BED3_CAEEL
ID BED3_CAEEL Reviewed; 599 AA.
AC Q19787;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Zinc finger BED domain-containing protein 3 {ECO:0000305};
GN Name=bed-3 {ECO:0000312|WormBase:F25H8.6};
GN ORFNames=F25H8.6 {ECO:0000312|WormBase:F25H8.6};
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|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 [2] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20005870; DOI=10.1016/j.ydbio.2009.12.005;
RA Inoue T., Sternberg P.W.;
RT "C. elegans BED domain transcription factor BED-3 controls lineage-specific
RT cell proliferation during organogenesis.";
RL Dev. Biol. 338:226-236(2010).
RN [3] {ECO:0000305}
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 371-GLN--VAL-599.
RX PubMed=24885717; DOI=10.1186/1471-213x-14-17;
RA Liu W.J., Reece-Hoyes J.S., Walhout A.J., Eisenmann D.M.;
RT "Multiple transcription factors directly regulate Hox gene lin-39
RT expression in ventral hypodermal cells of the C. elegans embryo and larva,
RT including the hypodermal fate regulators LIN-26 and ELT-6.";
RL BMC Dev. Biol. 14:17-17(2014).
CC -!- FUNCTION: Probable transcription factor (PubMed:20005870,
CC PubMed:24885717). Involved in vulval organogenesis (PubMed:20005870,
CC PubMed:24885717). During vulval development, may play a role in the
CC regulation of cell cycle regulators such as cul-1 (PubMed:20005870).
CC Positively modulates expression of homeobox protein lin-39, perhaps by
CC binding to regulatory regions of the lin-39 gene, acting in the vulval
CC lineage (PubMed:24885717). Plays a role in larval molting
CC (PubMed:20005870). {ECO:0000269|PubMed:20005870,
CC ECO:0000269|PubMed:24885717}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in neuronal cell bodies in the ventral
CC cord and HSN neurons. {ECO:0000269|PubMed:20005870}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the lateral hypodermal (seam) cells
CC and occasionally in the hyp7 hypodermal cell during the larval stages
CC of development with increased expression during the molting phase
CC between the L3 and L4 stages of larval development. Also expressed in
CC the vulval precursor cell desecendents of P5.p, P6.p and P7.p cells.
CC {ECO:0000269|PubMed:20005870}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in an egg-laying
CC defect and vulval cell-lineage defects including failed division of
CC vulval precursor cell descendents (PubMed:20005870). RNAi-mediated
CC knockdown causes a decrease in expression of lin-39 at the larval L3
CC stage (PubMed:24885717). Knockdown in L1 stage larvae, in a lin-39
CC mutant background, causes abnormal fusion of vulval precursor cells at
CC larval stage L2 (PubMed:24885717). {ECO:0000269|PubMed:20005870,
CC ECO:0000269|PubMed:24885717}.
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DR EMBL; BX284604; CAA93282.1; -; Genomic_DNA.
DR PIR; T21366; T21366.
DR RefSeq; NP_501785.1; NM_069384.3.
DR AlphaFoldDB; Q19787; -.
DR STRING; 6239.F25H8.6; -.
DR EPD; Q19787; -.
DR PaxDb; Q19787; -.
DR EnsemblMetazoa; F25H8.6.1; F25H8.6.1; WBGene00009133.
DR GeneID; 184940; -.
DR KEGG; cel:CELE_F25H8.6; -.
DR UCSC; F25H8.6; c. elegans.
DR CTD; 184940; -.
DR WormBase; F25H8.6; CE05731; WBGene00009133; bed-3.
DR eggNOG; KOG1121; Eukaryota.
DR HOGENOM; CLU_447081_0_0_1; -.
DR InParanoid; Q19787; -.
DR OMA; ERIHEEH; -.
DR OrthoDB; 223749at2759; -.
DR PRO; PR:Q19787; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00009133; Expressed in pharyngeal muscle cell (C elegans) and 10 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0018996; P:molting cycle, collagen and cuticulin-based cuticle; IMP:WormBase.
DR GO; GO:0051302; P:regulation of cell division; IMP:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0072327; P:vulval cell fate specification; IMP:WormBase.
DR InterPro; IPR003656; Znf_BED.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR Pfam; PF02892; zf-BED; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50808; ZF_BED; 1.
PE 1: Evidence at protein level;
KW Developmental protein; Metal-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..599
FT /note="Zinc finger BED domain-containing protein 3"
FT /evidence="ECO:0000305"
FT /id="PRO_0000436480"
FT ZN_FING 123..176
FT /note="BED-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT REGION 70..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..481
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00027"
FT MUTAGEN 371..599
FT /note="Missing: In sy702; causes decrease in lin-39
FT expression in L3 larvae."
FT /evidence="ECO:0000269|PubMed:24885717"
SQ SEQUENCE 599 AA; 66207 MW; 549C15FB95158CC7 CRC64;
MQTQSPFGPL LGISSSLLPS PVTVAAAAAA ANGHQGPVSL TTFPSAFAAF ASQIRNNQLQ
SLLQSQIQAL NGGMGSPGNG PGTPLSRNNY AHHHQQHQNQ QHVGKIRGTT EYPLRKRVGG
STVKTAKVWR YFDELPTIEQ AAECRICRKK IKATNSSTTG MIRHLRSCHV QEYQLVQEAR
QNSMIVKMEE KARAKLLREM NEKVITNGIE NTPIVKKESQ TESQKSPSAS SSASDTASSA
SSSHFSTNPL IGLPAPVAIK PPAPPTPSNS ILNLSQSQNQ CQNQNPMFQS QNIKNEPTDV
EEEDLEQKRS RDILHRPSDL GTKMFFSSPR TFNLTSAFSS ITPLEDHKFQ KKIEDDHKIH
MQIALMLLLD QQPCQIIDRP GIRSLFKFVL PEYHMPSGDV FQATIVPQLL NQMKQQIEAL
VHNSSSLSSI PDQVMTSSSA TSSYEDVSVN ESQMAGPNVG DEEEEIMEEE VEEDENVEIE
DDTSSASSSI DTDTCDAMAS FIHFIGNDAF PHDELISLLS VVTNLFTYFS TRPHVQTHLQ
MTIIQPTSQP LVQQVQFVTS NLSIISDYIR QTPDMQLLPL AVNQEAMLEK LVDHIDQLV
