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Database: UniProt
Entry: A0A2K6G408_PROCO
LinkDB: A0A2K6G408_PROCO
Original site: A0A2K6G408_PROCO 
ID   A0A2K6G408_PROCO        Unreviewed;       487 AA.
AC   A0A2K6G408;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Myocyte enhancer factor 2A {ECO:0000313|Ensembl:ENSPCOP00000020964.1};
GN   Name=MEF2A {ECO:0000313|Ensembl:ENSPCOP00000020964.1};
OS   Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS   coquereli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Indriidae; Propithecus.
OX   NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000020964.1, ECO:0000313|Proteomes:UP000233160};
RN   [1] {ECO:0000313|Ensembl:ENSPCOP00000020964.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_012499226.1; XM_012643772.1.
DR   AlphaFoldDB; A0A2K6G408; -.
DR   Ensembl; ENSPCOT00000031621.1; ENSPCOP00000020964.1; ENSPCOG00000022460.1.
DR   GeneID; 105809879; -.
DR   CTD; 4205; -.
DR   GeneTree; ENSGT00940000156205; -.
DR   OMA; MNTQRIS; -.
DR   OrthoDB; 448298at2759; -.
DR   Proteomes; UP000233160; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:UniProt.
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:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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; Transcription factor, MADS-box; 1.
DR   InterPro; IPR022102; HJURP_C.
DR   InterPro; IPR033896; MADS_MEF2-like.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   PANTHER; PTHR48019:SF109; MYOCYTE-SPECIFIC ENHANCER FACTOR 2A; 1.
DR   PANTHER; PTHR48019; SERUM RESPONSE FACTOR HOMOLOG; 1.
DR   Pfam; PF12347; HJURP_C; 1.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; SRF-like; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233160};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          1..61
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000259|PROSITE:PS50066"
FT   REGION          156..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          380..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..247
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..395
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        413..427
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   487 AA;  52321 MW;  A181BD88EA531898 CRC64;
     MGRKKIQITR IMDERNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS SNKLFQYAST
     DMDKVLLKYT EYNEPHESRT NSDIVETLRK KGLNGCESPD ADDYFEHSPL SEDRFSKLNE
     DSDFIFKRGP PGLPPQNFSM SVTVPVTSPN ALSYTNPGSS LVSPSLASSS TLADSSMLSP
     PQATLHRNVS PGAPQRPPST GNAGGMLSTT DLTVPNGAGT SPVGNGFVNS RASPNLIGTT
     GANSLGKVMP TKSPPPPGGG NLGMNSRKPD LRVVIPPSSK GMMPPLNTQR ISSSQATQPL
     ATPVVSVTTP SLPPQGLVYS AVPTAYNTDY SLTSADLSAL QGFNSPGMLS LGQVSAWQQH
     HLGQAALSSL VAGGQLSQGS NLSINTNQNI NIKSEPISPP RDRMTPSGFQ QQQQPQPPQP
     QPQPQPRQEM GRSPVDSLSS SSSSYDGSDR EDPRGDFHSP IVLGRPPNTE DRESPSVKRM
     RMDAWVT
//
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