Reviewed, UniProtKB/Swiss-Prot P60981 (DEST_HUMAN)

Names and origin

Protein names

Recommended name:
    Destrin
Alternative name(s):
    Actin-depolymerizing factor
      Short name=ADF

Gene names

Name:	DSTN
Synonyms:	ACTDP, DSN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	165 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
Tissue specificity	Widely distributed in various tissues.
Sequence similarities	Belongs to the actin-binding proteins ADF family. Contains 1 ADF-H domain.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	actin filament severing Ref.1 Traceable author statement. Source: ProtInc
Molecular function	actin binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 165	164	Destrin		PRO_0000214918
Regions
	Domain	4 – 153	150	ADF-H
	Motif	30 – 34	5	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	2	1	N-acetylalanine
	Modified residue	3	1	Phosphoserine
Natural variations
	Natural variant	139	1	G → E in a colorectal cancer sample; somatic mutation.		VAR_036459

Sequences

	Sequence		Length	Mass (Da)
	P60981-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 8868A3167924100E	FASTA	165	18,506
	10 20 30 40 50 60 MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV 70 80 90 100 110 120 GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS 130 140 150 160 KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments." Hawkins M., Pope B., Maciver S.K., Weeds A.G. Biochemistry 32:9985-9993(1993) [PubMed: 8399167] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[5]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13, ACETYLATION AT ALA-2. Tissue: Platelet.
[6]	Lubec G., Vishwanath V. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 54-69, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[7]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLU-139.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	S65738 mRNA. Translation: AAB28361.1. AL132765 Genomic DNA. Translation: CAC10585.1. CR457042 mRNA. Translation: CAG33323.1. BC009477 mRNA. Translation: AAH09477.1.
PIR	A54184.
RefSeq	NP_001011546.1. NP_006861.1.
UniGene	Hs.304192 Hs.705996
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P60981.
PTM databases
PhosphoSite	P60981.
2-D gel databases
OGP	P18282.
REPRODUCTION-2DPAGE	IPI00473014.
Genome annotation databases
Ensembl	ENSG00000125868. Homo sapiens. [Contig view]
GeneID	11034.
KEGG	hsa:11034.
Organism-specific databases
HGNC	HGNC:15750. DSTN.
MIM	609114. gene.
PharmGKB	PA27509.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P60981.
HOVERGEN	P60981.
Gene expression databases
ArrayExpress	P60981.
CleanEx	HS_DSTN.
GermOnline	ENSG00000125868. Homo sapiens.
Family and domain databases
InterPro	IPR002108. Cofilin_actin_bd. [Graphical view]
Pfam	PF00241. Cofilin_ADF. 1 hit. [Graphical view]
PRINTS	PR00006. COFILIN.
SMART	SM00102. ADF. 1 hit. [Graphical view]
PROSITE	PS51263. ADF_H. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
LinkHub	P60981.
NextBio	41930.
SOURCE	Search...

Entry information

Entry name

DEST_HUMAN

Accession

Primary (citable) accession number: P60981
Secondary accession number(s): P18282, Q5W166, Q6IAW2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	January 23, 2007
Last modified:	November 25, 2008
This is version 54 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)