PFN2

Profilin 2
PDB rendering based on 1d1j.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1D1J​
Identifiers
Symbols	PFN2 ; D3S1319E; PFL
External IDs	OMIM: 176590 MGI: 97550 HomoloGene: 1974 GeneCards: PFN2 Gene
Gene ontology Molecular function • adenyl-nucleotide exchange factor activity • actin monomer binding • protein binding • phosphatidylinositol-4,5-bisphosphate binding Cellular component • cytoplasm • cytoskeleton • terminal bouton • extracellular exosome Biological process • negative regulation of epithelial cell migration • actin cytoskeleton organization • negative regulation of actin filament polymerization • positive regulation of actin filament polymerization • positive regulation of actin filament bundle assembly • positive regulation of ATPase activity • positive regulation of peptidyl-serine phosphorylation • protein stabilization • positive regulation of stress fiber assembly • negative regulation of ruffle assembly • regulation of synaptic vesicle exocytosis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5217	18645
Ensembl	ENSG00000070087	ENSMUSG00000027805
UniProt	P35080	Q9JJV2
RefSeq (mRNA)	NM_002628	NM_019410
RefSeq (protein)	NP_002619	NP_062283
Location (UCSC)	Chr 3: 149.96 – 150.05 Mb	Chr 3: 57.84 – 57.85 Mb
PubMed search

Profilin-2 is a protein that in humans is encoded by the PFN2 gene.^[1][2][3]

The protein encoded by this gene is a ubiquitous actin monomer-binding protein belonging to the profilin family. It is thought to regulate actin polymerization in response to extracellular signals. There are two alternatively spliced transcript variants encoding different isoforms described for this gene.^[3]

Interactions

PFN2 has been shown to interact with ROCK1,^[4] Vasodilator-stimulated phosphoprotein,^[5][6] CCDC113^[7] and FMNL1.^[8]

References

1. Joensuu T, Blanco G, Pakarinen L, Sistonen P, Kaariainen H, Brown S, Chapelle A, Sankila EM (March 1997). "Refined mapping of the Usher syndrome type III locus on chromosome 3, exclusion of candidate genes, and identification of the putative mouse homologous region". Genomics 38 (3): 255–63. doi:10.1006/geno.1996.0626. PMID 8975700.
2. Honore B, Madsen P, Andersen AH, Leffers H (October 1993). "Cloning and expression of a novel human profilin variant, profilin II". FEBS Lett 330 (2): 151–5. doi:10.1016/0014-5793(93)80262-S. PMID 8365484.
3. "Entrez Gene: PFN2 profilin 2".
4. Da Silva, Jorge Santos; Medina Miguel; Zuliani Cecilia; Di Nardo Alessia; Witke Walter; Dotti Carlos G (September 2003). "RhoA/ROCK regulation of neuritogenesis via profilin IIa–mediated control of actin stability". J. Cell Biol. (United States) 162 (7): 1267–79. doi:10.1083/jcb.200304021. ISSN 0021-9525. PMC 2173969. PMID 14517206.
5. Reinhard, M; Giehl K; Abel K; Haffner C; Jarchau T; Hoppe V; Jockusch B M; Walter U (April 1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. (ENGLAND) 14 (8): 1583–9. ISSN 0261-4189. PMC 398250. PMID 7737110.
6. Harbeck, B; Hüttelmaier S; Schluter K; Jockusch B M; Illenberger S (October 2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. (UNITED STATES) 275 (40): 30817–25. doi:10.1074/jbc.M005066200. ISSN 0021-9258. PMID 10882740.
7. "Coiled-Coil Domain Containing 113". GeneCards. Retrieved 5/8/2013. Check date values in: |access-date= (help)
8. Yayoshi-Yamamoto, S; Taniuchi I; Watanabe T (September 2000). "FRL, a Novel Formin-Related Protein, Binds to Rac and Regulates Cell Motility and Survival of Macrophages". Mol. Cell. Biol. (UNITED STATES) 20 (18): 6872–81. doi:10.1128/MCB.20.18.6872-6881.2000. ISSN 0270-7306. PMC 86228. PMID 10958683.

