| SMART accession number: | SM00392
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| Description: |
Binds actin monomers, membrane polyphosphoinositides and poly-L-proline. |
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| Interpro abstract (IPR002097): |
Profilin is a small eukaryotic protein that binds to monomeric actin (G-actin) in a 1:1 ratio thus preventing the polymerisation of actin into filaments (F-actin). It can also in certain circumstance promote actin polymerisation. Profilin also binds to polyphosphoinositides such as PIP2. Overall sequence similarity among profilin from organisms which belong to different phyla (ranging from fungi to mammals) is low, but the N-terminal region is relatively well conserved. That region is thought to be involved in the binding to actin. A protein structurally similar to profilin is present in the genome of Variola virus and Vaccinia virus (gene A42R). Some of the proteins in this family are allergens. Allergies are hypersensitivity reactions of the immune system to specific substances called allergens (such as pollen, stings, drugs, or food) that, in most people, result in no symptoms. A nomenclature system has been established for antigens (allergens) that cause IgE-mediated atopic allergies in humans [WHO/IUIS Allergen Nomenclature Subcommittee King T.P., Hoffmann D., Loewenstein H., Marsh D.G., Platts-Mills T.A.E., Thomas W. Bull. World Health Organ. 72:797-806(1994)]. This nomenclature system is defined by a designation that is composed of the first three letters of the genus; a space; the first letter of the species name; a space and an arabic number. In the event that two species names have identical designations, they are discriminated from one another by adding one or more letters (as necessary) to each species designation. The allergens in this family include allergens with the following designations: Ara t 8, Bet v 2, Cyn d 12, Hel a 2, Mer a 1 and Phl p 11.
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| GO process: | cytoskeleton organization (GO:0007010) |
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| GO component: | actin cytoskeleton (GO:0015629) |
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| GO function: | actin binding (GO:0003779) |
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| Family alignment: |
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Click on the following links for more information.
- Evolution (species in which this domain is found)
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- Literature (relevant references for this domain)
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Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Sohn RH, Goldschmidt-Clermont PJ
- Profilin: at the crossroads of signal transduction and the actin cytoskeleton.
- Bioessays. 1994; 16: 465-72
- Display abstract
Despite its small size, profilin is an amazingly diverse and sophisticated protein whose precise role in cells continues to elude the understanding of researchers 15 years after its discovery. Its ubiquity, abundance and necessity for life in more evolved organisms certainly speaks for its extreme importance in cell function. So far, three ligands for profilin have been well-characterized in vitro: actin monomers, membrane polyphosphoinositides and poly-L-proline. In the years following its discovery, profilin's role in vivo progressed from that of a simple actin-binding protein which inhibits actin polymerization, to one which, as an important regulator of the cytoskeleton, can even promote actin polymerization under the appropriate circumstances. In addition, interactions with components of the phosphatidylinositol cycle and the RAS pathway in yeast implicate profilin as an important link through which the actin cytoskeleton is able to communicate with major signaling pathways.
- Metabolism (metabolic pathways involving proteins which contain this domain)
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| % proteins involved | KEGG pathway ID | Description |
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| 100.00 | map04810 | Regulation of actin cytoskeleton |
This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with PROF domain which could be assigned to a KEGG orthologous group, and not all proteins containing PROF domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%. |
- Structure (3D structures containing this domain)
3D Structures of PROF domains in PDB
| PDB code | Main view | Title | | 1a0k |  | Profilin i from arabidopsis thaliana |
| 1acf |  | Acanthamoeba castellanii profilin ib |
| 1awi |  | Human platelet profilin complexed with the l-pro10 peptide |
| 1cf0 |  | Human platelet profilin complexed with an l-pro10- iodotyrosine peptide |
| 1cjf |  | Profilin binds proline-rich ligands in two distinct amide backbone orientations |
| 1cqa |  | Birch pollen profilin |
| 1d1j |  | Crystal structure of human profilin ii |
| 1f2k |  | Crystal structure of acanthamoeba castellanii profilin ii, cubic crystal form |
| 1fik |  | Human platelet profilin i crystallized in low salt |
| 1fil |  | Human platelet profilin i crystallized in high salt actin- binding protein |
| 1g5u |  | Latex profilin hevb8 |
| 1hlu |  | Structure of bovine beta-actin-profilin complex with actin bound atp phosphates solvent accessible |
| 1k0k |  | Yeast profilin, cubic crystal form |
| 1pfl |  | Refined solution structure of human profilin i |
| 1pne |  | Crystallization and structure determination of bovine profilin at 2.0 angstroms resolution |
| 1prq |  | Acanthamoeba castellanii profilin ia |
| 1ypr |  | Saccharomyces cerevisiae (yeast) profilin |
| 2acg |  | Acanthamoeba castellanii profilin ii |
| 2btf |  | The structure of crystalline profilin-beta-actin |
| 2jkf |  | Plasmodium falciparum profilin |
| 2jkg |  | Plasmodium falciparum profilin |
| 2pav |  | Ternary complex of profilin-actin with the last poly-pro of human vasp |
| 2pbd |  | Ternary complex of profilin-actin with the poly-pro-gab domain of vasp* |
| 2prf |  | Three dimensional solution structure of acanthamoeba profilin i |
| 2v8c |  | Mouse profilin iia in complex with the proline-rich domain of vasp |
| 2v8f |  | Mouse profilin iia in complex with a double repeat from the fh1 domain of mdia1 |
| 2vk3 |  | Crystal structure of rat profilin 2a |
| 3chw |  | Complex of dictyostelium discoideum actin with profilin and the last poly-pro of human vasp |
| 3d9y |  | Crystal structure of profilin from schizosaccharomyces pombe |
| 3dav |  | Schizosaccharomyces pombe profilin crystallized from sodium formate |
| 3nul |  | Profilin i from arabidopsis thaliana |
- Links (links to other resources describing this domain)
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to expand nodes. To display all proteins with a PROF domain in a specific node, click on it.