Serine incorporator 3 encoded by SERINC3 gene is described as a carrier protein that incorporates a polar-amino acid serine into cell membranes. It is a member of the serine incorporator (SERINC) protein family that is conserved from yeast to mammals. The members of this family share between 30 and 80% homology, contain multiple hydrophobic domains and often include an N-terminal signal peptide. In mouse, at least five homologues have been identified, scattered over four different chromosomes, whereas human SERINC3 genes have been found on five different chromosomes. When comparing the sequence between human and mouse genes, it has been noted that most homologues between these two species locate on syntenic regions at the chromosome level suggesting evolutionary conservation. The conserved nature of the gene structure and of the sequence of the protein through evolution suggests an important biological role for SERINC family members.
|Basic Information of SERINC3|
|Protein Name||Serine incorporator 3|
|Aliases||TDE, TDE1, AIGP1, TMS-1, DIFF33, SBBI99|
|Organism||Homo sapiens (Human)|
SERINC protein function has not been studied in great detail and essentially relies on a small number of reports. SERINC3 and SERINC5 together restrict HIV-1 replication, and this restriction is evaded by Nef. Moreover, SERINC3 and SERINC5 are highly expressed in primary human HIV-1 target cells, which may suggest a potential strategy to combat HIV. Except for that function, human SERINC5 overexpression can be observed in tumor tissues of tumor-bearing transgenic mice. However, the ultimate role of SERINC5 in human cell transformation, and specifically, its possible role in human carcinogenesis, needs to be further investigated. The present study also underlies the ability of SERINC5 to interfere with programmed cell death, allowing cells to escape control mechanisms established in multicellular organisms to eliminate malfunctioning cells such as transformed cells.
Fig.1 Cytoplasmic host cell restrictions to human immunodeficiency virus types 1 (HIV-1) infection and virally encoded antagonists. (Fackler, 2015)
This article finds that HIV-1 Nef and MLV glycoGag efficiently down-regulate SERINC3 and SERINC5 form the cell surface, which prevents their incorporation into HIV-1 virions and consequently counteracts their inhibitory effect on HIV-1 infectivity.
This article establishes SERINC3/5 as restrictions to HIV replication in human cells and defines a novel activity for the HIV pathogenesis factor Nef.
This article suggests that the importance of the antiretroviral function of the SERINC proteins may be a relatively novel evolutionary advance.
This article reveals that SERINC5 and SERINC3 play an essential role against various retrovirus pathogens.
This article suggests that human TDE1 contributes directly to oncogenesis in vivo.
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