EGL43_CAEEL
ID EGL43_CAEEL Reviewed; 543 AA.
AC Q22024; Q22023; Q26336; Q26337; Q7JM79; Q7JPS6;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Zinc finger protein egl-43 {ECO:0000305};
DE AltName: Full=Egg-laying defective protein 43 {ECO:0000312|WormBase:R53.3a};
GN Name=egl-43 {ECO:0000312|WormBase:R53.3a};
GN ORFNames=R53.3 {ECO:0000312|WormBase:R53.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|EMBL:AAB28819.1, ECO:0000312|EMBL:AAB28820.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND FUNCTION.
RX PubMed=8224840; DOI=10.1101/gad.7.11.2097;
RA Garriga G., Guenther C., Horvitz H.R.;
RT "Migrations of the Caenorhabditis elegans HSNs are regulated by egl-43, a
RT gene encoding two zinc finger proteins.";
RL Genes Dev. 7:2097-2109(1993).
RN [2] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=10049362; DOI=10.1101/gad.13.4.472;
RA Baum P.D., Guenther C., Frank C.A., Pham B.V., Garriga G.;
RT "The Caenorhabditis elegans gene ham-2 links Hox patterning to migration of
RT the HSN motor neuron.";
RL Genes Dev. 13:472-483(1999).
RN [4] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17215301; DOI=10.1242/dev.02769;
RA Hwang B.J., Meruelo A.D., Sternberg P.W.;
RT "C. elegans EVI1 proto-oncogene, EGL-43, is necessary for Notch-mediated
RT cell fate specification and regulates cell invasion.";
RL Development 134:669-679(2007).
RN [5] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=17573066; DOI=10.1016/j.ydbio.2007.05.023;
RA Rimann I., Hajnal A.;
RT "Regulation of anchor cell invasion and uterine cell fates by the egl-43
RT Evi-1 proto-oncogene in Caenorhabditis elegans.";
RL Dev. Biol. 308:187-195(2007).
RN [6] {ECO:0000305}
RP FUNCTION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND DOMAIN.
RX PubMed=32203506; DOI=10.1371/journal.pgen.1008470;
RA Deng T., Stempor P., Appert A., Daube M., Ahringer J., Hajnal A.,
RA Lattmann E.;
RT "The Caenorhabditis elegans homolog of the Evi1 proto-oncogene, egl-43,
RT coordinates G1 cell cycle arrest with pro-invasive gene expression during
RT anchor cell invasion.";
RL PLoS Genet. 16:e1008470-e1008470(2020).
CC -!- FUNCTION: Probable transcription factor, required for migration of the
CC hermaphrodite-specific motor neurons (HSNs) from the tail to the gonad
CC primordium during HSN cell differentiation (PubMed:8224840,
CC PubMed:10049362). Required for phasmid neuron development
CC (PubMed:8224840). Required to specify the pi-cell fate of ventral
CC uterine precursor cell (VU) cells (PubMed:17573066).
CC {ECO:0000269|PubMed:10049362, ECO:0000269|PubMed:17573066,
CC ECO:0000269|PubMed:8224840}.
CC -!- FUNCTION: [Isoform a]: Probable transcription factor, involved in lin-
CC 12 (Notch)-dependent anchor cell (AC) and ventral uterine (VU)
CC precursor cell fate specification and in AC invasion (PubMed:17215301,
CC PubMed:17573066, PubMed:32203506). Prevents AC proliferation after AC
CC cell specification by repressing lin-12 expression (PubMed:32203506).
CC May form a positive feedback loop, together with the transcription
CC factor fos-1, that maintains mutual high levels of expression and so
CC activates AC invasion (PubMed:32203506). {ECO:0000269|PubMed:17215301,
CC ECO:0000269|PubMed:17573066, ECO:0000269|PubMed:32203506}.
