Detail Information for IndEnz0005000094
IED ID IndEnz0005000094
Enzyme Type ID lipase000094
Protein Name Oleosin H1
Allergen Ses i 4
Oleosin 17 kDa
allergen Ses i 4.0101
Gene Name
Organism Sesamum indicum (Oriental sesame) (Sesamum orientale)
Taxonomic Lineage cellular organisms Eukaryota Viridiplantae Streptophyta Streptophytina Embryophyta Tracheophyta Euphyllophyta Spermatophyta Magnoliopsida Mesangiospermae eudicotyledons Gunneridae Pentapetalae asterids lamiids Lamiales Pedaliaceae Sesamum Sesamum indicum (Oriental sesame) (Sesamum orientale)
Enzyme Sequence MADRDRPHPHQIQVHPQHPHRYEGGVKSLLPQKGPSTTQILAIITLLPISGTLLCLAGITLVGTLIGLAVATPVFVIFSPVLVPAAILIAGAVTAFLTSGAFGLTGLSSLSWVLNSFRRATGQGPLEYAKRGVQEGTLYVGEKTKQAGEAIKSTAKEGGREGTART
Enzyme Length 166
Uniprot Accession Number Q9FUJ9
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. {ECO:0000305}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Compositional bias (1); Initiator methionine (1); Modified residue (1); Motif (1); Region (1); Transmembrane (3)
Keywords Acetylation;Allergen;Lipid droplet;Membrane;Reference proteome;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Lipid droplet {ECO:0000255|RuleBase:RU000540, ECO:0000269|PubMed:12450125, ECO:0000269|PubMed:16436145}. Membrane {ECO:0000255|RuleBase:RU000540}; Multi-pass membrane protein {ECO:0000255|RuleBase:RU000540}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface. {ECO:0000305}.
Modified Residue MOD_RES 2; /note=N-acetylalanine; /evidence=ECO:0000250|UniProtKB:C3S7F0
Post Translational Modification
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif MOTIF 73..84; /note=Proline-knot; /evidence=ECO:0000305|PubMed:12450125
Gene Encoded By
Mass 17,373
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda