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Chromatin-remodeling complex ATPase chain Iswi (EC 3.6.4.-) (CHRAC 140 kDa subunit) (Nucleosome-remodeling factor 140 kDa subunit) (NURF-140) (Protein imitation swi)

 ISWI_DROME              Reviewed;        1027 AA.
Q24368; A4UZF0; B5X0J3; Q0E9A4; Q8SX14; Q9V6E8;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 174.
RecName: Full=Chromatin-remodeling complex ATPase chain Iswi;
EC=3.6.4.-;
AltName: Full=CHRAC 140 kDa subunit;
AltName: Full=Nucleosome-remodeling factor 140 kDa subunit;
Short=NURF-140;
AltName: Full=Protein imitation swi;
Name=Iswi; ORFNames=CG8625;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Iso-1; TISSUE=Embryo;
PubMed=7908117; DOI=10.1128/MCB.14.4.2225;
Elfring L.K., Deuring R., McCallum C.M., Peterson C.L., Tamkun J.W.;
"Identification and characterization of Drosophila relatives of the
yeast transcriptional activator SNF2/SWI2.";
Mol. Cell. Biol. 14:2225-2234(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C.,
Celniker S.E.;
Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 95-124; 175-186; 578-610 AND 775-787,
IDENTIFICATION IN THE NURF COMPLEX, FUNCTION, DEVELOPMENTAL STAGE, AND
SUBCELLULAR LOCATION.
PubMed=8521502; DOI=10.1016/0092-8674(95)90217-1;
Tsukiyama T., Daniel C., Tamkun J., Wu C.;
"ISWI, a member of the SWI2/SNF2 ATPase family, encodes the 140 kDa
subunit of the nucleosome remodeling factor.";
Cell 83:1021-1026(1995).
[7]
FUNCTION.
PubMed=8521501; DOI=10.1016/0092-8674(95)90216-3;
Tsukiyama T., Wu C.;
"Purification and properties of an ATP-dependent nucleosome remodeling
factor.";
Cell 83:1011-1020(1995).
[8]
FUNCTION.
PubMed=12502740; DOI=10.1101/gad.1032202;
Badenhorst P., Voas M., Rebay I., Wu C.;
"Biological functions of the ISWI chromatin remodeling complex NURF.";
Genes Dev. 16:3186-3198(2002).
[9]
FUNCTION.
PubMed=16264191; DOI=10.1101/gad.1342605;
Badenhorst P., Xiao H., Cherbas L., Kwon S.Y., Voas M., Rebay I.,
Cherbas P., Wu C.;
"The Drosophila nucleosome remodeling factor NURF is required for
Ecdysteroid signaling and metamorphosis.";
Genes Dev. 19:2540-2545(2005).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
[11]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 688-991.
PubMed=14536084; DOI=10.1016/S1097-2765(03)00273-9;
Grune T., Brzeski J., Eberharter A., Clapier C.R., Corona D.F.V.,
Becker P.B., Mueller C.W.;
"Crystal structure and functional analysis of a nucleosome recognition
module of the remodeling factor ISWI.";
Mol. Cell 12:449-460(2003).
-!- FUNCTION: Energy-transducing component of the chromatin-remodeling
complexes NURF (nucleosome-remodeling factor), ACF (ATP-utilizing
chromatin assembly and remodeling factor), and CHRAC (chromatin
accessibility complex). NURF catalyzes ATP-dependent nucleosome
sliding and facilitates transcription of chromatin. It is required
for homeotic gene expression, proper larval blood cell
development, normal male X chromosome morphology, ecdysteroid
signaling and metamorphosis. {ECO:0000269|PubMed:12502740,
ECO:0000269|PubMed:16264191, ECO:0000269|PubMed:8521501,
ECO:0000269|PubMed:8521502}.
-!- SUBUNIT: Component of the NURF complex composed of Caf1, E(bx),
Nurf-38 and Iswi. {ECO:0000269|PubMed:8521502}.
-!- INTERACTION:
P18824:arm; NbExp=2; IntAct=EBI-367628, EBI-216128;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00624, ECO:0000269|PubMed:8521502}.
-!- DEVELOPMENTAL STAGE: Present throughout embryonic, larval and
pupal development and in female adults. Present at low levels in
adult males (at protein level). {ECO:0000269|PubMed:8521502}.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI
subfamily. {ECO:0000305}.
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EMBL; L27127; AAA19868.1; -; mRNA.
EMBL; AE013599; AAF58479.1; -; Genomic_DNA.
EMBL; AE013599; AAM68638.1; -; Genomic_DNA.
EMBL; AY094908; AAM11261.1; -; mRNA.
EMBL; BT044562; ACI15757.1; -; mRNA.
