MEF2A_CHICK
ID MEF2A_CHICK Reviewed; 499 AA.
AC Q9W6U8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Myocyte-specific enhancer factor 2A;
GN Name=MEF2A;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE EXPRESSION.
RC TISSUE=Embryonic heart;
RX PubMed=10370120; DOI=10.1007/s004270050267;
RA Buchberger A., Arnold H.-H.;
RT "The MADS domain containing transcription factor cMef2a is expressed in
RT heart and skeletal muscle during embryonic chick development.";
RL Dev. Genes Evol. 209:376-381(1999).
CC -!- FUNCTION: Transcriptional activator which binds specifically to the
CC MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific
CC genes. Mediates cellular functions in skeletal and cardiac muscle
CC development,.
CC -!- SUBUNIT: Binds DNA as a homo- or heterodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251}.
CC -!- TISSUE SPECIFICITY: Expressed in both embryonic and adult tissues with
CC high expression in heart and skeletal muscle. Also expressed in gut,
CC lung and brain of E15 embryos and adults.
CC -!- DEVELOPMENTAL STAGE: First expressed in stage 8 embryos in the
CC precardiac region and the expression continues during the development
CC of the cardiac tube. Later expression in the atrium and ventricle. From
CC stage 13, expressed in somites. Expression here is limited to the
CC myotome and is not found in newly formed somites until the muscle-
CC specific transcription factors MyoD and myogenin are present.
CC {ECO:0000269|PubMed:10370120}.
CC -!- PTM: Sumoylation on Lys-402 is enhanced by PIAS1 and represses
CC transcriptional activity. Has no effect on nuclear location nor on DNA
CC binding. Sumoylated by SUMO1 and, to a lesser extent by SUMO2 and SUMO3
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Acetylation on Lys-402 activates transcriptional activity.
CC {ECO:0000250}.
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DR EMBL; AJ010072; CAB43712.1; -; mRNA.
DR AlphaFoldDB; Q9W6U8; -.
DR SMR; Q9W6U8; -.
DR STRING; 9031.ENSGALP00000011486; -.
DR PaxDb; Q9W6U8; -.
DR VEuPathDB; HostDB:geneid_395670; -.
DR eggNOG; KOG0014; Eukaryota.
DR InParanoid; Q9W6U8; -.
DR OrthoDB; 729387at2759; -.
DR PhylomeDB; Q9W6U8; -.
DR PRO; PR:Q9W6U8; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; 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; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; Activator; Apoptosis; Developmental protein; Differentiation;
KW DNA-binding; Isopeptide bond; Neurogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..499
FT /note="Myocyte-specific enhancer factor 2A"
FT /id="PRO_0000366971"
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 173..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..282
FT /note="Required for interaction with MAPKs"
FT /evidence="ECO:0000250"
FT REGION 288..295
FT /note="Beta domain"
FT /evidence="ECO:0000250"
FT REGION 380..499
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..439
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 117
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 248
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 253
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 281
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 402
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 402
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 499 AA; 53669 MW; 157AAEF450A67A09 CRC64;
MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST
DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCESPD ADDYFEHSPL SEDRFSKLNE
DSDFIFKRGP PGLPAQNFSM SVTVPVSNPN TLTYSNPGSS LVSPSLAASS SLTSTTMLSP
PQTTLHRNVS PGAPQRPPST GNAGGILGTT DLTVPNGAGT SPVGNGVWNS RASPSLLGTA
GGGNGLGKVM PTKSPPPPGG GGLGMNNRKP DLRVVIPPSS KGMMPPLTEE DELELNTQRI
SSSQSTQPLA TPVVSVTTPS FPPAGLVYSA MPTAYNTDYS LTSADLSAFE GFNSPGMLSL
GQVSPWQQHH LGPATLSSLV SGSQLSQGSN LSINTNQNIN IKSEPISPPR DRVNSSGFPQ
QQPPQQPQPP QPPQQPPQRQ EMGRSPVDSL SSSSSSYDGS DREDPRSDFH SPVVLGRPPN
SEDRESPSVK RMRMDTWVT
