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Sec23 homolog A (S. cerevisiae)
Protein SEC23A PDB 2nup.png
PDB rendering based on 2nup.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols SEC23A ; CLSD
External IDs OMIM610511 MGI1349635 HomoloGene4642 GeneCards: SEC23A Gene
RNA expression pattern
PBB GE SEC23A 204344 s at tn.png
PBB GE SEC23A 212887 at tn.png
More reference expression data
Species Human Mouse
Entrez 10484 20334
Ensembl ENSG00000100934 ENSMUSG00000020986
UniProt Q15436 Q01405
RefSeq (mRNA) NM_006364 NM_009147
RefSeq (protein) NP_006355 NP_033173
Location (UCSC) Chr 14:
39.5 – 39.58 Mb
Chr 12:
58.96 – 59.01 Mb
PubMed search [1] [2]

Sec23 homolog A (S. cerevisiae), also known as SEC23A, is a protein which in humans is encoded by the SEC23A gene.[1]


The protein encoded by this gene is a member of the SEC23 subfamily of the SEC23/SEC24 family. It contains a gelsolin domain.[2] It is part of a protein complex and found in the ribosome-free transitional face of the endoplasmic reticulum (ER) and associated vesicles. This protein has similarity to yeast Sec23p component of COPII. COPII is the coat protein complex responsible for vesicle budding from the ER. The encoded protein is suggested to play a role in the ER-Golgi protein trafficking.[1]

SEC23 interacts with both SEC16A and SEC16B.[citation needed]


SEC23A has been shown to interact with SEC24C,[3] Sec16A/p250 and iPLA1β/p125.[4]

Sec23 has also been shown to interact with TRAPPⅠ, Grh1p also known as GRASP65 and Dynactin. Because they are involved in anterograde vesicle transport from ER to Golgi, Sec23 is involved in vesicle transport.[5]


  1. ^ a b "Entrez Gene: SEC23A Sec23 homolog A (S. cerevisiae)". 
  2. ^ Ghoshdastider, U; Popp, D; Burtnick, L. D.; Robinson, R. C. (2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton 70 (11): 775–95. doi:10.1002/cm.21149. PMID 24155256.  edit
  3. ^ Pagano A, Letourneur F, Garcia-Estefania D, Carpentier JL, Orci L, Paccaud JP (Mar 1999). "Sec24 proteins and sorting at the endoplasmic reticulum". J. Biol. Chem. 274 (12): 7833–40. doi:10.1074/jbc.274.12.7833. PMID 10075675. 
  4. ^ p125 is localized in endoplasmic reticulum exit sites and involved in their organization.
  5. ^ Coordination of COPII vesicle trafficking by Sec23.

Further reading[edit]