SEC23A

Sec23 homolog A, COPII coat complex component
PDB rendering based on 2nup.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2NUP​, 2NUT​, 2YRC​, 2YRD​, 3EFO​, 3EG9​, 3EGD​, 3EGX​
Identifiers
Symbols	SEC23A ; CLSD
External IDs	OMIM: 610511 MGI: 1349635 HomoloGene: 4642 GeneCards: SEC23A Gene
Gene ontology Molecular function • protein binding • zinc ion binding Cellular component • Golgi membrane • endoplasmic reticulum • endoplasmic reticulum membrane • cytosol • ER to Golgi transport vesicle membrane • COPII vesicle coat • smooth endoplasmic reticulum membrane • perinuclear region of cytoplasm Biological process • antigen processing and presentation of peptide antigen via MHC class I • intracellular protein transport • ER to Golgi vesicle-mediated transport • vesicle-mediated transport • protein N-linked glycosylation via asparagine • antigen processing and presentation of exogenous peptide antigen via MHC class II • post-translational protein modification • cellular protein metabolic process • small molecule metabolic process • COPII vesicle coating • membrane organization Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
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: 39.03 – 39.11 Mb	Chr 12: 58.96 – 59.01 Mb
PubMed search

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

Function

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.

Interactions

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]

References

1. "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.
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

• Paccaud JP, Reith W, Carpentier JL, Ravazzola M, Amherdt M, Schekman R, Orci L (1996). "Cloning and functional characterization of mammalian homologues of the COPII component Sec23". Mol. Biol. Cell 7 (10): 1535–46. doi:10.1091/mbc.7.10.1535. PMC 276004. PMID 8898360.
• Pagano A, Letourneur F, Garcia-Estefania D, Carpentier JL, Orci L, Paccaud JP (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.
• Tang BL, Kausalya J, Low DY, Lock ML, Hong W (1999). "A family of mammalian proteins homologous to yeast Sec24p". Biochem. Biophys. Res. Commun. 258 (3): 679–84. doi:10.1006/bbrc.1999.0574. PMID 10329445.
• Boyadjiev SA, Justice CM, Eyaid W, McKusick VA, Lachman RS, Chowdry AB, Jabak M, Zwaan J, Wilson AF, Jabs EW (2003). "A novel dysmorphic syndrome with open calvarial sutures and sutural cataracts maps to chromosome 14q13-q21". Hum. Genet. 113 (1): 1–9. doi:10.1007/s00439-003-0932-6. PMID 12677423.
• Dudognon P, Maeder-Garavaglia C, Carpentier JL, Paccaud JP (2004). "Regulation of a COPII component by cytosolic O-glycosylation during mitosis". FEBS Lett. 561 (1-3): 44–50. doi:10.1016/S0014-5793(04)00109-7. PMID 15013749.
• Watson P, Forster R, Palmer KJ, Pepperkok R, Stephens DJ (2005). "Coupling of ER exit to microtubules through direct interaction of COPII with dynactin". Nat. Cell Biol. 7 (1): 48–55. doi:10.1038/ncb1206. PMC 1592520. PMID 15580264.
• Palmer KJ, Konkel JE, Stephens DJ (2005). "PCTAIRE protein kinases interact directly with the COPII complex and modulate secretory cargo transport". J. Cell. Sci. 118 (Pt 17): 3839–47. doi:10.1242/jcs.02496. PMID 16091426.
• Boyadjiev SA, Fromme JC, Ben J, Chong SS, Nauta C, Hur DJ, Zhang G, Hamamoto S, Schekman R, Ravazzola M, Orci L, Eyaid W (2006). "Cranio-lenticulo-sutural dysplasia is caused by a SEC23A mutation leading to abnormal endoplasmic-reticulum-to-Golgi trafficking". Nat. Genet. 38 (10): 1192–7. doi:10.1038/ng1876. PMID 16980979.
• Tu LC, Yan X, Hood L, Lin B (2007). "Proteomics analysis of the interactome of N-myc downstream regulated gene 1 and its interactions with the androgen response program in prostate cancer cells". Mol. Cell Proteomics 6 (4): 575–88. doi:10.1074/mcp.M600249-MCP200. PMID 17220478.