ANXA7

ANXA7
Identifiers
Aliases	ANXA7, ANX7, SNX, SYNEXIN, annexin A7
External IDs	MGI: 88031 HomoloGene: 36149 GeneCards: ANXA7
Gene ontology Molecular function • calcium ion binding • calcium-dependent protein binding • integrin binding • protein binding • calcium-dependent phospholipid binding • poly(A) RNA binding Cellular component • vesicle • cytosol • nuclear envelope • endoplasmic reticulum membrane • membrane • plasma membrane • chromaffin granule membrane • extracellular exosome • nucleus Biological process • hemostasis • epithelial cell differentiation • response to organic cyclic compound • response to salt stress • cellular calcium ion homeostasis • membrane fusion • negative regulation of gene expression • autophagy • response to calcium ion • regulation of cell shape • social behavior • cellular water homeostasis • cell proliferation Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	310	11750
Ensembl	ENSG00000138279	ENSMUSG00000021814
UniProt	P20073	Q07076
RefSeq (mRNA)	NM_001156 NM_004034 NM_001320879 NM_001320880	NM_001110794 NM_009674
RefSeq (protein)	NP_001147.1 NP_004025.1	NP_001104264.1 NP_033804.2
Location (UCSC)	Chr 10: 73.38 – 73.41 Mb	Chr 14: 20.46 – 20.48 Mb
PubMed search	[1]	[2]
Wikidata

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Annexin A7 is a protein that in humans is encoded by the ANXA7 gene.^[3][4]

Annexin VII is a member of the annexin family of calcium-dependent phospholipid binding proteins. The Annexin VII gene contains 14 exons and spans approximately 34 kb of DNA. An alternatively spliced cassette exon results in two mRNA transcripts of 2.0 and 2.4 kb which are predicted to generate two protein isoforms differing in their N-terminal domain. The alternative splicing event is tissue specific and the mRNA containing the cassette exon is prevalent in brain, heart and skeletal muscle. The transcripts also differ in their 3'-non coding regions by the use of two alternative poly(A) signals. The selection of poly(A) signals is independent of the mRNA splicing pattern. ~Annexin VII encodes a protein with a molecular weight of approximately 51 kDa with a unique, highly hydrophobic N-terminal domain of 167 amino acids and a conserved C-terminal region of 299 amino acids. The latter domain is composed of alternating hydrophobic and hydrophilic segments. Structural analysis of the protein suggests that Annexin VII is a membrane binding protein with diverse properties including voltage-sensitive calcium channel activity, ion selectivity and membrane fusion.^[4]

Interactions

ANXA7 has been shown to interact with ALG2^[5] and SRI.^[6]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Shirvan A, Srivastava M, Wang MG, Cultraro C, Magendzo K, McBride OW, Pollard HB, Burns AL (Jul 1994). "Divergent structure of the human synexin (annexin VII) gene and assignment to chromosome 10". Biochemistry. 33 (22): 6888–901. doi:10.1021/bi00188a019. PMID 7515686.
4. "Entrez Gene: ANXA7 annexin A7".
5. Satoh, Hirokazu; Nakano Yoshimi; Shibata Hideki; Maki Masatoshi (Nov 2002). "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner". Biochim. Biophys. Acta. Netherlands. 1600 (1–2): 61–7. doi:10.1016/S1570-9639(02)00445-4. ISSN 0006-3002. PMID 12445460.
6. Brownawell, A M; Creutz C E (Aug 1997). "Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII)". J. Biol. Chem. UNITED STATES. 272 (35): 22182–90. doi:10.1074/jbc.272.35.22182. ISSN 0021-9258. PMID 9268363.