CC -!- FUNCTION: [Isoform b]: Dispensable for anchor cell (AC) invasion and
CC for preventing AC proliferation. {ECO:0000269|PubMed:32203506}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10049362}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:R53.3a}; Synonyms=egl-43L
CC {ECO:0000303|PubMed:17573066};
CC IsoId=Q22024-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:R53.3b}; Synonyms=egl-43S
CC {ECO:0000303|PubMed:17573066};
CC IsoId=Q22024-2; Sequence=VSP_060814;
CC -!- DEVELOPMENTAL STAGE: Expressed in the hermaphrodite-specific motor
CC neuron (HSN) / phasmid sensory neuron B (PHB) precursor, and the
CC phasmid sensory neuron A (PHA) in the tail at ~400 minutes
CC embryogenesis (at protein level) (PubMed:10049362). Continues to be
CC expressed in PHA and PHB neurons of L1 larvae (PubMed:10049362).
CC Expressed in the HSN before and during HSN migration from the tail to
CC the gonad primordium of the embryo and down-regulated after migration
CC (at protein level) (PubMed:10049362). Expressed in the pre-anchor cell
CC (AC)/pre-ventral uterine (VU) cells at early L2 and maintained in their
CC 37 descendants at early L4 (PubMed:17215301, PubMed:32203506).
CC {ECO:0000269|PubMed:10049362, ECO:0000269|PubMed:17215301,
CC ECO:0000269|PubMed:32203506}.
CC -!- DEVELOPMENTAL STAGE: [Isoform a]: Expressed in the ventral uterine (VU)
CC cells of mid L2 larvae (Pn.p stage) and then in the anchor cell (AC)
CC beginning in mid L3 larvae (PubMed:17573066, PubMed:32203506).
CC Expression increases during AC invasion (PubMed:17573066).
CC {ECO:0000269|PubMed:17573066, ECO:0000269|PubMed:32203506}.
CC -!- DEVELOPMENTAL STAGE: [Isoform b]: Expressed, earlier than isoform a, in
CC the anchor cell (AC) at the Pn.p stage in mid L2 larvae
CC (PubMed:17573066). Expression decreases during AC invasion
CC (PubMed:17573066). {ECO:0000269|PubMed:17573066}.
CC -!- DOMAIN: The positive regulatory (PR) domain is required for egl-43
CC protein stability but is dispensable for anchor cell (AC) invasion and
CC preventing AC proliferation. {ECO:0000269|PubMed:32203506}.
CC -!- DOMAIN: The C2H2-type zinc-finger domains 1, 2 and 3 are dispensable
CC for anchor cell (AC) invasion and preventing AC proliferation.
CC {ECO:0000269|PubMed:32203506}.
CC -!- DOMAIN: The C2H2-type zinc-finger domains 4 and 5 may be required for
CC anchor cell (AC) invasion and preventing AC proliferation.
CC {ECO:0000269|PubMed:32203506}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes defects in anchor
CC cell (AC) and ventral uterine (VU) precursor cell specification and AC
CC invasion in the larval L3 and L4 stages (PubMed:17215301,
CC PubMed:17573066). RNAi-mediated knockdown on a lin-12 mutant background
CC reverses the AC-deficient phenotype (PubMed:17215301). RNAi-mediated
CC knockdown reduces expression of zmp-1, cdh-3 and him-4 in the AC
CC (PubMed:17215301, PubMed:17573066). RNAi-mediated knockdown reduces
CC expression of fos-1a in the anchor cell (AC) approximately three-fold
CC (PubMed:32203506). RNAi-mediated knockdown causes defects in vulval
CC morphogenesis (PubMed:17573066). {ECO:0000269|PubMed:17215301,
CC ECO:0000269|PubMed:17573066, ECO:0000269|PubMed:32203506}.
CC -!- DISRUPTION PHENOTYPE: [Isoform a]: RNAi-mediated knockdown causes
CC defects in anchor cell (AC) invasion, including increased CDK activity
CC and re-entry of the AC into the cell cycle, resulting in the presence
CC of two or more AC. {ECO:0000269|PubMed:17573066,
CC ECO:0000269|PubMed:32203506}.
CC -!- DISRUPTION PHENOTYPE: [Isoform b]: No defects in anchor cell (AC)
CC invasion or arrest in G1 seen upon RNAi-mediated knockdown.
