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Protein

Twinfilin-2

Gene

Twf2

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. May play a role in regulating the mature length of the middle and short rows of stereocilia.2 Publications

GO - Molecular functioni

  • actin monomer binding Source: BHF-UCL
  • ATP binding Source: MGI
  • phosphatidylinositol-4,5-bisphosphate binding Source: BHF-UCL
  • poly(A) RNA binding Source: MGI
  • protein kinase C binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cilium biogenesis/degradation

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Twinfilin-2
Alternative name(s):
A6-related protein
Short name:
mA6RP
Twinfilin-1-like protein
Gene namesi
Name:Twf2
Synonyms:Ptk9l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1346078. Twf2.

Subcellular locationi

GO - Cellular componenti

  • cell Source: GOC
  • cytoplasm Source: MGI
  • cytoskeleton Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • filopodium Source: BHF-UCL
  • growth cone Source: MGI
  • lamellipodium Source: BHF-UCL
  • myofibril Source: BHF-UCL
  • perinuclear region of cytoplasm Source: BHF-UCL
  • stereocilium Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Disruption phenotypei

Mice lacking isoform 1 develop normally to adulthood, are fertile, and do not exhibit obvious morphological or behavioral abnormalities.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 349348Twinfilin-2PRO_0000233137Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei14 – 141N6-acetyllysineBy similarity
Modified residuei309 – 3091PhosphotyrosineCombined sources
Modified residuei349 – 3491PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on both serine/threonine and tyrosine.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9Z0P5.
MaxQBiQ9Z0P5.
PaxDbiQ9Z0P5.
PRIDEiQ9Z0P5.

PTM databases

iPTMnetiQ9Z0P5.
PhosphoSiteiQ9Z0P5.

Expressioni

Tissue specificityi

Isoform 1 is ubiquitously expressed (at protein level). Isoform 2 expression is restricted to heart and skeletal muscle where it is the predominant form.2 Publications

Developmental stagei

Expression was relatively weak during all of the embryonic stages. At E14.5, a slight increase in the expression could be observed in heart, CNS, and PNS. At E18.5, it is strongly expressed in the inner ear, hair cells and in the head muscles. No expression is detected in the nasal epithelium or in the skin keratinocytes.1 Publication

Gene expression databases

BgeeiQ9Z0P5.
ExpressionAtlasiQ9Z0P5. baseline and differential.
GenevisibleiQ9Z0P5. MM.

Interactioni

Subunit structurei

Interacts with G-actin; ADP-actin form and capping protein (CP). Isoform 2 interacts (via its N-terminal ADF-H domain) with G-actin (ADP-bound form) with significantly higher affinity than isoform 1. May also be able to interact with TWF1 and phosphoinositides, PI(4,5)P2. When bound to PI(4,5)P2, it is down-regulated. Interacts with MYO7A.3 Publications

GO - Molecular functioni

  • actin monomer binding Source: BHF-UCL
  • protein kinase C binding Source: MGI

Protein-protein interaction databases

BioGridi204847. 1 interaction.
DIPiDIP-61549N.
IntActiQ9Z0P5. 2 interactions.
MINTiMINT-4131249.
STRINGi10090.ENSMUSP00000024047.

Structurei

3D structure databases

ProteinModelPortaliQ9Z0P5.
SMRiQ9Z0P5. Positions 6-137, 181-313.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 139136ADF-H 1PROSITE-ProRule annotationAdd
BLAST
Domaini177 – 313137ADF-H 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 ADF-H domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1747. Eukaryota.
ENOG410XS1J. LUCA.
GeneTreeiENSGT00530000063868.
HOGENOMiHOG000168296.
HOVERGENiHBG000848.
InParanoidiQ9Z0P5.
KOiK08870.
OMAiHATPELK.
OrthoDBiEOG79GT6W.
PhylomeDBiQ9Z0P5.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative promoter usage. AlignAdd to basket

