ID   DEST_BOVIN              Reviewed;         165 AA.
AC   Q5E9D5; Q3SZ77;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Destrin;
DE   AltName: Full=Actin-depolymerizing factor;
DE            Short=ADF;
GN   Name=DSTN;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P60981}.
CC   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC       {ECO:0000305}.
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DR   EMBL; BT020985; AAX09002.1; -; mRNA.
DR   EMBL; BC103074; AAI03075.1; -; mRNA.
DR   RefSeq; NP_001015586.1; NM_001015586.1.
DR   AlphaFoldDB; Q5E9D5; -.
DR   SMR; Q5E9D5; -.
DR   STRING; 9913.ENSBTAP00000020512; -.
DR   PaxDb; Q5E9D5; -.
DR   PeptideAtlas; Q5E9D5; -.
DR   PRIDE; Q5E9D5; -.
DR   Ensembl; ENSBTAT00000020512; ENSBTAP00000020512; ENSBTAG00000015434.
DR   GeneID; 513267; -.
DR   KEGG; bta:513267; -.
DR   CTD; 11034; -.
DR   VEuPathDB; HostDB:ENSBTAG00000015434; -.
DR   VGNC; VGNC:28226; DSTN.
DR   eggNOG; KOG1735; Eukaryota.
DR   GeneTree; ENSGT00950000183000; -.
DR   HOGENOM; CLU_094004_0_0_1; -.
DR   InParanoid; Q5E9D5; -.
DR   OMA; ITFYSWS; -.
DR   OrthoDB; 1370477at2759; -.
DR   TreeFam; TF328601; -.
DR   Proteomes; UP000009136; Chromosome 13.
DR   ExpressionAtlas; Q5E9D5; baseline and differential.
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; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Acetylation; Actin-binding; Phosphoprotein; Reference proteome;
KW   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_0000214917"
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   CONFLICT        2
FT                   /note="A -> D (in Ref. 2; AAI03075)"
FT                   /evidence="ECO:0000305"
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