PIR; A56533; A56533.
RefSeq; NP_523719.1; NM_078995.2.
RefSeq; NP_725203.1; NM_165930.2.
RefSeq; NP_725204.1; NM_165931.2.
UniGene; Dm.2581; -.
PDB; 1OFC; X-ray; 1.90 A; X=691-991.
PDBsum; 1OFC; -.
ProteinModelPortal; Q24368; -.
SMR; Q24368; -.
BioGrid; 62163; 14.
DIP; DIP-24067N; -.
IntAct; Q24368; 6.
MINT; MINT-252539; -.
STRING; 7227.FBpp0086954; -.
iPTMnet; Q24368; -.
PaxDb; Q24368; -.
PRIDE; Q24368; -.
EnsemblMetazoa; FBtr0087841; FBpp0086954; FBgn0011604.
EnsemblMetazoa; FBtr0087842; FBpp0086955; FBgn0011604.
EnsemblMetazoa; FBtr0087843; FBpp0086956; FBgn0011604.
GeneID; 36390; -.
KEGG; dme:Dmel_CG8625; -.
CTD; 36390; -.
FlyBase; FBgn0011604; Iswi.
eggNOG; KOG0385; Eukaryota.
eggNOG; COG0553; LUCA.
GeneTree; ENSGT00860000133761; -.
InParanoid; Q24368; -.
KO; K11654; -.
OMA; LEDYCHW; -.
OrthoDB; EOG091G01GJ; -.
PhylomeDB; Q24368; -.
Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
EvolutionaryTrace; Q24368; -.
GenomeRNAi; 36390; -.
PRO; PR:Q24368; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0011604; -.
ExpressionAtlas; Q24368; differential.
Genevisible; Q24368; DM.
GO; GO:0016590; C:ACF complex; IDA:FlyBase.
GO; GO:0008623; C:CHRAC; IDA:FlyBase.
GO; GO:0031010; C:ISWI-type complex; IDA:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0016589; C:NURF complex; IDA:FlyBase.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0031213; C:RSF complex; IPI:FlyBase.
GO; GO:0005667; C:transcription factor complex; IPI:FlyBase.
GO; GO:0005524; F:ATP binding; ISS:FlyBase.
GO; GO:0003677; F:DNA binding; IEA:InterPro.
GO; GO:0003678; F:DNA helicase activity; TAS:FlyBase.
GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:FlyBase.
GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
GO; GO:0070615; F:nucleosome-dependent ATPase activity; IDA:FlyBase.
GO; GO:0000166; F:nucleotide binding; TAS:FlyBase.
GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:FlyBase.
GO; GO:0006333; P:chromatin assembly or disassembly; IDA:FlyBase.
GO; GO:0006325; P:chromatin organization; IMP:FlyBase.
GO; GO:0006338; P:chromatin remodeling; ISS:FlyBase.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0048813; P:dendrite morphogenesis; IMP:FlyBase.
GO; GO:0035076; P:ecdysone receptor-mediated signaling pathway; IGI:FlyBase.
GO; GO:0007517; P:muscle organ development; IMP:FlyBase.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:FlyBase.
GO; GO:0035063; P:nuclear speck organization; IMP:FlyBase.
GO; GO:0006334; P:nucleosome assembly; IDA:FlyBase.
GO; GO:0042766; P:nucleosome mobilization; IDA:FlyBase.
GO; GO:0016584; P:nucleosome positioning; IDA:FlyBase.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:FlyBase.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; TAS:FlyBase.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:FlyBase.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:FlyBase.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:FlyBase.
GO; GO:0035092; P:sperm chromatin condensation; IMP:FlyBase.
GO; GO:0035041; P:sperm chromatin decondensation; IMP:FlyBase.
GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
GO; GO:0006351; P:transcription, DNA-templated; IDA:FlyBase.
InterPro; IPR020838; DBINO.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR009057; Homeobox-like.
InterPro; IPR029915; ISWI.
InterPro; IPR015194; ISWI_HAND-dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
InterPro; IPR015195; SLIDE.
InterPro; IPR000330; SNF2_N.
PANTHER; PTHR10799:SF812; PTHR10799:SF812; 1.
Pfam; PF13892; DBINO; 1.
Pfam; PF09110; HAND; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF09111; SLIDE; 1.
Pfam; PF00176; SNF2_N; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00717; SANT; 2.
SUPFAM; SSF101224; SSF101224; 1.
SUPFAM; SSF46689; SSF46689; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51293; SANT; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Chromatin regulator; Complete proteome;
Direct protein sequencing; Helicase; Hydrolase; Nucleotide-binding;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
Transcription regulation.
CHAIN 1 1027 Chromatin-remodeling complex ATPase chain
Iswi.
