TWF1

Twinfilin-1 is a protein that in humans is encoded by the TWF1 gene.[5][6] This gene encodes twinfilin, an actin monomer-binding protein conserved from yeast to mammals. Studies of the mouse counterpart suggest that this protein may be an actin monomer-binding protein, and its localization to cortical G-actin-rich structures may be regulated by the small GTPase RAC1.[6]

TWF1
Identifiers
Aliases	TWF1, A6, PTK9, twinfilin actin binding protein 1
External IDs	OMIM: 610932 MGI: 1100520 HomoloGene: 48140 GeneCards: TWF1
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q12 Start 43,793,723 bp[1] End 43,806,375 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15|15 E3 Start 94,577,951 bp[2] End 94,589,889 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0032403 macromolecular complex binding • protein tyrosine kinase activity • ATP binding • actin monomer binding • phosphatidylinositol-4,5-bisphosphate binding • cadherin binding • actin binding • GO:0001948 protein binding • actin filament binding Cellular component • intracellular • cytoskeleton • focal adhesion • filopodium • actin cytoskeleton • intercellular junction • perinuclear region of cytoplasm • myofibril • ruffle membrane • cytoplasm • cytosol • actin filament Biological process • regulation of actin phosphorylation • barbed-end actin filament capping • sequestering of actin monomers • negative regulation of actin filament polymerization • positive regulation of cardiac muscle hypertrophy • regulation of lamellipodium assembly • positive regulation of neuron projection development • peptidyl-tyrosine phosphorylation • actin filament depolymerization Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5756	19230
Ensembl	ENSG00000151239	ENSMUSG00000022451
UniProt	Q12792	Q91YR1
RefSeq (mRNA)	NM_001242397 NM_002822 NM_198974	NM_008971
RefSeq (protein)	NP_001229326 NP_002813	NP_032997
Location (UCSC)	Chr 12: 43.79 – 43.81 Mb	Chr 15: 94.58 – 94.59 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Model organisms

Twf1 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Normal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal[7]
Clinical chemistry	Normal[8]
Plasma immunoglobulins	Normal
Haematology	Normal
Micronucleus test	Normal
Heart weight	Normal
Eye Histopathology	Normal
Salmonella infection	Normal[9]
Citrobacter infection	Normal[10]
All tests and analysis from[11][12]

Model organisms have been used in the study of TWF1 function. A conditional knockout mouse line, called Twf1^{tm1a(EUCOMM)Wtsi}[13][14] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[15][16][17]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[11][18] Twenty three tests were carried out on mutant mice, but no significant abnormalities were observed.[11]

References

1. GRCh38: Ensembl release 89: ENSG00000151239 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000022451 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Beeler JF, LaRochelle WJ, Chedid M, Tronick SR, Aaronson SA (February 1994). "Prokaryotic expression cloning of a novel human tyrosine kinase". Mol. Cell. Biol. 14 (2): 982–8. PMC 358453. PMID 7507208.
6. "Entrez Gene: TWF1 twinfilin, actin-binding protein, homolog 1 (Drosophila)".
7. "Eye morphology data for Twf1". Wellcome Trust Sanger Institute.
8. "Clinical chemistry data for Twf1". Wellcome Trust Sanger Institute.
9. "Salmonella infection data for Twf1". Wellcome Trust Sanger Institute.
10. "Citrobacter infection data for Twf1". Wellcome Trust Sanger Institute.
11. Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
12. Mouse Resources Portal, Wellcome Trust Sanger Institute.
13. "International Knockout Mouse Consortium".
14. "Mouse Genome Informatics".
15. Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
16. Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
17. Collins FS, Rossant J, Wurst W (January 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
18. van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

Further reading

• Palmgren S, Vartiainen M, Lappalainen P (2002). "Twinfilin, a molecular mailman for actin monomers". J. Cell Sci. 115 (Pt 5): 881–6. PMID 11870207.
• Hassel S, Eichner A, Yakymovych M, et al. (2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel electrophoresis and mass spectrometry". Proteomics. 4 (5): 1346–58. doi:10.1002/pmic.200300770. PMID 15188402.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Vartiainen MK, Sarkkinen EM, Matilainen T, et al. (2003). "Mammals have two twinfilin isoforms whose subcellular localizations and tissue distributions are differentially regulated". J. Biol. Chem. 278 (36): 34347–55. doi:10.1074/jbc.M303642200. PMID 12807912.
• Galey D, Becker K, Haughey N, et al. (2003). "Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes". J. Neurovirol. 9 (3): 358–71. doi:10.1080/13550280390201119. PMID 12775419.
• 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.
• Ojala PJ, Paavilainen VO, Vartiainen MK, et al. (2003). "The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers". Mol. Biol. Cell. 13 (11): 3811–21. doi:10.1091/mbc.E02-03-0157. PMC 133594. PMID 12429826.
• Paavilainen VO, Merckel MC, Falck S, et al. (2003). "Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin". J. Biol. Chem. 277 (45): 43089–95. doi:10.1074/jbc.M208225200. PMID 12207032.