Q8H2C9 · PROF1_ARTVU
- ProteinProfilin-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids133 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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 binding to PIP2, it inhibits the formation of IP3 and DG (By similarity).
Possesses high binding affinity for poly(L-proline) (PubMed:27231348).
Possesses high binding affinity for poly(L-proline) (PubMed:27231348).
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 | |
Molecular Function | oligopeptide binding | |
Biological Process | sequestering of actin monomers |
Keywords
- Molecular function
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProfilin-1
- Alternative names
- Allergen nameArt v 4.01
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > asterids > campanulids > Asterales > Asteraceae > Asteroideae > Anthemideae > Artemisiinae > Artemisia
Accessions
- Primary accessionQ8H2C9
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Chain | PRO_0000199620 | 2-133 | Profilin-1 | |||
Sequence: SWQTYVDDHLMCDIEGTGQHLTSAAIFGTDGTVWAKSASFPEFKPNEIDAIIKEFNEAGQLAPTGLFLGGAKYMVIQGEAGAVIRGKKGAGGICIKKTGQAMVFGIYDEPVAPGQCNMVVERLGDYLLDQGM | ||||||
Disulfide bond | 95↔117 | |||||
Sequence: CIKKTGQAMVFGIYDEPVAPGQC |
Keywords
- PTM
Interaction
Subunit
Dimer and tetramer (PubMed:12530543).
Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio
Occurs in many kinds of cells as a complex with monomeric actin in a 1:1 ratio
Structure
Sequence
- Sequence statusComplete
- Length133
- Mass (Da)14,207
- Last updated2007-01-23 v3
- Checksum96FA8A3D7CA54E3D
Mass Spectrometry
Keywords
- Technical term