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InterPro: IPR002097 Profilin/allergen
Protein matches
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UniProtKB Matches: 697 proteins |
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Accession
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IPR002097 Profilin |
Type
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Family |
Signatures
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InterPro Relationships
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Children
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IPR005454 Profilin, Mammalian
IPR005455 Profilin, plant
IPR016814 Profilin, apicomplexa
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GO Term annotation
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Process
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GO:0007010 cytoskeleton organization
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Function
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GO:0003779 actin binding
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Component
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GO:0015629 actin cytoskeleton
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InterPro annotation
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Entry Details in BioMart
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Abstract
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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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Structural links
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Database links
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Additional Reading
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Baek K, Liu X, Ferron F, Shu S, Korn ED, Dominguez R.
Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 11748-53
[PubMed: 18689676]
http://dx.doi.org/10.1073/pnas.0805852105
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Haarer BK, Brown SS.
Structure and function of profilin.
Cell Motil. Cytoskeleton 17 1990 71-4
[PubMed: 2257632]
http://dx.doi.org/10.1002/cm.970170202
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Sohn RH, Goldschmidt-Clermont PJ.
Profilin: at the crossroads of signal transduction and the actin cytoskeleton.
Bioessays 16 1994 465-72
[PubMed: 7945274]
http://dx.doi.org/10.1002/bies.950160705
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Kursula P, Kursula I, Massimi M, Song YH, Downer J, Stanley WA, Witke W, Wilmanns M.
High-resolution structural analysis of mammalian profilin 2a complex formation with two physiological ligands: the formin homology 1 domain of mDia1 and the proline-rich domain of VASP.
J. Mol. Biol. 375 2008 270-90
[PubMed: 18001770]
http://dx.doi.org/10.1016/j.jmb.2007.10.050
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Metzler WJ, Farmer BT 2nd, Constantine KL, Friedrichs MS, Lavoie T, Mueller L.
Refined solution structure of human profilin I.
Protein Sci. 4 1995 450-9
[PubMed: 7795529]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=7795529&action=stream&blobtype=pdf
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Nodelman IM, Bowman GD, Lindberg U, Schutt CE.
X-ray structure determination of human profilin II: A comparative structural analysis of human profilins.
J. Mol. Biol. 294 1999 1271-85
[PubMed: 10600384]
http://dx.doi.org/10.1006/jmbi.1999.3318
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Mahoney NM, Rozwarski DA, Fedorov E, Fedorov AA, Almo SC.
Profilin binds proline-rich ligands in two distinct amide backbone orientations.
Nat. Struct. Biol. 6 1999 666-71
[PubMed: 10404225]
http://dx.doi.org/10.1038/10722
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Ferron F, Rebowski G, Lee SH, Dominguez R.
Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP.
EMBO J. 26 2007 4597-606
[PubMed: 17914456]
http://dx.doi.org/10.1038/sj.emboj.7601874
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InterPro 23.1
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