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Protein

Destrin

Gene

Dstn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

  1. actin filament depolymerization Source: InterPro
  2. actin filament severing Source: InterPro
  3. positive regulation of actin filament depolymerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Destrin
Alternative name(s):
Actin-depolymerizing factor
Short name:
ADF
Gene namesi
Name:Dstn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 3

Organism-specific databases

RGDi1588366. Dstn.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 165164DestrinPRO_0000214921Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei3 – 31Phosphoserine1 Publication
Modified residuei19 – 191N6-acetyllysineBy similarity

Post-translational modificationi

ISGylated.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ7M0E3.
PRIDEiQ7M0E3.

PTM databases

PhosphoSiteiQ7M0E3.

Expressioni

Gene expression databases

GenevestigatoriQ7M0E3.

Interactioni

Protein-protein interaction databases

IntActiQ7M0E3. 1 interaction.
MINTiMINT-4568380.
STRINGi10116.ENSRNOP00000007794.

Structurei

3D structure databases

ProteinModelPortaliQ7M0E3.
SMRiQ7M0E3. Positions 2-165.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 153150ADF-HPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi30 – 345Nuclear localization signalSequence Analysis

Sequence similaritiesi

Belongs to the actin-binding proteins ADF family.Curated
Contains 1 ADF-H domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG294392.
GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiQ7M0E3.
KOiK10363.
OMAiGSGECRY.
OrthoDBiEOG7353Z9.
PhylomeDBiQ7M0E3.
TreeFamiTF328601.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
IPR029924. Dstn.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF18. PTHR11913:SF18. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSiPR00006. COFILIN.
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q7M0E3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIVVE
60 70 80 90 100
EGKEILVGDV GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM
110 120 130 140 150
FFLWAPEQAP LKSKMIYASS KDAIKKKFPG IKHEYQANGP EDLNRTSIAE
160
KLGGSLIVAF EGSPV
Length:165
Mass (Da):18,534
Last modified:February 20, 2007 - v3
Checksum:iD395B8A5642A0D79
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141K → L AA sequence (PubMed:9877327).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CF111187 mRNA. No translation available.
PIRiJE0223.
RefSeqiNP_001028838.1. NM_001033666.1.
UniGeneiRn.102412.

Genome annotation databases

EnsembliENSRNOT00000007794; ENSRNOP00000007794; ENSRNOG00000005924.
GeneIDi502674.
KEGGirno:502674.
UCSCiRGD:1588366. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CF111187 mRNA. No translation available.
PIRiJE0223.
RefSeqiNP_001028838.1. NM_001033666.1.
UniGeneiRn.102412.

3D structure databases

ProteinModelPortaliQ7M0E3.
SMRiQ7M0E3. Positions 2-165.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7M0E3. 1 interaction.
MINTiMINT-4568380.
STRINGi10116.ENSRNOP00000007794.

PTM databases

PhosphoSiteiQ7M0E3.

Proteomic databases

PaxDbiQ7M0E3.
PRIDEiQ7M0E3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000007794; ENSRNOP00000007794; ENSRNOG00000005924.
GeneIDi502674.
KEGGirno:502674.
UCSCiRGD:1588366. rat.

Organism-specific databases

CTDi11034.
RGDi1588366. Dstn.

Phylogenomic databases

eggNOGiNOG294392.
GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiQ7M0E3.
KOiK10363.
OMAiGSGECRY.
OrthoDBiEOG7353Z9.
PhylomeDBiQ7M0E3.
TreeFamiTF328601.

Miscellaneous databases

NextBioi712150.

Gene expression databases

GenevestigatoriQ7M0E3.

Family and domain databases

Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin/Destrin.
IPR029924. Dstn.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF18. PTHR11913:SF18. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSiPR00006. COFILIN.
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Lung.
  2. "Complete amino acid sequences and phosphorylation sites, determined by Edman degradation and mass spectrometry, of rat parotid destrin- and cofilin-like proteins."
    Kanamori T., Suzuki M., Titani K.
    Arch. Oral Biol. 43:955-967(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-165, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-3, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Parotid gland.
  3. Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 46-69; 82-92 AND 133-145, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain, Hippocampus and Spinal cord.
  4. Lubec G., Chen W.-Q.
    Submitted (FEB-2007) to UniProtKB
    Cited for: ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiDEST_RAT
AccessioniPrimary (citable) accession number: Q7M0E3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2005
Last sequence update: February 20, 2007
Last modified: March 4, 2015
This is version 82 of the entry and version 3 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. 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.