node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
CRT1 | CRT2 | O04151 | Q38858 | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | 0.948 |
CRT1 | CRT3 | O04151 | O04153 | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. | 0.916 |
CRT2 | CRT1 | Q38858 | O04151 | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | 0.948 |
CRT2 | CRT3 | Q38858 | O04153 | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. | 0.919 |
CRT3 | CRT1 | O04153 | O04151 | Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. | Calreticulin-1; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | 0.916 |
CRT3 | CRT2 | O04153 | Q38858 | Calreticulin-3; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Required for elongation factor Tu receptor (EFR) accumulation and for EFR, but not flagellin-sensing 2 (FLS2) signaling. | Calreticulin-2; Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). | 0.919 |
PRF1 | VLN5 | Q42449 | Q9LVC6 | Profilin-1; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. Coordinates the stochastic dynamic properties of actin filaments by modulating formin- mediated actin nucleation and assembly during axial cell expansion. Binds G-actin and poly-L-proline in vitro. Inhib [...] | Villin-5; Major actin filament stabilizing factor and regulator of actin dynamics. Binds actin and actin filament bundles in a Ca(2+)- insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts synergistically with VLN2 (AC O81644) to regulate polarized pollen tube growth. Belongs to the villin/gelsolin family. | 0.855 |
PRF2 | VLN5 | Q42418 | Q9LVC6 | Profilin-2; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds G- actin and poly-L-proline with low affinity in vitro. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. May be involved in the cross-talk between vesicular trafficking and the actin cytoskeleton. At high concentrations, profilin prevents the pol [...] | Villin-5; Major actin filament stabilizing factor and regulator of actin dynamics. Binds actin and actin filament bundles in a Ca(2+)- insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts synergistically with VLN2 (AC O81644) to regulate polarized pollen tube growth. Belongs to the villin/gelsolin family. | 0.855 |
PRF3 | VLN5 | Q9FE63 | Q9LVC6 | Profilin-3; Binds to actin monomers and regulates the organization of the actin cytoskeleton. Can increase the critical concentration (Cc) of actin assembly in vitro. Acts as downstream effector of the hydrogen sulfide signaling to regulate the assembly and depolymerization of F-actin. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (Probable). Binding to the poly-proline motif of formin induces oligomerization of PRF3. PRF3 oligomers inhibit formin-mediated actin assembly to modulate plant immunity triggered by pathog [...] | Villin-5; Major actin filament stabilizing factor and regulator of actin dynamics. Binds actin and actin filament bundles in a Ca(2+)- insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts synergistically with VLN2 (AC O81644) to regulate polarized pollen tube growth. Belongs to the villin/gelsolin family. | 0.854 |
PRF4 | VLN5 | Q38904 | Q9LVC6 | Profilin-4; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF5 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips. | Villin-5; Major actin filament stabilizing factor and regulator of actin dynamics. Binds actin and actin filament bundles in a Ca(2+)- insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts synergistically with VLN2 (AC O81644) to regulate polarized pollen tube growth. Belongs to the villin/gelsolin family. | 0.856 |
PRF5 | VLN5 | Q38905 | Q9LVC6 | Profilin-5; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF4 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips. | Villin-5; Major actin filament stabilizing factor and regulator of actin dynamics. Binds actin and actin filament bundles in a Ca(2+)- insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts synergistically with VLN2 (AC O81644) to regulate polarized pollen tube growth. Belongs to the villin/gelsolin family. | 0.854 |
VLN5 | PRF1 | Q9LVC6 | Q42449 | Villin-5; Major actin filament stabilizing factor and regulator of actin dynamics. Binds actin and actin filament bundles in a Ca(2+)- insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts synergistically with VLN2 (AC O81644) to regulate polarized pollen tube growth. Belongs to the villin/gelsolin family. | Profilin-1; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. Coordinates the stochastic dynamic properties of actin filaments by modulating formin- mediated actin nucleation and assembly during axial cell expansion. Binds G-actin and poly-L-proline in vitro. Inhib [...] | 0.855 |
VLN5 | PRF2 | Q9LVC6 | Q42418 | Villin-5; Major actin filament stabilizing factor and regulator of actin dynamics. Binds actin and actin filament bundles in a Ca(2+)- insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts synergistically with VLN2 (AC O81644) to regulate polarized pollen tube growth. Belongs to the villin/gelsolin family. | Profilin-2; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Binds G- actin and poly-L-proline with low affinity in vitro. Binds ACT1, ACT7 and ACT11 and inhibits actin polymerization. May be involved in the cross-talk between vesicular trafficking and the actin cytoskeleton. At high concentrations, profilin prevents the pol [...] | 0.855 |
VLN5 | PRF3 | Q9LVC6 | Q9FE63 | Villin-5; Major actin filament stabilizing factor and regulator of actin dynamics. Binds actin and actin filament bundles in a Ca(2+)- insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts synergistically with VLN2 (AC O81644) to regulate polarized pollen tube growth. Belongs to the villin/gelsolin family. | Profilin-3; Binds to actin monomers and regulates the organization of the actin cytoskeleton. Can increase the critical concentration (Cc) of actin assembly in vitro. Acts as downstream effector of the hydrogen sulfide signaling to regulate the assembly and depolymerization of F-actin. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (Probable). Binding to the poly-proline motif of formin induces oligomerization of PRF3. PRF3 oligomers inhibit formin-mediated actin assembly to modulate plant immunity triggered by pathog [...] | 0.854 |
VLN5 | PRF4 | Q9LVC6 | Q38904 | Villin-5; Major actin filament stabilizing factor and regulator of actin dynamics. Binds actin and actin filament bundles in a Ca(2+)- insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts synergistically with VLN2 (AC O81644) to regulate polarized pollen tube growth. Belongs to the villin/gelsolin family. | Profilin-4; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF5 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips. | 0.856 |
VLN5 | PRF5 | Q9LVC6 | Q38905 | Villin-5; Major actin filament stabilizing factor and regulator of actin dynamics. Binds actin and actin filament bundles in a Ca(2+)- insensitive manner, but caps the barbed end of actin filaments and is able to sever them in a calcium-dependent manner. Required for the construction of actin collars in pollen tubes. Acts synergistically with VLN2 (AC O81644) to regulate polarized pollen tube growth. Belongs to the villin/gelsolin family. | Profilin-5; Binds to actin monomers and regulates the organization of the actin cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. At low concentrations, associates with the poly-proline motif of formins to enhance actin filament elongation rate. Acts redundantly with PRF4 to regulate apical actin polymerization at the tip of pollen tube and control polarized pollen tube growth. Functions probably by favoring formin-mediated actin polymerization at pollen tube tips. | 0.854 |