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Sec16 homolog A, endoplasmic reticulum export factor (SEC16A)

Target
SEC16A
Molecular classification
Other (scaffold protein)
01

Overview

Sec16 homolog A, endoplasmic reticulum export factor (SEC16A), is a large hydrophilic peripheral membrane protein that serves as a molecular scaffold crucial for forming endoplasmic reticulum exit sites (ERES)[1][2][5]. It organizes and defines these sites on the ER membrane, enabling budding of COPII-coated vesicles that mediate transport of secretory cargo from the ER to the Golgi apparatus[1][2]. SEC16A facilitates recruitment of COPII coat proteins and interacts with components such as SAR1A, MIA3/TANGO, and RAB10[1]. It is required for both conventional (COPII-mediated, ER-Golgi) and unconventional (Golgi-bypassing, GRASP-mediated) protein secretion pathways[5]. SEC16A is essential for proper cellular cargo trafficking, and its dysfunction is involved in rare diseases like craniolenticulosutural dysplasia and amelogenesis imperfecta, as well as potentially in neurodegeneration (notably Parkinson’s disease) due to its role in managing ER export stress responses[2][5]. SEC16A is not a classical therapeutic target such as a receptor, enzyme, or transporter; rather, it is a central organizer of vesicle trafficking machinery. There are no known drugs directly targeting SEC16A in current clinical or preclinical use[1][5]. No established biomarker or approved drug interactions are reported for SEC16A.

Other names
Protein transport protein Sec16ASEC16AKIAA0310SEC16SEC16Lp250Sec16LSEC16 homolog A
02

Biological functions

Protein transport from endoplasmic reticulum (ER) to Golgi apparatusOrganization of ER exit sites (ERES)COPII vesicle formationScaffold for vesicle traffickingAutophagy (participates in autophagosome formation)
03

Disease associations

Cancer (inferred from general ER stress/trafficking context, but no direct strong link)Craniolenticulosutural dysplasiaAmelogenesis imperfecta, type IIIaNeurodegenerative disease (implicated in pathogenesis of Parkinson's disease via ER export dysfunction[2])
04

Safety considerations

Disruption may cause broad cellular transport defectsDysregulation can affect secretory and stress response pathways

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