/FTId=PRO_0000074333.
DOMAIN 140 305 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 435 586 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 795 847 SANT 1. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
DOMAIN 898 962 SANT 2. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
NP_BIND 153 160 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
MOTIF 256 259 DEAH box.
COMPBIAS 978 981 Poly-Lys.
COMPBIAS 1023 1027 Poly-Lys.
MOD_RES 67 67 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CONFLICT 645 645 E -> D (in Ref. 4; AAM11261).
{ECO:0000305}.
HELIX 698 705 {ECO:0000244|PDB:1OFC}.
HELIX 727 729 {ECO:0000244|PDB:1OFC}.
HELIX 733 749 {ECO:0000244|PDB:1OFC}.
HELIX 766 776 {ECO:0000244|PDB:1OFC}.
HELIX 783 792 {ECO:0000244|PDB:1OFC}.
HELIX 802 815 {ECO:0000244|PDB:1OFC}.
HELIX 820 823 {ECO:0000244|PDB:1OFC}.
HELIX 832 845 {ECO:0000244|PDB:1OFC}.
HELIX 846 848 {ECO:0000244|PDB:1OFC}.
HELIX 852 881 {ECO:0000244|PDB:1OFC}.
HELIX 886 889 {ECO:0000244|PDB:1OFC}.
HELIX 904 917 {ECO:0000244|PDB:1OFC}.
HELIX 924 934 {ECO:0000244|PDB:1OFC}.
HELIX 936 938 {ECO:0000244|PDB:1OFC}.
HELIX 942 945 {ECO:0000244|PDB:1OFC}.
HELIX 949 974 {ECO:0000244|PDB:1OFC}.
SEQUENCE 1027 AA; 118873 MW; 008FC81AE15E071F CRC64;
MSKTDTAAVE ATEENSNETT SDAATSSSGE KEAEFDNKIE ADRSRRFDFL LKQTEIFTHF
MTNSAKSPTK PKGRPKKIKD KDKEKDVADH RHRKTEQEED EELLAEDSAT KEIFRFDASP
AYIKSGEMRD YQIRGLNWMI SLYENGINGI LADEMGLGKT LQTISLLGYL KHFKNQAGPH
IVIVPKSTLQ NWVNEFKKWC PSLRAVCLIG DQDTRNTFIR DVLMPGEWDV CVTSYEMCIR
EKSVFKKFNW RYLVIDEAHR IKNEKSKLSE ILREFKTANR LLITGTPLQN NLHELWALLN
FLLPDVFNSS EDFDEWFNTN TCLGDDALIT RLHAVLKPFL LRRLKAEVEK RLKPKKEMKI
FVGLSKMQRD WYTKVLLKDI DVVNGAGKVE KMRLQNILMQ LRKCTNHPYL FDGAEPGPPY
TTDTHLVYNS GKMAILDKLL PKLQEQGSRV LIFSQMTRML DILEDYCHWR NYNYCRLDGQ
TPHEDRNRQI QEFNMDNSAK FLFMLSTRAG GLGINLATAD VVIIYDSDWN PQMDLQAMDR
AHRIGQKKQV RVFRLITEST VEEKIVERAE VKLRLDKMVI QGGRLVDNRS NQLNKDEMLN
IIRFGANQVF SSKETDITDE DIDVILERGE AKTAEQKAAL DSLGESSLRT FTMDTNGEAG
TSSVYQFEGE DWREKQKLNA LGNWIEPPKR ERKANYAVDA YFREALRVSE PKAPKAPRPP
KQPIVQDFQF FPPRLFELLD QEIYYFRKTV GYKVPKNTEL GSDATKVQRE EQRKIDEAEP
LTEEEIQEKE NLLSQGFTAW TKRDFNQFIK ANEKYGRDDI DNIAKDVEGK TPEEVIEYNA
VFWERCTELQ DIERIMGQIE RGEGKIQRRL SIKKALDQKM SRYRAPFHQL RLQYGNNKGK
NYTEIEDRFL VCMLHKLGFD KENVYEELRA AIRASPQFRF DWFIKSRTAL ELQRRCNTLI
TLIERENIEL EEKERAEKKK KAPKGSVSAG SGSASSNTPA PAPQPKASQK RKSEVVATSS
NSKKKKK


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25-194 DPF3 is a muscle-specific component of the BAF complex, a multiprotein complex involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleoso 0.05 mg
EIAAB38775 ATP-dependent helicase SMARCA1,Homo sapiens,Human,Nucleosome-remodeling factor subunit SNF2L,Probable global transcription activator SNF2L1,SMARCA1,SNF2L,SNF2L1,SWI_SNF-related matrix-associated actin


 

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