MEF2_CAEEL
ID MEF2_CAEEL Reviewed; 340 AA.
AC Q9U325; G5EGT3;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=MEF2 transcription factor homolog {ECO:0000312|WormBase:W10D5.1};
GN Name=mef-2 {ECO:0000312|WormBase:W10D5.1};
GN Synonyms=CeMef-2 {ECO:0000303|PubMed:10882527};
GN ORFNames=W10D5.1 {ECO:0000312|WormBase:W10D5.1};
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:AAA79336.1, ECO:0000312|EMBL:AAA79337.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=10882527; DOI=10.1006/dbio.2000.9758;
RA Dichoso D., Brodigan T., Chwoe K.Y., Lee J.S., Llacer R., Park M.,
RA Corsi A.K., Kostas S.A., Fire A., Ahnn J., Krause M.;
RT "The MADS-Box factor CeMEF2 is not essential for Caenorhabditis elegans
RT myogenesis and development.";
RL Dev. Biol. 223:431-440(2000).
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 INTERACTION WITH HDA-4.
RX PubMed=12054517; DOI=10.1016/s0006-291x(02)00374-1;
RA Choi K.Y., Ji Y.J., Jee C., Kim do H., Ahnn J.;
RT "Characterization of CeHDA-7, a class II histone deacetylase interacting
RT with MEF-2 in Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 293:1295-1300(2002).
RN [4] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF THR-20 AND LEU-38.
RX PubMed=17170704; DOI=10.1038/sj.emboj.7601479;
RA van der Linden A.M., Nolan K.M., Sengupta P.;
RT "KIN-29 SIK regulates chemoreceptor gene expression via an MEF2
RT transcription factor and a class II HDAC.";
RL EMBO J. 26:358-370(2007).
RN [5]
RP FUNCTION, AND INDUCTION BY MIR-1.
RX PubMed=18510933; DOI=10.1016/j.cell.2008.04.035;
RA Simon D.J., Madison J.M., Conery A.L., Thompson-Peer K.L., Soskis M.,
RA Ruvkun G.B., Kaplan J.M., Kim J.K.;
RT "The microRNA miR-1 regulates a MEF-2-dependent retrograde signal at
RT neuromuscular junctions.";
RL Cell 133:903-915(2008).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=18832350; DOI=10.1534/genetics.108.094771;
RA van der Linden A.M., Wiener S., You Y.J., Kim K., Avery L., Sengupta P.;
RT "The EGL-4 PKG acts with KIN-29 salt-inducible kinase and protein kinase A
RT to regulate chemoreceptor gene expression and sensory behaviors in
RT Caenorhabditis elegans.";
RL Genetics 180:1475-1491(2008).
RN [7] {ECO:0000305}
RP FUNCTION, AND INDUCTION.
RX PubMed=27487365; DOI=10.1371/journal.pgen.1006237;
RA Gruner M., Grubbs J., McDonagh A., Valdes D., Winbush A.,
RA van der Linden A.M.;
RT "Cell-Autonomous and Non-Cell-Autonomous Regulation of a Feeding State-
RT Dependent Chemoreceptor Gene via MEF-2 and bHLH Transcription Factors.";
RL PLoS Genet. 12:E1006237-E1006237(2016).
CC -!- FUNCTION: Transcription regulator (PubMed:17170704, PubMed:27487365).
CC Binds specifically to the MEF2 element, 5'-
CC [TC]TA[AT][AT][AT][AT]TA[AG]-3' in the regulatory elements of target
CC genes, such as chemoreceptors str-1 and srh-234 (PubMed:10882527,
CC PubMed:17170704, PubMed:27487365). Involved in transduction of sensory
CC signals, together with egl-4, kin-29 and hda-4; binding to histone
CC deacetylase hda-4 enables negative modulation of chemoreceptor gene
CC expression in chemosensory neurons (PubMed:17170704, PubMed:18832350).
CC In response to starvation, negatively modulates expression of
CC chemoreceptor srh-234 in ADL sensory neurons, acting in concert with
CC basic helix-loop-helix (bHLH) transcription factors (PubMed:27487365).
CC Plays a role in regulating muscle sensitivity to acetylcholine (ACh)
CC and the magnitude of presynaptic ACh release via a retrograde signal,
CC perhaps by indirectly decreasing Ras-related protein Rab-3 activity
CC (PubMed:18510933). {ECO:0000269|PubMed:10882527,
CC ECO:0000269|PubMed:17170704, ECO:0000269|PubMed:18510933,
CC ECO:0000269|PubMed:18832350, ECO:0000269|PubMed:27487365}.
CC -!- SUBUNIT: Interacts with histone deacetylase hda-4 isoform b.
CC {ECO:0000269|PubMed:12054517}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
CC -!- DEVELOPMENTAL STAGE: Expressed broadly throughout most of development.
CC {ECO:0000269|PubMed:10882527}.
CC -!- INDUCTION: Down-regulated by microRNA mir-1 (PubMed:18510933). Up-
CC regulated in many head neurons during prolonged starvation
CC (PubMed:27487365). {ECO:0000269|PubMed:18510933,
CC ECO:0000269|PubMed:27487365}.
CC -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
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DR EMBL; U36198; AAA79336.1; -; mRNA.
DR EMBL; U36199; AAA79337.1; -; Genomic_DNA.
DR EMBL; BX284601; CAB61037.1; -; Genomic_DNA.
DR RefSeq; NP_492441.1; NM_060040.5.
DR AlphaFoldDB; Q9U325; -.
DR SMR; Q9U325; -.
DR STRING; 6239.W10D5.1; -.
DR EPD; Q9U325; -.
DR PaxDb; Q9U325; -.
DR EnsemblMetazoa; W10D5.1.1; W10D5.1.1; WBGene00003182.
DR GeneID; 172732; -.
DR KEGG; cel:CELE_W10D5.1; -.
DR CTD; 172732; -.
DR WormBase; W10D5.1; CE25156; WBGene00003182; mef-2.
DR eggNOG; KOG0014; Eukaryota.
DR GeneTree; ENSGT00940000169350; -.
DR HOGENOM; CLU_855856_0_0_1; -.
DR InParanoid; Q9U325; -.
DR OMA; DCELVAP; -.
DR OrthoDB; 1238285at2759; -.
DR Reactome; R-CEL-525793; Myogenesis.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003182; Expressed in larva and 3 other tissues.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IMP:UniProtKB.
DR GO; GO:0014056; P:regulation of acetylcholine secretion, neurotransmission; IGI:WormBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IMP:UniProtKB.
DR CDD; cd00265; MADS_MEF2_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR033896; MADS_MEF2-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF00319; SRF-TF; 1.
DR PRINTS; PR00404; MADSDOMAIN.
DR SMART; SM00432; MADS; 1.
DR SUPFAM; SSF55455; SSF55455; 1.
DR PROSITE; PS00350; MADS_BOX_1; 1.
DR PROSITE; PS50066; MADS_BOX_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..340
FT /note="MEF2 transcription factor homolog"
FT /id="PRO_0000453925"
FT DOMAIN 1..61
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT REGION 90..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 20
FT /note="T->I: In oy65; Suppresses several phenotypes in a
FT Ser/Thr kinase kin-29 mutant background; dauer pheromone
FT hypersensitivity, reduced chemoreceptor gene expression and
FT also decreased body length."
FT /evidence="ECO:0000269|PubMed:17170704"
FT MUTAGEN 38
FT /note="L->F: In oy63; Suppresses several phenotypes in a
FT Ser/Thr kinase kin-29 mutant background; dauer pheromone
FT hypersensitivity, reduced chemoreceptor gene expression and
FT also decreased body length."
FT /evidence="ECO:0000269|PubMed:17170704"
FT CONFLICT 216
FT /note="F -> I (in Ref. 1; AAA79336/AAA79337)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="C -> G (in Ref. 1; AAA79336/AAA79337)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 340 AA; 36460 MW; 1B0DC4CE7165BAC6 CRC64;
MGRKKIQITR IQDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIVFNS TNKLFQYAST
DMDKVLLKYT EYNEPHESRT NNDIMEALNR KEGNQGGGNS DDESPGPSTS PVIQITMPAV
VNGHSSNNSV ASAASASAAA VAAAAAAVAA VEGTSSGAAA AAAALQASNA QRHHNLNLYQ
NLIFNPNYTR HLNQRNDPLS STSVAPSSSS SKHLDFPPST SFAYDTSRLH PIAAADADCD
LVPSSRAAAD QNIWSSALQQ RPVSQPAPSI SNSSTNGISN GTSSLLSPNV SSLNGHSVLD
LGGPNLPYKL DPNTYVKMEP HSPPEKRPRI TTEWRPQQLT
