MEF2A_XENLA
ID MEF2A_XENLA Reviewed; 516 AA.
AC Q03414; Q7ZX04; Q9PSD9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Myocyte-specific enhancer factor 2A homolog;
DE Short=XMEF2A1;
DE Short=xMEF2A;
DE AltName: Full=Serum response factor-like protein 2;
DE Short=SL-2;
GN Name=mef2a; Synonyms=sl2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Neurula;
RX PubMed=1281451; DOI=10.1002/j.1460-2075.1992.tb05605.x;
RA Chambers A.E., Kotecha S., Towers N., Mohun T.J.;
RT "Muscle-specific expression of SRF-related genes in the early embryo of
RT Xenopus laevis.";
RL EMBO J. 11:4981-4991(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DNA-BINDING, AND TISSUE SPECIFICITY.
RC TISSUE=Tail bud;
RX PubMed=7813786; DOI=10.1006/dbio.1994.1347;
RA Wong M.-W., Pisegna M., Lu M.-F., Leibham D., Perry M.;
RT "Activation of Xenopus MyoD transcription by members of the MEF2 protein
RT family.";
RL Dev. Biol. 166:683-695(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tail bud;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH HDAC9.
RX PubMed=10487760; DOI=10.1093/emboj/18.18.5085;
RA Sparrow D.B., Miska E.A., Langley E., Reynaud-Deonauth S., Kotecha S.,
RA Towers N., Spohr G., Kouzarides T., Mohun T.J.;
RT "MEF-2 function is modified by a novel co-repressor, MITR.";
RL EMBO J. 18:5085-5098(1999).
RN [5]
RP FUNCTION, INTERACTION WITH NLK2, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP PHOSPHORYLATION AT THR-343 AND SER-386 BY NLK2, AND MUTAGENESIS OF THR-343;
RP THR-350; SER-386 AND SER-439.
RX PubMed=17785444; DOI=10.1128/mcb.01481-07;
RA Satoh K., Ohnishi J., Sato A., Takeyama M., Iemura S., Natsume T.,
RA Shibuya H.;
RT "Nemo-like kinase-myocyte enhancer factor 2A signaling regulates anterior
RT formation in Xenopus development.";
RL Mol. Cell. Biol. 27:7623-7630(2007).
CC -!- FUNCTION: May regulate muscle-specific transcription in the embryo and
CC may regulate transcription of a variety of cell types in the adult.
CC Binds to the sequence 5'-CTA[TA]4TAR-3'. Acts downstream of nlk2 in
CC anterior neural development, including eye formation.
CC {ECO:0000269|PubMed:17785444, ECO:0000269|PubMed:7813786}.
CC -!- SUBUNIT: Interacts with hdac9 and nlk2. {ECO:0000269|PubMed:10487760,
CC ECO:0000269|PubMed:17785444}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Restricted to the somitic mesoderm of early
CC embryos. Expressed in the head region of neurula stage embryos and in
CC body muscle (myotomes) of the tadpole. Expressed in all tissues
CC examined in the adult. {ECO:0000269|PubMed:1281451,
CC ECO:0000269|PubMed:17785444, ECO:0000269|PubMed:7813786}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Zygotic
CC expression begins after the neurula stage. {ECO:0000269|PubMed:1281451,
CC ECO:0000269|PubMed:17785444}.
CC -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA79530.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z19123; CAA79530.1; ALT_FRAME; mRNA.
DR EMBL; BC046368; AAH46368.1; -; mRNA.
DR PIR; S28060; S28060.
DR RefSeq; NP_001095216.1; NM_001101746.1.
DR AlphaFoldDB; Q03414; -.
DR SMR; Q03414; -.
DR iPTMnet; Q03414; -.
DR MaxQB; Q03414; -.
DR DNASU; 380452; -.
DR GeneID; 380452; -.
DR KEGG; xla:380452; -.
DR CTD; 380452; -.
DR Xenbase; XB-GENE-487398; mef2a.L.
DR OrthoDB; 729387at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 380452; Expressed in heart and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IC:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR CDD; cd00265; MADS_MEF2_like; 1.
DR Gene3D; 3.40.1810.10; -; 1.
DR InterPro; IPR022102; HJURP_C.
DR InterPro; IPR033896; MADS_MEF2-like.
DR InterPro; IPR002100; TF_MADSbox.
DR InterPro; IPR036879; TF_MADSbox_sf.
DR Pfam; PF12347; HJURP_C; 1.
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 Activator; Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..516
FT /note="Myocyte-specific enhancer factor 2A homolog"
FT /id="PRO_0000199430"
FT DOMAIN 3..57
FT /note="MADS-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT DNA_BIND 58..86
FT /note="Mef2-type"
FT /evidence="ECO:0000255"
FT REGION 1..100
FT /note="Interaction with hdac9"
FT REGION 318..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 343
FT /note="Phosphothreonine; by NLK"
FT /evidence="ECO:0000269|PubMed:17785444"
FT MOD_RES 386
FT /note="Phosphoserine; by NLK"
FT /evidence="ECO:0000269|PubMed:17785444"
FT MUTAGEN 343
FT /note="T->A: Significantly reduces phosphorylation by NLK.
FT Further reduces phosphorylation by NLK; when associated
FT with A-386."
FT /evidence="ECO:0000269|PubMed:17785444"
FT MUTAGEN 350
FT /note="T->A: No effect on phosphorylation by NLK."
FT /evidence="ECO:0000269|PubMed:17785444"
FT MUTAGEN 386
FT /note="S->A: Significantly reduces phosphorylation by NLK.
FT Further reduces phosphorylation by NLK; when associated
FT with A-343."
FT /evidence="ECO:0000269|PubMed:17785444"
FT MUTAGEN 439
FT /note="S->A: No effect on phosphorylation by NLK."
FT /evidence="ECO:0000269|PubMed:17785444"
FT CONFLICT 4
FT /note="K -> R (in Ref. 1; CAA79530)"
FT /evidence="ECO:0000305"
FT CONFLICT 9
FT /note="T -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="E -> D (in Ref. 1; CAA79530)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="R -> K (in Ref. 1; CAA79530)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="T -> I (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="P -> T (in Ref. 3; AAH46368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 516 AA; 56346 MW; 49932BF25747A12E CRC64;
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST
DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCESPD DQRYFEEETF SKLIEDSDFV
FKRDPALNKK ENRGCDSPDP DGSYVLTPHT EEKYKKINEE FDNMMRSHKI SPGLPQQTFP
MSVTVPVSNP NTLPYSSPGN TMVTASLAAS ASLTDARMLS PPPTTLHRNV VSPGLPQRPP
STGNAGVMLC SSDLSVPNGA GTSPVGNGFV NPRASPSHLG PTGGNVLGKV MPTKSPPPPG
GNLVMNSRKP DLRVVIPPSS KGMMPPLNTQ RVTSSQGTQP LATPIVSVAT PSLAPQGLIY
SAMPTAYNTD YPLTSADLSM LQGFNSPGIL PLGQVSAWQQ HHVGQAALSS FVATGQLSQG
SNLSINTNQN INIKSEPISP PRDRITPSGF QSHQHHQHQP RPEMDSLSSS SSSYDGSDRE
DVRNDFHSPI GLGRPANNED RDSPSVKRMR MDAWVT
