A4KA32 · PROF5_PHLPR
- ProteinProfilin-5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids131 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations (By similarity).
Miscellaneous
The variability of the residues taking part of IgE-binding epitopes might be responsible of the difference in cross-reactivity among olive pollen cultivars, and between distantly related pollen species, leading to a variable range of allergy reactions among atopic patients.
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 | cell cortex | |
Cellular Component | cytoskeleton | |
Molecular Function | actin monomer binding | |
Biological Process | sequestering of actin monomers |
Keywords
- Molecular function
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProfilin-5
- Alternative names
- Allergen namePhl p 12
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Pooideae > Poodae > Poeae > Poeae Chloroplast Group 2 (Poeae type) > Poodinae > Phleinae > Phleum
Accessions
- Primary accessionA4KA32
Subcellular Location
Phenotypes & Variants
Allergenic properties
Causes an allergic reaction in human.
Keywords
- Disease
Protein family/group databases
PTM/Processing
Features
Showing features for initiator methionine, chain, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000425059 | 2-131 | Profilin-5 | |||
Sequence: SWQAYVDEHLMCEIEGHHLASAAILGHDGTVWAQSADFPQFKPEEITGIMKDFDEPGHLAPTGMFVAAAKYMVIQGEPGAVIRGKKGAGGITIKKTGQALVVGIYDEPMTPGQCNMVVERLGDYLVKQGL | ||||||
Disulfide bond | 13↔115 | |||||
Sequence: CEIEGHHLASAAILGHDGTVWAQSADFPQFKPEEITGIMKDFDEPGHLAPTGMFVAAAKYMVIQGEPGAVIRGKKGAGGITIKKTGQALVVGIYDEPMTPGQC | ||||||
Modified residue | 111 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated by MAP kinases.
Keywords
- PTM
Interaction
Subunit
Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio.
Structure
Sequence
- Sequence statusComplete
- Length131
- Mass (Da)14,115
- Last updated2007-05-01 v1
- Checksum06521C72343AEE3A
Polymorphism
Several isoforms of the allergen exist due to polymorphism.