CONFLICT 166 166 P -> S (in Ref. 5; AAA16846).
{ECO:0000305}.
CONFLICT 175 175 Q -> K (in Ref. 5; AAA16846).
{ECO:0000305}.
CONFLICT 189 189 H -> R (in Ref. 5; AAA16846).
{ECO:0000305}.
SEQUENCE 352 AA; 38829 MW; 6A3E426B0FE54406 CRC64;
MGGLYSEYLN PEKVLEHYNY TKETLDMQET TSRKVASAFI IILCCAIVVE NLLVLIAVAR
NSKFHSAMYL FLGNLAASDL LAGVAFVANT LLSGHVTLSL TPVQWFAREG SAFITLSASV
FSLLAIAIER QVALAKVKLY GSDKSCRMLM LIGASWLISL ILGGLPILGW NCLNQLEACS
TVLPLYAKHY VLCVVTIFSV ILLAIVALYV RIYFVVRSSH ADVAGPQTLA LLKTVTIVLG
VFIICWLPAF SILLLDSTCP VRACPVLYKA HYFFAFATLN SLLNPVIYTW RSRDLRREVL
RPLQCWRRGK GVTGRRGGNP GHRLLPLRSS SSLERGMHMP TSPTFLEGNT VV


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