SEC31A

SEC31 homolog A, COPII coat complex component
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3WXA​
Identifiers
Symbols	SEC31A ; ABP125; ABP130; HSPC275; HSPC334; SEC31L1
External IDs	OMIM: 610257 MGI: 1916412 HomoloGene: 42056 GeneCards: SEC31A Gene
Gene ontology Molecular function • protein binding • calcium-dependent protein binding Cellular component • Golgi membrane • cytoplasm • endoplasmic reticulum • endoplasmic reticulum membrane • cytosol • ER to Golgi transport vesicle membrane • vesicle coat • COPII vesicle coat • ER to Golgi transport vesicle • intracellular membrane-bounded organelle • perinuclear region of cytoplasm • endoplasmic reticulum exit site Biological process • antigen processing and presentation of peptide antigen via MHC class I • ER to Golgi vesicle-mediated transport • protein transport • protein N-linked glycosylation via asparagine • antigen processing and presentation of exogenous peptide antigen via MHC class II • endoplasmic reticulum unfolded protein response • IRE1-mediated unfolded protein response • post-translational protein modification • cellular protein metabolic process • COPII vesicle coating • response to calcium ion • membrane organization Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	22872	69162
Ensembl	ENSG00000138674	ENSMUSG00000035325
UniProt	O94979	Q3UPL0
RefSeq (mRNA)	NM_001077206	NM_026969
RefSeq (protein)	NP_001070674	NP_081245
Location (UCSC)	Chr 4: 82.82 – 82.9 Mb	Chr 5: 100.36 – 100.42 Mb
PubMed search

Protein transport protein Sec31A is a protein that in humans is encoded by the SEC31A gene.^[1][2][3]

The protein encoded by this gene is similar to yeast Sec31 protein. Yeast SEC31 protein is known to be a component of the COPII protein complex which is responsible for vesicle budding from endoplasmic reticulum (ER). This protein was found to colocalize with SEC13, one of the other components of COPII , in the subcellular structures corresponding to the vesicle transport function. An immunodepletion experiment confirmed that this protein is required for ER-Golgi transport. Alternative splicing results in multiple transcript variants encoding different isoforms.^[3]

References

1. Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (May 1999). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res 5 (6): 355–64. doi:10.1093/dnares/5.6.355. PMID 10048485.
2. Tang BL, Zhang T, Low DY, Wong ET, Horstmann H, Hong W (Jun 2000). "Mammalian homologues of yeast sec31p. An ubiquitously expressed form is localized to endoplasmic reticulum (ER) exit sites and is essential for ER-Golgi transport". J Biol Chem 275 (18): 13597–604. doi:10.1074/jbc.275.18.13597. PMID 10788476.
3. "Entrez Gene: SEC31A SEC31 homolog A (S. cerevisiae)".

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Kim JH, Hong JA, Pih KT, Hwang I (2001). "Identification and isolation of differentially expressed genes in osmotically stressed human oral keratinocytes". Arch. Oral Biol. 46 (4): 335–41. doi:10.1016/S0003-9969(00)00133-3. PMID 11269867.
• Wistow G, Bernstein SL, Wyatt MK, et al. (2002). "Expressed sequence tag analysis of human RPE/choroid for the NEIBank Project: over 6000 non-redundant transcripts, novel genes and splice variants". Mol. Vis. 8: 205–20. PMID 12107410.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Loïodice I, Alves A, Rabut G, et al. (2005). "The Entire Nup107-160 Complex, Including Three New Members, Is Targeted as One Entity to Kinetochores in Mitosis". Mol. Biol. Cell 15 (7): 3333–44. doi:10.1091/mbc.E03-12-0878. PMC 452587. PMID 15146057.
• Panagopoulos I, Nilsson T, Domanski HA, et al. (2006). "Fusion of the SEC31L1 and ALK genes in an inflammatory myofibroblastic tumor". Int. J. Cancer 118 (5): 1181–6. doi:10.1002/ijc.21490. PMID 16161041.
• Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Stagg SM, Gürkan C, Fowler DM, et al. (2006). "Structure of the Sec13/31 COPII coat cage". Nature 439 (7073): 234–8. doi:10.1038/nature04339. PMID 16407955.
• Yamasaki A, Tani K, Yamamoto A, et al. (2007). "The Ca2+-binding Protein ALG-2 Is Recruited to Endoplasmic Reticulum Exit Sites by Sec31A and Stabilizes the Localization of Sec31A". Mol. Biol. Cell 17 (11): 4876–87. doi:10.1091/mbc.E06-05-0444. PMC 1635383. PMID 16957052.
• Shibata H, Suzuki H, Yoshida H, Maki M (2007). "ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit sites in a Ca2+-dependent manner". Biochem. Biophys. Res. Commun. 353 (3): 756–63. doi:10.1016/j.bbrc.2006.12.101. PMID 17196169.
• la Cour JM, Mollerup J, Berchtold MW (2007). "ALG-2 oscillates in subcellular localization, unitemporally with calcium oscillations". Biochem. Biophys. Res. Commun. 353 (4): 1063–7. doi:10.1016/j.bbrc.2006.12.143. PMID 17214967.