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Destrin (Actin-depolymerizing factor) (ADF) (Sid 23)

 DEST_MOUSE              Reviewed;         165 AA.
Q9R0P5;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
28-MAR-2018, entry version 140.
RecName: Full=Destrin;
AltName: Full=Actin-depolymerizing factor;
Short=ADF;
AltName: Full=Sid 23;
Name=Dstn; Synonyms=Dsn, Sid23;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T.;
"Mouse actin depolymerizing factor sid23.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cecum;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
PROTEIN SEQUENCE OF 54-69 AND 133-145, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[4]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=11809832; DOI=10.1091/mbc.01-07-0331;
Vartiainen M.K., Mustonen T., Mattila P.K., Ojala P.J., Thesleff I.,
Partanen J., Lappalainen P.;
"The three mouse actin-depolymerizing factor/cofilins evolved to
fulfill cell-type-specific requirements for actin dynamics.";
Mol. Biol. Cell 13:183-194(2002).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F-
actin) and binds to actin monomers (G-actin). Acts in a pH-
independent manner.
-!- TISSUE SPECIFICITY: Widely expressed. Not found in skeletal
muscle. {ECO:0000269|PubMed:11809832}.
-!- DEVELOPMENTAL STAGE: In E10.5 embryo somites is expressed in a
superficial patch of cells (adaxial region).
{ECO:0000269|PubMed:11809832}.
-!- PTM: ISGylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
{ECO:0000305}.
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EMBL; AB025406; BAA84691.1; -; mRNA.
EMBL; AK078898; BAC37447.1; -; mRNA.
CCDS; CCDS16812.1; -.
RefSeq; NP_062745.1; NM_019771.2.
UniGene; Mm.28919; -.
ProteinModelPortal; Q9R0P5; -.
BioGrid; 207975; 8.
IntAct; Q9R0P5; 10.
MINT; Q9R0P5; -.
STRING; 10090.ENSMUSP00000099461; -.
iPTMnet; Q9R0P5; -.
PhosphoSitePlus; Q9R0P5; -.
SwissPalm; Q9R0P5; -.
REPRODUCTION-2DPAGE; IPI00127942; -.
REPRODUCTION-2DPAGE; Q9R0P5; -.
EPD; Q9R0P5; -.
MaxQB; Q9R0P5; -.
PaxDb; Q9R0P5; -.
PRIDE; Q9R0P5; -.
Ensembl; ENSMUST00000103172; ENSMUSP00000099461; ENSMUSG00000015932.
GeneID; 56431; -.
KEGG; mmu:56431; -.
UCSC; uc008mqi.2; mouse.
CTD; 11034; -.
MGI; MGI:1929270; Dstn.
eggNOG; KOG1735; Eukaryota.
eggNOG; ENOG41122P5; LUCA.
GeneTree; ENSGT00440000033289; -.
HOGENOM; HOG000039697; -.
HOVERGEN; HBG000381; -.
InParanoid; Q9R0P5; -.
KO; K10363; -.
OMA; QMLPEKD; -.
OrthoDB; EOG091G0PWC; -.
PhylomeDB; Q9R0P5; -.
TreeFam; TF328601; -.
PRO; PR:Q9R0P5; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000015932; -.
CleanEx; MM_DSTN; -.
ExpressionAtlas; Q9R0P5; baseline and differential.
Genevisible; Q9R0P5; MM.
GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0051015; F:actin filament binding; IDA:UniProtKB.
GO; GO:0030042; P:actin filament depolymerization; IDA:UniProtKB.
GO; GO:0030043; P:actin filament fragmentation; IDA:UniProtKB.
GO; GO:0051014; P:actin filament severing; IEA:InterPro.
GO; GO:0030836; P:positive regulation of actin filament depolymerization; IMP:MGI.
CDD; cd11286; ADF_cofilin_like; 1.
Gene3D; 3.40.20.10; -; 1.
InterPro; IPR002108; ADF-H.
InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
InterPro; IPR017904; ADF/Cofilin.
InterPro; IPR029924; Dstn.
PANTHER; PTHR11913; PTHR11913; 1.
PANTHER; PTHR11913:SF18; PTHR11913:SF18; 1.
Pfam; PF00241; Cofilin_ADF; 1.
PRINTS; PR00006; COFILIN.
SMART; SM00102; ADF; 1.
PROSITE; PS51263; ADF_H; 1.
1: Evidence at protein level;
Acetylation; Actin-binding; Complete proteome;
Direct protein sequencing; Phosphoprotein; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19131326}.
CHAIN 2 165 Destrin.
/FTId=PRO_0000214919.
DOMAIN 4 153 ADF-H. {ECO:0000255|PROSITE-
ProRule:PRU00599}.
MOTIF 30 34 Nuclear localization signal.
{ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:19131326}.
MOD_RES 19 19 N6-acetyllysine.
{ECO:0000250|UniProtKB:P60981}.
SEQUENCE 165 AA; 18522 MW; 42BD07984C9B3667 CRC64;
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIVVE EGKEILVGDV
GATITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPEQAP LKSKMIYASS
KDAIKKKFPG IKHEYQANGP EDLNRTCIAE KLGGSLIVAF EGSPV


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