Full text data of DSTN
DSTN
(ACTDP, DSN)
[Confidence: low (only semi-automatic identification from reviews)]
Destrin (Actin-depolymerizing factor; ADF)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Destrin (Actin-depolymerizing factor; ADF)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P60981
ID DEST_HUMAN Reviewed; 165 AA.
AC P60981; B2R6N2; B4DYA6; P18282; Q5W166; Q6IAW2;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Destrin;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
GN Name=DSTN; Synonyms=ACTDP, DSN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8399167; DOI=10.1021/bi00089a014;
RA Hawkins M., Pope B., Maciver S.K., Weeds A.G.;
RT "Human actin depolymerizing factor mediates a pH-sensitive destruction
RT of actin filaments.";
RL Biochemistry 32:9985-9993(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-13, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 54-69, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP ISGYLATION.
RX PubMed=16815975; DOI=10.1073/pnas.0600397103;
RA Wong J.J., Pung Y.F., Sze N.S., Chin K.C.;
RT "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates
RT type I IFN-induced ISGylation of protein targets.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-139.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F-
CC actin) and binds to actin monomers (G-actin). Acts in a pH-
CC independent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60981-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60981-2; Sequence=VSP_043069;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely distributed in various tissues.
CC -!- PTM: ISGylated (Probable).
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC -!- SIMILARITY: Contains 1 ADF-H domain.
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DR EMBL; S65738; AAB28361.1; -; mRNA.
DR EMBL; CR457042; CAG33323.1; -; mRNA.
DR EMBL; AK302338; BAG63668.1; -; mRNA.
DR EMBL; AK312645; BAG35529.1; -; mRNA.
DR EMBL; AL132765; CAC10585.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10274.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10275.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10276.1; -; Genomic_DNA.
DR EMBL; BC009477; AAH09477.1; -; mRNA.
DR PIR; A54184; A54184.
DR RefSeq; NP_001011546.1; NM_001011546.1.
DR RefSeq; NP_006861.1; NM_006870.3.
DR RefSeq; XP_005260710.1; XM_005260653.1.
DR RefSeq; XP_005260711.1; XM_005260654.1.
DR UniGene; Hs.304192; -.
DR UniGene; Hs.705996; -.
DR ProteinModelPortal; P60981; -.
DR SMR; P60981; 2-165.
DR IntAct; P60981; 3.
DR MINT; MINT-5001125; -.
DR STRING; 9606.ENSP00000246069; -.
DR PhosphoSite; P60981; -.
DR DMDM; 46577586; -.
DR OGP; P18282; -.
DR REPRODUCTION-2DPAGE; IPI00473014; -.
DR UCD-2DPAGE; P60981; -.
DR PaxDb; P60981; -.
DR PRIDE; P60981; -.
DR DNASU; 11034; -.
DR Ensembl; ENST00000246069; ENSP00000246069; ENSG00000125868.
DR Ensembl; ENST00000543261; ENSP00000444808; ENSG00000125868.
DR GeneID; 11034; -.
DR KEGG; hsa:11034; -.
DR UCSC; uc002wpq.3; human.
DR CTD; 11034; -.
DR GeneCards; GC20P017550; -.
DR HGNC; HGNC:15750; DSTN.
DR HPA; CAB037094; -.
DR MIM; 609114; gene.
DR neXtProt; NX_P60981; -.
DR PharmGKB; PA27509; -.
DR eggNOG; NOG294392; -.
DR HOGENOM; HOG000039697; -.
DR HOVERGEN; HBG000381; -.
DR InParanoid; P60981; -.
DR KO; K10363; -.
DR OMA; QMLPEKD; -.
DR OrthoDB; EOG7353Z9; -.
DR PhylomeDB; P60981; -.
DR ChiTaRS; DSTN; human.
DR GenomeRNAi; 11034; -.
DR NextBio; 41930; -.
DR PRO; PR:P60981; -.
DR ArrayExpress; P60981; -.
