SEC23A

SEC23A
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2NUP, 2NUT, 2YRC, 2YRD, 3EFO, 3EG9, 3EGD, 3EGX
Identifiers
Aliases	SEC23A, CLSD, Sec23 homolog A, coat complex II component, hSec23A, Sec23 homolog A, COPII coat complex component
External IDs	OMIM: 610511; MGI: 1349635; HomoloGene: 4642; GeneCards: SEC23A; OMA:SEC23A - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q21.1 Start 39,031,919 bp End 39,109,646 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12|12 C1 Start 59,005,169 bp End 59,058,803 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa tibia stromal cell of endometrium Achilles tendon seminal vesicula saphenous vein parietal pleura smooth muscle tissue superficial temporal artery tail of epididymis Top expressed in calvaria body of femur dermis extensor digitorum longus muscle pineal gland jejunum cumulus cell atrium ascending aorta ankle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding zinc ion binding metal ion binding GTPase activator activity Cellular component membrane Golgi membrane perinuclear region of cytoplasm COPII-coated ER to Golgi transport vesicle endoplasmic reticulum extrinsic component of membrane COPII vesicle coat endoplasmic reticulum exit site cytoplasm endoplasmic reticulum membrane cytosol ER to Golgi transport vesicle membrane cytoplasmic vesicle Biological process antigen processing and presentation of exogenous peptide antigen via MHC class II antigen processing and presentation of peptide antigen via MHC class I endoplasmic reticulum to Golgi vesicle-mediated transport COPII vesicle coating protein transport intracellular protein transport vesicle-mediated transport COPII-coated vesicle cargo loading COPII-coated vesicle budding regulation of COPII vesicle coating Golgi organization regulation of cell shape macroautophagy positive regulation of GTPase activity protein localization to plasma membrane Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10484 20334 Ensembl ENSG00000100934 ENSMUSG00000020986 UniProt Q15436 Q01405 RefSeq (mRNA) NM_006364 NM_009147 NM_001361956 RefSeq (protein) NP_006355 NP_033173 NP_001348885 Location (UCSC) Chr 14: 39.03 – 39.11 Mb Chr 12: 59.01 – 59.06 Mb PubMed search
Wikidata
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Sec23 homolog A (S. cerevisiae), also known as SEC23A, is a protein which in humans is encoded by the SEC23A gene.

Function

The protein encoded by this gene is a member of the SEC23 subfamily of the SEC23/SEC24 family. It contains a gelsolin domain. 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.

SEC23 interacts with both SEC16A and SEC16B.

Interactions

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

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.

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.

External links

• PDBe-KB provides an overview of all the structure information available in the PDB for Human Protein transport protein Sec23A