ID   S1PR1_RAT               Reviewed;         383 AA.
AC   P48303; Q4V7F6;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   24-JAN-2024, entry version 168.
DE   RecName: Full=Sphingosine 1-phosphate receptor 1;
DE            Short=S1P receptor 1;
DE            Short=S1P1;
DE   AltName: Full=Endothelial differentiation G-protein coupled receptor 1;
DE   AltName: Full=Sphingosine 1-phosphate receptor Edg-1;
DE            Short=S1P receptor Edg-1;
DE   AltName: CD_antigen=CD363;
GN   Name=S1pr1; Synonyms=Edg1;
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], AND DEVELOPMENTAL STAGE.
RC   TISSUE=Cerebellum;
RX   PubMed=7959012; DOI=10.1016/0378-1119(94)90171-6;
RA   Lado D.C., Browe C.S., Gaskin A.A., Borden J.M., Maclennan A.J.;
RT   "Cloning of the rat edg-1 immediate-early gene: expression pattern suggests
RT   diverse functions.";
RL   Gene 149:331-336(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: G-protein coupled receptor for the bioactive lysosphingolipid
CC       sphingosine 1-phosphate (S1P) that seems to be coupled to the G(i)
CC       subclass of heteromeric G proteins. Signaling leads to the activation
CC       of RAC1, SRC, PTK2/FAK1 and MAP kinases. Plays an important role in
CC       cell migration, probably via its role in the reorganization of the
CC       actin cytoskeleton and the formation of lamellipodia in response to
CC       stimuli that increase the activity of the sphingosine kinase SPHK1.
CC       Required for normal chemotaxis toward sphingosine 1-phosphate. Required
CC       for normal embryonic heart development and normal cardiac
CC       morphogenesis. Plays an important role in the regulation of sprouting
CC       angiogenesis and vascular maturation. Inhibits sprouting angiogenesis
CC       to prevent excessive sprouting during blood vessel development.
CC       Required for normal egress of mature T-cells from the thymus into the
CC       blood stream and into peripheral lymphoid organs. Plays a role in the
CC       migration of osteoclast precursor cells, the regulation of bone
CC       mineralization and bone homeostasis. Plays a role in responses to
CC       oxidized 1-palmitoyl-2-arachidonoyl-sn-glycero-3-phosphocholine by
CC       pulmonary endothelial cells and in the protection against ventilator-
CC       induced lung injury (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with GNAI1 and GNAI3. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Endosome {ECO:0000250}. Membrane raft
CC       {ECO:0000250}. Note=Recruited to caveolin-enriched plasma membrane
CC       microdomains in response to oxidized 1-palmitoyl-2-arachidonoyl-sn-
CC       glycero-3-phosphocholine. Ligand binding leads to receptor
CC       internalization (By similarity). {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: First detected at embryonic day 15. At postnatal
CC       day 14 detected in skin, spleen, liver, kidney, heart, testicle, lung
CC       and brain. At adulthood is most abundant in brain.
CC       {ECO:0000269|PubMed:7959012}.
CC   -!- PTM: Palmitoylated by ZDHHC5. Palmitoylation is required for targeting
CC       to plasma membrane, enabling G(i) coupling.
CC       {ECO:0000250|UniProtKB:P21453}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; U10303; AAA83418.1; -; mRNA.
DR   EMBL; BC097938; AAH97938.1; -; mRNA.
DR   PIR; I53870; I53870.
DR   RefSeq; NP_058997.1; NM_017301.2.
DR   RefSeq; XP_008759681.1; XM_008761459.2.
DR   AlphaFoldDB; P48303; -.
DR   SMR; P48303; -.
DR   STRING; 10116.ENSRNOP00000052627; -.
DR   BindingDB; P48303; -.
DR   ChEMBL; CHEMBL1914263; -.
DR   GlyCosmos; P48303; 1 site, 2 glycans.
DR   GlyGen; P48303; 1 site, 2 N-linked glycans (1 site).
DR   iPTMnet; P48303; -.
DR   PhosphoSitePlus; P48303; -.
DR   SwissPalm; P48303; -.
DR   PaxDb; 10116-ENSRNOP00000052627; -.
DR   Ensembl; ENSRNOT00000018318.4; ENSRNOP00000052627.1; ENSRNOG00000013683.4.
DR   Ensembl; ENSRNOT00055001746; ENSRNOP00055001361; ENSRNOG00055001051.
DR   Ensembl; ENSRNOT00060001259; ENSRNOP00060000541; ENSRNOG00060000950.
DR   Ensembl; ENSRNOT00065038878; ENSRNOP00065031535; ENSRNOG00065022778.
DR   GeneID; 29733; -.
DR   KEGG; rno:29733; -.
DR   UCSC; RGD:61958; rat.
DR   AGR; RGD:61958; -.
DR   CTD; 1901; -.
DR   RGD; 61958; S1pr1.
