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Protein

Twinfilin-1

Gene

Twf1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. actin monomer binding Source: BHF-UCL
  2. ATP binding Source: MGI
  3. phosphatidylinositol-4,5-bisphosphate binding Source: BHF-UCL
  4. protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  1. barbed-end actin filament capping Source: BHF-UCL
  2. negative regulation of actin filament polymerization Source: BHF-UCL
  3. peptidyl-tyrosine phosphorylation Source: GOC
  4. regulation of actin phosphorylation Source: MGI
  5. sequestering of actin monomers Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Twinfilin-1
Alternative name(s):
Protein A6
Gene namesi
Name:Twf1
Synonyms:Ptk9
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1100520. Twf1.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication
Note: Diffuse cytoplasmic localization with perinuclear and G-actin-rich cortical actin structures sublocalization. Also found at membrane ruffles and cell-cell contacts.

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. cell-cell junction Source: BHF-UCL
  3. cytoplasm Source: MGI
  4. filopodium Source: BHF-UCL
  5. focal adhesion Source: MGI
  6. myofibril Source: BHF-UCL
  7. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 350349Twinfilin-1PRO_0000214951Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei143 – 1431PhosphoserineBy similarity
Modified residuei309 – 3091Phosphotyrosine2 Publications
Modified residuei349 – 3491Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated on serine and threonine residues.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ91YR1.
PaxDbiQ91YR1.
PRIDEiQ91YR1.

PTM databases

PhosphoSiteiQ91YR1.

Expressioni

Tissue specificityi

Widely expressed with highest levels in brain, liver and kidney. Also expressed in heart, lung and testis. Not detected in spleen or skeletal muscle.3 Publications

Developmental stagei

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.1 Publication

Gene expression databases

BgeeiQ91YR1.
ExpressionAtlasiQ91YR1. baseline and differential.
GenevestigatoriQ91YR1.

Interactioni

Subunit structurei

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.4 Publications

Protein-protein interaction databases

BioGridi202468. 1 interaction.
DIPiDIP-33923N.
IntActiQ91YR1. 3 interactions.
MINTiMINT-1869546.

Structurei

Secondary structure

1
350
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2111Combined sources
Turni22 – 243Combined sources
Beta strandi26 – 327Combined sources
Beta strandi34 – 4310Combined sources
Helixi49 – 579Combined sources
Helixi58 – 603Combined sources
Beta strandi67 – 7711Combined sources
Beta strandi80 – 889Combined sources
Helixi95 – 11218Combined sources
Helixi114 – 1163Combined sources
Beta strandi117 – 1259Combined sources
Helixi126 – 1294Combined sources
Helixi131 – 1388Combined sources
Helixi184 – 19411Combined sources
Beta strandi199 – 2068Combined sources
Turni207 – 2104Combined sources
Beta strandi211 – 2166Combined sources
Helixi222 – 2243Combined sources
Helixi226 – 2283Combined sources
Beta strandi231 – 2333Combined sources
Beta strandi235 – 24511Combined sources
Beta strandi248 – 25811Combined sources
Beta strandi262 – 2643Combined sources
Helixi266 – 2749Combined sources
Helixi276 – 28712Combined sources
Beta strandi291 – 30212Combined sources
Helixi305 – 3128Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M4JX-ray1.60A/B1-142[»]
2D8BNMR-A161-313[»]
2HD7NMR-A176-316[»]
3DAWX-ray2.55B167-322[»]
ProteinModelPortaliQ91YR1.
SMRiQ91YR1. Positions 7-139, 161-313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91YR1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 139138ADF-H 1PROSITE-ProRule annotationAdd
BLAST
Domaini175 – 313139ADF-H 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 ADF-H domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG263290.
GeneTreeiENSGT00530000063868.
HOGENOMiHOG000168296.
HOVERGENiHBG000848.
InParanoidiQ91YR1.
KOiK08870.
OMAiTVFIYSM.
OrthoDBiEOG79GT6W.
PhylomeDBiQ91YR1.
TreeFamiTF352598.

