9.A.78.1.2
Protein retinal degeneration B, RdgB, of 1259 aas, possibly with a central 8 TMSs unit in a 4 + 4 TMS arrangement. It catalyzes the transfer of phosphatidylinositol (PI) and phosphatidic acid (PA) between membranes (Garner et al. 2012). It may control the phosphatidylinositol concentration in transport vesicles
from the subrhabdomeric cisternae (SRC) to the rhabdomere as well as functioning as a calcium transporter (Vihtelic et al. 1991). Lipid transfer proteins mediate the transfer of lipids between organelle
membranes, and the loss of function of these proteins has been linked
to neurodegeneration. In Drosophila photoreceptors, depletion of retinal degeneration B (RDGB), a
phosphatidylinositol transfer protein, leads to defective
phototransduction and retinal degeneration.
RDGB is localized to membrane contact sites through the interaction of
its FFAT motif with the ER integral protein VAP. To identify regulators
of RDGB function in vivo, Mishra et al. 2024 depleted more than 300 VAP-interacting
proteins and identified a set of 52 suppressors of rdgB. The
molecular identity of these suppressors indicates a role of novel lipids
in regulating RDGB function and of transcriptional and ubiquitination
processes in mediating retinal degeneration in rdgB. The human homologs of several of these molecules have been implicated in
neurodevelopmental diseases, underscoring the importance of VAP-mediated
processes in these disorders.
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| Accession Number: | P43125 |
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| Protein Name: | Protein retinal degeneration B |
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| Length: | 1259 |
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| Molecular Weight: | 138895.00 |
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| Species: | Drosophila melanogaster (Fruit fly) [7227] |
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| Number of TMSs: | 2 |
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| Substrate |
calcium(2+), phosphoinositide, phosphatidic acid |
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1: MLIKEYRIPL PLTVEEYRIA QLYMIAKKSR EESHGEGSGV EIIINEPYKD GPGGNGQYTK
61: KIYHVGNHLP GWIKSLLPKS ALTVEEEAWN AYPYTRTRYT CPFVEKFSLD IETYYYPDNG
121: YQDNVFQLSG SDLRNRIVDV IDIVKDQLWG GDYVKEEDPK HFVSDKTGRG PLAEDWLEEY
181: WREVKGKKQP TPRNMSLMTA YKICRVEFRY WGMQTKLEKF IHDVALRKMM LRAHRQAWAW
241: QDEWFGLTIE DIRELERQTQ LALAKKMGGG EECSDDSVSE PYVSTAATAA STTGSERKKS
301: APAVPPIVTQ QPPSAEASSD EEGEEEEDDD EDENDAIGTG VDLSANQGGS AQRSRSQSIQ
361: MAQKGKFGSK GALHSPVGSA HSFDLQVANW RMERLEVDSK SNSDEEFFDC LDTNETNSLA
421: KWSSLELLGE GDDSPPPHGG PSSAASVGGR GNSRQEDSIF NQDFLMRVAS ERGNKRQLRS
481: SASVDRSHDS SPPGSPSTPS CPTTILILVV HAGSVLDAAS ELTAKKSDVT TFRGSFEAVM
541: RQHYPSLLTH VTIKMVPCPS ICTDALGILS SLSPYSFDAS PSAADIPNIA DVPIGAIPLL
601: SVASPEFHET VNKTVAAANI VYHEFLKSEE GHGFSGQIVM LGDSMGSLLA YEALCRSNGS
661: QPGTASGASN SGGDAATNIN THNPLSPRNS RLDDDERFIE ADLDAKRLLV APSPRRRRSS
721: SSSDSRATKL DFEVCDFFMF GSPLSVVLAA RKLHDAKAAL PRPNCHQVYN LFHPTDPIAS
781: RLEPLLSARF SILAPVNVPR YAKYPLGNGQ PLHLLEVIQS HPQHFNDGNN LLAGRRLSDA
841: SMQSTISGLI ENVSLSTIHA LQNKWWGTKR LDYALYCPEG LSNFPAHALP HLFHASYWES
901: PDVIAFILRQ IGKFEGIPFV GSNDDKDNAS FHPGQPREKW IKKRTSVKLK NVAANHRAND
961: VIVQEGREQR LNARFMYGPL DMITLHGEKV DVHIMKDPPA GEWTFLSTEV TDKNGRISYS
1021: IPDQVSLGYG IYPVKMVVRG DHTSVDCYMA VVPPLTECVV FSIDGSFTAS MSVTGRDPKV
1081: RAGAVDVCRH WQELGYLLIY ITGRPDMQQQ RVVSWLSQHN FPHGLISFAD GLSTDPLGHK
1141: TAYLNNLVQN HGISITAAYG SSKDISVYTN VGMRTDQIFI VGKVGKKLQS NATVLSDGYA
1201: AHLAGLQAVG GSRPAKGNAR MVIPRGCFNL PGQTANPRRR RYLERKTVSS CCLMVFQTT