S1PR2_DANRE
ID S1PR2_DANRE Reviewed; 370 AA.
AC Q9I8K8;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Sphingosine 1-phosphate receptor 2;
DE Short=S1P receptor 2;
DE Short=S1P2;
DE AltName: Full=Sphingosine 1-phosphate receptor Edg-5;
DE Short=S1P receptor Edg-5;
GN Name=s1pr2; Synonyms=edg5;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND VARIANTS MIL HIS-150 AND CYS-167.
RX PubMed=10910360; DOI=10.1038/35018092;
RA Kupperman E., An S., Osborne N., Waldron S., Stainier D.Y.R.;
RT "A sphingosine-1-phosphate receptor regulates cell migration during
RT vertebrate heart development.";
RL Nature 406:192-195(2000).
CC -!- FUNCTION: Receptor for the lysosphingolipid sphingosine 1-phosphate
CC (S1P) (PubMed:10910360). S1P receptor is critical for cell migration
CC and epithelial integrity during vertebrate embryogenesis
CC (PubMed:10910360). Receptor for the chemokine-like protein FAM19A5 (By
CC similarity). Mediates the inhibitory effect of FAM19A5 on vascular
CC smooth muscle cell proliferation and migration (By similarity).
CC {ECO:0000250|UniProtKB:P47752, ECO:0000269|PubMed:10910360}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- DEVELOPMENTAL STAGE: The expression pattern is complex and dynamic.
CC Maternal expression is found in a diffuse pattern throughout the
CC blastoderm, and this pattern persists through the onset of
CC gastrulation. More pronounced expression can be seen at tailbud stage
CC in the anterior portion of the embryo and along the embryonic axis, and
CC at the 16-somite stage in the midbrain/hindbrain boundary and the tip
CC of the tail where blisters later develop in receptor mutants. At the
CC 18-somite stage, expression appears just lateral to the midline, and as
CC the myocardial precursors migrate to the midline, their location
CC overlaps with this domain of receptor expression.
CC -!- DISEASE: Note=Defects in s1pr2 are a cause of heart development
CC abnormality named miles apart (mil). In all vertebrates, the myocardial
CC progenitors involute early during gastrulation and come to occupy
CC bilateral positions in the anterior lateral plate mesoderm (LPM).
CC During somitogenesis, these cells undergo a second phase of migration
CC toward the midline and fuse to form the definitive heart tube. Defects
CC in S1PR2 disrupt this process, leading to the formation of two
CC laterally positioned hearts (cardia bifida). The mil phenotype for
CC which two recessive alleles exist, mil(m93) and mil(te273) are fully
CC penetrant. Mil(m93)/mil(te273) transheterozygous embryos display the
CC same phenotype as homozygotes for either single mutant allele. In
CC addition to cardia bifida, mil mutants display epithelial tail
CC blisters, indicative of a defect in epithelial integrity.
CC {ECO:0000269|PubMed:10910360}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF260256; AAF88001.1; -; mRNA.
DR RefSeq; NP_001153442.1; NM_001159970.1.
DR AlphaFoldDB; Q9I8K8; -.
DR SMR; Q9I8K8; -.
DR STRING; 7955.ENSDARP00000053105; -.
DR PaxDb; Q9I8K8; -.
DR PRIDE; Q9I8K8; -.
DR Ensembl; ENSDART00000053106; ENSDARP00000053105; ENSDARG00000036548.
DR GeneID; 170457; -.
DR KEGG; dre:170457; -.
DR CTD; 9294; -.
DR ZFIN; ZDB-GENE-020123-2; s1pr2.
DR eggNOG; ENOG502QVQY; Eukaryota.
DR GeneTree; ENSGT01050000244887; -.
DR HOGENOM; CLU_047979_1_0_1; -.
DR InParanoid; Q9I8K8; -.
DR OMA; CPVRACP; -.
DR OrthoDB; 981486at2759; -.
DR PhylomeDB; Q9I8K8; -.
DR TreeFam; TF330052; -.
DR Reactome; R-DRE-418594; G alpha (i) signalling events.
