Fig 1.
Limax innexin transcripts expressed in the central nervous system.
Alignment of deduced amino acid sequences of the Limax innexin homologs identified in the transcriptome of the central nervous system. Limax innexin 9 and 11 had transcript variants: Limax innexin 9x1-9x4 and Limax innexin 11x1-11x2. The boxes show the four predicted transmembrane domains (TM1 to TM4), while the red arrows indicate two extracellular loops (EC1 and EC2). The black asterisks indicate the extracellular cysteine residues in the extracellular loops, while the red asterisk indicates the additional cysteine residue. The black arrow-heads indicate the P-X-X-X-W motif.
Fig 2.
Phylogenetic tree of molluscan innexins.
Phylogenetic analysis of molluscan innexins was performed using the maximum likelihood method with Homo sapiens pannexins as the outgroup. The percentage of replicate trees in which the associated taxa clustered together in the bootstrap test (2000 replicates) is shown next to the branches (only values greater than 50 are displayed). Sequence accession numbers are indicated next to species names. The names of Limax innexin homologs are in bold font.
Fig 3.
Protein sequence alignment of molluscan innexin orthologs in Group 1.
Alignment of deduced amino acid sequences of Limax innexin 1 and 2 with orthologous innexin sequences. The boxes show the four transmembrane domains, while the asterisks indicate the extracellular cysteine residues. The potential S-nitrosylation sites are shaded in black. The phosphorylation sites are indicated with shading or box in magenta (protein kinase C), yellow (protein kinase A), blue (casein kinase 1), cyan (casein kinase 2), orange (P34cdc), and gray (protein kinase G).
Fig 4.
Protein sequence alignment of molluscan innexin orthologs in Group 2.
Alignment of deduced amino acid sequences of Limax innexin 3 and 4 with orthologous innexin sequences. The boxes show the four transmembrane domains, while the asterisks indicate the extracellular cysteine residues. The potential S-nitrosylation sites are shaded in black. The phosphorylation sites are indicated with shading or box in magenta (protein kinase C), yellow (protein kinase A), blue (casein kinase 1), cyan (casein kinase 2), orange (P34cdc2), green (p38-mitogen-activated protein kinase), light green (proto-oncogene tyrosine-protein kinase Src), and gray (protein kinase G). Potential N-glycosylation sites are underlined with bold red lines.
Fig 5.
Protein sequence alignment of molluscan innexin orthologs in Group 3.
Alignment of deduced amino acid sequences of Limax innexin 5 with orthologous innexin sequences. The boxes show the four transmembrane domains, while the asterisks indicate the extracellular cysteine residues. The potential S-nitrosylation sites are shaded in black. The phosphorylation sites are indicated with shading or box in magenta (protein kinase C), yellow (protein kinase A), blue (casein kinase 1), cyan (casein kinase 2), orange (P34cdc2), and gray (protein kinase G).
Fig 6.
Protein sequence alignment of molluscan innexin orthologs in Group 4.
Alignment of deduced amino acid sequences of Limax innexin 6 and 7 with orthologous innexin sequences. The boxes show the four transmembrane domains, while the asterisks indicate the extracellular cysteine residues. The potential S-nitrosylation sites are shaded in black. The phosphorylation sites are indicated with shading or box in magenta (protein kinase C), yellow (protein kinase A), blue (casein kinase 1), cyan (casein kinase 2), orange (P34cdc2), green (p38-mitogen-activated protein kinase), light green (proto-oncogene tyrosine-protein kinase Src), and gray (protein kinase G).
Fig 7.
Protein sequence alignment of molluscan innexin orthologs in Group 5.
Alignment of deduced amino acid sequences of Limax innexin 8 and 9 with orthologous innexin sequences. The boxes show the four transmembrane domains, while the asterisks indicate the extracellular cysteine residues. The potential S-nitrosylation sites are shaded in black. The phosphorylation sites are indicated with shading or box in magenta (protein kinase C), yellow (protein kinase A), blue (casein kinase 1), cyan (casein kinase 2), green (p38-mitogen-activated protein kinase), and gray (protein kinase G). Potential N-glycosylation sites are underlined with bold red lines.
Fig 8.
Protein sequence alignment of molluscan innexin orthologs in Group 6.
Alignment of deduced amino acid sequences of Limax innexin 10 with orthologous innexin sequences. The boxes show the four transmembrane domains, while the asterisks indicate the extracellular cysteine residues. The phosphorylation sites are indicated with shading or box in magenta (protein kinase C), yellow (protein kinase A), cyan (casein kinase 2), orange (P34cdc2), green (p38-mitogen-activated protein kinase), and gray (protein kinase G).
Fig 9.
Protein sequence alignment of molluscan innexin orthologs in Group 7.
Alignment of deduced amino acid sequences of Limax innexin 11 and 12 with orthologous innexin sequences. The boxes show the four transmembrane domains, while the asterisks indicate the extracellular cysteine residues. The potential S-nitrosylation sites are shaded in black. The phosphorylation sites are indicated with shading or box in magenta (protein kinase C), yellow (protein kinase A), blue (casein kinase 1), cyan (casein kinase 2), orange (P34cdc2), green (p38-mitogen-activated protein kinase), and gray (protein kinase G). Potential N-glycosylation sites are underlined with bold red lines.
Fig 10.
Summary of the predicted modification sites in the innexin orthologs of the seven groups.
The conserved modification sites between Limax innexin sequence and at least one other ortholog sequence are shown.
Table 1.
Summary of identified Limax innexin circular RNAs (circRNAs) in the central nervous system.