ISW1_CAEEL
ID ISW1_CAEEL Reviewed; 1009 AA.
AC P41877;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Chromatin-remodeling complex ATPase chain isw-1;
DE EC=3.6.4.-;
DE AltName: Full=Nucleosome-remodeling factor subunit isw-1;
GN Name=isw-1 {ECO:0000312|WormBase:F37A4.8};
GN ORFNames=F37A4.8 {ECO:0000312|WormBase:F37A4.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP FUNCTION, AND SUBUNIT.
RX PubMed=16774993; DOI=10.1242/dev.02444;
RA Andersen E.C., Lu X., Horvitz H.R.;
RT "C. elegans ISWI and NURF301 antagonize an Rb-like pathway in the
RT determination of multiple cell fates.";
RL Development 133:2695-2704(2006).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=16710447; DOI=10.1371/journal.pgen.0020074;
RA Cui M., Kim E.B., Han M.;
RT "Diverse chromatin remodeling genes antagonize the Rb-involved SynMuv
RT pathways in C. elegans.";
RL PLoS Genet. 2:E74-E74(2006).
CC -!- FUNCTION: Energy-transducing component of a NURF-like (nucleosome-
CC remodeling factor-like) complex, which would catalyze ATP-dependent
CC nucleosome sliding and facilitate transcription of chromatin
CC (Probable). Involved in vulval cell fates.
CC {ECO:0000269|PubMed:16774993, ECO:0000305}.
CC -!- SUBUNIT: Part of a nucleosome-remodeling factor-like (NURF-like)
CC complex containing nurf-1 and isw-1. {ECO:0000305|PubMed:16774993}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in sterility
CC (PubMed:16710447). RNAi-mediated knockdown at 25 degrees Celsius
CC rescues the larval lethality phenotype of the mep-1 (q660) single
CC mutants (PubMed:16710447). {ECO:0000269|PubMed:16710447}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000305}.
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DR EMBL; BX284603; CCD70709.1; -; Genomic_DNA.
DR PIR; S44645; S44645.
DR RefSeq; NP_498468.2; NM_066067.5.
DR AlphaFoldDB; P41877; -.
DR SMR; P41877; -.
DR BioGRID; 41160; 4.
DR STRING; 6239.F37A4.8; -.
DR iPTMnet; P41877; -.
DR EPD; P41877; -.
DR PaxDb; P41877; -.
DR PeptideAtlas; P41877; -.
DR EnsemblMetazoa; F37A4.8.1; F37A4.8.1; WBGene00002169.
DR GeneID; 175944; -.
DR KEGG; cel:CELE_F37A4.8; -.
DR UCSC; F37A4.8; c. elegans.
DR CTD; 175944; -.
DR WormBase; F37A4.8; CE29792; WBGene00002169; isw-1.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000157297; -.
DR HOGENOM; CLU_000315_0_0_1; -.
DR InParanoid; P41877; -.
DR OMA; IHDWQFF; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; P41877; -.
DR PRO; PR:P41877; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00002169; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:WormBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0040026; P:positive regulation of vulval development; IGI:WormBase.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.1040.30; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; SSF101224; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Activator; ATP-binding; Chromatin regulator; Developmental protein;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1009
FT /note="Chromatin-remodeling complex ATPase chain isw-1"
FT /id="PRO_0000074317"
FT DOMAIN 144..309
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 439..590
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 797..848
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 899..963
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 260..263
FT /note="DEAH box"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1009 AA; 116675 MW; 54678CF403F40825 CRC64;
MSVHESSNEI NDEPMDTDSN IPESSGNDPS MEVDDEPESS DAADSFKRFE RLLQKTENFS
HCLSSGDAKL ATGAPVDTKK RGRPSKKNGI DGDHRHRKTE QEEDEEMVAD AIKSDDLVIF
DKSPFYIENG EMRDYQVRGL NWLASLQHNK INGILADEMG LGKTLQTISM IGYMKHYKNK
ASPHLVIVPK STLQNWANEF KKWCPSINAV VLIGDEAARN QVLRDVILPQ KFDVCCTTYE
MMLKVKTQLK KLNWRYIIID EAHRIKNEKS KLSETVRELN SENRLLITGT PLQNNLHELW
ALLNFLLPDI FTSSDDFDSW FSNDAMSGNT DLVQRLHKVL QPFLLRRIKS DVEKSLLPKK
EVKVYVGLSK MQREWYTKVL MKDIDIINGA GKVEKARLMN ILMHLRKCVN HPYLFDGAEP
GPPFTTDQHL VDNSGKMVVL DKLLMKFKEQ GSRVLIFSQF SRMLDLLEDF CWWRHYEYCR
LDGSTPHEDR SNAIEAYNAP DSKKFIFMLT TRAGGLGINL ATADVVIIYD SDWNPQSDLQ
AMDRAHRIGQ KKQVRVFRLI TENTVDERII EKAEAKLRLD NIVIQQGRMS EAQKTLGKGD
MISMIRHGAE QVFAAKDSTI SDDDIDTILE KAEVKTAELN EKMGKIDENN LRNMTFEDNA
KFTVYQFEGE NYKAKQADGM GHFWIEPPKR ERKANYQVDL YYKEAMRAGN PTEKQSKAPR
PKLPQVFDFQ FYPRRLFELL DKEIYHYRKT IGYVAERPKD VPPKEAEKRQ AEEQKLINNA
RPLTDKEQEE KAELLTQSVT DWTKREFQQF VRGNEKYGRE DLESIAKEME RPLEEIQSYA
KVFWERIEEL QDSEKVLSQI EKGEARIQRK YAVKKALDAK IAKYKAPFQQ LRISYGTNKG
KTYTEEEDRF LVCETHRLGH DKENVFEELR QSVRMAPQFR FDWFLKSRTA MELQRRCNTL
ITLIEREMGE VVESKPVIVT AADKKKSVAK DLSKSSGTPT AKKVKATPK
