Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955332144  180 TKADAWEREELEKIKERYEKLLETIDSWEKRKKAKAIRKLNKHQhSESERKRAKVLKKYQDKMSYISQIAGGARAQAEER 259
Cdd:pfam03763   4 SKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIE-EKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 955332144  260 RRSEVLKAKEKANIIRTTGKIPGP 283
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106

Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955332144  180 TKADAWEREELEKIKERYEKLLETIDSWEKRKKAKAIRKLNKHQhSESERKRAKVLKKYQDKMSYISQIAGGARAQAEER 259
Cdd:pfam03763   4 SKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIE-EKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 955332144  260 RRSEVLKAKEKANIIRTTGKIPGP 283
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106

Remorin, C-terminal region; Remorins are plant-specific plasma membrane-associated proteins. In tobacco remorin co-purifies with lipid rafts. Most remorins have a variable, proline-rich N-half and a more conserved C-half that is predicted to form coiled coils. Consistent with this, circular dichroism studies have demonstrated that much of the protein is alpha-helical. Remorins exist in plasma membrane preparations as oligomeric structures and form filaments in vitro. The proteins can bind polyanions including the extracellular matrix component oligogalacturonic acid (OGA). In vitro, remorin in plasma membrane preparations is phosphorylated (principally on threonine residues) in the presence of OGA and thus co-purifies with a protein kinases(s). The biological functions of remorins are unknown but roles as components of the membrane/cytoskeleton are possible.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955332144  180 TKADAWEREELEKIKERYEKLLETIDSWEKRKKAKAIRKLNKHQhSESERKRAKVLKKYQDKMSYISQIAGGARAQAEER 259
Cdd:pfam03763   4 SKADAWEEAEKAKIENRYKREEAKIQAWENLKKAKAEAELRKIE-EKLEKKRAEALEKMKNKLARIHKKAEEKRASAEAK 82

                          90       100
                  ....*....|....*....|....
gi 955332144  260 RRSEVLKAKEKANIIRTTGKIPGP 283
Cdd:pfam03763  83 RGEEELKTEEKAAKIRATGKIPSK 106