Isoform 1 (identifier: Q9Z0P5-1) [UniParc]FASTAAdd to basket

Also known as: Twf2a

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAHQTGIHAT EELKEFFAKA RAGSIRLIKV IIEDEQLVLG ASQEPVGRWD
60 70 80 90 100
QDYDRAVLPL LDAQEPCYLL FRLDSQNAQG FEWLFLAWSP DNSPVRLKML
110 120 130 140 150
YAATRATVKK EFGGGHIKDE LFGTVKDDLS LAGYQKHLSS CAAPAPLTSA
160 170 180 190 200
ERELQQIRIN EVKTEISVES KHQTLQGLAF PLQPEAQRAL QQLKQKTVNY
210 220 230 240 250
IQLKLDLERE TIELVHTEPT NVAQLPSRIP RDAARYHFFL YKHTHEGDAL
260 270 280 290 300
ESVVFIYSMP GYKCSIKERM LYSSCKSRLL DSVEQDFQLE IAKKIEIGDG
310 320 330 340
AELTAEFLYD EVHPKQHAFK QAFAKPKGPG GKRGHKRLIR GPGENGEDS
Length:349
Mass (Da):39,471
Last modified:May 1, 1999 - v1
Checksum:iA9F20CBD45B8B477
GO
Isoform 2 (identifier: Q9Z0P5-2) [UniParc]FASTAAdd to basket

Also known as: Twf2b

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: MAHQTGIH → MFLVLI

Show »
Length:347
Mass (Da):39,312
Checksum:iF21EB7C4133B0FD5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021Q → R in BAE41799 (PubMed:16141072).Curated
Sequence conflicti226 – 2261P → L in BAB22293 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 88MAHQTGIH → MFLVLI in isoform 2. 2 PublicationsVSP_018053

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17808 mRNA. Translation: CAB38083.1.
AY267189 mRNA. Translation: AAP31405.1.
AK002699 mRNA. Translation: BAB22293.1.
AK084026 mRNA. Translation: BAC39101.1.
AK087422 mRNA. Translation: BAC39867.1.
AK155204 mRNA. Translation: BAE33117.1.
AK157886 mRNA. Translation: BAE34246.1.
AK166900 mRNA. Translation: BAE39103.1.
AK170441 mRNA. Translation: BAE41799.1.
BC003338 mRNA. Translation: AAH03338.1.
CCDSiCCDS23473.1. [Q9Z0P5-1]
RefSeqiNP_036006.1. NM_011876.3. [Q9Z0P5-1]
UniGeneiMm.274346.

Genome annotation databases

EnsembliENSMUST00000024047; ENSMUSP00000024047; ENSMUSG00000023277. [Q9Z0P5-1]
ENSMUST00000188650; ENSMUSP00000140339; ENSMUSG00000023277. [Q9Z0P5-2]
GeneIDi23999.
KEGGimmu:23999.
UCSCiuc009rjf.1. mouse. [Q9Z0P5-1]
uc009rjg.1. mouse. [Q9Z0P5-2]

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Web resourcesi

Protein Spotlight

Molecular embrace - Issue 73 of August 2006

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17808 mRNA. Translation: CAB38083.1.
AY267189 mRNA. Translation: AAP31405.1.
AK002699 mRNA. Translation: BAB22293.1.
AK084026 mRNA. Translation: BAC39101.1.
AK087422 mRNA. Translation: BAC39867.1.
AK155204 mRNA. Translation: BAE33117.1.
AK157886 mRNA. Translation: BAE34246.1.
AK166900 mRNA. Translation: BAE39103.1.
AK170441 mRNA. Translation: BAE41799.1.
BC003338 mRNA. Translation: AAH03338.1.
CCDSiCCDS23473.1. [Q9Z0P5-1]
RefSeqiNP_036006.1. NM_011876.3. [Q9Z0P5-1]
UniGeneiMm.274346.

