Anti-Sec16A

This gene encodes a protein that forms part of the Sec16 complex. This protein has a role in protein transport from the endoplasmic reticulum (ER) to the Golgi and mediates COPII vesicle formation at the transitional ER. Alternative splicing results in multiple transcript variants that encode different protein isoforms. [provided by RefSeq, Feb 2013], Protein function: Acts as a molecular scaffold that plays a key role in the organization of the endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). SAR1A-GTP-dependent assembly of SEC16A on the ER membrane forms an organized scaffold defining an ERES. Required for secretory cargo traffic from the endoplasmic reticulum to the Golgi apparatus (PubMed:17192411, PubMed:17005010, PubMed:17428803, PubMed:21768384, PubMed:22355596). Mediates the recruitment of MIA3/TANGO to ERES (PubMed:28442536). Regulates both conventional (ER/Golgi-dependent) and GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane (PubMed:28067262). Positively regulates the protein stability of E3 ubiquitin-protein ligases RNF152 and RNF183 and the ER localization of RNF183 (PubMed:29300766). Acts as a RAB10 effector in the regulation of insulin-induced SLC2A4/GLUT4 glucose transporter- enriched vesicles delivery to the cell membrane in adipocytes. [The UniProt Consortium] Recommended dilutions: Immunohistochemistry: 1/100 - 1/300. ELISA: 1/20000. Not yet tested in other applications.. Cellular localization: Endoplasmic reticulum membrane , Peripheral membrane protein . Golgi apparatus membrane , Peripheral membrane protein . Cytoplasm, perinuclear region . Cytoplasm, cytosol . Microsome membrane . SAR1A activity is required to maintain SEC16A localization at discrete locations on the ER membrane perhaps by preventing its dissociation (PubMed:17192411). Localizes to endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER). MIA3 and LRRK2 are required for its proper localization to ERES (PubMed:25201882, PubMed:28442536, PubMed:19638414, PubMed:17428803, PubMed:22355596). Recruited to microsomal membrane in SAR1-dependent manner (PubMed:17428803). .