Serine incorporator 2 (SERINC2)

Serine incorporator 2 (SERINC2) is a **transmembrane protein** that functions in the incorporation of the amino acid serine into membrane phospholipids, primarily facilitating the synthesis of **phosphatidylserine and sphingolipids**, both of which are crucial for cell membrane architecture and cellular signaling[1][2][3][4]. This protein is a member of the **SERINC family** (SERINC1–5), and together they play a central role in regulating membrane lipid composition. SERINC2 possesses multiple transmembrane domains (typically 10–11) and is highly conserved among eukaryotes, showing no amino acid homology to other protein families except distant SERINC homologs[1][4]. Although the SERINC family has established roles as restriction factors for some viral infections (notably SERINC3 and SERINC5 for HIV), **human SERINC2 does not directly restrict viruses or integrate into viral particles**[1]. Importantly, **SERINC2 is highly expressed in certain tumor types**, including lung adenocarcinoma and gliomas, where its expression correlates with more aggressive disease[2][3]. Knockdown of SERINC2 impairs cancer cell proliferation, migration, and invasion in experimental models, possibly through effects on membrane lipid synthesis and the PI3K/AKT signaling pathway[2][3]. No drugs are known to specifically target SERINC2, though its involvement in tumor progression and altered expression in infection suggests potential as a prognostic biomarker and theoretical therapeutic target, subject to further research[2][3]. **Note**: SERINC2 is distinct from SERINC3 and SERINC5, which are directly implicated in retroviral restriction. At present, there is no evidence of direct drug interactions with SERINC2, nor is it recognized as a druggable target in current clinical or preclinical pipelines[1][3].

Other names

TDE2LFKSG84UNQ263/PRO300PRO0899TDE2Tumor differentially expressed protein 2-liketumor differentially expressed protein 2

None specifically reported for direct drug targeting; possible indirect effects via modulation of membrane lipid synthesis