Combined Automated Annotation using Multiple IEA Methods
A bipartite structural organization defines the SERINC family of HIV-1 restriction factors.
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Cryo-EM of purified Drosophila SERINC (DmSERINC/TMS1) shows a hexamer of ten-helix protomers in a new membrane fold, with two extracellular disulphides and cytoplasmic termini.
"Each of the six identical DmSERINC subunits consists of ten transmembrane helices (TM) arranged into two subdomains"
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A subdomain-B groove binds an acyl chain, and phosphatidylserine alters HDX there. PS, cholesterol and sulfatide stabilise the protein.
"the cryo-EM map revealed presence of an acyl chain bound at this site"
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Ectopic DmSERINC expression in HEK293T cells restricts Nef-deficient HIV-1. This heterologous assay is not evidence of a physiological antiviral process in the fly.
"Ectopic expression of DmSERINC during production of Nef-deficient HIV-1 virions strongly suppressed their infectivity"
Antiviral HIV-1 SERINC restriction factors disrupt virus membrane asymmetry.
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Purified human SERINC proteins flip PS, PE and PC in proteoliposomes. This is family context only, from different PANTHER subfamilies.
"purified hSERINCs reconstituted into proteoliposomes induce flipping of"
Disruption of Transmembrane Phosphatidylserine Asymmetry by HIV-1 Incorporated SERINC5 Is Not Responsible for Virus Restriction.
Serinc isoform and structure-residue analysis
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M9PCT1 is a full-length splice isoform. It is identical to isoform A except for a 7-residue cytosolic-loop deletion and keeps all structurally named DmSERINC residues.
"M9PCT1 carries all 18 named residues"
FlyBase gene description for Serinc (DROME)