CC {ECO:0000269|PubMed:32203506}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB28819.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB28820.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; S66757; AAB28819.1; ALT_FRAME; mRNA.
DR EMBL; S66936; AAB28820.1; ALT_FRAME; mRNA.
DR EMBL; BX284602; CAA91352.1; -; Genomic_DNA.
DR EMBL; BX284602; CAA91353.1; -; Genomic_DNA.
DR PIR; A49073; A49073.
DR PIR; E88280; E88280.
DR RefSeq; NP_001022288.1; NM_001027117.4. [Q22024-1]
DR RefSeq; NP_496149.3; NM_063748.4.
DR AlphaFoldDB; Q22024; -.
DR IntAct; Q22024; 33.
DR STRING; 6239.R53.3a; -.
DR EPD; Q22024; -.
DR PaxDb; Q22024; -.
DR PeptideAtlas; Q22024; -.
DR EnsemblMetazoa; R53.3a.1; R53.3a.1; WBGene00001207. [Q22024-1]
DR EnsemblMetazoa; R53.3b.1; R53.3b.1; WBGene00001207. [Q22024-2]
DR EnsemblMetazoa; R53.3b.2; R53.3b.2; WBGene00001207. [Q22024-2]
DR GeneID; 174552; -.
DR KEGG; cel:CELE_R53.3; -.
DR UCSC; R53.3a; c. elegans.
DR CTD; 174552; -.
DR WormBase; R53.3a; CE03572; WBGene00001207; egl-43.
DR WormBase; R53.3b; CE03573; WBGene00001207; egl-43.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157208; -.
DR HOGENOM; CLU_863905_0_0_1; -.
DR InParanoid; Q22024; -.
DR OMA; HCSLKPF; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q22024; -.
DR Reactome; R-CEL-3214841; PKMTs methylate histone lysines.
DR Reactome; R-CEL-8943724; Regulation of PTEN gene transcription.
DR SignaLink; Q22024; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00001207; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q22024; baseline.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0042659; P:regulation of cell fate specification; IMP:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:WormBase.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR SMART; SM00355; ZnF_C2H2; 5.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Metal-binding; Neurogenesis;
KW Nucleus; Reference proteome; Repeat; Transcription; Zinc; Zinc-finger.
FT CHAIN 1..543
FT /note="Zinc finger protein egl-43"
FT /id="PRO_0000451575"
FT ZN_FING 159..181
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 187..209
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 213..233
FT /note="C2H2-type 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 444..466
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 472..495
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 2..62
FT /note="Positive regulatory (PR) domain"
FT /evidence="ECO:0000305|PubMed:32203506"
FT REGION 299..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..363
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..530
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..221
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_060814"
SQ SEQUENCE 543 AA; 59357 MW; E3A287994095DA82 CRC64;
MSIDTDFLTS VEVKEDELHG NVLIAVTQIA LGRTIGVIDK ATPNDSNALL ILNLIKEADD
GEDANICMRQ EDRKTFLQTS KIINIGERLL LQRLSEEECD EEDQDDLENL ILLKDEDRPD
STQSCTKSSS EDSNLNGFEE YIREHGELVP GQTPPDGSHK CGVCPKSFSS ASGLKQHSHI
HCSLKPFRCH LCPKSYTQFS NLCRHRRVHS DGWTCPTCQS QMPSQAALTK HRPVCEMTAL
YKPLMAQLAG LSGAGGLGSV PYWPHILQMA TQAPHFPLAF LAANPEAYKL MQQTTCASPD
AECSSGHASE SSPTTTEPVD LTATPKPPST SEMETTSKSD DGEDRDSIGD SGNDDDDDSE
AGVLDESSTT TSTKKRPTSH TISDILAAPQ LGAQALNSTF LGMLQRSLNY NPAVPSPHSF
LRAMSGAKAS SSPSSSSGSG KDRYTCKFCQ KVFPRSANLT RHLRTHTGEQ PYKCQYCERS
FSISSNLQRH VRNIHNKPNT SLTPHNHHRQ RSLHNSTSTS TTTTTVHHPL LHLPGTSVPV
PKV
