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ANNAT1 annexin D1

AnnAt1, oxy5
Encodes a member of the annexin gene family, a diverse, multigene family of calcium-dependent, membrane-binding proteins. The protein was determined to have peroxidase activity. This activity is thought to be dependent on the presence of post-translational modifications (most likely phosphorylation). The protein was shown to be present as a mixture of monomer and homodimer. The homodimerization seems to be dependent on the presence of Ca2+ or H2O2. The dimerization was prevented by the addition of DTT, ?-mercaptoethanol and TCEP. Annat1 mRNA is expressed in flowers, roots,leaves and stems and is most abundant in stems. mRNA levels are increased in response to oxidative stress. Developmental expression patterns suggest a role in Golgi-mediated polysaccharide secretion. (from NCBI)
Papers on AnnAt1
Arabidopsis annexins AnnAt1 and AnnAt4 interact with each other and regulate drought and salt stress responses.
Park et al., Seoul, South Korea. In Plant Cell Physiol, 2010
AnnAt1 and AnnAt4 interact with each other in a Ca2+-dependent manner and function to regulate responses to drought and salt stress.
The role of annexin 1 in drought stress in Arabidopsis.
Hennig et al., Warsaw, Poland. In Plant Physiol, 2009
AnnAt1 has a role in oxidative protection.
Potential role of annexin AnnAt1 from Arabidopsis thaliana in pH-mediated cellular response to environmental stimuli.
Pikula et al., Warsaw, Poland. In Plant Cell Physiol, 2007
The pH-sensitive ion channel activity of AnnAt1 may play a role in intracellular ion homeostasis.
Peroxidase activity of annexin 1 from Arabidopsis thaliana.
Pikula et al., Warsaw, Poland. In Biochem Biophys Res Commun, 2005
recombinant annexin 1 has peroxidase activity.
Proteomic identification of annexins, calcium-dependent membrane binding proteins that mediate osmotic stress and abscisic acid signal transduction in Arabidopsis.
Park et al., Kwangju, South Korea. In Plant Cell, 2004
results collectively suggest that AnnAt1 and AnnAt4 play important roles in osmotic stress and ABA signaling in a Ca2+-dependent manner
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