S1PR1_RAT
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 03-AUG-2022, entry version 160.
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 GlyGen; P48303; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; P48303; -.
DR PhosphoSitePlus; P48303; -.
DR SwissPalm; P48303; -.
DR PaxDb; P48303; -.
DR PRIDE; P48303; -.
DR Ensembl; ENSRNOT00000018318; ENSRNOP00000052627; ENSRNOG00000013683.
DR GeneID; 29733; -.
DR KEGG; rno:29733; -.
DR UCSC; RGD:61958; rat.
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; HPNKEEV; -.
DR OrthoDB; 981486at2759; -.
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 tissues.
DR Genevisible; P48303; RN.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
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; IBA:GO_Central.
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:0031532; P:actin cytoskeleton reorganization; 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; IEA:Ensembl.
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: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:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IMP:RGD.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA: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 InterPro; IPR000987; EDG1_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004061; S1P_rcpt.
DR PANTHER; PTHR22750:SF16; PTHR22750:SF16; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01523; S1PRECEPTOR.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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
