GenomeNet

Database: UniProt
Entry: G5EBZ4
LinkDB: G5EBZ4
Original site: G5EBZ4 
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   16-OCT-2019, entry version 61.
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;
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
RT   cell 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [3] {ECO:0000305}
RP   FUNCTION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, INTERACTION WITH
RP   PIE-1, 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
RT   to 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-
RT   1/ETS to the promoter of lin-39/Hox during vulval development in C.
RT   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.,
RA   Kaeser-Pebernard S., 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
CC       negatively regulates specification of vulval cell fate
CC       (PubMed:11076750, PubMed:21060680). This negative regulation is
CC       thought to be mediated via interaction with the promoter of lin-
CC       39, a key regulator in vulva development, and is dependent on the
CC       presence lin-1 (PubMed:17466968). Contributes to negative
CC       regulation of lag-2 which is expressed in the gut during larval
CC       development (PubMed:21060680). Has a broad role in development
CC       (PubMed:21060680). In association with akir-1, plays a role in
CC       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
CC       that contains let-418, mep-1 and hda-1 (PubMed:21060680).
CC       Component of a NURD complex that contains let-418, hda-1, lin-40
CC       and lin-53 (PubMed:21060680). Interacts with lin-1
CC       (PubMed:17466968). Interacts with pie-1 (PubMed:12507426).
CC       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       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
CC       progeny. {ECO:0000269|PubMed:12507426,
CC       ECO:0000269|PubMed:17921522}.
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   SMR; G5EBZ4; -.
DR   BioGrid; 44019; 2.
DR   IntAct; G5EBZ4; 2.
DR   STRING; 6239.F26F12.7; -.
DR   EPD; G5EBZ4; -.
DR   PaxDb; G5EBZ4; -.
DR   PeptideAtlas; G5EBZ4; -.
DR   PRIDE; 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   eggNOG; COG0553; LUCA.
DR   GeneTree; ENSGT00940000169383; -.
DR   InParanoid; G5EBZ4; -.
DR   KO; K11643; -.
DR   OMA; TWERDDM; -.
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   PRO; PR:G5EBZ4; -.
DR   Proteomes; UP000001940; Chromosome V.
DR   Bgee; WBGene00002637; Expressed in 5 organ(s), highest expression level in multi-cellular organism.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008134; F:transcription factor binding; IPI:WormBase.
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   InterPro; IPR012957; CHD_C2.
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; IPR009462; DUF1086.
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_N; 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; Complete proteome; Helicase; Hydrolase; Metal-binding;
KW   Nucleotide-binding; Nucleus; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1829       Protein let-418.
FT                                /FTId=PRO_0000419006.
FT   DOMAIN      401    458       Chromo 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      489    550       Chromo 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      614    798       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      930   1093       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   ZN_FING     256    303       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     317    365       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   NP_BIND     627    634       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   MOTIF       749    752       DEAH box. {ECO:0000255}.
FT   COMPBIAS    574    578       Poly-Lys. {ECO:0000255}.
FT   COMPBIAS   1143   1216       Glu-rich. {ECO:0000255}.
FT   COMPBIAS   1249   1253       Poly-Asp. {ECO:0000255}.
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
//
DBGET integrated database retrieval system