DEST_RAT
ID DEST_RAT Reviewed; 165 AA.
AC Q7M0E3;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Destrin;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
GN Name=Dstn;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Lung;
RX PubMed=12947022; DOI=10.1165/rcmb.2003-0214oc;
RA Shultz M.A., Zhang L., Gu Y.-Z., Baker G.L., Fannuchi M.V., Padua A.M.,
RA Gurske W.A., Morin D., Penn S.G., Jovanovich S.B., Plopper C.G.,
RA Buckpitt A.R.;
RT "Gene expression analysis in response to lung toxicants: I. Sequencing and
RT microarray development.";
RL Am. J. Respir. Cell Mol. Biol. 30:296-310(2004).
RN [2]
RP PROTEIN SEQUENCE OF 2-165, ACETYLATION AT ALA-2, PHOSPHORYLATION AT SER-3,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Parotid gland;
RX PubMed=9877327; DOI=10.1016/s0003-9969(98)00083-1;
RA Kanamori T., Suzuki M., Titani K.;
RT "Complete amino acid sequences and phosphorylation sites, determined by
RT Edman degradation and mass spectrometry, of rat parotid destrin- and
RT cofilin-like proteins.";
RL Arch. Oral Biol. 43:955-967(1998).
RN [3]
RP PROTEIN SEQUENCE OF 46-69; 82-92 AND 133-145, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Diao W., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RA Lubec G., Chen W.-Q.;
RL Submitted (FEB-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
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; CF111187; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; JE0223; JE0223.
DR RefSeq; NP_001028838.1; NM_001033666.1.
DR AlphaFoldDB; Q7M0E3; -.
DR SMR; Q7M0E3; -.
DR IntAct; Q7M0E3; 1.
DR STRING; 10116.ENSRNOP00000007794; -.
DR iPTMnet; Q7M0E3; -.
DR PhosphoSitePlus; Q7M0E3; -.
DR SwissPalm; Q7M0E3; -.
DR jPOST; Q7M0E3; -.
DR PaxDb; Q7M0E3; -.
DR PRIDE; Q7M0E3; -.
DR Ensembl; ENSRNOT00000007794; ENSRNOP00000007794; ENSRNOG00000005924.
DR GeneID; 502674; -.
DR KEGG; rno:502674; -.
DR UCSC; RGD:1588366; rat.
DR CTD; 11034; -.
DR RGD; 1588366; Dstn.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR HOGENOM; CLU_094004_0_0_1; -.
DR InParanoid; Q7M0E3; -.
DR OMA; ITFYSWS; -.
DR OrthoDB; 1370477at2759; -.
DR PhylomeDB; Q7M0E3; -.
DR TreeFam; TF328601; -.
DR PRO; PR:Q7M0E3; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000005924; Expressed in jejunum and 19 other tissues.
DR Genevisible; Q7M0E3; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; ISO:RGD.
DR GO; GO:0030043; P:actin filament fragmentation; ISO:RGD.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; ISO:RGD.
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; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9877327, ECO:0000269|Ref.4"
FT CHAIN 2..165
FT /note="Destrin"
FT /id="PRO_0000214921"
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:0000269|PubMed:9877327, ECO:0000269|Ref.4"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:9877327,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60981"
FT CONFLICT 114
FT /note="K -> L (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 165 AA; 18534 MW; D395B8A5642A0D79 CRC64;
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIVVE EGKEILVGDV
GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPEQAP LKSKMIYASS
KDAIKKKFPG IKHEYQANGP EDLNRTSIAE KLGGSLIVAF EGSPV
