sphingosine 1-phosphate receptor 5 (endothelial differentiation sphingolipid G-protein-coupled receptor 8, S1PR5, EDG8)

Function: 1) receptor for the lysosphingolipid sphingosine 1-phosphate 2) coupled to Gi, Go & G12 heteromeric G-proteins 3) role in transformation of radial glial cells into astrocytes - may affect proliferation of astrocytes 4) membrane Structure: - belongs to the G-protein coupled receptor 1 family Alternative splicing: named isoforms=2 Expression: - widely expressed in the brain - most prominently in corpus callosum - detected in spleen, peripheral blood leukocytes, placenta, lung, aorta, fetal spleen - isoform 1 is predominently expressed in peripheral tissues - isoform 2 is expressed in brain, spleen & peripheral blood leucocytes - at 24 weeks of gestation, fragments of radial glial fibers are positive within the cortical plate & subplate of allocortical areas - these positive fragments often appear enlarged as varicosities, some terminate at blood vessels - between 28-30 weeks of gestation, all iso- & allocortical areas contain immunolabelled radial glial fibers revealing curvature next to sulci - after 32 weeks of gestation, radial glial fibers gradually disappear; instead positive transitional stages between radial glia & astrocytes are found Pathology: - overexpressed in large granular lymphocyte syndrome

Properties

SIZE: MW = 42 kD entity length = 398 aa COMPARTMENT: cellular membrane MOTIF: exoplasmic domain {1-40} MOTIF: N-glycosylation site {N20} transmembrane domain {41-61} cytoplasmic loop {62-70} transmembrane domain {71-91} exoplasmic loop {92-111} transmembrane domain {112-132} cytoplasmic loop {133-151} transmembrane domain {152-172} exoplasmic loop {173-192} transmembrane domain {193-213} cytoplasmic loop {214-252} transmembrane domain {253-273} exoplasmic loop {274-287} transmembrane domain {288-308} cytoplasmic domain {309-398} MOTIF: cysteine residue {C323} MODIFICATION: palmitate COMPARTMENT: membrane

Database Correlations

OMIM 605146 UniProt Q9H228 Pfam PF00001

References

UniProt :accession Q9H228