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Q9R0P5 (DEST_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Destrin
Alternative name(s):
Actin-depolymerizing factor
Short name=ADF
Sid 23
Gene names
Name:Dstn
Synonyms:Dsn, Sid23
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length165 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Actin-depolymerizing protein. Severs actin filaments (F-actin) and binds to actin monomers (G-actin). Acts in a pH-independent manner.

Post-translational modification

ISGylated By similarity.

Sequence similarities

Belongs to the actin-binding proteins ADF family.

Contains 1 ADF-H domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 165164Destrin
PRO_0000214919

Regions

Domain4 – 153150ADF-H
Motif30 – 345Nuclear localization signal Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue31Phosphoserine Ref.4 Ref.5
Modified residue191N6-acetyllysine By similarity
Modified residue1141N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9R0P5 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 42BD07984C9B3667

FASTA16518,522
        10         20         30         40         50         60 
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIVVE EGKEILVGDV 

        70         80         90        100        110        120 
GATITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPEQAP LKSKMIYASS 

       130        140        150        160 
KDAIKKKFPG IKHEYQANGP EDLNRTCIAE KLGGSLIVAF EGSPV 

« Hide

References

« Hide 'large scale' references
[1]"Mouse actin depolymerizing factor sid23."
Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cecum.
[3]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 54-69 AND 133-145, MASS SPECTROMETRY.
Tissue: Hippocampus.
[4]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY.
Tissue: Melanoma.
[5]"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: 19131326] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB025406 mRNA. Translation: BAA84691.1.
AK078898 mRNA. Translation: BAC37447.1.
IPIIPI00127942.
RefSeqNP_062745.1. NM_019771.2.
UniGeneMm.28919.

3D structure databases

ProteinModelPortalQ9R0P5.
SMRQ9R0P5. Positions 2-165.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9R0P5. 2 interactions.
STRINGQ9R0P5.

PTM databases

PhosphoSiteQ9R0P5.

2D gel databases

REPRODUCTION-2DPAGEIPI00127942.
Q9R0P5.

Proteomic databases

PRIDEQ9R0P5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103172; ENSMUSP00000099461; ENSMUSG00000015932.
GeneID56431.
KEGGmmu:56431.

Organism-specific databases

CTD11034.
MGIMGI:1929270. Dstn.

Phylogenomic databases

GeneTreeENSGT00440000033289.
HOGENOMHBG628477.
HOVERGENHBG000381.
InParanoidQ9R0P5.
OMAQMLPEKD.
OrthoDBEOG4FR0SR.
PhylomeDBQ9R0P5.

Gene expression databases

ArrayExpressQ9R0P5.
BgeeQ9R0P5.
CleanExMM_DSTN.
GenevestigatorQ9R0P5.
GermOnlineENSMUSG00000015932. Mus musculus.

Family and domain databases

InterProIPR002108. Actin-bd_cofilin/tropomyosin.
IPR017904. ADF/Cofilin/Destrin.
[Graphical view]
KOK10363.
PfamPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSPR00006. COFILIN.
SMARTSM00102. ADF. 1 hit.
[Graphical view]
PROSITEPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio312606.
SOURCESearch...

Entry information

Entry nameDEST_MOUSE
AccessionPrimary (citable) accession number: Q9R0P5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families