DR Bgee; P60981; -.
DR CleanEx; HS_DSTN; -.
DR Genevestigator; P60981; -.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:InterPro.
DR GO; GO:0051014; P:actin filament severing; TAS:ProtInc.
DR GO; GO:0008154; P:actin polymerization or depolymerization; TAS:ProtInc.
DR GO; GO:0006928; P:cellular component movement; IEA:Ensembl.
DR GO; GO:0000910; P:cytokinesis; IEA:Ensembl.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IEA:Ensembl.
DR InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR InterPro; IPR017904; ADF/Cofilin/Destrin.
DR PANTHER; PTHR11913; PTHR11913; 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; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 165 Destrin.
FT /FTId=PRO_0000214918.
FT DOMAIN 4 153 ADF-H.
FT MOTIF 30 34 Nuclear localization signal (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 3 3 Phosphoserine.
FT MOD_RES 19 19 N6-acetyllysine.
FT VAR_SEQ 1 17 Missing (in isoform 2).
FT /FTId=VSP_043069.
FT VARIANT 139 139 G -> E (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036459.
SQ SEQUENCE 165 AA; 18506 MW; 8868A3167924100E CRC64;
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV
GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS
KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPV
//
ID DEST_HUMAN Reviewed; 165 AA.
AC P60981; B2R6N2; B4DYA6; P18282; Q5W166; Q6IAW2;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 102.
DE RecName: Full=Destrin;
DE AltName: Full=Actin-depolymerizing factor;
DE Short=ADF;
GN Name=DSTN; Synonyms=ACTDP, DSN;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8399167; DOI=10.1021/bi00089a014;
RA Hawkins M., Pope B., Maciver S.K., Weeds A.G.;
RT "Human actin depolymerizing factor mediates a pH-sensitive destruction
RT of actin filaments.";
RL Biochemistry 32:9985-9993(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-13, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 54-69, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP ISGYLATION.
RX PubMed=16815975; DOI=10.1073/pnas.0600397103;
RA Wong J.J., Pung Y.F., Sze N.S., Chin K.C.;
RT "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates
RT type I IFN-induced ISGylation of protein targets.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-19, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-3, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] GLU-139.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Actin-depolymerizing protein. Severs actin filaments (F-
CC actin) and binds to actin monomers (G-actin). Acts in a pH-
CC independent manner.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P60981-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P60981-2; Sequence=VSP_043069;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely distributed in various tissues.
CC -!- PTM: ISGylated (Probable).
CC -!- SIMILARITY: Belongs to the actin-binding proteins ADF family.
CC -!- SIMILARITY: Contains 1 ADF-H domain.
CC -----------------------------------------------------------------------
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CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; S65738; AAB28361.1; -; mRNA.
DR EMBL; CR457042; CAG33323.1; -; mRNA.
DR EMBL; AK302338; BAG63668.1; -; mRNA.
DR EMBL; AK312645; BAG35529.1; -; mRNA.
DR EMBL; AL132765; CAC10585.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10274.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10275.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10276.1; -; Genomic_DNA.
DR EMBL; BC009477; AAH09477.1; -; mRNA.
DR PIR; A54184; A54184.
DR RefSeq; NP_001011546.1; NM_001011546.1.
DR RefSeq; NP_006861.1; NM_006870.3.
DR RefSeq; XP_005260710.1; XM_005260653.1.
DR RefSeq; XP_005260711.1; XM_005260654.1.
DR UniGene; Hs.304192; -.
DR UniGene; Hs.705996; -.
DR ProteinModelPortal; P60981; -.
DR SMR; P60981; 2-165.
DR IntAct; P60981; 3.
DR MINT; MINT-5001125; -.
DR STRING; 9606.ENSP00000246069; -.
DR PhosphoSite; P60981; -.
DR DMDM; 46577586; -.
DR OGP; P18282; -.
DR REPRODUCTION-2DPAGE; IPI00473014; -.
