ID   S1PR2_RAT               Reviewed;         352 AA.
AC   P47752; Q54AI6;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=Sphingosine 1-phosphate receptor 2;
DE            Short=S1P receptor 2;
DE            Short=S1P2;
DE   AltName: Full=AGR16;
DE   AltName: Full=Endothelial differentiation G-protein coupled receptor 5;
DE   AltName: Full=G-protein coupled receptor H218;
DE   AltName: Full=Sphingosine 1-phosphate receptor Edg-5;
DE            Short=S1P receptor Edg-5;
GN   Name=S1pr2; Synonyms=Edg5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Aortic smooth muscle;
RX   PubMed=8382486; DOI=10.1006/bbrc.1993.1163;
RA   Okazaki H., Ishizaka N., Sakurai T., Kurokawa K., Goto K., Kumada M.,
RA   Takuwa Y.;
RT   "Molecular cloning of a novel putative G protein-coupled receptor expressed
RT   in the cardiovascular system.";
RL   Biochem. Biophys. Res. Commun. 190:1104-1109(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain, and Lung;
RX   PubMed=8087418; DOI=10.1006/mcne.1994.1024;
RA   Maclennan A.J., Browe C.S., Gaskin A.A., Lado D.C., Shaw G.;
RT   "Cloning and characterization of a putative G-protein coupled receptor
RT   potentially involved in development.";
RL   Mol. Cell. Neurosci. 5:201-209(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=9409733; DOI=10.1016/s0014-5793(97)01301-x;
RA   An S., Bleu T., Huang W., Hallmark O.G., Coughlin S.R., Goetzl E.J.;
RT   "Identification of cDNAs encoding two G protein-coupled receptors for
RT   lysosphingolipids.";
RL   FEBS Lett. 417:279-282(1997).
RN   [4]
RP   PHARMACOLOGICAL CHARACTERIZATION.
RX   PubMed=10383399; DOI=10.1074/jbc.274.27.18997;
RA   Ancellin N., Hla T.;
RT   "Differential pharmacological properties and signal transduction of the
RT   sphingosine 1-phosphate receptors EDG-1, EDG-3, and EDG-5.";
RL   J. Biol. Chem. 274:18997-19002(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=29453251; DOI=10.1161/circulationaha.117.032398;
RA   Wang Y., Chen D., Zhang Y., Wang P., Zheng C., Zhang S., Yu B., Zhang L.,
RA   Zhao G., Ma B., Cai Z., Xie N., Huang S., Liu Z., Mo X., Guan Y., Wang X.,
RA   Fu Y., Ma D., Wang Y., Kong W.;
RT   "Novel Adipokine, FAM19A5, Inhibits Neointima Formation After Injury
RT   Through Sphingosine-1-Phosphate Receptor 2.";
RL   Circulation 138:48-63(2018).
CC   -!- FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate
CC       (S1P) (PubMed:10383399). S1P is a bioactive lysophospholipid that
CC       elicits diverse physiological effects on most types of cells and
CC       tissues (PubMed:10383399). Receptor for the chemokine-like protein
CC       FAM19A5 (PubMed:29453251). Mediates the inhibitory effect of FAM19A5 on
CC       vascular smooth muscle cell proliferation and migration
CC       (PubMed:29453251). {ECO:0000269|PubMed:10383399,
CC       ECO:0000269|PubMed:29453251}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in all developing tissues with highest
CC       levels detected in primitive, transformed cells. Relative abundance:
CC       lung > kidney = skin = gut > spleen > brain > liver.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AB016931; BAA32454.1; -; mRNA.
DR   EMBL; U10699; AAA19241.1; -; mRNA.
DR   EMBL; AF022138; AAC53494.1; -; mRNA.
DR   PIR; JC1465; JC1465.
DR   RefSeq; NP_058888.1; NM_017192.1.
DR   AlphaFoldDB; P47752; -.
DR   SMR; P47752; -.
DR   STRING; 10116.ENSRNOP00000028034; -.
