ID EGL27_CAEEL Reviewed; 1129 AA.
AC Q09228; J7RNK9; Q09229; Q86LT4; Q8MQF3; Q9XYD0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 27-MAR-2024, entry version 171.
DE RecName: Full=Egg-laying defective protein 27;
GN Name=egl-27 {ECO:0000312|WormBase:C04A2.3a};
GN ORFNames=C04A2.3 {ECO:0000312|WormBase:C04A2.3a};
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 [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=9927605; DOI=10.1242/dev.126.5.1055;
RA Herman M.A., Ch'ng Q., Hettenbach S.M., Ratliff T.M., Kenyon C.,
RA Herman R.K.;
RT "EGL-27 is similar to a metastasis-associated factor and controls cell
RT polarity and cell migration in C. elegans.";
RL Development 126:1055-1064(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=10226007; DOI=10.1242/dev.126.11.2483;
RA Solari F., Bateman A., Ahringer J.;
RT "The Caenorhabditis elegans genes egl-27 and egr-1 are similar to MTA1, a
RT member of a chromatin regulatory complex, and are redundantly required for
RT embryonic patterning.";
RL Development 126:2483-2494(1999).
RN [3]
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 [4]
RP FUNCTION, INTERACTION WITH CEH-6; SEM-4 AND SOX-2, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, DOMAIN, AND DISRUPTION PHENOTYPE.
RX PubMed=22493276; DOI=10.1073/pnas.1117031109;
RA Kagias K., Ahier A., Fischer N., Jarriault S.;
RT "Members of the NODE (Nanog and Oct4-associated deacetylase) complex and
RT SOX-2 promote the initiation of a natural cellular reprogramming event in
RT vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:6596-6601(2012).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23271974; DOI=10.1371/journal.pgen.1003108;
RA Xu X., Kim S.K.;
RT "The GATA transcription factor egl-27 delays aging by promoting stress
RT resistance in Caenorhabditis elegans.";
RL PLoS Genet. 8:E1003108-E1003108(2012).
RN [6]
RP INTERACTION WITH WDR-5.1.
RX PubMed=25124442; DOI=10.1126/science.1255885;
RA Zuryn S., Ahier A., Portoso M., White E.R., Morin M.C., Margueron R.,
RA Jarriault S.;
RT "Sequential histone-modifying activities determine the robustness of
RT transdifferentiation.";
RL Science 345:826-829(2014).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=25446273; DOI=10.1016/j.ydbio.2014.10.014;
RA Krueger A.V., Jelier R., Dzyubachyk O., Zimmerman T., Meijering E.,
RA Lehner B.;
RT "Comprehensive single cell-resolution analysis of the role of chromatin
RT regulators in early C. elegans embryogenesis.";
RL Dev. Biol. 398:153-162(2015).
CC -!- FUNCTION: Transcription factor which promotes stress survival and
CC delays aging. Required for cell cycle progression and development of
CC the mesodermal and endodermal embryonic lineages (PubMed:25446273).
CC Required for normal T-cell polarity, for correct migration of QL
CC neuroblast descendants and other cells, for embryonic patterning and
CC for the embryonic expression of hlh-8. Also required for the
CC transdifferentiation of the Y rectal epithelial cell to the PDA motor
CC neuron during larval development. {ECO:0000269|PubMed:10226007,
CC ECO:0000269|PubMed:22493276, ECO:0000269|PubMed:23271974,
CC ECO:0000269|PubMed:25446273, ECO:0000269|PubMed:9927605}.
CC -!- SUBUNIT: Interacts with ceh-6, sem-4 and sox-2 (PubMed:22493276).
CC Interacts with wdr-5.1 (PubMed:25124442). {ECO:0000269|PubMed:22493276,
CC ECO:0000269|PubMed:25124442}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:10226007,
CC ECO:0000269|PubMed:22493276, ECO:0000269|PubMed:9927605}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=a {ECO:0000312|WormBase:C04A2.3a};
CC IsoId=Q09228-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:C04A2.3b};
CC IsoId=Q09228-2; Sequence=VSP_047939, VSP_001608;
CC Name=c {ECO:0000312|WormBase:C04A2.3c};
CC IsoId=Q09228-3; Sequence=VSP_019864, VSP_001609;
CC Name=d {ECO:0000312|WormBase:C04A2.3d};
CC IsoId=Q09228-4; Sequence=VSP_047940, VSP_001608;
CC -!- TISSUE SPECIFICITY: Expression detected in anterior intestine and head
CC region. {ECO:0000269|PubMed:23271974}.
CC -!- DEVELOPMENTAL STAGE: Expression detected from the 50-cell stage of
CC embryogenesis through to adulthood. In the adult, expression increases
CC two-fold between day 4 and day 14. {ECO:0000269|PubMed:10226007,
CC ECO:0000269|PubMed:22493276, ECO:0000269|PubMed:23271974,
CC ECO:0000269|PubMed:9927605}.