DR UCD-2DPAGE; P60981; -.
DR PaxDb; P60981; -.
DR PRIDE; P60981; -.
DR DNASU; 11034; -.
DR Ensembl; ENST00000246069; ENSP00000246069; ENSG00000125868.
DR Ensembl; ENST00000543261; ENSP00000444808; ENSG00000125868.
DR GeneID; 11034; -.
DR KEGG; hsa:11034; -.
DR UCSC; uc002wpq.3; human.
DR CTD; 11034; -.
DR GeneCards; GC20P017550; -.
DR HGNC; HGNC:15750; DSTN.
DR HPA; CAB037094; -.
DR MIM; 609114; gene.
DR neXtProt; NX_P60981; -.
DR PharmGKB; PA27509; -.
DR eggNOG; NOG294392; -.
DR HOGENOM; HOG000039697; -.
DR HOVERGEN; HBG000381; -.
DR InParanoid; P60981; -.
DR KO; K10363; -.
DR OMA; QMLPEKD; -.
DR OrthoDB; EOG7353Z9; -.
DR PhylomeDB; P60981; -.
DR ChiTaRS; DSTN; human.
DR GenomeRNAi; 11034; -.
DR NextBio; 41930; -.
DR PRO; PR:P60981; -.
DR ArrayExpress; P60981; -.
DR Bgee; P60981; -.
DR CleanEx; HS_DSTN; -.
DR Genevestigator; P60981; -.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:InterPro.
DR GO; GO:0051014; P:actin filament severing; TAS:ProtInc.
DR GO; GO:0008154; P:actin polymerization or depolymerization; TAS:ProtInc.
DR GO; GO:0006928; P:cellular component movement; IEA:Ensembl.
DR GO; GO:0000910; P:cytokinesis; IEA:Ensembl.
DR GO; GO:0030836; P:positive regulation of actin filament depolymerization; IEA:Ensembl.
DR InterPro; IPR002108; Actin-bd_cofilin/tropomyosin.
DR InterPro; IPR017904; ADF/Cofilin/Destrin.
DR PANTHER; PTHR11913; PTHR11913; 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; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 165 Destrin.
FT /FTId=PRO_0000214918.
FT DOMAIN 4 153 ADF-H.
FT MOTIF 30 34 Nuclear localization signal (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 3 3 Phosphoserine.
FT MOD_RES 19 19 N6-acetyllysine.
FT VAR_SEQ 1 17 Missing (in isoform 2).
FT /FTId=VSP_043069.
FT VARIANT 139 139 G -> E (in a colorectal cancer sample;
FT somatic mutation).
FT /FTId=VAR_036459.
SQ SEQUENCE 165 AA; 18506 MW; 8868A3167924100E CRC64;
MASGVQVADE VCRIFYDMKV RKCSTPEEIK KRKKAVIFCL SADKKCIIVE EGKEILVGDV
GVTITDPFKH FVGMLPEKDC RYALYDASFE TKESRKEELM FFLWAPELAP LKSKMIYASS
KDAIKKKFQG IKHECQANGP EDLNRACIAE KLGGSLIVAF EGCPV
//
MIM
609114
*RECORD*
*FIELD* NO
609114
*FIELD* TI
*609114 DESTRIN; DSTN
;;ACTIN DEPOLYMERIZING FACTOR; ADF
*FIELD* TX
DESCRIPTION
Destrin is an essential actin regulatory protein belonging to the
read moreactin-depolymerizing factor (ADF)/cofilin family (see 601442). This
family of proteins is responsible for enhancing the turnover rate of
actin in vivo.
CLONING
ADF was first isolated from chick embryo brains as a protein that
promoted the disassembly of actin filaments (Bamburg et al., 1980).
Hawkins et al. (1993) cloned human ADF from an embryonic brain cDNA
library. They found that the deduced 165-amino acid protein is 100% and
95% identical to porcine destrin (Moriyama et al., 1990) chick ADF,
respectively.
