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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

  • actin monomer binding Source: BHF-UCL
  • ATP binding Source: MGI
  • cadherin binding involved in cell-cell adhesion Source: MGI
  • phosphatidylinositol-4,5-bisphosphate binding Source: BHF-UCL
  • protein complex binding Source: MGI
  • protein tyrosine kinase activity Source: UniProtKB

GO - Biological processi

  • barbed-end actin filament capping Source: BHF-UCL
  • negative regulation of actin filament polymerization Source: BHF-UCL
  • regulation of actin phosphorylation Source: MGI
  • 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
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1100520. Twf1.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • cell-cell adherens junction Source: MGI
  • cell-cell junction Source: BHF-UCL
  • cytoplasm Source: MGI
  • filopodium Source: BHF-UCL
  • focal adhesion Source: MGI
  • myofibril Source: BHF-UCL
  • perinuclear region of cytoplasm Source: BHF-UCL
  • ruffle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002149512 – 350Twinfilin-1Add BLAST349

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineBy similarity1
Modified residuei143PhosphoserineBy similarity1
Modified residuei277PhosphoserineBy similarity1
Modified residuei309PhosphotyrosineCombined sources1
Modified residuei349PhosphothreonineCombined sources1

Post-translational modificationi

Phosphorylated on serine and threonine residues.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ91YR1.
MaxQBiQ91YR1.
PaxDbiQ91YR1.
PeptideAtlasiQ91YR1.
PRIDEiQ91YR1.

PTM databases

iPTMnetiQ91YR1.
PhosphoSitePlusiQ91YR1.

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

BgeeiENSMUSG00000022451.
ExpressionAtlasiQ91YR1. baseline and differential.
GenevisibleiQ91YR1. MM.

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

GO - Molecular functioni

  • actin monomer binding Source: BHF-UCL
  • cadherin binding involved in cell-cell adhesion Source: MGI
  • protein complex binding Source: MGI

Protein-protein interaction databases

BioGridi202468. 1 interactor.
DIPiDIP-33923N.
IntActiQ91YR1. 3 interactors.
MINTiMINT-1869546.
STRINGi10090.ENSMUSP00000023087.

Structurei

Secondary structure

1350
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 21Combined sources11
Turni22 – 24Combined sources3
Beta strandi26 – 32Combined sources7
Beta strandi34 – 43Combined sources10
Helixi49 – 57Combined sources9
Helixi58 – 60Combined sources3
Beta strandi67 – 77Combined sources11
Beta strandi80 – 88Combined sources9
Helixi95 – 112Combined sources18
Helixi114 – 116Combined sources3
Beta strandi117 – 125Combined sources9
Helixi126 – 129Combined sources4
Helixi131 – 138Combined sources8
Helixi184 – 194Combined sources11
Beta strandi199 – 206Combined sources8
Turni207 – 210Combined sources4
Beta strandi211 – 216Combined sources6
Helixi222 – 224Combined sources3
Helixi226 – 228Combined sources3
Beta strandi231 – 233Combined sources3
Beta strandi235 – 245Combined sources11
Beta strandi248 – 258Combined sources11
Beta strandi262 – 264Combined sources3
Helixi266 – 274Combined sources9
Helixi276 – 287Combined sources12
Beta strandi291 – 302Combined sources12
Helixi305 – 312Combined sources8

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ91YR1.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 139ADF-H 1PROSITE-ProRule annotationAdd BLAST138
Domaini175 – 313ADF-H 2PROSITE-ProRule annotationAdd BLAST139

Sequence similaritiesi

Contains 2 ADF-H domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1747. Eukaryota.
ENOG410XS1J. LUCA.
GeneTreeiENSGT00530000063868.
HOGENOMiHOG000168296.
HOVERGENiHBG000848.
InParanoidiQ91YR1.
KOiK08870.
OMAiYDYLQFR.
OrthoDBiEOG091G0BWK.
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)DescriptionActionsGraphical viewLength
Sequence conflicti345A → R in AAB66592 (PubMed:9249064).Curated1
Sequence conflicti345A → R in AAP31404 (PubMed:12807912).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti51Q → H.1 Publication1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M4JX-ray1.60A/B1-142[»]
2D8BNMR-A161-313[»]
2HD7NMR-A176-316[»]
3DAWX-ray2.55B167-322[»]
ProteinModelPortaliQ91YR1.
SMRiQ91YR1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202468. 1 interactor.
DIPiDIP-33923N.
IntActiQ91YR1. 3 interactors.
MINTiMINT-1869546.
STRINGi10090.ENSMUSP00000023087.

PTM databases

iPTMnetiQ91YR1.
PhosphoSitePlusiQ91YR1.

Proteomic databases

EPDiQ91YR1.
MaxQBiQ91YR1.
PaxDbiQ91YR1.
PeptideAtlasiQ91YR1.
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

eggNOGiKOG1747. Eukaryota.
ENOG410XS1J. LUCA.
GeneTreeiENSGT00530000063868.
HOGENOMiHOG000168296.
HOVERGENiHBG000848.
InParanoidiQ91YR1.
KOiK08870.
OMAiYDYLQFR.
OrthoDBiEOG091G0BWK.
PhylomeDBiQ91YR1.
TreeFamiTF352598.

Miscellaneous databases

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

Gene expression databases

BgeeiENSMUSG00000022451.
ExpressionAtlasiQ91YR1. baseline and differential.
GenevisibleiQ91YR1. 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...

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: November 30, 2016
This is version 133 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

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.