Profilin-1

Details

Name
Profilin-1
Synonyms
  • Epididymis tissue protein Li 184a
  • Profilin I
Gene Name
PFN1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0012867|Profilin-1
MAGWNAYIDNLMADGTCQDAAIVGYKDSPSVWAAVPGKTFVNITPAEVGVLVGKDRSSFY
VNGLTLGGQKCSVIRDSLLQDGEFSMDLRTKSTGGAPTFNVTVTKTDKTLVLLMGKEGVH
GGLINKKCYEMASHLRRSQY
Number of residues
140
Molecular Weight
15054.145
Theoretical pI
8.46
GO Classification
Functions
actin binding / actin monomer binding / adenyl-nucleotide exchange factor activity / phosphatidylinositol-4,5-bisphosphate binding / poly(A) RNA binding / proline-rich region binding
Processes
actin cytoskeleton organization / blood coagulation / negative regulation of actin filament bundle assembly / negative regulation of actin filament polymerization / negative regulation of stress fiber assembly / neural tube closure / platelet activation / platelet degranulation / positive regulation of actin filament bundle assembly / positive regulation of actin filament polymerization / positive regulation of ATPase activity / positive regulation of epithelial cell migration / positive regulation of ruffle assembly / protein stabilization / regulation of transcription from RNA polymerase II promoter
Components
blood microparticle / cell cortex / cytoplasm / cytoskeleton / cytosol / extracellular exosome / focal adhesion / membrane / nucleus
General Function
Proline-rich region binding
Specific 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. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0012868|Profilin-1 (PFN1)
ATGGCCGGGTGGAACGCCTACATCGACAACCTCATGGCGGACGGGACCTGTCAGGACGCG
GCCATCGTGGGCTACAAGGACTCGCCCTCCGTCTGGGCCGCCGTCCCCGGGAAAACGTTC
GTCAACATCACGCCAGCTGAGGTGGGTGTCCTGGTTGGCAAAGACCGGTCAAGTTTTTAC
GTGAATGGGCTGACACTTGGGGGCCAGAAATGTTCGGTGATCCGGGACTCACTGCTGCAG
GATGGGGAATTTAGCATGGATCTTCGTACCAAGAGCACCGGTGGGGCCCCCACCTTCAAT
GTCACTGTCACCAAGACTGACAAGACGCTAGTCCTGCTGATGGGCAAAGAAGGTGTCCAC
GGTGGTTTGATCAACAAGAAATGTTATGAAATGGCCTCCCACCTTCGGCGTTCCCAGTAC
TGA
Chromosome Location
17
Locus
17p13.3
External Identifiers
ResourceLink
UniProtKB IDP07737
UniProtKB Entry NamePROF1_HUMAN
GenBank Protein ID190386
GenBank Gene IDJ03191
HGNC IDHGNC:8881
General References
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  5. Ampe C, Markey F, Lindberg U, Vandekerckhove J: The primary structure of human platelet profilin: reinvestigation of the calf spleen profilin sequence. FEBS Lett. 1988 Feb 8;228(1):17-21. [Article]
  6. Gieselmann R, Kwiatkowski DJ, Janmey PA, Witke W: Distinct biochemical characteristics of the two human profilin isoforms. Eur J Biochem. 1995 May 1;229(3):621-8. [Article]
  7. Stuven T, Hartmann E, Gorlich D: Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes. EMBO J. 2003 Nov 3;22(21):5928-40. [Article]
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  18. Metzler WJ, Constantine KL, Friedrichs MS, Bell AJ, Ernst EG, Lavoie TB, Mueller L: Characterization of the three-dimensional solution structure of human profilin: 1H, 13C, and 15N NMR assignments and global folding pattern. Biochemistry. 1993 Dec 21;32(50):13818-29. [Article]
  19. Mahoney NM, Janmey PA, Almo SC: Structure of the profilin-poly-L-proline complex involved in morphogenesis and cytoskeletal regulation. Nat Struct Biol. 1997 Nov;4(11):953-60. [Article]
  20. Mahoney NM, Rozwarski DA, Fedorov E, Fedorov AA, Almo SC: Profilin binds proline-rich ligands in two distinct amide backbone orientations. Nat Struct Biol. 1999 Jul;6(7):666-71. [Article]
  21. 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. 2007 Oct 31;26(21):4597-606. Epub 2007 Oct 4. [Article]
  22. 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. 2008 Aug 19;105(33):11748-53. doi: 10.1073/pnas.0805852105. Epub 2008 Aug 8. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB079087-HYDROXY-4-METHYL-3-(2-HYDROXY-ETHYL)COUMARINexperimentalunknownDetails
DB11638Artenimolapproved, experimental, investigationalunknownligandDetails