Further reading

• Qualmann B, Kessels MM (2003). "Endocytosis and the cytoskeleton". Int. Rev. Cytol. International Review of Cytology 220: 93–144. doi:10.1016/S0074-7696(02)20004-2. ISBN 978-0-12-364624-8. PMID 12224553.
• Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
• Kwiatkowski DJ, Bruns GA (1988). "Human profilin. Molecular cloning, sequence comparison, and chromosomal analysis". J. Biol. Chem. 263 (12): 5910–5. PMID 3356709.
• Reinhard M, Giehl K, Abel K, et al. (1995). "The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins". EMBO J. 14 (8): 1583–9. PMC 398250. PMID 7737110.
• Gieselmann R, Kwiatkowski DJ, Janmey PA, Witke W (1995). "Distinct biochemical characteristics of the two human profilin isoforms". Eur. J. Biochem. 229 (3): 621–8. doi:10.1111/j.1432-1033.1995.tb20506.x. PMID 7758455.
• Naylor SL, Carritt B, Boileau C, et al. (1996). "Report of the sixth international workshop on human chromosome 3 mapping 1995". Cytogenet. Cell Genet. 72 (4): 255–70. doi:10.1159/000134204. PMID 8641130.
• Witke W, Podtelejnikov AV, Di Nardo A, et al. (1998). "In mouse brain profilin I and profilin II associate with regulators of the endocytic pathway and actin assembly". EMBO J. 17 (4): 967–76. doi:10.1093/emboj/17.4.967. PMC 1170446. PMID 9463375.
• Nodelman IM, Bowman GD, Lindberg U, Schutt CE (2000). "X-ray structure determination of human profilin II: A comparative structural analysis of human profilins". J. Mol. Biol. 294 (5): 1271–85. doi:10.1006/jmbi.1999.3318. PMID 10600384.
• Harbeck B, Hüttelmaier S, Schluter K, et al. (2000). "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin". J. Biol. Chem. 275 (40): 30817–25. doi:10.1074/jbc.M005066200. PMID 10882740.
• Lambrechts A, Kwiatkowski AV, Lanier LM, et al. (2000). "cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains". J. Biol. Chem. 275 (46): 36143–51. doi:10.1074/jbc.M006274200. PMID 10945997.
• Lambrechts A, Braun A, Jonckheere V, et al. (2000). "Profilin II Is Alternatively Spliced, Resulting in Profilin Isoforms That Are Differentially Expressed and Have Distinct Biochemical Properties". Mol. Cell. Biol. 20 (21): 8209–19. doi:10.1128/MCB.20.21.8209-8219.2000. PMC 86430. PMID 11027290.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Tojo H, Kaieda I, Hattori H, et al. (2004). "The Formin family protein, formin homolog overexpressed in spleen, interacts with the insulin-responsive aminopeptidase and profilin IIa". Mol. Endocrinol. 17 (7): 1216–29. doi:10.1210/me.2003-0056. PMID 12677009.
• Da Silva JS, Medina M, Zuliani C, et al. (2003). "RhoA/ROCK regulation of neuritogenesis via profilin IIa–mediated control of actin stability". J. Cell Biol. 162 (7): 1267–79. doi:10.1083/jcb.200304021. PMC 2173969. PMID 14517206.
• Goehler H, Lalowski M, Stelzl U, et al. (2004). "A protein interaction network links GIT1, an enhancer of huntingtin aggregation, to Huntington's disease". Mol. Cell 15 (6): 853–65. doi:10.1016/j.molcel.2004.09.016. PMID 15383276.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Lederer M, Jockusch BM, Rothkegel M (2005). "Profilin regulates the activity of p42POP, a novel Myb-related transcription factor". J. Cell. Sci. 118 (Pt 2): 331–41. doi:10.1242/jcs.01618. PMID 15615774.