DR Reactome; R-DRE-419408; Lysosphingolipid and LPA receptors.
DR PRO; PR:Q9I8K8; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 3.
DR Bgee; ENSDARG00000036548; Expressed in zone of skin and 42 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0038036; F:sphingosine-1-phosphate receptor activity; IBA:GO_Central.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0048901; P:anterior lateral line neuromast development; IMP:ZFIN.
DR GO; GO:0035676; P:anterior lateral line neuromast hair cell development; IMP:ZFIN.
DR GO; GO:0003319; P:cardioblast migration to the midline involved in heart rudiment formation; IMP:ZFIN.
DR GO; GO:0042074; P:cell migration involved in gastrulation; IMP:ZFIN.
DR GO; GO:0060973; P:cell migration involved in heart development; IMP:ZFIN.
DR GO; GO:0003318; P:cell migration to the midline involved in heart development; IMP:ZFIN.
DR GO; GO:0060026; P:convergent extension; IMP:ZFIN.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IDA:ZFIN.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:ZFIN.
DR GO; GO:0003143; P:embryonic heart tube morphogenesis; IMP:ZFIN.
DR GO; GO:0048703; P:embryonic viscerocranium morphogenesis; IGI:ZFIN.
DR GO; GO:0007492; P:endoderm development; IMP:ZFIN.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0003007; P:heart morphogenesis; IMP:ZFIN.
DR GO; GO:0003315; P:heart rudiment formation; IMP:ZFIN.
DR GO; GO:0008078; P:mesodermal cell migration; IGI:ZFIN.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:ZFIN.
DR GO; GO:0048840; P:otolith development; IMP:ZFIN.
DR GO; GO:0035677; P:posterior lateral line neuromast hair cell development; IMP:ZFIN.
DR GO; GO:0061035; P:regulation of cartilage development; IMP:ZFIN.
DR GO; GO:0019222; P:regulation of metabolic process; IBA:GO_Central.
DR GO; GO:0060872; P:semicircular canal development; IMP:ZFIN.
DR GO; GO:0003376; P:sphingosine-1-phosphate receptor signaling pathway; IMP:ZFIN.
DR GO; GO:0001944; P:vasculature development; IGI:ZFIN.
DR InterPro; IPR004063; EDG5_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR004061; S1P_rcpt.
DR PANTHER; PTHR22750:SF17; PTHR22750:SF17; 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 Cell membrane; Disease variant; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..370
FT /note="Sphingosine 1-phosphate receptor 2"
FT /id="PRO_0000069430"
FT TOPO_DOM 1..57
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 58..78
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 79..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 88..108
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 109..128
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 129..149
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 150..167
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 168..193
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 194..219
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 220..230
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 231..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 255..275
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 276..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..370
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT LIPID 325
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 150
FT /note="R -> H (in mil; allele m93; lack of S1P-mediated
FT signaling)"
FT /evidence="ECO:0000269|PubMed:10910360"
FT VARIANT 167
FT /note="R -> C (in mil; allele te273; lack of S1P-mediated
FT signaling)"
FT /evidence="ECO:0000269|PubMed:10910360"
SQ SEQUENCE 370 AA; 41777 MW; 8C6B3A06DEEA6757 CRC64;
MTTCRLFAGF CQAVTMSKYS QYFNKTLIQV HYLTAKEMTA EELRDRIESK QSLSSLNILF
VVICSIIILE NLLVLIAVFR NKKFHSAMFF FIGNLAFSDL LAGSAYIANI FLSGPRTFHL
TPVQWFIREG TAFIALSASV FSLLAIAIER YIAITKVKVY GSNKTCRMFL LIGACWVMSI
LLGGLPIIGW NCINNLDDCS AVLPLNTRYY IRFVVTIFSI ILLSIVILYV RIYLIVRTSH
QEATNSPAYA LLKTVTIVLG VFIICWLPAF TILLLDTSCK MKQCPILNNA GIFFSFATLN
SALNPLIYTL RSKDMRKEFL RVLCCWGLLN CGRPPHRCMV PLKSSSSMEH CTNKHEHQSI
PIMQDCTTCV