3D structure databases

ProteinModelPortaliQ9Z0P5.
SMRiQ9Z0P5. Positions 6-137, 181-313.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204847. 1 interaction.
DIPiDIP-61549N.
IntActiQ9Z0P5. 2 interactions.
MINTiMINT-4131249.
STRINGi10090.ENSMUSP00000024047.

PTM databases

iPTMnetiQ9Z0P5.
PhosphoSiteiQ9Z0P5.

Proteomic databases

EPDiQ9Z0P5.
MaxQBiQ9Z0P5.
PaxDbiQ9Z0P5.
PRIDEiQ9Z0P5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000024047; ENSMUSP00000024047; ENSMUSG00000023277. [Q9Z0P5-1]
ENSMUST00000188650; ENSMUSP00000140339; ENSMUSG00000023277. [Q9Z0P5-2]
GeneIDi23999.
KEGGimmu:23999.
UCSCiuc009rjf.1. mouse. [Q9Z0P5-1]
uc009rjg.1. mouse. [Q9Z0P5-2]

Organism-specific databases

CTDi11344.
MGIiMGI:1346078. Twf2.

Phylogenomic databases

eggNOGiKOG1747. Eukaryota.
ENOG410XS1J. LUCA.
GeneTreeiENSGT00530000063868.
HOGENOMiHOG000168296.
HOVERGENiHBG000848.
InParanoidiQ9Z0P5.
KOiK08870.
OMAiHATPELK.
OrthoDBiEOG79GT6W.
PhylomeDBiQ9Z0P5.
TreeFamiTF352598.

Miscellaneous databases

PROiQ9Z0P5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z0P5.
ExpressionAtlasiQ9Z0P5. baseline and differential.
GenevisibleiQ9Z0P5. MM.

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, expression and characterization of an A6 related protein."
    Rohwer A., Kittstein W., Marks F., Gschwendt M.
    Eur. J. Biochem. 263:518-525(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  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] (ISOFORM 1), INTERACTION WITH TWF1 AND PHOSPHOINOSITIDE, DEVELOPMENTAL STAGE.
    Strain: NMRI.
  3. "Two biochemically distinct and tissue-specific twinfilin isoforms are generated from the mouse Twf2 gene by alternative promoter usage."
    Nevalainen E.M., Skwarek-Maruszewska A., Braun A., Moser M., Lappalainen P.
    Biochem. J. 417:593-600(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE PROMOTER USAGE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  4. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Eye, Inner ear, Kidney and Spinal ganglion.
  5. "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] (ISOFORM 1).
    Strain: NMRI.
    Tissue: Mammary tumor.
  6. Lubec G., Klug S., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 30-48; 56-72; 111-136; 172-188; 197-204; 210-228 AND 294-315, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  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. "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.
  9. "Twinfilin 2 regulates actin filament lengths in cochlear stereocilia."
    Peng A.W., Belyantseva I.A., Hsu P.D., Friedman T.B., Heller S.
    J. Neurosci. 29:15083-15088(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
    Strain: C57BL/6J.
    Tissue: Cochlea.
  10. "MyosinVIIa interacts with Twinfilin-2 at the tips of mechanosensory stereocilia in the inner ear."
    Rzadzinska A.K., Nevalainen E.M., Prosser H.M., Lappalainen P., Steel K.P.
    PLoS ONE 4:E7097-E7097(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYO7A, SUBCELLULAR LOCATION.
    Strain: C3Heb/FeJ.
    Tissue: Inner ear.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen and Testis.
  12. Cited for: DISRUPTION PHENOTYPE.
    Strain: C57BL/6J.

Entry informationi

Entry nameiTWF2_MOUSE
AccessioniPrimary (citable) accession number: Q9Z0P5
Secondary accession number(s): Q3TD06
, Q3TZG2, Q8BN77, Q9DCK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: May 1, 1999
Last modified: June 8, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

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 one 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.