Disease relevance of ANXA9

• The ANX31 gene locus was mapped by fluorescence in situ hybridization to human chromosome 1q21, remote from ten other paralogous human annexins on different chromosomes but near the epidermal differentiation gene complex, the S100A gene cluster and a breast-cancer translocation region [1].
• Pemphigus vulgaris antibody identifies pemphaxin. A novel keratinocyte annexin-like molecule binding acetylcholine [2].

High impact information on ANXA9

• Moreover and in contrast to other annexins this binding appears to be irreversible as the liposome-bound annexin A9 cannot be released by Ca(2+) chelation [3].
• DNA fragments of 1931 and 2790 bp corresponding to ANXA9 and SLC27A3 respectively were isolated, and 14 and 6 single nucleotide polymorphisms (SNPs) respectively were found in each gene [4].
• Additional antigens include the novel epithelial acetylcholine receptors (alpha9 and pemphaxin) [5].
• On the basis of comparative mapping between cattle/sheep and human for milk trait quantitative trait loci (QTL) on BTA3/OAR1, annexin A9 (ANXA9) and solute carrier family 27 (fatty acid transporter), member 3 (SLC27A3) were selected as candidate genes for fat content (FC) in sheep milk [4].
• For ANXA9 one SNP was located in exon 5 (A-->G 951) resulting in an amino acid change from histidine to arginine [6].

Biological context of ANXA9

• On the basis of fine mapping of a quantitative trait loci region of BTA3 for milk fat content, an examination of the comparative map between cattle and human indicates that the annexin 9 protein gene (ANXA9) and the fatty acid transport protein type 3 gene (SLC27A3) are two strong candidate genes [6].
• Screening of a keratinocyte lambdagt11 cDNA library with this antibody identified clones carrying cDNA inserts encoding a novel molecule exhibiting approximately 40% similarity with annexin-2, named pemphaxin (PX) [2].
• By employing 2.5 kb of the most 5' flanking region of the gene, containing 5' non-coding sequence, exon I and intron I in luciferase reporter assays in annexin A9 positive HEPA 1-6 cells, we reveal the existence of a minimal promoter located at the 3' flank of intron I [7].

Associations of ANXA9 with chemical compounds

• Annexin A9 is an atypical member of the annexin family of Ca(2+) and phospholipid-binding proteins, initially identified in EST data bases [7].

Other interactions of ANXA9

• Conversely, a tandem pair of novel annexins from the amphioxus Branchiostoma floridae resembled annexin A13 in gene structure and conserved the charged amino acids associated with the internal hydrophilic pore, but were devoid of external type 2 calcium-binding sites and incorporated K/RGD motifs instead, like annexin A9 [8].

References