GENE FUNCTION
Hawkins et al. (1993) showed that human destrin expressed in E. coli
behaved like native destrin from porcine brain. It bound to G-actin at
pH 8, thereby sequestering monomers and preventing polymerization. It
did not cosediment with F-actin at this pH, but severed actin filaments
in a calcium-insensitive manner. By contrast, at pH values below 7,
destrin bound to actin filaments in a highly cooperative manner and at a
1:1 ratio to filament subunits. When the pH was raised to 8.0, the
decorated filaments were rapidly severed and depolymerized.
MAPPING
Deloukas et al. (2001) assembled a physical map of human chromosome 20
and annotated 727 genes, one of which was destrin.
ANIMAL MODEL
Corneal disease-1 (corn1) and corn1(2J) are spontaneous mouse mutants
that develop irregular thickening of the corneal epithelium, similar to
that observed in human corneal surface disease. These autosomal
recessive mutations cause an increase in the rate of proliferation of
the corneal epithelial cells. Ikeda et al. (2003) reported that the
phenotypes in both mutants are caused by mutations in the destrin gene.
By positional cloning, they identified a deletion encompassing the
entire coding sequence of the destrin gene in corn1 mice and a point
mutation, pro106 to ser (P106S), in corn1(2J) mice. In situ analysis
showed that destrin was highly expressed in the corneal epithelium. The
corn1 mutations increased the content of filamentous actin in corneal
epithelial cells. Ikeda et al. (2003) suggested that there is an in vivo
connection between remodeling of the actin cytoskeleton and the control
of cell proliferation, at least in the corneal epithelium.
*FIELD* RF
1. Bamburg, J. R.; Harris, H. E.; Weeds, A. G.: Partial purification
and characterization of an actin depolymerizing factor from brain. FEBS
Lett. 121: 178-182, 1980.
2. Deloukas, P.; Matthews, L. H.; Ashurst, J.; Burton, J.; Gilbert,
J. G. R.; Jones, M.; Stavrides, G.; Almeida, J. P.; Babbage, A. K.;
Bagguley, C. L.; Bailey, J.; Barlow, K. F.; and 115 others: The
DNA sequence and comparative analysis of human chromosome 20. Nature 414:
865-871, 2001.
3. Hawkins, M.; Pope, B.; Maciver, S. K.; Weeds, A. G.: Human actin
depolymerizing factor mediates a pH-sensitive destruction of actin
filaments. Biochemistry 32: 9985-9993, 1993.
4. Ikeda, S.; Cunningham, L. A.; Boggess, D.; Hawes, N.; Hobson, C.
D.; Sundberg, J. P.; Naggert, J. K.; Smith, R. S.; Nishina, P. M.
: Aberrant actin cytoskeleton leads to accelerated proliferation of
corneal epithelial cells in mice deficient for destrin (actin depolymerizing
factor). Hum. Molec. Genet. 12: 1029-1036, 2003. Note: Erratum:
Hum. Molec. Genet. 12: 1359 only, 2003.
5. Moriyama, K.; Nishida, E.; Yonezawa, N.; Sakai, H.; Matsumoto,
S.; Iida, K.; Yahara, I.: Destrin, a mammalian actin-depolymerizing
protein, is closely related to cofilin: cloning and expression of
porcine brain destrin cDNA. J. Biol. Chem. 265: 5768-5773, 1990.
*FIELD* CD
George E. Tiller: 12/16/2004
*FIELD* ED
carol: 02/27/2008
carol: 1/27/2005
tkritzer: 1/27/2005
*RECORD*
*FIELD* NO
609114
*FIELD* TI
*609114 DESTRIN; DSTN
;;ACTIN DEPOLYMERIZING FACTOR; ADF
*FIELD* TX
DESCRIPTION
Destrin is an essential actin regulatory protein belonging to the
read moreactin-depolymerizing factor (ADF)/cofilin family (see 601442). This
family of proteins is responsible for enhancing the turnover rate of
actin in vivo.