Family and domain databases

Gene3Di3.40.20.10. 2 hits.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR028458. Twinfilin.
[Graphical view]
PANTHERiPTHR13759. PTHR13759. 1 hit.
PfamiPF00241. Cofilin_ADF. 2 hits.
[Graphical view]
SMARTiSM00102. ADF. 2 hits.
[Graphical view]
PROSITEiPS51263. ADF_H. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q91YR1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSHQTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVVG SCSPPSDSWE
60 70 80 90 100
QDYDSFVLPL LEDKQPCYVL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML
110 120 130 140 150
YAATRATLKK EFGGGHIKDE VFGTVKEDVS LHGYKKYLLS QSSPAPLTAA
160 170 180 190 200
EEELRQIKIN EVQTDVSVDT KHQTLQGVAF PISRDAFQAL EKLSKKQLNY
210 220 230 240 250
VQLEIDIKNE TIILANTENT ELRDLPKRIP KDSARYHFFL YKHSHEGDYL
260 270 280 290 300
ESVVFIYSMP GYTCSIRERM LYSSCKSPLL EIVERQLQMD VIRKIEIDNG
310 320 330 340 350
DELTADFLYD EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAEAEATTD
Length:350
Mass (Da):40,079
Last modified:April 4, 2006 - v2
Checksum:i643CBBA18D38D4E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti345 – 3451A → R in AAB66592. (PubMed:9249064)Curated
Sequence conflicti345 – 3451A → R in AAP31404. (PubMed:12807912)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti51 – 511Q → H.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27773.1.
RefSeqiNP_032997.3. NM_008971.4.
UniGeneiMm.490250.

Genome annotation databases

EnsembliENSMUST00000023087; ENSMUSP00000023087; ENSMUSG00000022451.
GeneIDi19230.
KEGGimmu:19230.
UCSCiuc007xjl.1. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Protein Spotlight

Molecular embrace - Issue 73 of August 2006

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS27773.1.
RefSeqiNP_032997.3. NM_008971.4.
UniGeneiMm.490250.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M4JX-ray1.60A/B1-142[»]
2D8BNMR-A161-313[»]
2HD7NMR-A176-316[»]
3DAWX-ray2.55B167-322[»]
ProteinModelPortaliQ91YR1.
SMRiQ91YR1. Positions 7-139, 161-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202468. 1 interaction.
DIPiDIP-33923N.
IntActiQ91YR1. 3 interactions.
MINTiMINT-1869546.

PTM databases

PhosphoSiteiQ91YR1.

Proteomic databases

MaxQBiQ91YR1.
PaxDbiQ91YR1.
PRIDEiQ91YR1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023087; ENSMUSP00000023087; ENSMUSG00000022451.
GeneIDi19230.
KEGGimmu:19230.
UCSCiuc007xjl.1. mouse.

Organism-specific databases

CTDi5756.
MGIiMGI:1100520. Twf1.

Phylogenomic databases

eggNOGiNOG263290.
GeneTreeiENSGT00530000063868.
HOGENOMiHOG000168296.
HOVERGENiHBG000848.
InParanoidiQ91YR1.
KOiK08870.
OMAiTVFIYSM.
OrthoDBiEOG79GT6W.
PhylomeDBiQ91YR1.
TreeFamiTF352598.

Miscellaneous databases

ChiTaRSiTwf1. mouse.
EvolutionaryTraceiQ91YR1.
NextBioi296036.
PROiQ91YR1.
SOURCEiSearch...

Gene expression databases

BgeeiQ91YR1.
ExpressionAtlasiQ91YR1. baseline and differential.
GenevestigatoriQ91YR1.

Family and domain databases

Gene3Di3.40.20.10. 2 hits.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR028458. Twinfilin.
[Graphical view]
PANTHERiPTHR13759. PTHR13759. 1 hit.
PfamiPF00241. Cofilin_ADF. 2 hits.
[Graphical view]
SMARTiSM00102. ADF. 2 hits.
[Graphical view]
PROSITEiPS51263. ADF_H. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: STRUCTURE BY NMR OF 161-313.

Entry informationi

Entry nameiTWF1_MOUSE
AccessioniPrimary (citable) accession number: Q91YR1
Secondary accession number(s): O09132, Q52L77, Q80X09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: April 4, 2006
Last modified: February 4, 2015
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.