title: Angiomotin belongs to a novel protein family with conserved coiled-coil and PDZ binding domains.
abstract: 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.
authors.affiliation: Department of Oncology and Pathology, Karolinska Institutet, CCK R8:03 Karolinska Hospital, S-171 76 Stockholm, Sweden. anders.bratt@cck.ki.se
authors.forename: Anders
authors.initials: A
authors.lastname: Bratt
authors.forename: William J
authors.initials: WJ
authors.lastname: Wilson
authors.forename: Boris
authors.initials: B
authors.lastname: Troyanovsky
authors.forename: Karin
authors.initials: K
authors.lastname: Aase
authors.forename: Reto
authors.initials: R
authors.lastname: Kessler
authors.forename: Erwin G
authors.initials: EG
authors.lastname: Van Meir
authors.forename: Lars
authors.initials: L
authors.lastname: Holmgren
authors.forename: Erwin G Van
authors.initials: EG
authors.lastname: Meir
mesh_terms: D000595:Amino Acid Sequence; D000091082:Angiomotins; D000818:Animals; D001665:Binding Sites / Q000235:genetics; D002352:Carrier Proteins / Q000235:genetics*; D017124:Conserved Sequence / Q000235:genetics*; D018076:DNA, Complementary / Q000737:chemistry / Q000235:genetics; D005260:Female; D015870:Gene Expression; D006801:Humans; D036341:Intercellular Signaling Peptides and Proteins; D008297:Male; D008565:Membrane Proteins; D051379:Mice; D008840:Microfilament Proteins; D008969:Molecular Sequence Data; D010802:Phylogeny; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
chemical_list: C423985:AMOT protein, human; D000091082:Angiomotins; D002352:Carrier Proteins; D018076:DNA, Complementary; D036341:Intercellular Signaling Peptides and Proteins; D008565:Membrane Proteins; D008840:Microfilament Proteins