DR   BindingDB; P47752; -.
DR   ChEMBL; CHEMBL3616360; -.
DR   GuidetoPHARMACOLOGY; 276; -.
DR   GlyCosmos; P47752; 1 site, No reported glycans.
DR   GlyGen; P47752; 1 site.
DR   iPTMnet; P47752; -.
DR   PhosphoSitePlus; P47752; -.
DR   PaxDb; 10116-ENSRNOP00000028034; -.
DR   Ensembl; ENSRNOT00000107018.1; ENSRNOP00000080559.1; ENSRNOG00000020653.5.
DR   Ensembl; ENSRNOT00055022387; ENSRNOP00055018159; ENSRNOG00055013081.
DR   Ensembl; ENSRNOT00060048608; ENSRNOP00060040523; ENSRNOG00060027995.
DR   Ensembl; ENSRNOT00065019323; ENSRNOP00065014767; ENSRNOG00065011906.
DR   GeneID; 29415; -.
DR   KEGG; rno:29415; -.
DR   UCSC; RGD:68334; rat.
DR   AGR; RGD:68334; -.
DR   CTD; 9294; -.
DR   RGD; 68334; S1pr2.
DR   eggNOG; ENOG502QVQY; Eukaryota.
DR   GeneTree; ENSGT01050000244887; -.
DR   HOGENOM; CLU_047979_1_0_1; -.
DR   InParanoid; P47752; -.
DR   OrthoDB; 4607247at2759; -.
DR   PhylomeDB; P47752; -.
DR   TreeFam; TF330052; -.
DR   Reactome; R-RNO-418594; G alpha (i) signalling events.
DR   Reactome; R-RNO-419408; Lysosphingolipid and LPA receptors.
DR   PRO; PR:P47752; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000020653; Expressed in lung and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0098794; C:postsynapse; IEA:GOC.
DR   GO; GO:0008528; F:G protein-coupled peptide receptor activity; IDA:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IDA:RGD.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR   GO; GO:0005178; F:integrin binding; ISO:RGD.
DR   GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; ISO:RGD.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0046847; P:filopodium assembly; ISO:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR   GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; ISO:RGD.
DR   GO; GO:0014912; P:negative regulation of smooth muscle cell migration; IGI:MGI.
DR   GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; IGI:MGI.
DR   GO; GO:1903142; P:positive regulation of establishment of endothelial barrier; ISO:RGD.
DR   GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:RGD.
DR   GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR   GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; ISO:RGD.
DR   CDD; cd15347; 7tmA_S1PR2_Edg5; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR004063; EDG5_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   InterPro; IPR004061; S1P_rcpt.
DR   PANTHER; PTHR22750; G-PROTEIN COUPLED RECEPTOR; 1.
DR   PANTHER; PTHR22750:SF17; SPHINGOSINE 1-PHOSPHATE RECEPTOR 2; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR01525; EDG5RECEPTOR.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PRINTS; PR01523; S1PRECEPTOR.
DR   SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR   SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P47752; RN.
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_0000069429"
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   LIPID           305
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        19
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   352 AA;  38735 MW;  9C933A18E756CE1E CRC64;
     MGGLYSEYLN PEKVQEHYNY TKETLDMQET PSRKVASAFI IILCCAIVVE NLLVLIAVAR
     NSKFHSAMYL FLGNLAASDL LAGVAFVANT LLSGPVTLSL TPLQWFAREG SAFITLSASV
     FSLLAIAIER QVAIAKVKLY GSDKSCRMLM LIGASWLISL ILGGLPILGW NCLDHLEACS
     TVLPLYAKHY VLCVVTIFSV ILLAIVALYV RIYFVVRSSH ADVAGPQTLA LLKTVTIVLG
     VFIICWLPAF SILLLDSTCP VRACPVLYKA HYFFAFATLN SLLNPVIYTW RSRDLRREVL
     RPLLCWRQGK GATGRRGGNP GHRLLPLRSS SSLERGLHMP TSPTFLEGNT VV
//