nsLTP1: Non-specific lipid-transfer protein type 1 (nsLTP1) subfamily; Plant nsLTPs are small, soluble proteins that facilitate the transfer of fatty acids, phospholipids, glycolipids, and steroids between membranes. In addition to lipid transport and assembly, nsLTPs also play a key role in the defense of plants against pathogens. There are two closely-related types of nsLTPs, types 1 and 2, which differ in protein sequence, molecular weight, and biological properties. nsLTPs contain an internal hydrophobic cavity, which serves as the binding site for lipids. The hydrophobic cavity accommodates various fatty acid ligands containing from ten to 18 carbon atoms. In general, the cavity is larger in nsLTP1 than in nsLTP2. nsLTP1 proteins are located in extracellular layers and in vacuolar structures. They may be involved in the formation of cutin layers on plant surfaces by transporting cutin monomers. Many nsLTP1 proteins have been characterized as allergens in humans.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4154350   18 IECSDVLSRPVHCLSYFVTPRATltPTSACCRESEEVLGMANSMGAKEDLCNCFVGLIRGFRP-NPNKIEGLLSSCALQL 96
Cdd:cd01960   1 ISCGQVTSLLAPCLGYLTGGGPA--PSPACCSGVKSLNGLAKTTADRQAACNCLKSAAAGISGlNPGRAAGLPGKCGVSI 78

                        90
                ....*....|....
gi 4154350   97 FFPIDPVTalpDCT 110
Cdd:cd01960  79 PYPISPST---DCS 89

nsLTP1: Non-specific lipid-transfer protein type 1 (nsLTP1) subfamily; Plant nsLTPs are small, soluble proteins that facilitate the transfer of fatty acids, phospholipids, glycolipids, and steroids between membranes. In addition to lipid transport and assembly, nsLTPs also play a key role in the defense of plants against pathogens. There are two closely-related types of nsLTPs, types 1 and 2, which differ in protein sequence, molecular weight, and biological properties. nsLTPs contain an internal hydrophobic cavity, which serves as the binding site for lipids. The hydrophobic cavity accommodates various fatty acid ligands containing from ten to 18 carbon atoms. In general, the cavity is larger in nsLTP1 than in nsLTP2. nsLTP1 proteins are located in extracellular layers and in vacuolar structures. They may be involved in the formation of cutin layers on plant surfaces by transporting cutin monomers. Many nsLTP1 proteins have been characterized as allergens in humans.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4154350   18 IECSDVLSRPVHCLSYFVTPRATltPTSACCRESEEVLGMANSMGAKEDLCNCFVGLIRGFRP-NPNKIEGLLSSCALQL 96
Cdd:cd01960   1 ISCGQVTSLLAPCLGYLTGGGPA--PSPACCSGVKSLNGLAKTTADRQAACNCLKSAAAGISGlNPGRAAGLPGKCGVSI 78

                        90
                ....*....|....
gi 4154350   97 FFPIDPVTalpDCT 110
Cdd:cd01960  79 PYPISPST---DCS 89

nsLTP1: Non-specific lipid-transfer protein type 1 (nsLTP1) subfamily; Plant nsLTPs are small, soluble proteins that facilitate the transfer of fatty acids, phospholipids, glycolipids, and steroids between membranes. In addition to lipid transport and assembly, nsLTPs also play a key role in the defense of plants against pathogens. There are two closely-related types of nsLTPs, types 1 and 2, which differ in protein sequence, molecular weight, and biological properties. nsLTPs contain an internal hydrophobic cavity, which serves as the binding site for lipids. The hydrophobic cavity accommodates various fatty acid ligands containing from ten to 18 carbon atoms. In general, the cavity is larger in nsLTP1 than in nsLTP2. nsLTP1 proteins are located in extracellular layers and in vacuolar structures. They may be involved in the formation of cutin layers on plant surfaces by transporting cutin monomers. Many nsLTP1 proteins have been characterized as allergens in humans.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4154350   18 IECSDVLSRPVHCLSYFVTPRATltPTSACCRESEEVLGMANSMGAKEDLCNCFVGLIRGFRP-NPNKIEGLLSSCALQL 96
Cdd:cd01960   1 ISCGQVTSLLAPCLGYLTGGGPA--PSPACCSGVKSLNGLAKTTADRQAACNCLKSAAAGISGlNPGRAAGLPGKCGVSI 78

                        90
                ....*....|....
gi 4154350   97 FFPIDPVTalpDCT 110
Cdd:cd01960  79 PYPISPST---DCS 89