Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Serinc, an activity-regulated protein family, incorporates serine into membrane lipid synthesis.
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Serinc family proteins facilitate synthesis of serine-derived membrane lipids.
"facilitates the synthesis of two serine-derived lipids, phosphatidylserine and sphingolipids."
Large-scale proteomics and phosphoproteomics of urinary exosomes.
SERINC3 and SERINC5 restrict HIV-1 infectivity and are counteracted by Nef.
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SERINC3 and SERINC5 jointly restrict HIV-1 replication.
"SERINC3 and SERINC5 together restricted HIV-1 replication"
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SERINC5 is the more potent of the two restriction factors in single-gene knockout experiments.
"Nef−, EnvHXB2-pseudotyped HIV-1 particles produced in JurkatTAg clones lacking either SERINC3 or SERINC5 were ~5-fold or 13- to 20-fold more infectious, respectively, than particles produced in the parental cells"
HIV-1 Nef promotes infection by excluding SERINC5 from virion incorporation.
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SERINC5 localizes to the plasma membrane, enters budding virions, and impairs target-cell penetration.
"SERINC5 localizes to the plasma membrane, where it is efficiently incorporated into budding HIV-1 virions and impairs subsequent virion penetration of susceptible target cells."
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HIV-1 Nef removes SERINC5 from the virion assembly route.
"Nef redirects SERINC5 to a Rab7-positive endosomal compartment and thereby excludes it from HIV-1 particles."
Antiviral HIV-1 SERINC restriction factors disrupt virus membrane asymmetry.
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Purified human SERINC proteins flip PS, PE, and PC.
"purified hSERINCs reconstituted into proteoliposomes induce flipping of phosphatidylserine (PS), phosphatidylethanolamine and phosphatidylcholine."
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SERINC5 exposes phosphatidylserine on retroviral particles.
"The incorporation of hSERINC5 resulted in the exposure of PS on the surface of virus particles"
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SERINC-mediated phosphatidylserine exposure correlates with reduced retroviral infectivity.
"SERINC3, SERINC5 and the scramblase TMEM16F expose PS on the surface of HIV-1 and reduce infectivity"
Disruption of Transmembrane Phosphatidylserine Asymmetry by HIV-1 Incorporated SERINC5 Is Not Responsible for Virus Restriction.
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Virion-incorporated SERINC5 eliminates phosphatidylserine asymmetry.
"This asymmetry is completely lost upon incorporation of SER5 or TMEM16F."
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External phosphatidylserine is not the principal cause of SERINC5-mediated restriction.
"PS externalization is likely not the key driver for infectivity reduction by SER5."
SERINC3,5,(1,2,4) transport L-Ser from cytosol to plasma membrane
UniProtKB record for human SERINC5 (Q86VE9)
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Reviewed UniProt summarizes human SERINC5 topology, scramblase activity, antiviral function, locations, and four isoforms.
"Functions as a scramblase that flips"
Manual deep-research synthesis for human SERINC5
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Manual synthesis separates established scrambling and antiviral roles from their unresolved mechanistic relationship.
"Scrambling and antiviral restriction are both well established, but the causal link is not."
Manual SERINC5 curation notes