posted on 2017-06-17, 05:00authored byMizuki Sasaki, Yasuko Akiyama-Oda, Hiroki Oda
Amino acid alignment of selected classical cadherins from arthropods and non-arthropod bilaterians. The classical cadherins shown are as follows: DE-cadherin (DE, fruit fly); Tc1-cadherin (Tc1, beetle); Am1-cadherin (Am1, honey bee); Ap1-cadherin (Ap1, aphid); Gb1-cadherin (Gb1, cricket); Fc1-cadherin (Fc1, springtail); Af1-cadherin (Af1, brine shrimp); Dp1-cadherin (Dp1, water flea); Ea1-cadherin (Ea1, copepod); Le1-cadherin (Le1, sea slater); Ha1-cadherin (Ha1, amphipod); Sm1-cadherin (Sm1, centipede); DN-cadherin (DN, fruit fly); Am2-cadherin (Am2, honey bee); Dp2-cadherin (Dp2, water flea); Le2-cadherin (Le2, sea slater); Cm-cadherin (Cm, shrimp); Sm2-cadherin (Sm2, centipede); Mo-cadherin (Mo, mite); Pt1-cadherin (Pt1, spider); Pt2-cadherin (Pt2, spider); Ct-cadherin (Ct, polychaete); Lg-cadherin (Lg, snail); LvG-cadherin (LvG, sea urchin); Bf-cadherin (Bf, amphioxus); Pn-cadherin (Pn, fish); Ta-cadherin (Ta, placozoan); and Mm5-cadherin (Mm5, mouse). The amino acid sequence of Pt1-cadherin is duplicated; one of the duplicates is placed at the top as a reference to show the domain subdivisions. The “-” character indicates introduced gaps. All residues of each cadherin sequence are shown, although some parts of the sequences were aligned poorly or not at all. Excluding the reference sequence, the amino acid sequences derived from different exons are distinguished using arbitrary background colors to indicate the exon-exon junctions in the transcripts. (PDF 385 kb)
Funding
Japan Society for the Promotion of Science (JSPS) Grants-in-Aid for Scientific Research (KAKENHI)