DR   eggNOG; ENOG502QSFG; Eukaryota.
DR   GeneTree; ENSGT01050000244887; -.
DR   HOGENOM; CLU_047979_1_0_1; -.
DR   InParanoid; P48303; -.
DR   OMA; LSCCKCP; -.
DR   OrthoDB; 4607247at2759; -.
DR   PhylomeDB; P48303; -.
DR   TreeFam; TF330052; -.
DR   Reactome; R-RNO-419408; Lysosphingolipid and LPA receptors.
DR   PRO; PR:P48303; -.
DR   Proteomes; UP000002494; Chromosome 2.
DR   Bgee; ENSRNOG00000013683; Expressed in Ammon's horn and 19 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IMP:RGD.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; ISO:RGD.
DR   GO; GO:0046625; F:sphingolipid binding; IDA:RGD.
DR   GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; ISS:UniProtKB.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IMP:RGD.
DR   GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR   GO; GO:0001955; P:blood vessel maturation; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISO:RGD.
DR   GO; GO:0003245; P:cardiac muscle tissue growth involved in heart morphogenesis; ISS:UniProtKB.
DR   GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR   GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR   GO; GO:0006935; P:chemotaxis; ISS:UniProtKB.
DR   GO; GO:0045446; P:endothelial cell differentiation; IEP:RGD.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR   GO; GO:0061384; P:heart trabecula morphogenesis; ISS:UniProtKB.
DR   GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR   GO; GO:0030595; P:leukocyte chemotaxis; ISO:RGD.
DR   GO; GO:0051497; P:negative regulation of stress fiber assembly; IDA:RGD.
DR   GO; GO:0030182; P:neuron differentiation; IEP:RGD.
DR   GO; GO:0007200; P:phospholipase C-activating G protein-coupled receptor signaling pathway; IMP:RGD.
DR   GO; GO:0030335; P:positive regulation of cell migration; IDA:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0050927; P:positive regulation of positive chemotaxis; IDA:RGD.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR   GO; GO:0030500; P:regulation of bone mineralization; ISS:UniProtKB.
DR   GO; GO:0045124; P:regulation of bone resorption; ISS:UniProtKB.
DR   GO; GO:0030155; P:regulation of cell adhesion; 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; ISS:UniProtKB.
DR   GO; GO:0072678; P:T cell migration; ISS:UniProtKB.
DR   GO; GO:0019226; P:transmission of nerve impulse; IEP:RGD.
DR   CDD; cd15346; 7tmA_S1PR1_Edg1; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR000987; EDG1.
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:SF16; SPHINGOSINE 1-PHOSPHATE RECEPTOR 1; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00642; EDG1RECEPTOR.
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; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
DR   Genevisible; P48303; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Angiogenesis; Cell membrane; Chemotaxis; Disulfide bond;
KW   Endosome; G-protein coupled receptor; Glycoprotein; Lipoprotein; Membrane;
KW   Palmitate; Phosphoprotein; Receptor; Reference proteome; Transducer;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..383
FT                   /note="Sphingosine 1-phosphate receptor 1"
FT                   /id="PRO_0000069414"
FT   TOPO_DOM        1..47
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        48..69
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        70..83
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        84..105
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        106..117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        118..139
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        140..161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        162..183
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        184..197
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        198..225
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        226..258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        259..279
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        280..290
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        291..311
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000250"
FT   TOPO_DOM        312..383
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          349..383
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        369..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         121..122
FT                   /ligand="sphing-4-enine 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:60119"
FT                   /evidence="ECO:0000250"
FT   BINDING         266..270
FT                   /ligand="sphing-4-enine 1-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:60119"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:O08530"
FT   MOD_RES         237
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P21453"
FT   MOD_RES         352
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         354
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000255"
FT   LIPID           329
FT                   /note="S-palmitoyl cysteine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        185..192
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT   DISULFID        283..288
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   383 AA;  42746 MW;  090BA6AEE09DB4F3 CRC64;
     MVSSTSIPVV KALRSQVSDY GNYDIIVRHY NYTGKLNIGV EKDHGIKLTS VVFILICCLI
     ILENIFVLLT IWKTKKFHRP MYYFIGNLAL SDLLAGVAYT ANLLLSGATT YKLTPAQWFL
     REGSMFVALS ASVFSLLAIA IERYITMLKM KLHNGSNSSR SFLLISACWV ISLILGGLPI
     MGWNCISSLS SCSTVLPLYH KHYILFCTTV FTLLLLSIVI LYCRIYSLVR TRSRRLTFRK
     NISKASRSSE KSLALLKTVI IVLSVFIACW APLFILLLLD VGCKAKTCDI LYKAEYFLVL
     AVLNSGTNPI IYTLTNKEMR RAFIRIISCC KCPNGDSAGK FKRPIIPGME FSRSKSDNSS
     HPQKDDGDNP ETIMSSGNVN SSS
//