DEST_PIG
ID DEST_PIG Reviewed; 165 AA.
AC P60982; P18282;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Destrin;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
GN Name=DSTN; Synonyms=DSN;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 53-69 AND 96-112.
RC TISSUE=Brain;
RX PubMed=2156828; DOI=10.1016/s0021-9258(19)39429-3;
RA Moriyama K., Nishida E., Yonezawa N., Sakai H., Matsumoto S., Iida K.,
RA Yahara I.;
RT "Destrin, a mammalian actin-depolymerizing protein, is closely related to
RT cofilin. Cloning and expression of porcine brain destrin cDNA.";
RL J. Biol. Chem. 265:5768-5773(1990).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=8674111; DOI=10.1016/s0092-8674(00)81305-7;
RA Hatanaka H., Ogura K., Moriyama K., Ichikawa S., Yahara I., Inagaki F.;
RT "Tertiary structure of destrin and structural similarity between two actin-
RT regulating protein families.";
RL Cell 85:1047-1055(1996).
CC -!- FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F-
CC actin) and binds to actin monomers (G-actin). Acts in a pH-independent
CC manner. {ECO:0000250|UniProtKB:P60981, ECO:0000250|UniProtKB:Q9R0P5}.
CC -!- TISSUE SPECIFICITY: Widely distributed in various tissues.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P60981}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D90053; BAA14105.1; -; mRNA.
DR PIR; A35179; A35179.
DR RefSeq; NP_001004031.1; NM_001004031.1.
DR PDB; 1AK6; NMR; -; A=2-165.
DR PDB; 1AK7; NMR; -; A=2-165.
DR PDBsum; 1AK6; -.
DR PDBsum; 1AK7; -.
DR AlphaFoldDB; P60982; -.
DR SMR; P60982; -.
DR STRING; 9823.ENSSSCP00000007548; -.
DR PaxDb; P60982; -.
DR PeptideAtlas; P60982; -.
DR PRIDE; P60982; -.
DR Ensembl; ENSSSCT00000007757; ENSSSCP00000007548; ENSSSCG00000007085.
DR Ensembl; ENSSSCT00025099547; ENSSSCP00025043847; ENSSSCG00025072367.
DR Ensembl; ENSSSCT00030053720; ENSSSCP00030024522; ENSSSCG00030038598.
DR Ensembl; ENSSSCT00035010647; ENSSSCP00035003619; ENSSSCG00035008527.
DR Ensembl; ENSSSCT00040077141; ENSSSCP00040033147; ENSSSCG00040056908.
DR Ensembl; ENSSSCT00045048344; ENSSSCP00045033606; ENSSSCG00045028358.
DR Ensembl; ENSSSCT00060014441; ENSSSCP00060005600; ENSSSCG00060011069.
DR GeneID; 445516; -.
DR KEGG; ssc:445516; -.
DR CTD; 11034; -.
DR VGNC; VGNC:108715; DSTN.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR HOGENOM; CLU_094004_0_0_1; -.
DR InParanoid; P60982; -.
DR OMA; ITFYSWS; -.
DR OrthoDB; 1370477at2759; -.
DR EvolutionaryTrace; P60982; -.
DR Proteomes; UP000008227; Chromosome 17.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000007085; Expressed in oocyte and 46 other tissues.
DR ExpressionAtlas; P60982; baseline and differential.
DR Genevisible; P60982; SS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISS:AgBase.
DR GO; GO:0005737; C:cytoplasm; ISS:AgBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030042; P:actin filament depolymerization; IBA:GO_Central.
DR GO; GO:0030043; P:actin filament fragmentation; IBA:GO_Central.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISS:AgBase.
DR CDD; cd11286; ADF_cofilin_like; 1.
DR Gene3D; 3.40.20.10; -; 1.
DR InterPro; IPR002108; ADF-H.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR017904; ADF/Cofilin.
DR InterPro; IPR029924; Dstn.
DR PANTHER; PTHR11913; PTHR11913; 1.
DR PANTHER; PTHR11913:SF18; PTHR11913:SF18; 1.
DR Pfam; PF00241; Cofilin_ADF; 1.
DR PRINTS; PR00006; COFILIN.
DR SMART; SM00102; ADF; 1.
DR PROSITE; PS51263; ADF_H; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P60981"
FT CHAIN 2..165
FT /note="Destrin"
FT /id="PRO_0000214920"
FT DOMAIN 4..153
FT /note="ADF-H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00599"
FT MOTIF 30..34
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P60981"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P60981"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60981"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:1AK6"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1AK6"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:1AK6"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:1AK6"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:1AK7"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1AK7"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1AK6"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:1AK6"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1AK6"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:1AK6"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:1AK7"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:1AK7"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1AK7"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:1AK6"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:1AK6"
FT HELIX 111..115
FT /evidence="ECO:0007829|PDB:1AK6"
FT HELIX 117..127
FT /evidence="ECO:0007829|PDB:1AK6"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1AK6"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:1AK6"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:1AK6"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:1AK6"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:1AK7"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:1AK6"
SQ SEQUENCE 165 AA; 18506 MW; 8868A3167924100E CRC64;
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV
GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS
KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPV
