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Database: UniProt
Entry: ISW1_CAEEL
LinkDB: ISW1_CAEEL
Original site: 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   24-JAN-2024, entry version 184.
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; 5.
DR   STRING; 6239.F37A4.8.1; -.
DR   iPTMnet; P41877; -.
DR   EPD; P41877; -.
DR   PaxDb; 6239-F37A4-8; -.
DR   PeptideAtlas; P41877; -.
DR   EnsemblMetazoa; F37A4.8.1; F37A4.8.1; WBGene00002169.
DR   UCSC; F37A4.8; c. elegans.
DR   AGR; WB:WBGene00002169; -.
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; VHDYQFF; -.
DR   OrthoDB; 5482994at2759; -.
DR   PhylomeDB; P41877; -.
DR   PRO; PR:P41877; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00002169; Expressed in germ line (C elegans) and 4 other cell types or 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   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 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   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-1; 1.
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; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//
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