Further reading

• Creutz CE, Moss S, Edwardson JM, et al. (1992). "Differential recognition of secretory vesicles by annexins. European Molecular Biology Organization Course "Advanced Techniques for Studying Secretion"". Biochem. Biophys. Res. Commun. 184 (1): 347–52. doi:10.1016/0006-291X(92)91199-Z. PMID 1533123.
• Magendzo K, Shirvan A, Cultraro C, et al. (1991). "Alternative splicing of human synexin mRNA in brain, cardiac, and skeletal muscle alters the unique N-terminal domain". J. Biol. Chem. 266 (5): 3228–32. PMID 1825209.
• Burns AL, Magendzo K, Shirvan A, et al. (1989). "Calcium channel activity of purified human synexin and structure of the human synexin gene". Proc. Natl. Acad. Sci. U.S.A. 86 (10): 3798–802. doi:10.1073/pnas.86.10.3798. PMC 287228. PMID 2542947.
• Selbert S, Fischer P, Pongratz D, et al. (1995). "Expression and localization of annexin VII (synexin) in muscle cells". J. Cell. Sci. 108 (1): 85–95. PMID 7738119.
• Zhang-Keck ZY, Srivastava M, Kozak CA, et al. (1994). "Genomic organization and chromosomal localization of the mouse synexin gene". Biochem. J. 301 (Pt 3): 835–45. PMC 1137063. PMID 8053909.
• 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.
• Brownawell AM, Creutz CE (1997). "Calcium-dependent binding of sorcin to the N-terminal domain of synexin (annexin VII)". J. Biol. Chem. 272 (35): 22182–90. doi:10.1074/jbc.272.35.22182. PMID 9268363.
• 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.
• Clemen CS, Hofmann A, Zamparelli C, Noegel AA (2000). "Expression and localisation of annexin VII (synexin) isoforms in differentiating myoblasts". J. Muscle Res. Cell. Motil. 20 (7): 669–79. doi:10.1023/A:1005524623337. PMID 10672515.
• Caohuy H, Pollard HB (2001). "Activation of annexin 7 by protein kinase C in vitro and in vivo". J. Biol. Chem. 276 (16): 12813–21. doi:10.1074/jbc.M008482200. PMID 11278415.
• Srivastava M, Bubendorf L, Srikantan V, et al. (2001). "ANX7, a candidate tumor suppressor gene for prostate cancer". Proc. Natl. Acad. Sci. U.S.A. 98 (8): 4575–80. doi:10.1073/pnas.071055798. PMC 31876. PMID 11287641.
• Clemen CS, Herr C, Lie AA, et al. (2001). "Annexin VII: an astroglial protein exhibiting a Ca2+-dependent subcellular distribution". NeuroReport. 12 (6): 1139–44. doi:10.1097/00001756-200105080-00018. PMID 11338180.
• Yu F, Finley RL, Raz A, Kim HR (2002). "Galectin-3 translocates to the perinuclear membranes and inhibits cytochrome c release from the mitochondria. A role for synexin in galectin-3 translocation". J. Biol. Chem. 277 (18): 15819–27. doi:10.1074/jbc.M200154200. PMID 11839755.
• Caohuy H, Pollard HB (2002). "Protein kinase C and guanosine triphosphate combine to potentiate calcium-dependent membrane fusion driven by annexin 7". J. Biol. Chem. 277 (28): 25217–25. doi:10.1074/jbc.M202452200. PMID 11994295.
• Satoh H, Nakano Y, Shibata H, Maki M (2002). "The penta-EF-hand domain of ALG-2 interacts with amino-terminal domains of both annexin VII and annexin XI in a Ca2+-dependent manner". Biochim. Biophys. Acta. 1600 (1–2): 61–7. doi:10.1016/S1570-9639(02)00445-4. PMID 12445460.
• 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.
• Castle J, Garrett-Engele P, Armour CD, et al. (2004). "Optimization of oligonucleotide arrays and RNA amplification protocols for analysis of transcript structure and alternative splicing". Genome Biol. 4 (10): R66. doi:10.1186/gb-2003-4-10-r66. PMC 328455. PMID 14519201.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.