ID   DEST_CHICK              Reviewed;         165 AA.
AC   P18359; Q5ZLP1;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Destrin;
DE   AltName: Full=Actin-depolymerizing factor;
DE            Short=ADF;
GN   Name=DSTN; Synonyms=DSN; ORFNames=RCJMB04_5f14;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 101-111 AND 116-134.
RC   TISSUE=Brain;
RX   PubMed=2223773; DOI=10.1021/bi00484a009;
RA   Adams M.E., Minamide L.S., Duester G., Bamburg J.R.;
RT   "Nucleotide sequence and expression of a cDNA encoding chick brain actin
RT   depolymerizing factor.";
RL   Biochemistry 29:7414-7420(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RX   PubMed=1699599; DOI=10.1021/bi00484a010;
RA   Abe H., Endo T., Yamamoto K., Obinata T.;
RT   "Sequence of cDNAs encoding actin depolymerizing factor and cofilin of
RT   embryonic chicken skeletal muscle: two functionally distinct actin-
RT   regulatory proteins exhibit high structural homology.";
RL   Biochemistry 29:7420-7425(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
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   -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC       {ECO:0000305}.
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DR   EMBL; J02912; AAA48575.1; -; mRNA.
DR   EMBL; M55660; AAA48573.1; -; mRNA.
DR   EMBL; AJ719693; CAG31352.1; -; mRNA.
DR   PIR; A35702; A35702.
DR   RefSeq; NP_990859.1; NM_205528.1.
DR   AlphaFoldDB; P18359; -.
DR   SMR; P18359; -.
DR   BioGRID; 676783; 2.
DR   IntAct; P18359; 1.
DR   STRING; 9031.ENSGALP00000014097; -.
DR   iPTMnet; P18359; -.
DR   PaxDb; P18359; -.
DR   GeneID; 396539; -.
DR   KEGG; gga:396539; -.
DR   CTD; 11034; -.
DR   VEuPathDB; HostDB:geneid_396539; -.
DR   eggNOG; KOG1735; Eukaryota.
DR   InParanoid; P18359; -.
DR   OrthoDB; 1370477at2759; -.
DR   PhylomeDB; P18359; -.
DR   TreeFam; TF328601; -.
DR   PRO; PR:P18359; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IEA:InterPro.
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   Acetylation; Actin-binding; Direct protein sequencing; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..165
FT                   /note="Destrin"
FT                   /id="PRO_0000214922"
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"
FT   CONFLICT        73
FT                   /note="E -> Q (in Ref. 3; CAG31352)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   165 AA;  18533 MW;  7EDD20D24519B629 CRC64;
     MASGVQVADE VCRIFYDMKV RKCSTPEEVK KRKKAVIFCL SPDKKCIIVE EGKEILVGDV
     GVTVTDPFKH FVEMLPEKDC RYALYDASFE TKESKKEELM FFLWAPEQAP LKSKMIYASS
     KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLVVAF EGSPV