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InterPro: IPR002097 Profilin/allergen

Protein matchesHelp
UniProtKB
Matches:
697 proteins
AccessionHelp IPR002097 Profilin
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR005454 Profilin, Mammalian
IPR005455 Profilin, plant
IPR016814 Profilin, apicomplexa
GO Term annotationHelp
Process GO:0007010 cytoskeleton organization
Function GO:0003779 actin binding
Component GO:0015629 actin cytoskeleton
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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.

Structural linksHelp
SCOP: d.110.1.1
CATH: 3.30.450.30
Database linksHelp
PDBe-motif: PS00414
PROSITE doc: PDOC00372
PANDIT: PF00235
Blocks: IPB002097

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002097 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P07274 Profilin

P07737 Profilin-1

P25843 Profilin

Q20025 Profilin-2

Q9JJV2 Profilin-2

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR005454 Profilin, Mammalian
IPR002097 Profilin/allergen
IPR005455 Profilin, plant
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp

Additional ReadingHelp
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
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
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
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
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
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
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
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