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Q91YR1 (TWF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Twinfilin-1
Alternative name(s):
Protein A6
Gene names
Name:Twf1
Synonyms:Ptk9
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. Ref.1 Ref.5 Ref.6 Ref.8

Subunit structure

Interacts with G-actin; ADP-actin form and capping protein (CP). May also be able to interact with TWF2 and phosphoinositides, PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated. Ref.2 Ref.5 Ref.6 Ref.8

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Note: Diffuse cytoplasmic localization with perinuclear and G-actin-rich cortical actin structures sublocalization. Also found at membrane ruffles and cell-cell contacts. Ref.5

Tissue specificity

Widely expressed with highest levels in brain, liver and kidney. Also expressed in heart, lung and testis. Not detected in spleen or skeletal muscle. Ref.1 Ref.2 Ref.5

Developmental stage

Expression was widespread throughout the embryonic stages analyzed; E10.5, E12.5, E14.5 and E18.5. At E14.5, strongest expression was observed in the developing central and peripheral nervous system (CNS and PNS, respectively) and in the olfactory sensory epithelium. In the CNS, the proliferating neuronal precursors in the ventricular zone expressed it more than the postmitotic neurons. At E18.5, highest expression levels were detected in the mechanosensory hair cells of the inner ear and in the differentiated keratinocytes of the skin. Ref.2

Post-translational modification

Phosphorylated on serine and threonine residues By similarity. UniProtKB Q12792

Sequence similarities

Belongs to the actin-binding proteins ADF family. Twinfilin subfamily.

Contains 2 ADF-H domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 350349Twinfilin-1
PRO_0000214951

Regions

Domain2 – 139138ADF-H 1
Domain175 – 313139ADF-H 2

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue1431Phosphoserine By similarity
Modified residue3091Phosphotyrosine Ref.7 Ref.9
Modified residue3491Phosphothreonine Ref.10

Natural variations

Natural variant511Q → H. Ref.4

Experimental info

Sequence conflict3451A → R in AAB66592. Ref.1
Sequence conflict3451A → R in AAP31404. Ref.2

Secondary structure

................................................. 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q91YR1 [UniParc].

Last modified April 4, 2006. Version 2.
Checksum: 643CBBA18D38D4E0

FASTA35040,079
        10         20         30         40         50         60 
MSHQTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVVG SCSPPSDSWE QDYDSFVLPL 

        70         80         90        100        110        120 
LEDKQPCYVL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML YAATRATLKK EFGGGHIKDE 

       130        140        150        160        170        180 
VFGTVKEDVS LHGYKKYLLS QSSPAPLTAA EEELRQIKIN EVQTDVSVDT KHQTLQGVAF 

       190        200        210        220        230        240 
PISRDAFQAL EKLSKKQLNY VQLEIDIKNE TIILANTENT ELRDLPKRIP KDSARYHFFL 

       250        260        270        280        290        300 
YKHSHEGDYL ESVVFIYSMP GYTCSIRERM LYSSCKSPLL EIVERQLQMD VIRKIEIDNG 

