S1PR1_DANRE
ID S1PR1_DANRE Reviewed; 362 AA.
AC Q9DDK4; Q6DI49;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Sphingosine 1-phosphate receptor 1;
DE Short=S1P receptor 1;
DE Short=S1P1;
DE AltName: Full=Sphingosine 1-phosphate receptor Edg-1;
DE Short=S1P receptor Edg-1;
GN Name=s1pr1; Synonyms=edg1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG45430.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11112429; DOI=10.1006/bbrc.2000.3933;
RA Im D.-S., Ungar A.R., Lynch K.R.;
RT "Characterization of a zebrafish (Danio rerio) sphingosine 1-phosphate
RT receptor expressed in the embryonic brain.";
RL Biochem. Biophys. Res. Commun. 279:139-143(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH75741.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH75741.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-2004) 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.
CC {ECO:0000269|PubMed:11112429}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: Embryonic brain. Not detected during blastula or
CC gastrula stages. At the 4-5 somite stage, expressed in the diencephalon
CC just posterior to the optic vesicles, and weakly in the hindbrain. By
CC the 14 somite stage, there is widespread expression in the CNS,
CC particularly in the ventral diencephalon, optic stalks and anterior
CC hindbrain. {ECO:0000269|PubMed:11112429}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF321294; AAG45430.1; -; mRNA.
DR EMBL; BC075741; AAH75741.1; -; mRNA.
DR PIR; JC7559; JC7559.
DR RefSeq; NP_571766.3; NM_131691.3.
DR AlphaFoldDB; Q9DDK4; -.
DR SMR; Q9DDK4; -.
DR STRING; 7955.ENSDARP00000062632; -.
DR PaxDb; Q9DDK4; -.
DR GeneID; 64617; -.
DR KEGG; dre:64617; -.
DR CTD; 1901; -.
DR ZFIN; ZDB-GENE-001228-2; s1pr1.
DR eggNOG; ENOG502QSFG; Eukaryota.
DR InParanoid; Q9DDK4; -.
DR OrthoDB; 981486at2759; -.
DR PhylomeDB; Q9DDK4; -.
DR Reactome; R-DRE-419408; Lysosphingolipid and LPA receptors.
DR PRO; PR:Q9DDK4; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IC:UniProtKB.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
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:0070915; F:lysophosphatidic acid receptor activity; IDA:UniProtKB.
DR GO; GO:0038036; F:sphingosine-1-phosphate receptor activity; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:ZFIN.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0008078; P:mesodermal cell migration; IGI:ZFIN.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IMP:ZFIN.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:ZFIN.
DR GO; GO:0060312; P:regulation of blood vessel remodeling; IMP:ZFIN.
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:0002040; P:sprouting angiogenesis; IMP:ZFIN.
DR GO; GO:0001944; P:vasculature development; IMP:ZFIN.
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 Cell membrane; Chemotaxis; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..362
FT /note="Sphingosine 1-phosphate receptor 1"
FT /id="PRO_0000069415"
FT TOPO_DOM 1..25
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 26..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 48..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 62..83
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 84..95
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 96..117
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 118..139
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 140..161
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 162..175
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 176..203
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 204..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 239..259
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 260..270
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 271..291
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 292..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 328..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99..100
FT /ligand="sphing-4-enine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:60119"
FT /evidence="ECO:0000250"
FT BINDING 246..250
FT /ligand="sphing-4-enine 1-phosphate"
FT /ligand_id="ChEBI:CHEBI:60119"
FT /evidence="ECO:0000250"
FT LIPID 309
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P18871"
FT CARBOHYD 10
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 163..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 263..268
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 167
FT /note="M -> I (in Ref. 1; AAG45430)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 362 AA; 40601 MW; EF779D90CF6108C3 CRC64;
MDDLIARHYN FTGKFRKVHK DPGLKADSVV FIIVCCFIIL ENVLVLLTIW RTKKFHKPMY
YFIGNLALSD LLAGVVYTAN ILLSGANTYK LTPTQWFFRE GSMFVALAAS VFSLLAIAIE
RHLTMLKMKL HNNGKTCRVF MLISTVWFIA AILGGLPVMG WNCIDSMNNC STVLPLYHKA
YILFCTTVFS VILMAIVILY ARIYALVRTR SRKLVFRKVA NGRGSNKSSE KSMALLKTVI
IVLSCFIACW APLFILLLLD VACQTLTCSI LYKAEWFLAL AVLNSAMNPL IYTLTSNEMR
RAFIKMLNCG VCVQPSGKFS RPIMGAEFSR SKSDNSSHPN KDEPEYSPRE TIVSSGNITS
SS