CLONING
ADF was first isolated from chick embryo brains as a protein that
promoted the disassembly of actin filaments (Bamburg et al., 1980).
Hawkins et al. (1993) cloned human ADF from an embryonic brain cDNA
library. They found that the deduced 165-amino acid protein is 100% and
95% identical to porcine destrin (Moriyama et al., 1990) chick ADF,
respectively.
GENE FUNCTION
Hawkins et al. (1993) showed that human destrin expressed in E. coli
behaved like native destrin from porcine brain. It bound to G-actin at
pH 8, thereby sequestering monomers and preventing polymerization. It
did not cosediment with F-actin at this pH, but severed actin filaments
in a calcium-insensitive manner. By contrast, at pH values below 7,
destrin bound to actin filaments in a highly cooperative manner and at a
1:1 ratio to filament subunits. When the pH was raised to 8.0, the
decorated filaments were rapidly severed and depolymerized.
MAPPING
Deloukas et al. (2001) assembled a physical map of human chromosome 20
and annotated 727 genes, one of which was destrin.
ANIMAL MODEL
Corneal disease-1 (corn1) and corn1(2J) are spontaneous mouse mutants
that develop irregular thickening of the corneal epithelium, similar to
that observed in human corneal surface disease. These autosomal
recessive mutations cause an increase in the rate of proliferation of
the corneal epithelial cells. Ikeda et al. (2003) reported that the
phenotypes in both mutants are caused by mutations in the destrin gene.
By positional cloning, they identified a deletion encompassing the
entire coding sequence of the destrin gene in corn1 mice and a point
mutation, pro106 to ser (P106S), in corn1(2J) mice. In situ analysis
showed that destrin was highly expressed in the corneal epithelium. The
corn1 mutations increased the content of filamentous actin in corneal
epithelial cells. Ikeda et al. (2003) suggested that there is an in vivo
connection between remodeling of the actin cytoskeleton and the control
of cell proliferation, at least in the corneal epithelium.
*FIELD* RF
1. Bamburg, J. R.; Harris, H. E.; Weeds, A. G.: Partial purification
and characterization of an actin depolymerizing factor from brain. FEBS
Lett. 121: 178-182, 1980.
2. Deloukas, P.; Matthews, L. H.; Ashurst, J.; Burton, J.; Gilbert,
J. G. R.; Jones, M.; Stavrides, G.; Almeida, J. P.; Babbage, A. K.;
Bagguley, C. L.; Bailey, J.; Barlow, K. F.; and 115 others: The
DNA sequence and comparative analysis of human chromosome 20. Nature 414:
865-871, 2001.
3. Hawkins, M.; Pope, B.; Maciver, S. K.; Weeds, A. G.: Human actin
depolymerizing factor mediates a pH-sensitive destruction of actin
filaments. Biochemistry 32: 9985-9993, 1993.
4. Ikeda, S.; Cunningham, L. A.; Boggess, D.; Hawes, N.; Hobson, C.
D.; Sundberg, J. P.; Naggert, J. K.; Smith, R. S.; Nishina, P. M.
: Aberrant actin cytoskeleton leads to accelerated proliferation of
corneal epithelial cells in mice deficient for destrin (actin depolymerizing
factor). Hum. Molec. Genet. 12: 1029-1036, 2003. Note: Erratum:
Hum. Molec. Genet. 12: 1359 only, 2003.
5. Moriyama, K.; Nishida, E.; Yonezawa, N.; Sakai, H.; Matsumoto,
S.; Iida, K.; Yahara, I.: Destrin, a mammalian actin-depolymerizing
protein, is closely related to cofilin: cloning and expression of
porcine brain destrin cDNA. J. Biol. Chem. 265: 5768-5773, 1990.
*FIELD* CD
George E. Tiller: 12/16/2004
*FIELD* ED
carol: 02/27/2008
carol: 1/27/2005
tkritzer: 1/27/2005