CC -!- INDUCTION: By starvation, heat stress, oxidative stress, and UV stress.
CC {ECO:0000269|PubMed:23271974}.
CC -!- DOMAIN: The SANT domain and GATA-type zinc finger are required for
CC conversion of the Y rectal cell to the PDA neuron.
CC {ECO:0000269|PubMed:22493276}.
CC -!- DISRUPTION PHENOTYPE: Shortened lifespan and reduced survival in
CC response to heat stress. Impaired differentiation of the Y rectal cell
CC to the PDA neuron with the Y cell remaining undifferentiated in its
CC original rectal location. Double RNAi-mediated knockdown with lin-40
CC results in delayed cell cycle progression in mesodermal and endodermal
CC embryonic lineages, but accelerated cell cycle progression in a subset
CC of embryonic lineages (PubMed:25446273). {ECO:0000269|PubMed:22493276,
CC ECO:0000269|PubMed:23271974, ECO:0000269|PubMed:25446273}.
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DR EMBL; AF096618; AAD27790.1; -; mRNA.
DR EMBL; BX284602; CCD62843.1; -; Genomic_DNA.
DR EMBL; BX284602; CCD62844.2; -; Genomic_DNA.
DR EMBL; BX284602; CCD62845.1; -; Genomic_DNA.
DR EMBL; BX284602; CCM09405.1; -; Genomic_DNA.
DR PIR; T43674; T43674.
DR RefSeq; NP_001021911.2; NM_001026740.4.
DR RefSeq; NP_001021912.1; NM_001026741.2.
DR RefSeq; NP_001263660.1; NM_001276731.1. [Q09228-4]
DR RefSeq; NP_741012.1; NM_171011.3. [Q09228-1]
DR AlphaFoldDB; Q09228; -.
DR BioGRID; 39459; 20.
DR DIP; DIP-61372N; -.
DR IntAct; Q09228; 7.
DR STRING; 6239.C04A2.3a.1; -.
DR iPTMnet; Q09228; -.
DR EPD; Q09228; -.
DR PaxDb; 6239-C04A2-3a; -.
DR PeptideAtlas; Q09228; -.
DR EnsemblMetazoa; C04A2.3a.1; C04A2.3a.1; WBGene00001194. [Q09228-1]
DR EnsemblMetazoa; C04A2.3b.1; C04A2.3b.1; WBGene00001194. [Q09228-2]
DR EnsemblMetazoa; C04A2.3c.1; C04A2.3c.1; WBGene00001194. [Q09228-3]
DR EnsemblMetazoa; C04A2.3c.2; C04A2.3c.2; WBGene00001194. [Q09228-3]
DR EnsemblMetazoa; C04A2.3c.3; C04A2.3c.3; WBGene00001194. [Q09228-3]
DR EnsemblMetazoa; C04A2.3c.4; C04A2.3c.4; WBGene00001194. [Q09228-3]
DR EnsemblMetazoa; C04A2.3c.5; C04A2.3c.5; WBGene00001194. [Q09228-3]
DR EnsemblMetazoa; C04A2.3c.6; C04A2.3c.6; WBGene00001194. [Q09228-3]
DR EnsemblMetazoa; C04A2.3c.7; C04A2.3c.7; WBGene00001194. [Q09228-3]
DR EnsemblMetazoa; C04A2.3d.1; C04A2.3d.1; WBGene00001194. [Q09228-4]
DR GeneID; 174121; -.
DR KEGG; cel:CELE_C04A2.3; -.
DR UCSC; C04A2.3a; c. elegans. [Q09228-1]
DR AGR; WB:WBGene00001194; -.
DR WormBase; C04A2.3a; CE31287; WBGene00001194; egl-27. [Q09228-1]
DR WormBase; C04A2.3b; CE47754; WBGene00001194; egl-27. [Q09228-2]
DR WormBase; C04A2.3c; CE33268; WBGene00001194; egl-27. [Q09228-3]
DR WormBase; C04A2.3d; CE47784; WBGene00001194; egl-27. [Q09228-4]
DR eggNOG; KOG2133; Eukaryota.
DR GeneTree; ENSGT00940000153615; -.
DR HOGENOM; CLU_012470_0_0_1; -.
DR InParanoid; Q09228; -.
DR OMA; HHANGLL; -.
DR OrthoDB; 3349425at2759; -.
DR SignaLink; Q09228; -.
DR PRO; PR:Q09228; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001194; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR ExpressionAtlas; Q09228; baseline and differential.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016581; C:NuRD complex; ISS:WormBase.
