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 24-JAN-2024, entry version 128. 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 GlyGen; Q7M0E3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q7M0E3; -. DR PhosphoSitePlus; Q7M0E3; -. DR SwissPalm; Q7M0E3; -. DR jPOST; Q7M0E3; -. DR PaxDb; 10116-ENSRNOP00000007794; -. DR Ensembl; ENSRNOT00000007794.7; ENSRNOP00000007794.5; ENSRNOG00000005924.7. DR Ensembl; ENSRNOT00055040829; ENSRNOP00055033166; ENSRNOG00055023785. DR Ensembl; ENSRNOT00060002115; ENSRNOP00060001310; ENSRNOG00060001435. DR Ensembl; ENSRNOT00065047921; ENSRNOP00065039329; ENSRNOG00065027795. DR GeneID; 502674; -. DR KEGG; rno:502674; -. DR UCSC; RGD:1588366; rat. DR AGR; RGD:1588366; -. 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; 3380386at2759; -. DR PhylomeDB; Q7M0E3; -. DR TreeFam; TF328601; -. DR PRO; PR:Q7M0E3; -. DR Proteomes; UP000002494; Chromosome 3. DR Bgee; ENSRNOG00000005924; Expressed in jejunum and 19 other cell types or tissues. 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:0048870; P:cell motility; ISO:RGD. 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; Severin; 1. DR InterPro; IPR002108; ADF-H. DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf. DR InterPro; IPR017904; ADF/Cofilin. DR PANTHER; PTHR11913; COFILIN-RELATED; 1. DR PANTHER; PTHR11913:SF18; DESTRIN; 1. DR Pfam; PF00241; Cofilin_ADF; 1. DR PRINTS; PR00006; COFILIN. DR SMART; SM00102; ADF; 1. DR SUPFAM; SSF55753; Actin depolymerizing proteins; 1. DR PROSITE; PS51263; ADF_H; 1. DR Genevisible; Q7M0E3; RN. 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 //