S1PR2_MOUSE
ID S1PR2_MOUSE Reviewed; 352 AA.
AC P52592; Q8C3Q7; Q9R236;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Sphingosine 1-phosphate receptor 2;
DE Short=S1P receptor 2;
DE Short=S1P2;
DE AltName: Full=Endothelial differentiation G-protein coupled receptor 5;
DE AltName: Full=Lysophospholipid receptor B2;
DE AltName: Full=Sphingosine 1-phosphate receptor Edg-5;
DE Short=S1P receptor Edg-5;
GN Name=S1pr2; Synonyms=Edg5, Gpcr13, Lpb2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=129/SvJ;
RX PubMed=9931453; DOI=10.1016/s0378-1119(98)00589-7;
RA Zhang G., Contos J.J.A., Weiner J.A., Fukushima N., Chun J.;
RT "Comparative analysis of three murine G-protein coupled receptors activated
RT by sphingosine-1-phosphate.";
RL Gene 227:89-99(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Forelimb, and Lung;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 62-241.
RC TISSUE=Testis;
RX PubMed=8288218; DOI=10.1006/geno.1993.1452;
RA Wilkie T.M., Chen Y., Gilbert D.J., Moore K.J., Yu L., Simon M.I.,
RA Copeland N.G., Jenkins N.A.;
RT "Identification, chromosomal location, and genome organization of mammalian
RT G-protein-coupled receptors.";
RL Genomics 18:175-184(1993).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-19.
RC TISSUE=Myoblast;
RX PubMed=19656770; DOI=10.1074/mcp.m900195-mcp200;
RA Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D.,
RA Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.;
RT "The mouse C2C12 myoblast cell surface N-linked glycoproteome:
RT identification, glycosite occupancy, and membrane orientation.";
RL Mol. Cell. Proteomics 8:2555-2569(2009).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-19.
RX PubMed=19349973; DOI=10.1038/nbt.1532;
RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
RA Schiess R., Aebersold R., Watts J.D.;
RT "Mass-spectrometric identification and relative quantification of N-linked
RT cell surface glycoproteins.";
RL Nat. Biotechnol. 27:378-386(2009).
CC -!- FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate
CC (S1P) (By similarity). S1P is a bioactive lysophospholipid that elicits
CC diverse physiological effects on most types of cells and tissues (By
CC similarity). Receptor for the chemokine-like protein FAM19A5 (By
CC similarity). Mediates the inhibitory effect of FAM19A5 on vascular
CC smooth muscle cell proliferation and migration (By similarity).
CC {ECO:0000250|UniProtKB:P47752}.
CC -!- INTERACTION:
CC P52592; Q99P72: Rtn4; NbExp=2; IntAct=EBI-16091339, EBI-3869532;
CC P52592; Q9JK11-1: Rtn4; Xeno; NbExp=3; IntAct=EBI-16091339, EBI-919989;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Most abundant in heart and lung; low, but clearly
CC observed in kidney, liver and thymus; much lower but detectable in
CC brain, testis, stomach and intestine. Not significantly detected in any
CC of the sections of embryonic day (E) 14-18, except in embryonic brain.
CC {ECO:0000269|PubMed:9931453}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF108020; AAD16976.1; -; Genomic_DNA.
DR EMBL; AK085114; BAC39368.1; -; mRNA.
DR EMBL; AK134275; BAE22078.1; -; mRNA.
DR EMBL; AK151062; BAE30079.1; -; mRNA.
DR EMBL; AK159605; BAE35224.1; -; mRNA.
DR EMBL; AK170436; BAE41795.1; -; mRNA.
DR EMBL; CH466522; EDL25146.1; -; Genomic_DNA.
DR EMBL; BC096760; AAH96760.1; -; mRNA.
DR EMBL; L20334; AAA16846.1; -; mRNA.
DR CCDS; CCDS22888.1; -.
DR PIR; E48909; E48909.
DR RefSeq; NP_034463.2; NM_010333.4.
DR RefSeq; XP_006510082.1; XM_006510019.3.
DR AlphaFoldDB; P52592; -.
DR SMR; P52592; -.
DR DIP; DIP-60681N; -.
DR IntAct; P52592; 3.
DR STRING; 10090.ENSMUSP00000053394; -.
DR GuidetoPHARMACOLOGY; 276; -.
DR GlyGen; P52592; 1 site.
DR iPTMnet; P52592; -.
DR PhosphoSitePlus; P52592; -.
DR SwissPalm; P52592; -.
DR MaxQB; P52592; -.
DR PaxDb; P52592; -.
DR PeptideAtlas; P52592; -.
DR PRIDE; P52592; -.
DR ProteomicsDB; 260751; -.
DR Antibodypedia; 65016; 327 antibodies from 34 providers.
DR DNASU; 14739; -.
DR Ensembl; ENSMUST00000054197; ENSMUSP00000053394; ENSMUSG00000043895.
DR GeneID; 14739; -.
DR KEGG; mmu:14739; -.
DR UCSC; uc009ojt.2; mouse.
DR CTD; 9294; -.
DR MGI; MGI:99569; S1pr2.
DR VEuPathDB; HostDB:ENSMUSG00000043895; -.
DR eggNOG; ENOG502QVQY; Eukaryota.
DR GeneTree; ENSGT01050000244887; -.
DR HOGENOM; CLU_047979_1_0_1; -.
DR InParanoid; P52592; -.
DR OMA; CPVRACP; -.
DR OrthoDB; 981486at2759; -.
DR PhylomeDB; P52592; -.
DR TreeFam; TF330052; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR Reactome; R-MMU-419408; Lysosphingolipid and LPA receptors.
DR BioGRID-ORCS; 14739; 3 hits in 72 CRISPR screens.
DR ChiTaRS; S1pr2; mouse.
DR PRO; PR:P52592; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P52592; protein.
DR Bgee; ENSMUSG00000043895; Expressed in decidua and 187 other tissues.
DR ExpressionAtlas; P52592; baseline and differential.
DR Genevisible; P52592; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0008528; F:G protein-coupled peptide receptor activity; ISO:MGI.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
DR GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; ISO:MGI.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISO:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0046847; P:filopodium assembly; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IMP:MGI.
DR GO; GO:0014912; P:negative regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; ISO:MGI.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IMP:UniProtKB.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; IMP:UniProtKB.
DR InterPro; IPR004063; EDG5_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004061; S1P_rcpt.
DR PANTHER; PTHR22750:SF17; PTHR22750:SF17; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR01525; EDG5RECEPTOR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01523; S1PRECEPTOR.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Lipoprotein;
KW Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..352
FT /note="Sphingosine 1-phosphate receptor 2"
FT /id="PRO_0000069428"
FT TOPO_DOM 1..34
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 35..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 60..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 67..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 96..109
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 110..128
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 129..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 148..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 174..189
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 190..210
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 211..233
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 234..255
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 256..271
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 272..292
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 293..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 333..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 305
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973,
FT ECO:0000269|PubMed:19656770"
FT CONFLICT 110
FT /note="G -> V (in Ref. 1; AAD16976 and 5; AAA16846)"
FT /evidence="ECO:0000305"
FT CONFLICT 166
FT /note="P -> S (in Ref. 5; AAA16846)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="Q -> K (in Ref. 5; AAA16846)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="H -> R (in Ref. 5; AAA16846)"
FT /evidence="ECO:0000305"
SQ 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