DR GO; GO:0003682; F:chromatin binding; IDA:WormBase.
DR GO; GO:0019899; F:enzyme binding; IPI:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:WormBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0010171; P:body morphogenesis; IMP:WormBase.
DR GO; GO:0007155; P:cell adhesion; IMP:WormBase.
DR GO; GO:0001708; P:cell fate specification; IMP:WormBase.
DR GO; GO:0018991; P:egg-laying behavior; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0008544; P:epidermis development; IMP:WormBase.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:UniProtKB.
DR GO; GO:0031581; P:hemidesmosome assembly; IGI:WormBase.
DR GO; GO:0007498; P:mesoderm development; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IMP:WormBase.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0060290; P:transdifferentiation; IMP:WormBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:WormBase.
DR CDD; cd04709; BAH_MTA; 1.
DR CDD; cd11661; SANT_MTA3_like; 1.
DR CDD; cd00202; ZnF_GATA; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 4.10.1240.50; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR000679; Znf_GATA.
DR PANTHER; PTHR13859; ATROPHIN-RELATED; 1.
DR PANTHER; PTHR13859:SF11; GRUNGE, ISOFORM J; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF00320; GATA; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00401; ZnF_GATA; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Metal-binding;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1129
FT /note="Egg-laying defective protein 27"
FT /id="PRO_0000083511"
FT DOMAIN 87..223
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT DOMAIN 224..327
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 332..384
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 439..485
FT /note="GATA-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 982..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 489..517
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..934
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1035
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..515
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_019864"
FT VAR_SEQ 1..238
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_047940"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:10226007"
FT /id="VSP_047939"
FT VAR_SEQ 294..296
FT /note="Missing (in isoform b and isoform d)"
FT /evidence="ECO:0000303|PubMed:10226007"
FT /id="VSP_001608"
FT VAR_SEQ 886..887
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_001609"
FT CONFLICT 671
FT /note="P -> L (in Ref. 1; AAD27790)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1129 AA; 128359 MW; 6E0F88BBC0AF43E8 CRC64;
MSRFDSQCSS EDVNKEDECV PSSSEDSQDG VSSPMENDDE PEFSQKHYDI EPCYYSLTGK
SDRNCRGIVY RYRQDSDLKG FQSHDGTLYR LRDSVFVEVS QNEPYVIAAI CGFKYTKRDH
VVVKLTRYFR ADDIPEISLN LMKQERAELE INPHLCPQSL NRELFNSELQ ITQPVSCLRG
KCIVEYVKDV RHARTVADFS LDNDTFFFCL HYNQDSTKLA STHYAIRVGT SFQATLPPMA
ECSVGDDSDR DELLYRPNSI ESGEEEDYIK LARCYRTYTL SGNHMLDSQK NARSLQVSDL
LMDEAIIQLH RSGYKIDDAL SELNANDIIL TTDVDNMTQD DAKKFAKGIK QLGKNFSRIH
RELLPHHSRE QLVSYYYLWK KTPEATKPKQ AARRVNPTSI KRPTKEKVKA SRPTSTEYLD
FDSASESDVE NNGPSGRACH HCYGAESKDW HHANGLLLCT DCRLHYKKYG QLRQIANRPS
QVPACLFKRS NSDEEESGVR TRAGKKEQRR RTPSSMSETP DRRSPSTVSN GAPNLTAEET
PTKKLNGSVK RAPKRPLHNG VINNVEKSNS SEEPASPTTP PPTLTNGLTN GHGPESSTPN
GETISKRMKV EPSYDDDDDE EEGKMTIDEG DDDPMPVLNG FKKEESVEEI KLELNGTIKK
ENGVETDPTT PTCSMEAENE VCETPAVVSV EIRDETNGET NSDLKDDENV EPDSPEDTFE
LGSNVEFETK NAMFVRSIVR SCGPRCARTD LIFKIKVGGV WEKSIKEKEE RKKVHLQNQR
IQDSEKVAIQ QNQIKKEQQQ SQPTPQQIHQ QQAQQNAQHL QQLQQAVMLG HLPPEVLRQM
MPPQFGVDPT AILMQQMMAG QQSQGVNAAF QHQMALQQQL EAHQVQFQLM MAHQHQQKMI
AEQQQQQRHA AAQQLREREQ REQRERERER QHQQQAQQAL HQQQQQHAAA AANQLNPAMM
QMMALMANSA ASQQDIARLM EMAAQQQQQQ QQAAQAQAQR DQERERRERE AREREAARER
EREQAAREAA ARDQAAREHA QAVQAAAAAA QQAQALTPDM QHMHLLQQLM LNPALMMQLQ
QAQAQQQQQQ PQVTNPLQML QHGMAAQSAN QAEMMRRIHP EPAMRPQHQ
//
