| IED ID | IndEnz0005000339 |
| Enzyme Type ID | lipase000339 |
| Protein Name |
Oleosin Fragment |
| Gene Name | |
| Organism | Helianthus annuus (Common sunflower) |
| Taxonomic Lineage | cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids campanulids Asterales Asteraceae Asteroideae Heliantheae alliance Heliantheae Helianthus Helianthus annuus (Common sunflower) |
| Enzyme Sequence | TTTTYDRHFTTTQPHYRQDDRSRYDQQTHSQSTSRTLAIIALLPVGGILLGLAALTFIGTLIGLALATPLFVIFSPIIVPAVLTIGLAVTGFLASGTFGLTGLSSLSYLFNMVRQTAGSVPESLDYVKGTLQDAGEYAGQKTKDFGQKIQSTAHEMGDQGQVGVHAQVGGGKEGRKSGDRT |
| Enzyme Length | 181 |
| Uniprot Accession Number | P29529 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Non-terminal residue (1); Region (4); Transmembrane (3) |
| Keywords | Lipid droplet;Membrane;Transmembrane;Transmembrane helix |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Lipid droplet. Membrane; Multi-pass membrane protein. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 19,205 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |