Annexin A7

Annexin A7 is a protein that in humans is encoded by the ANXA7 gene.

ANXA7
Identifiers
Aliases	ANXA7, ANX7, SNX, SYNEXIN, annexin A7
External IDs	OMIM: 186360; MGI: 88031; HomoloGene: 36149; GeneCards: ANXA7; OMA:ANXA7 - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10q22.2 Start 73,375,101 bp End 73,414,076 bp
Gene location (Mouse) Chr. Chromosome 14 (mouse) Band 14 A3|14 11.53 cM Start 20,505,328 bp End 20,530,201 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in oocyte islet of Langerhans secondary oocyte beta cell tendon tail of epididymis Achilles tendon gastrocnemius muscle right coronary artery mucosa of paranasal sinus Top expressed in skin of external ear lacrimal gland stroma of bone marrow endothelial cell of lymphatic vessel epithelium of stomach primary oocyte esophagus mucous cell of stomach lip ankle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function calcium ion binding calcium-dependent protein binding integrin binding protein binding calcium-dependent phospholipid binding RNA binding identical protein binding Cellular component vesicle cytosol nuclear envelope endoplasmic reticulum membrane membrane plasma membrane chromaffin granule membrane extracellular exosome nucleus collagen-containing extracellular matrix 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 population proliferation Sources:Amigo / QuickGO
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 NM_001374757 RefSeq (protein) NP_001147 NP_001307808 NP_001307809 NP_004025 NP_001104264 NP_033804 NP_001361686 Location (UCSC) Chr 10: 73.38 – 73.41 Mb Chr 14: 20.51 – 20.53 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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.

Interactions

ANXA7 has been shown to interact with ALG2 and SRI.

External links

• Human ANXA7 genome location and ANXA7 gene details page in the UCSC Genome Browser.

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. doi:10.1016/S0021-9258(18)49978-4. 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. Bibcode:1989PNAS...86.3798B. 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. doi:10.1242/jcs.108.1.85. 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. doi:10.1042/bj3010835. 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. S2CID 20610226.
• 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. Bibcode:2001PNAS...98.4575S. 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. S2CID 28417182.
• 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.