Rfabg, Lpp, RfaBp, lipophorin, ApoLII
Lipophorin - bears lipid-linked morphogens on its surface - required for long-range signaling activity of Wingless and Hedgehog - lipophorin receptors recruit the lipoprotein Lipid Transfer Particle (LTP) to the plasma membrane to mediate lipid uptake
Gene model reviewed during 5.47
Low-frequency RNA-Seq exon junction(s) not annotated.
Gene model reviewed during 5.55
May be modified covalently by lipidation.
Cleaved into 2 chains by furin protease. However, prevention of cleavage does not impair its function (By similarity).
Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\apolpp using the Feature Mapper tool.
apolpp localizes to the perineurium and CNS. The protein moiety of Lpp, apolipophorin, undergoes furin dependent cleavage, generating apolipophorin I (ApoLI) and apolipophorin II (ApoLII) both of which circulate on low-density lipophorin particles in the hemolymph. Both cross the perineurium and localize to different places in the larval brain (as shown with tagged proteins).
Isolated from a pullout assay for proteins contained in clots from larval hemolymph and identified by mass spec.
GBrowse - Visual display of RNA-Seq signalsView Dmel\apolpp in GBrowse 2
Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete
Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.
For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.
In vitro studies reveal RfaBp gene is transcriptionally regulated by retinoic acid.
RfaBp levels are high in retinoid replete flies, nearly zero in deprived flies and high for retinoic acid supplemented medium. This is important evidence that RfaBp expression is controlled by retinoids and other transcription activators.
Isolated using a rat antibody from a head cDNA library.
RfaBp encodes a retinoid- and fatty-acid binding glycoprotein that is a member of the proapolipophorin gene family. RfaBp encodes a 3351 amino acid protein. The protein is initially dispersed throughout the embryonic amnioserosa sac and later concentrates at skeletal muscle epidermis apodemeal contact junctions during larval development.
There is preliminary evidence that retinoid (vitamin A) deprivation reduces RfaBp protein levels.