LE418_CAEEL
ID LE418_CAEEL Reviewed; 1829 AA.
AC G5EBZ4;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein let-418 {ECO:0000312|EMBL:CCD62685.1};
DE AltName: Full=Lethal protein 418;
GN Name=let-418 {ECO:0000312|WormBase:F26F12.7};
GN Synonyms=evl-11 {ECO:0000303|PubMed:11076750};
GN ORFNames=F26F12.7 {ECO:0000312|WormBase:F26F12.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG29838.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:AAG29838.1};
RX PubMed=11076750; DOI=10.1242/dev.127.24.5277;
RA von Zelewsky T., Palladino F., Brunschwig K., Tobler H., Hajnal A.,
RA Mueller F.;
RT "The C. elegans Mi-2 chromatin-remodelling proteins function in vulval cell
RT fate determination.";
RL Development 127:5277-5284(2000).
RN [2]
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 [3] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, INTERACTION WITH PIE-1,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=12507426; DOI=10.1016/s0092-8674(02)01202-3;
RA Unhavaithaya Y., Shin T.H., Miliaras N., Lee J., Oyama T., Mello C.C.;
RT "MEP-1 and a homolog of the NURD complex component Mi-2 act together to
RT maintain germline-soma distinctions in C. elegans.";
RL Cell 111:991-1002(2002).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH LIN-1, AND SUBCELLULAR LOCATION.
RX PubMed=17466968; DOI=10.1016/j.ydbio.2007.03.026;
RA Guerry F., Marti C.O., Zhang Y., Moroni P.S., Jaquiery E., Muller F.;
RT "The Mi-2 nucleosome-remodeling protein LET-418 is targeted via LIN-1/ETS
RT to the promoter of lin-39/Hox during vulval development in C. elegans.";
RL Dev. Biol. 306:469-479(2007).
RN [5] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=17921522; DOI=10.1093/dnares/dsm016;
RA Eki T., Ishihara T., Katsura I., Hanaoka F.;
RT "A genome-wide survey and systematic RNAi-based characterization of
RT helicase-like genes in Caenorhabditis elegans.";
RL DNA Res. 14:183-199(2007).
RN [6] {ECO:0000305}
RP FUNCTION, AND IDENTIFICATION IN THE MEC AND NURD COMPLEX.
RX PubMed=21060680; DOI=10.1371/journal.pone.0013681;
RA Passannante M., Marti C.O., Pfefferli C., Moroni P.S., Kaeser-Pebernard S.,
RA Puoti A., Hunziker P., Wicky C., Muller F.;
RT "Different Mi-2 complexes for various developmental functions in
RT Caenorhabditis elegans.";
RL PLoS ONE 5:E13681-E13695(2010).
RN [7]
RP FUNCTION, AND INTERACTION WITH AKIR-1.
RX PubMed=30036395; DOI=10.1371/journal.pgen.1007494;
RA Polanowska J., Chen J.X., Soule J., Omi S., Belougne J., Taffoni C.,
RA Pujol N., Selbach M., Zugasti O., Ewbank J.J.;
RT "Evolutionary plasticity in the innate immune function of Akirin.";
RL PLoS Genet. 14:E1007494-E1007494(2018).
CC -!- FUNCTION: Part of a NuRD (Nucleosome Remodeling and Deacetylase)
CC complex which is implicated in the synMuv B pathway that negatively
CC regulates specification of vulval cell fate (PubMed:11076750,
CC PubMed:21060680). This negative regulation is thought to be mediated
CC via interaction with the promoter of lin-39, a key regulator in vulva
CC development, and is dependent on the presence lin-1 (PubMed:17466968).
CC Contributes to negative regulation of lag-2 which is expressed in the
CC gut during larval development (PubMed:21060680). Has a broad role in
CC development (PubMed:21060680). In association with akir-1, plays a role
CC in regulating the transcription of antimicrobial peptide genes in
CC response to fungal infection (PubMed:30036395).
CC {ECO:0000269|PubMed:11076750, ECO:0000269|PubMed:12507426,
CC ECO:0000269|PubMed:17466968, ECO:0000269|PubMed:21060680,
CC ECO:0000269|PubMed:30036395}.
