ID   MEF2D_XENLA             Reviewed;         498 AA.
AC   Q03413;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Myocyte-specific enhancer factor 2D homolog;
DE   AltName: Full=Serum response factor-like protein 1;
DE            Short=SL-1;
GN   Name=mef2d; Synonyms=sl1;
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].
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   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).
CC   -!- FUNCTION: May regulate muscle-specific transcription in the embryo and
CC       may regulate transcription of a variety of cell types in the adult. It
CC       binds to the sequence 5'-CTA[TA]4TAR-3'.
CC   -!- SUBUNIT: Binds DNA as a multimer, probably as a dimer. Interacts with
CC       hdac9. {ECO:0000269|PubMed:10487760}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Restricted to the somitic mesoderm of early embryos
CC       and to the body muscle (myotomes) of the tadpole. Expressed in all
CC       tissues examined in the adult.
CC   -!- DEVELOPMENTAL STAGE: Expression begins in the late gastrula.
CC   -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
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DR   EMBL; Z19124; CAA79531.1; -; mRNA.
DR   PIR; S28059; S28059.
DR   RefSeq; NP_001095265.1; NM_001101795.1.
DR   AlphaFoldDB; Q03413; -.
DR   SMR; Q03413; -.
DR   BioGRID; 100665; 1.
DR   GeneID; 399340; -.
DR   KEGG; xla:399340; -.
DR   CTD; 399340; -.
DR   Xenbase; XB-GENE-6254040; mef2d.S.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 399340; Expressed in muscle tissue and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:InterPro.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:InterPro.
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; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..498
FT                   /note="Myocyte-specific enhancer factor 2D homolog"
FT                   /id="PRO_0000199437"
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          173..215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          243..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          411..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..457
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   498 AA;  54071 MW;  9E98D13D80AAF510 CRC64;
     MGRKKIQIQR ITDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNH SNKLFQYAST
     DMDKVLLKYT EYNEPHESRT NADIIETLRK KGFNGCDSPE PDGDDSIDQS PLMEDKYRKS
     SEDLDILFKR YGSAVPAPNF AMPVTVPVTN QNALHFSNPG GSLITQSLMT SSLTDPRLLS
     PPQPSLQRNT VSPGLPQRPA SAGAMLGGEL NNSNGTCPSP VGNGYISARA SPGLLPVSNG
     NSLGKVIQAK SPPSPNQNSQ LGANSRKPDL RVITSQGGKG LMHHLTEEQL EMSVQRLGGV
     SQATHSLTTP VVSVATPSLL SHHGLPFSAM STAYNTDYQL TSADLASLST FSSPGSLSLG
     NVTAWQHQQQ QQQQHNQPQQ LIPVSLSNLV SSSHLPHTAT LTVNTNPINI SIKREPASPN
     RERSTGTPLS CFSHQSRHEA TGRSPVDSLS SNASSFEGND REDPRGDYTS SLGLLRPSGD
     TESESQSVKR MRLDAWVT