Destrin

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Structures	Swiss-model
Domains	InterPro

Destrin (actin binding protein)
Destrin (actin binding protein)
	Nuclear magnetic resonance determined configuration of the tertiary structure of Destrin.
Identifiers
Symbol	DSTN
Alt. symbols	ADF
NCBI gene	11034
HGNC	15750
OMIM	609114
RefSeq	NM_006870
UniProt	P60981
Other data
Locus	Chr. 20 p12.1
Structures
Search for
Structures	Swiss-model
Domains	InterPro

DSTN
Identifiers
Aliases	DSTN, ACTDP, ADF, HEL32, bA462D18.2, destrin, actin depolymerizing factor
External IDs	OMIM: 609114; MGI: 1929270; HomoloGene: 21362; GeneCards: DSTN; OMA:DSTN - orthologs
Gene location (Human)
Chr.	Chromosome 20 (human)
End	17,609,919 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	143,785,244 bp
RNA expression pattern
	Top expressed in
	saphenous vein; ; urethra; ; popliteal artery; ; tibial arteries; ; right coronary artery; ; Descending thoracic aorta; ; vena cava; ; ascending aorta; ; superficial temporal artery; ; tail of epididymis;
	Top expressed in
	Ileal epithelium; ; tunica media of zone of aorta; ; transitional epithelium of urinary bladder; ; corneal stroma; ; left colon; ; umbilical cord; ; lobe of prostate; ; cervix; ; right lung lobe; ; nasal epithelium;
	More reference expression data
	n/a
Gene ontology
Molecular function	actin binding; protein binding; actin filament binding;
Cellular component	extracellular exosome; cytoplasm; actin cytoskeleton; cortical actin cytoskeleton; intracellular anatomical structure;
Biological process	actin polymerization or depolymerization; positive regulation of actin filament depolymerization; actin filament severing; actin filament depolymerization; actin filament fragmentation;
	Sources:Amigo / QuickGO
Orthologs
	11034
	56431
	ENSG00000125868
	ENSMUSG00000015932
	P60981
	Q9R0P5
	NM_001011546; NM_006870
	NM_019771
	NP_001011546; NP_006861
	NP_062745
	Wikidata
View/Edit Human	View/Edit Mouse

Destrin or DSTN (also known as actin depolymerizing factor or ADF) is a protein which in humans is encoded by the DSTN gene.^[6]^[7]^[8] Destrin is a component protein in microfilaments.

The product of this gene belongs to the actin-binding proteins ADF (Actin-Depolymerizing Factor)/cofilin family. This family of proteins is responsible for enhancing the turnover rate of actin in vivo. This gene encodes the actin depolymerizing protein that severs actin filaments (F-actin) and binds to actin monomers (G-actin). Two transcript variants encoding distinct isoforms have been identified for this gene.^[6]

Structure

The tertiary structure of destrin was determined by the use of triple-resonance multidimensional nuclear magnetic resonance, or NMR for short.^[5] The secondary and tertiary structures of destrin are similar to the gelsolin family which is another actin-regulating protein family.

There are three ordered layers to destrin which is a globular protein. There is a central β sheet that is composed of one parallel strand and three antiparallel strands. This β sheet is between a long α helix along with a shorter one and two shorter helices on the opposite side. The four helices are parallel to the β strands.^[5]

Function

In a variety of eukaryotes, destrin regulates actin in the cytoskeleton. Destrin binds actin and is thought to connect it as gelsolin segment-1 does. Furthermore, the binding of actin by destrin and cofilin is regulated negatively by phosphorylation. Destrin can also sever actin filaments.^[5]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000125868 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000015932 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 3 4 PDB: 1AK6; Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F (June 1996). "Tertiary structure of destrin and structural similarity between two actin-regulating protein families". Cell. 85 (7): 1047–55. doi:10.1016/S0092-8674(00)81305-7. PMID 8674111. S2CID 11470231.
1 2 "Entrez Gene: Destrin".
↑ Hawkins M, Pope B, Maciver SK, Weeds AG (September 1993). "Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments". Biochemistry. 32 (38): 9985–93. doi:10.1021/bi00089a014. PMID 8399167.
↑ Deloukas P, Matthews LH, Ashurst J, et al. (2001). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.

External links

Destrin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Ramachandran Plot for destrin: "MolProbity Ramachandran analysis for 1ak6" (PDF). www.rcsb.org. Archived from the original (PDF) on 2012-10-12.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000125868 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000015932 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8674111-5] 1 2 3 4 PDB: 1AK6; Hatanaka H, Ogura K, Moriyama K, Ichikawa S, Yahara I, Inagaki F (June 1996). "Tertiary structure of destrin and structural similarity between two actin-regulating protein families". Cell. 85 (7): 1047–55. doi:10.1016/S0092-8674(00)81305-7. PMID 8674111. S2CID 11470231.

[entrez-6] 1 2 "Entrez Gene: Destrin".

[pmid8399167-7] Hawkins M, Pope B, Maciver SK, Weeds AG (September 1993). "Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments". Biochemistry. 32 (38): 9985–93. doi:10.1021/bi00089a014. PMID 8399167.

[pmid11780052-8] Deloukas P, Matthews LH, Ashurst J, et al. (2001). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. Bibcode:2001Natur.414..865D. doi:10.1038/414865a. PMID 11780052.

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