S1PR1_BOVIN
ID S1PR1_BOVIN Reviewed; 382 AA.
AC Q5E9P3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: S1P-induced endothelial cell migration requires the PKB/AKT1-
CC mediated phosphorylation of the third intracellular loop at the Thr-236
CC residue. {ECO:0000250}.
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; BT020877; AAX08894.1; -; mRNA.
DR EMBL; BC114045; AAI14046.1; -; mRNA.
DR RefSeq; NP_001013603.2; NM_001013585.4.
DR AlphaFoldDB; Q5E9P3; -.
DR SMR; Q5E9P3; -.
DR STRING; 9913.ENSBTAP00000007861; -.
DR PaxDb; Q5E9P3; -.
DR Ensembl; ENSBTAT00000007861; ENSBTAP00000007861; ENSBTAG00000005990.
DR GeneID; 281135; -.
DR KEGG; bta:281135; -.
DR CTD; 1901; -.
DR VEuPathDB; HostDB:ENSBTAG00000005990; -.
DR VGNC; VGNC:34252; S1PR1.
DR eggNOG; ENOG502QSFG; Eukaryota.
DR GeneTree; ENSGT01050000244887; -.
DR HOGENOM; CLU_047979_1_0_1; -.
DR InParanoid; Q5E9P3; -.
DR OMA; HPNKEEV; -.
DR OrthoDB; 981486at2759; -.
DR TreeFam; TF330052; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000005990; Expressed in bone marrow and 101 other tissues.
DR ExpressionAtlas; Q5E9P3; baseline and differential.
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; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0001955; P:blood vessel maturation; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
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:0061384; P:heart trabecula morphogenesis; ISS:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:0030595; P:leukocyte chemotaxis; IEA:Ensembl.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
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; IEA:Ensembl.
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 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 2: Evidence at transcript 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..382
FT /note="Sphingosine 1-phosphate receptor 1"
FT /id="PRO_0000244621"
FT TOPO_DOM 1..46
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 47..68
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 69..82
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 83..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 105..116
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 117..138
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 139..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 161..182
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 183..196
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 197..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 225..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 258..278
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 279..289
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 290..310
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 311..382
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 349..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 120..121
FT /ligand="sphing-4-enine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:60119"
FT /evidence="ECO:0000250"
FT BINDING 265..269
FT /ligand="sphing-4-enine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:60119"
FT /evidence="ECO:0000250"
FT MOD_RES 10
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O08530"
FT MOD_RES 236
FT /note="Phosphothreonine; by PKB/AKT1"
FT /evidence="ECO:0000250|UniProtKB:P21453"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08530"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000255"
FT LIPID 328
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 184..191
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 282..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 382 AA; 42949 MW; 81C19138BDFB8880 CRC64;
MGSTRIPLVK ALHSPVSDYV NYDIIVRHYN YTGKLKISAD KDNGIKLISV VFILICCFII
LENIFVLLTI WKTKKFHRPM YYFIGNLALS DLLAGVAYTA NLLLSGATTY KLTPAQWFLR
EGSMFVALSA SVFSLLAIAI ERYITMLKMK LHNGSNRFRS FLLISACWVI SLILGGLPIM
GWNCISTLPS CSTVLPLYHK HYILFCTTVF TLLLLSIVIL YCRIYSLVRT RSRRLTFRKN
ISKASRSSEK SLALLKTVII VLGVFIACWA PLFILLLLDV GCKVKTCDIL FRTEYFLVLA
VLNSGTNPII YTLSNKEMRR AFVRIMSCCK CPSRDSASKF TRPIIAGMEF SRSKSDNSSH
PQKDDGDNPE TIMSSGNVNS SS
