Angiomotin belongs to a novel protein family with conserved coiled-coil and PDZ binding domains

• Published in: Gene Vol. 298; no. 1; pp. 69 - 77
• Main Authors: Bratt, Anders, Wilson, William J., Troyanovsky, Boris, Aase, Karin, Kessler, Reto, Meir, Erwin G.V., Holmgren, Lars
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 18-09-2002
• Subjects: Amino Acid Sequence; Amotl1; Angiomotin; Angiomotin-like 1; Angiostatin; Animals; Binding Sites - genetics; Carrier Proteins - genetics; Conserved Sequence - genetics; DNA, Complementary - chemistry; DNA, Complementary - genetics; Female; Gene Expression; Humans; Intercellular Signaling Peptides and Proteins; JEAP; Junction-enriched and -associated protein; Leman coiled-coil protein; Male; Medicin och hälsovetenskap; Membrane Proteins; Mice; Molecular Sequence Data; Phylogeny; Sequence Alignment; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Angiomotin; JEAP; Amotl1; RT–PCR, reverse transcription–polymerase chain reaction; JEAP, junction-enriched and -associated protein; EST, expressed sequence tag; Leman coiled-coil protein; Junction-enriched and -associated protein; Amotl 1, angiomotin-like 1; LCCP, leman coiled-coil protein; Amotl 2, angiomotin-like 2; Angiostatin; Angiomotin-like 1
• ISSN: 0378-1119; 1879-0038
• DOI: 10.1016/S0378-1119(02)00928-9

Angiomotin has previously been identified in a yeast two-hybrid screen by its ability to bind to angiostatin, an inhibitor of novel formation of blood vessels (angiogenesis). Angiomotin mediates the inhibitory effect of angiostatin on endothelial cell migration and tube formation in vitro. Here we report that two human protein sequences, of which one is novel and one has been cloned previously, are similar to angiomotin and are members of a novel protein family, which we propose to call motins. These two genes have been named angiomotin-like 1 (
amotl1) and angiomotin-like 2 (
amotl2). We have cloned mouse angiomotin and identified
amotl1 and
amotl2 homologs in mice. The alignment of the amino acid sequences encoded by these six sequences spans 455 residues of which 64% was conserved in all six proteins. Sequence analysis showed that these sequences all share putative coiled-coil domains and PDZ-binding motifs. Sequence information from GenBank indicate that motins can be found in several species including the frog
Xenopus
laevis, the pufferfish
Fugu
rubripes and the nematode
Caenorhabditis
elegans. Further phylogenetic analysis indicates that
amotl2 is an evolutionary outgroup in relation to angiomotin and
amotl1. Northern blot analysis shows distinct expression patterns for each motin in various mouse tissues.