CC -!- SUBUNIT: Component of the MEC (MEP-1-containing complex) complex that
CC contains let-418, mep-1 and hda-1 (PubMed:21060680). Component of a
CC NURD complex that contains let-418, hda-1, lin-40 and lin-53
CC (PubMed:21060680). Interacts with lin-1 (PubMed:17466968). Interacts
CC with pie-1 (PubMed:12507426). Interacts with akir-1 (PubMed:30036395).
CC {ECO:0000269|PubMed:12507426, ECO:0000269|PubMed:17466968,
CC ECO:0000269|PubMed:21060680, ECO:0000269|PubMed:30036395}.
CC -!- INTERACTION:
CC G5EBZ4; Q21502: mep-1; NbExp=2; IntAct=EBI-3831970, EBI-319858;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11076750,
CC ECO:0000269|PubMed:17466968}.
CC -!- TISSUE SPECIFICITY: Expressed in embryos and larva.
CC {ECO:0000269|PubMed:12507426}.
CC -!- DEVELOPMENTAL STAGE: Expressed in all interphase nuclei throughout
CC development. {ECO:0000269|PubMed:12507426}.
CC -!- DISRUPTION PHENOTYPE: Larval arrest, protruding vulva, sterile progeny.
CC {ECO:0000269|PubMed:12507426, ECO:0000269|PubMed:17921522}.
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DR EMBL; AF308445; AAG29838.1; -; mRNA.
DR EMBL; BX284605; CCD62685.1; -; Genomic_DNA.
DR PIR; T34239; T34239.
DR RefSeq; NP_504523.1; NM_072122.4.
DR AlphaFoldDB; G5EBZ4; -.
DR SMR; G5EBZ4; -.
DR BioGRID; 44019; 12.
DR IntAct; G5EBZ4; 2.
DR STRING; 6239.F26F12.7; -.
DR EPD; G5EBZ4; -.
DR PaxDb; G5EBZ4; -.
DR PeptideAtlas; G5EBZ4; -.
DR EnsemblMetazoa; F26F12.7.1; F26F12.7.1; WBGene00002637.
DR GeneID; 178970; -.
DR KEGG; cel:CELE_F26F12.7; -.
DR CTD; 178970; -.
DR WormBase; F26F12.7; CE17716; WBGene00002637; let-418.
DR eggNOG; KOG0383; Eukaryota.
DR GeneTree; ENSGT00940000169383; -.
DR HOGENOM; CLU_000315_22_1_1; -.
DR InParanoid; G5EBZ4; -.
DR OMA; DSPIKFH; -.
DR OrthoDB; 47497at2759; -.
DR PhylomeDB; G5EBZ4; -.
DR Reactome; R-CEL-3214815; HDACs deacetylate histones.
DR Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-CEL-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-CEL-9031628; NGF-stimulated transcription.
DR PRO; PR:G5EBZ4; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00002637; Expressed in embryo and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016581; C:NuRD complex; ISS:WormBase.
DR GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:WormBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008134; F:transcription factor binding; IPI:WormBase.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:WormBase.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0040027; P:negative regulation of vulval development; IMP:WormBase.
DR Gene3D; 3.30.40.10; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR012957; CHD_C2.
DR InterPro; IPR009462; CHD_II_SANT-like.
DR InterPro; IPR012958; CHD_N.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR009463; DUF1087.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF08074; CHDCT2; 1.
DR Pfam; PF08073; CHDNT; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF06461; DUF1086; 1.
DR Pfam; PF06465; DUF1087; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01146; DUF1086; 1.