       310        320        330        340        350 
DELTADFLYD EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAEAEATTD 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of the mouse homolog of the human A6 gene."
Beeler J.F., Patel B.K.R., Chedid M., LaRochelle W.J.
Gene 193:31-37(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[2]"Mammals have two twinfilin isoforms whose subcellular localizations and tissue distributions are differentially regulated."
Vartiainen M.K., Sarkkinen E.M., Matilainen T., Salminen M., Lappalainen P.
J. Biol. Chem. 278:34347-34355(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH TWF2 AND PHOSPHOINOSITIDE, DEVELOPMENTAL STAGE.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-51.
Strain: NMRI.
Tissue: Mammary gland and Mammary tumor.
[5]"Mouse A6/twinfilin is an actin monomer-binding protein that localizes to the regions of rapid actin dynamics."
Vartiainen M., Ojala P.J., Auvinen P., Peranen J., Lappalainen P.
Mol. Cell. Biol. 20:1772-1783(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[6]"Biological role and structural mechanism of twinfilin-capping protein interaction."
Falck S., Paavilainen V.O., Wear M.A., Grossmann J.G., Cooper J.A., Lappalainen P.
EMBO J. 23:3010-3019(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH G-ACTIN AND CAPPING PROTEINS.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Mammalian twinfilin sequesters ADP-G-actin and caps filament barbed ends: implications in motility."
Helfer E., Nevalainen E.M., Naumanen P., Romero S., Didry D., Pantaloni D., Lappalainen P., Carlier M.-F.
EMBO J. 25:1184-1195(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH G-ACTIN AND CAPPING PROTEINS.
[9]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[10]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[11]"Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin."
Paavilainen V.O., Merckel M.C., Falck S., Ojala P.J., Pohl E., Wilmanns M., Lappalainen P.
J. Biol. Chem. 277:43089-43095(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-142.
[12]"NMR solution structures of actin depolymerizing factor homology domains."
Goroncy A.K., Koshiba S., Tochio N., Tomizawa T., Sato M., Inoue M., Watanabe S., Hayashizaki Y., Tanaka A., Kigawa T., Yokoyama S.
Protein Sci. 18:2384-2392(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 161-313.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Molecular embrace - Issue 73 of August 2006

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U82324 mRNA. Translation: AAB66592.1.
AY267188 mRNA. Translation: AAP31404.1.
AK147990 mRNA. Translation: BAE28272.1.
AK150852 mRNA. Translation: BAE29908.1.
BC015081 mRNA. Translation: AAH15081.1.
BC094034 mRNA. Translation: AAH94034.1.
CCDSCCDS27773.1.
RefSeqNP_032997.3. NM_008971.4.
UniGeneMm.490250.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1M4JX-ray1.60A/B1-142[»]
2D8BNMR-A161-313[»]
2HD7NMR-A176-316[»]
3DAWX-ray2.55B167-322[»]
ProteinModelPortalQ91YR1.
SMRQ91YR1. Positions 7-139, 161-313.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202468. 1 interaction.
IntActQ91YR1. 3 interactions.
MINTMINT-1869546.

PTM databases

PhosphoSiteQ91YR1.

Proteomic databases

MaxQBQ91YR1.
PaxDbQ91YR1.
PRIDEQ91YR1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023087; ENSMUSP00000023087; ENSMUSG00000022451.
GeneID19230.
KEGGmmu:19230.
UCSCuc007xjl.1. mouse.

Organism-specific databases

CTD5756.
MGIMGI:1100520. Twf1.

Phylogenomic databases

eggNOGNOG263290.
GeneTreeENSGT00530000063868.
HOGENOMHOG000168296.
HOVERGENHBG000848.
InParanoidQ91YR1.
KOK08870.
OMATVFIYSM.
OrthoDBEOG79GT6W.
PhylomeDBQ91YR1.
TreeFamTF352598.

Gene expression databases

ArrayExpressQ91YR1.
BgeeQ91YR1.
GenevestigatorQ91YR1.

Family and domain databases

Gene3D3.40.20.10. 2 hits.
InterProIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR028458. Twinfilin.
[Graphical view]
PANTHERPTHR13759. PTHR13759. 1 hit.
PfamPF00241. Cofilin_ADF. 2 hits.
[Graphical view]
SMARTSM00102. ADF. 2 hits.
[Graphical view]
PROSITEPS51263. ADF_H. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTWF1. mouse.
EvolutionaryTraceQ91YR1.
NextBio296036.
PROQ91YR1.
SOURCESearch...

Entry information

Entry nameTWF1_MOUSE
AccessionPrimary (citable) accession number: Q91YR1
Secondary accession number(s): O09132, Q52L77, Q80X09
Entry history
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: April 4, 2006
Last modified: July 9, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot