DNA size 66.31 kb, mRNA size 6888 bp, 12 exons.

Angiomotin protein is 1084 amino acid residues in length. It contains two coiled coil domains 429-689 (261), 721-751 (31), a PDZ-binding motif 1081-1084 (4), a SMC_prok_B region 429-549 (121), and an angiomotin_C terminal 599-794 (196). Phosphorylations occur on S305, S312, S712, S714, T717, Y719, and T1061. Phosphorylated upon DNA damage, probably by ATM or ATR.
Isoforms:
- Isoform 1: p130 angiomotin
1084 amino acids, 118085 Da. This isoform has been chosen as the canonical sequence.
- Isoform 2: p80 angiomotin
675 amino acids, 72540 Da. The isoform differs from the canonical sequence with N-terminal alternative splicing region 1-409 (409) missing, which mediates the binding of angiomotin to F-actin stress fibres. The SMC_prok_B region is also missing in this isoform.

Expressed in placenta and skeletal muscle. Predominantly expressed in endothelial cells of capillaries, larger vessels of the placenta.

Cell junction, tight junction. Localized on the cell surface. May act as a transmembrane protein.

Mediates inhibitory effect of angiostatin on tube formation and the migration of endothelial cells toward growth factors during the formation of new blood vessels in the larger vessels of the placenta. Isoform-1 is found to control cell shape by association with F-actin fibres through N-terminal part of protein. The isoform 2 (p80) promotes angiogenesis, in part, by conferring a hypermigratory phenotype to endothelial cells.

The percent identity below represents identity of AMOT over an aligned region in Unigene.
Mus musculus: 88.1 (percent identity)
Oryctolagus cuniculus: 79
Sus scrofa: 72
Danio rerio: 68.9
Fugu rubripes: 65
Xenopus laevis: 61.8
Caenorhabditis elegans: 46
Saccharomyces cerevisiae: 47
Drosophila melanogaster: 36

Several polymorphisms have been found but none of them has shown any association with a disease. Furthermore, endothelial cells expressing mutated angiomotins have been reported failure in their function, including failure to migrate and inhibition of angiogenesis. Mutation with deletion of three amino acids from PDZ-binding motif results in inhibition of chemotaxis, embryos with this mutation may lead to death on embryonic day 9.5.