DR SMART; SM01147; DUF1087; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..1829
FT /note="Protein let-418"
FT /id="PRO_0000419006"
FT DOMAIN 401..458
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 489..550
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 614..798
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 930..1093
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 256..303
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 317..365
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1168..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1745..1829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 749..752
FT /note="DEAH box"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..39
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1192
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1270..1288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1470..1492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1749..1767
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1784..1803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 627..634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1829 AA; 209151 MW; 1A887E990C63B661 CRC64;
MSTEEDPSLV DAEESMEEGS VTQDATEETE EEEEQEQGDE AGPSERKRSS RKKGGKGGKK
GSKKSAAAAS KVEIPDPYNS TSEEVCAAIG LTDVEFDYDE EEFQGISNLK TFSSIIKPQI
LEANPGTNVS KMYPMFQVKY KEYQDHMAAQ GKPVQKQARG SKTPAVSTPV IPPRSAPTKT
RSARRKRRDS DAPDSDQEFE AFIKQQEQLE DDLVKDKEDA RIKRAAEREE KKKGALEAAR
AAKKAKLEKG EEAENNDYCE ECKQDGELLL CDTCPRAYHT VCIDENMEEP PEGDWSCAHC
IEHGPEVVKE EPAKQNDEFC KICKETENLL LCDSCVCSFH AYCIDPPLTE VPKEETWSCP
RCETVKPEHK IEKILCWRWK EIPYPEPLEA GKEASSDDAM LKPPRKMEPR REREFFVKWK
YLSYWQCSWV SEMLLEVHFR MLILLYWRKN DSDAPPEFEE SVTSRHHSDN DPYKLRERFY
QYGIKPEWMQ IHRIINHQSY AKSQQDYLVK WKELSYDQAT WERDDSNIAN YEEAIIKYWQ
HRESKLNEDI PKNVQKMIAK HREAKGLPPK EDEKKKKKRE KIDIRKKYEV QPDYVTETGG
KLHPYQLEGL NWLRHCWSNG TDAILADEMG LGKTVQSLTF LYSLMKEGHC KGPFLIAAPL
STIINWEREA EQWCPDFYVV TYVGLRDARV VLREHEFSFV EGAVRSGPKA SKMKTTENMK
FHVLLTSYET INMDKTILSS IEWGALVVDE AHRLKNNQSL FFKNLNEYTI HYRVLLTGTP
LQNNLEELFH LLNFLSKERF NQLEAFTAEF NEISKEDQIE KLHNLLGPHM LRRLKADVLT
GMPSKSELIV RVELSAMQKK WYKNILTRNF DALNVKNGGT QMSLMNVLME LKKCCNHPYL
FVKAELEAPK EKNGMYEGTA LIKNSGKFVL LQKMLRKLKD GGHRVLIFSQ MTRMLDIMED
LCEYEGYRYE RIDGSIMGQM RQDAIDRYNA PGAQQFIFLL STRAGGLGIN LATADTVIIY
DSDWNPHNDI QAFSRAHRLG QKHKVMIYRF VTKKSVEEKI TSVAKKKMLL NHLVVRAGLG
GKEGKTMSKT ELDDVLRWGT EELFSEDLDA AEGEGSEKKG AAAQEIVWDD AAVDALLDRS
NKEETPAGED GEEKAEWQNE YLSSFKVASY QTKETEGQEE EEEEETEVIK EDEKEPDPDY
WEKLLKHHYE QDREIELQKL GKGKRVRKQI NYASENMGTD WSKQNQTQDD DDDNESYRGS
DNGDGLNSDE DDYDEKKKRR RDEEKMPPLM AKVNGQVEIL GFNPRQRKAF YGAVMRWGMP
PQDSHQSQWL VRDLRNKSEK VFRAYASLFM RHLCEPGADG HDTFNDGVPR EGLNRQHVLG
RIGLLSLVRR KVQEFEQYNG QWSMPEIQDE VLAKAANGSA QGSSRSTPKP KEEPKEEPME
KEDATETVNG ATSEPATDAE SEQNAPVDEP MDTDEAKEPK EEPIETEKPR AARPSFKFNI
CDGGFTELHS LWANEEKVAR NGKEYEIWYR RHDYWLLAGV VVHGYGRFQA NFNDIINDPR
FSVLNEPFKE VGAEATGSDI KAKFMQRRFK LIEQSLVIEE QLRRAAHANR HLQPDNVGPL
AQRFADLENI AESQANIAKE SSAGNRNANA VLHKTLVQLD EILSDMKADV SRLPSTFTQL
ATVTERLNMT ERQILSRLTT KDEDAIANRS VLPPPGPFVT PILRQQMDGI QPKFAALYSK
FMSENGERME EDEPVEAEEE EGVKQEPDDE TQDSAEAPPV LSAEVNSDDS NDVPSTSAAA
AVSSETAADA EPASAEDQAP TDEPEPMET
