CEH60_CAEEL
ID CEH60_CAEEL Reviewed; 360 AA.
AC Q45EK2;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Homeobox protein ceh-60 {ECO:0000305};
GN Name=ceh-60 {ECO:0000312|WormBase:F22A3.5};
GN ORFNames=F22A3.5 {ECO:0000312|WormBase:F22A3.5};
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, INTERACTION WITH UNC-62; PQM-1, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=30956009; DOI=10.1016/j.devcel.2019.03.002;
RA Dowen R.H.;
RT "CEH-60/PBX and UNC-62/MEIS Coordinate a Metabolic Switch that Supports
RT Reproduction in C. elegans.";
RL Dev. Cell 49:235-250.e7(2019).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH UNC-62, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP 241-GLN--GLY-360.
RX PubMed=31675356; DOI=10.1371/journal.pbio.3000499;
RA Van de Walle P., Geens E., Baggerman G., Jose Naranjo-Galindo F.,
RA Askjaer P., Schoofs L., Temmerman L.;
RT "CEH-60/PBX regulates vitellogenesis and cuticle permeability through
RT intestinal interaction with UNC-62/MEIS in Caenorhabditis elegans.";
RL PLoS Biol. 17:e3000499-e3000499(2019).
CC -!- FUNCTION: Probable transcription regulator which binds to DNA,
CC repressing genes involved in longevity and stress, while activating
CC genes involved in reproduction, such as the vitellogenins
CC (PubMed:30956009, PubMed:31675356). Associates with homeobox unc-62 to
CC regulate gene expression, including repression of genes involved in
CC innate immunity (PubMed:30956009, PubMed:31675356). Required for
CC intestinal expression of vitellogenin genes (PubMed:30956009,
CC PubMed:31675356). Negatively modulates longevity, probably
CC independently of effects on vitellogenesis (PubMed:30956009). Involved
CC in lipid homeostasis, contributing to the reallocation of intestinal
CC lipids to the germline and to the formation of the cuticle
CC (PubMed:30956009, PubMed:31675356). Associates with transcriptional
CC regulator pqm-1 at the daf-16 associated element within the promoters
CC of stress-responsive genes to regulate expression (PubMed:30956009).
CC {ECO:0000269|PubMed:30956009, ECO:0000269|PubMed:31675356}.
CC -!- SUBUNIT: Forms a heterodimer with homeobox unc-62 (PubMed:30956009,
CC PubMed:31675356). Interacts with pqm-1 (PubMed:30956009).
CC {ECO:0000269|PubMed:30956009, ECO:0000269|PubMed:31675356}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000269|PubMed:30956009}. Note=Localizes to the nucleus in an unc-
CC 62-dependent manner. {ECO:0000269|PubMed:30956009}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the intestine at the L4 larval stage
CC and persists into adulthood (PubMed:30956009, PubMed:31675356).
CC Expressed in sensory AWC neurons, pharyngeal muscle cells pm6, and
CC intestine, in the adult (PubMed:30956009, PubMed:31675356).
CC {ECO:0000269|PubMed:30956009, ECO:0000269|PubMed:31675356}.
CC -!- DISRUPTION PHENOTYPE: RNAi mediated knockdown targeted to the intestine
CC represses expression of vitellogenin genes.
CC {ECO:0000269|PubMed:30956009}.
CC -!- SIMILARITY: Belongs to the TALE/PBX homeobox family. {ECO:0000305}.
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DR EMBL; BX284606; CCD64582.2; -; Genomic_DNA.
DR RefSeq; NP_509101.4; NM_076700.4.
DR AlphaFoldDB; Q45EK2; -.
DR SMR; Q45EK2; -.
DR IntAct; Q45EK2; 2.
DR STRING; 6239.F22A3.5; -.
DR PaxDb; Q45EK2; -.
DR PeptideAtlas; Q45EK2; -.
DR EnsemblMetazoa; F22A3.5.1; F22A3.5.1; WBGene00017690.
DR GeneID; 184803; -.
DR KEGG; cel:CELE_F22A3.5; -.
DR UCSC; F22A3.5; c. elegans.
DR CTD; 184803; -.
DR WormBase; F22A3.5; CE47258; WBGene00017690; ceh-60.
DR eggNOG; KOG0774; Eukaryota.
DR GeneTree; ENSGT00940000169683; -.
DR HOGENOM; CLU_769949_0_0_1; -.
DR InParanoid; Q45EK2; -.
DR OMA; AKQCNIK; -.
DR OrthoDB; 804740at2759; -.
DR PhylomeDB; Q45EK2; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00017690; Expressed in material anatomical entity and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IGI:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR008422; Homeobox_KN_domain.
DR Pfam; PF05920; Homeobox_KN; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS51978; PBC; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Homeobox; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..360
FT /note="Homeobox protein ceh-60"
FT /id="PRO_0000452276"
FT DOMAIN 1..179
FT /note="PBC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322"
FT DNA_BIND 180..242
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..82
FT /note="PBC-A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322"
FT REGION 85..179
FT /note="PBC-B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01322"
FT MUTAGEN 241..360
FT /note="Missing: In lst466; increased accumulation of
FT intestinal fat in adults. Significant reduction in cuticle
FT permeability."
FT /evidence="ECO:0000269|PubMed:31675356"
SQ SEQUENCE 360 AA; 41778 MW; 92758E5D370E6DEC CRC64;
MDNLIKQLQM SVSSENVDRN FIEKCIEMNP CRRMLHEVLL ERKDILRSRM NLVALYDTDE
QSSEIEEILA QFENPTFPLE EVNTEKDEEW QPLERKYLDG INRIKEDTIM KQIQLDKDME
KALTNSEEVL RNHRDFRPID EKDFSNIRQS ISKRFEHSKN NIRGEAATKI LVLRREIEQQ
GRKRRNFDKN TTDILQNWFH DHRQNPYPSD QEKAELAKQC NIKISQVNNW FGNQRIRTKQ
QALRMQEDER ERAASMANEA QAIQNSLNSS TVASSSNMST SGLINIPLVN PTMQSMVIPA
VQPGLLGNPN AFLHQPHYFT AGGQMSLNDN GNGQQFFTDY ETFGLAQSDT ESFNQMGYLG
