DEST_MOUSE
ID DEST_MOUSE Reviewed; 165 AA.
AC Q9R0P5;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Destrin;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
DE AltName: Full=Sid 23;
GN Name=Dstn; Synonyms=Dsn, Sid23;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
RT "Mouse actin depolymerizing factor sid23.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cecum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PROTEIN SEQUENCE OF 54-69 AND 133-145, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=11809832; DOI=10.1091/mbc.01-07-0331;
RA Vartiainen M.K., Mustonen T., Mattila P.K., Ojala P.J., Thesleff I.,
RA Partanen J., Lappalainen P.;
RT "The three mouse actin-depolymerizing factor/cofilins evolved to fulfill
RT cell-type-specific requirements for actin dynamics.";
RL Mol. Biol. Cell 13:183-194(2002).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC -!- TISSUE SPECIFICITY: Widely expressed. Not found in skeletal muscle.
CC {ECO:0000269|PubMed:11809832}.
CC -!- DEVELOPMENTAL STAGE: In 10.5 dpc embryo somites is expressed in a
CC superficial patch of cells (adaxial region).
CC {ECO:0000269|PubMed:11809832}.
CC -!- PTM: ISGylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC {ECO:0000305}.
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DR EMBL; AB025406; BAA84691.1; -; mRNA.
DR EMBL; AK078898; BAC37447.1; -; mRNA.
DR CCDS; CCDS16812.1; -.
DR RefSeq; NP_062745.1; NM_019771.2.
DR AlphaFoldDB; Q9R0P5; -.
DR SMR; Q9R0P5; -.
DR BioGRID; 207975; 15.
DR IntAct; Q9R0P5; 7.
DR MINT; Q9R0P5; -.
DR STRING; 10090.ENSMUSP00000099461; -.
DR iPTMnet; Q9R0P5; -.
DR PhosphoSitePlus; Q9R0P5; -.
DR SwissPalm; Q9R0P5; -.
DR REPRODUCTION-2DPAGE; IPI00127942; -.
DR REPRODUCTION-2DPAGE; Q9R0P5; -.
DR EPD; Q9R0P5; -.
DR jPOST; Q9R0P5; -.
DR MaxQB; Q9R0P5; -.
DR PaxDb; Q9R0P5; -.
DR PRIDE; Q9R0P5; -.
DR ProteomicsDB; 277982; -.
DR Antibodypedia; 9232; 422 antibodies from 28 providers.
DR DNASU; 56431; -.
DR Ensembl; ENSMUST00000103172; ENSMUSP00000099461; ENSMUSG00000015932.
DR GeneID; 56431; -.
DR KEGG; mmu:56431; -.
DR UCSC; uc008mqi.2; mouse.
DR CTD; 11034; -.
DR MGI; MGI:1929270; Dstn.
DR VEuPathDB; HostDB:ENSMUSG00000015932; -.
DR eggNOG; KOG1735; Eukaryota.
DR GeneTree; ENSGT00950000183000; -.
DR HOGENOM; CLU_094004_0_0_1; -.
DR InParanoid; Q9R0P5; -.
DR OMA; ITFYSWS; -.
DR OrthoDB; 1370477at2759; -.
DR PhylomeDB; Q9R0P5; -.
DR TreeFam; TF328601; -.
DR BioGRID-ORCS; 56431; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Dstn; mouse.
DR PRO; PR:Q9R0P5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9R0P5; protein.
DR Bgee; ENSMUSG00000015932; Expressed in ileal epithelium and 272 other tissues.
DR ExpressionAtlas; Q9R0P5; baseline and differential.
DR Genevisible; Q9R0P5; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
DR GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
DR GO; GO:0030043; P:actin filament fragmentation; IDA:UniProtKB.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IMP:MGI.
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:0007744|PubMed:19131326"
FT CHAIN 2..165
FT /note="Destrin"
FT /id="PRO_0000214919"
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:0007744|PubMed:19131326"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 19
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P60981"
SQ SEQUENCE 165 AA; 18522 MW; 42BD07984C9B3667 CRC64;
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIVVE EGKEILVGDV
GATITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPEQAP LKSKMIYASS
KDAIKKKFPG IKHEYQANGP EDLNRTCIAE KLGGSLIVAF EGSPV
