Q39165 · OLEO2_ARATH
- ProteinOleosin 21.2 kDa
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids199 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
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 (By similarity).
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Cellular Component | monolayer-surrounded lipid storage body | |
Molecular Function | mRNA binding | |
Biological Process | lipid storage | |
Biological Process | response to freezing | |
Biological Process | seed germination | |
Biological Process | seed oilbody biogenesis |
Names & Taxonomy
Protein names
- Recommended nameOleosin 21.2 kDa
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ39165
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Note: Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface (By similarity).
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 51-71 | Helical | ||||
Sequence: STQVLSLLIGVPVVGSLLALA | ||||||
Transmembrane | 72-92 | Helical | ||||
Sequence: GLLLAGSVIGLMVALPLFLLF | ||||||
Transmembrane | 96-116 | Helical | ||||
Sequence: IVPAALTIGLAMTGFLASGMF |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Modified residue | 2 | N-acetylalanine | ||||
Sequence: A | ||||||
Chain | PRO_0000108128 | 2-199 | Oleosin 21.2 kDa | |||
Sequence: ADTHRVDRTDRHFQFQSPYEGGRGQGQYEGDRGYGGGGYKSMMPESGPSSTQVLSLLIGVPVVGSLLALAGLLLAGSVIGLMVALPLFLLFSPVIVPAALTIGLAMTGFLASGMFGLTGLSSISWVMNYLRGTRRTVPEQLEYAKRRMADAVGYAGQKGKEMGQHVQNKAQDVKQYDISKPHDTTTKGHETQGRTTAA |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
In siliques, expression is first detected at stage 7 when the siliques are green-brown. Expression then rises steadily to reach a maximum at maturity.
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MADTHRVDRTDRHFQ | ||||||
Region | 1-31 | Disordered | ||||
Sequence: MADTHRVDRTDRHFQFQSPYEGGRGQGQYEG | ||||||
Region | 2-56 | Polar | ||||
Sequence: ADTHRVDRTDRHFQFQSPYEGGRGQGQYEGDRGYGGGGYKSMMPESGPSSTQVLS | ||||||
Region | 57-128 | Hydrophobic | ||||
Sequence: LLIGVPVVGSLLALAGLLLAGSVIGLMVALPLFLLFSPVIVPAALTIGLAMTGFLASGMFGLTGLSSISWVM | ||||||
Region | 159-199 | Disordered | ||||
Sequence: KGKEMGQHVQNKAQDVKQYDISKPHDTTTKGHETQGRTTAA | ||||||
Compositional bias | 176-190 | Basic and acidic residues | ||||
Sequence: QYDISKPHDTTTKGH |
Sequence similarities
Belongs to the oleosin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length199
- Mass (Da)21,279
- Last updated1996-11-01 v1
- Checksum0CC71620528F8BDF
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MADTHRVDRTDRHFQ | ||||||
Sequence conflict | 93 | in Ref. 6; CAA79025 | ||||
Sequence: S → A | ||||||
Sequence conflict | 100 | in Ref. 2; CAA63022 | ||||
Sequence: A → G | ||||||
Sequence conflict | 135 | in Ref. 2; CAA63022 | ||||
Sequence: R → K | ||||||
Compositional bias | 176-190 | Basic and acidic residues | ||||
Sequence: QYDISKPHDTTTKGH | ||||||
Sequence conflict | 195 | in Ref. 2; CAA63022 | ||||
Sequence: R → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L40954 EMBL· GenBank· DDBJ | AAA87295.1 EMBL· GenBank· DDBJ | mRNA | ||
X91956 EMBL· GenBank· DDBJ | CAA63022.1 EMBL· GenBank· DDBJ | mRNA | ||
AB006702 EMBL· GenBank· DDBJ | BAB11599.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002688 EMBL· GenBank· DDBJ | AED94546.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY057590 EMBL· GenBank· DDBJ | AAL14385.1 EMBL· GenBank· DDBJ | mRNA | ||
AY113011 EMBL· GenBank· DDBJ | AAM47319.1 EMBL· GenBank· DDBJ | mRNA | ||
Z17657 EMBL· GenBank· DDBJ | CAA79025.1 EMBL· GenBank· DDBJ | mRNA |