MECP2_MACFA
ID MECP2_MACFA Reviewed; 486 AA.
AC Q95LG8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Methyl-CpG-binding protein 2;
DE Short=MeCp-2 protein;
DE Short=MeCp2;
GN Name=MECP2;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Muramatsu S.;
RT "Excessive hand-wringing in a MPTP-treated monkey.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Chromosomal protein that binds to methylated DNA. It can bind
CC specifically to a single methyl-CpG pair. It is not influenced by
CC sequences flanking the methyl-CpGs. Mediates transcriptional repression
CC through interaction with histone deacetylase and the corepressor SIN3A.
CC Binds both 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC)-
CC containing DNA, with a preference for 5-methylcytosine (5mC).
CC {ECO:0000250|UniProtKB:Q9Z2D6}.
CC -!- SUBUNIT: Interacts with FNBP3. Interacts with CDKL5. Interacts with
CC ATRX; MECP2 recruits ATRX to pericentric heterochromatin in neuronal
CC cells. Interacts with NCOR2. Interacts with TBL1XR1; bridges
CC interaction between MECP2 and NCOR1. Interacts with TBL1X; recruits
CC TBL1X to the heterochromatin foci (By similarity).
CC {ECO:0000250|UniProtKB:P51608, ECO:0000250|UniProtKB:Q9Z2D6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Z2D6}.
CC Note=Colocalized with methyl-CpG in the genome. Colocalized with TBL1X
CC to the heterochromatin foci. {ECO:0000250|UniProtKB:P51608}.
CC -!- PTM: Phosphorylated on Ser-423 in brain upon synaptic activity, which
CC attenuates its repressor activity and seems to regulate dendritic
CC growth and spine maturation. {ECO:0000250}.
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DR EMBL; AF295597; AAK97131.1; -; mRNA.
DR RefSeq; NP_001271476.1; NM_001284547.1.
DR AlphaFoldDB; Q95LG8; -.
DR BMRB; Q95LG8; -.
DR SMR; Q95LG8; -.
DR STRING; 9541.XP_005595019.1; -.
DR Ensembl; ENSMFAT00000035479; ENSMFAP00000020503; ENSMFAG00000033178.
DR GeneID; 102135563; -.
DR CTD; 4204; -.
DR VEuPathDB; HostDB:ENSMFAG00000033178; -.
DR eggNOG; KOG4161; Eukaryota.
DR GeneTree; ENSGT00530000063687; -.
DR OrthoDB; 1431783at2759; -.
DR Proteomes; UP000233100; Chromosome X.
DR Bgee; ENSMFAG00000033178; Expressed in skeletal muscle tissue and 13 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR017353; Me_CpG-bd_MeCP2.
DR InterPro; IPR045138; MeCP2/MBD4.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR PANTHER; PTHR15074; PTHR15074; 1.
DR Pfam; PF01429; MBD; 1.
DR PIRSF; PIRSF038006; Methyl_CpG_bd_MeCP2; 1.
DR SMART; SM00391; MBD; 1.
DR SUPFAM; SSF54171; SSF54171; 1.
DR PROSITE; PS50982; MBD; 1.
PE 2: Evidence at transcript level;
KW Acetylation; DNA-binding; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..486
FT /note="Methyl-CpG-binding protein 2"
FT /id="PRO_0000096346"
FT DOMAIN 90..162
FT /note="MBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00338"
FT DNA_BIND 185..197
FT /note="A.T hook 1"
FT DNA_BIND 265..277
FT /note="A.T hook 2"
FT REGION 1..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..309
FT /note="Interaction with NCOR2"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D6"
FT REGION 285..309
FT /note="Interaction with TBL1XR1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D6"
FT REGION 324..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..400
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..486
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00566"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51608"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51608"
FT MOD_RES 162
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D6"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51608"
FT MOD_RES 229
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51608"
FT MOD_RES 321
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D6"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z2D6"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51608"
FT MOD_RES 449
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51608"
SQ SEQUENCE 486 AA; 52427 MW; 3471B61D90D92A7D CRC64;
MVAGMLGLRE EKSEDQDLQG LKDKPLKFKK VKKDKKEDKE GKHEPVQPSA HHSAEPAEAG
KAETSEGSGS APAVPEASAS PKQRRSIIRD RGPMYDDPTL PEGWTRKLKQ RKSGRSAGKY
DVYLINPQGK AFRSKVELIA YFEKVGDTSL DPNDFDFTVT GRGSPSRREQ KPPKKPKSPK
APGTGRGRGR PKGSGTTRPK AATSEGVQVK RVLEKSPGKL LVKMPFQTSP GGKAEGGGAT
TSTQVMVIKR PGRKRKAEAD PQAIPKKRGR KPGSVVAAAA AEAKKKAVKE SSIRSVQETV
LPIKKRKTRE TVSIEVKEVV KPLLVSTLGE KSGKGLKTCK SPGRKSKESS PKGRSSSASS
PPKKEHHHHH HHSESPKAPV PLLPPLPPPP PEPESSEDPT SPPEPQDLSS SVCKEEKMPR
GGSLESDGCP KEPAKTQPAV ATAATAAEKY KHRGEGERKD IVSSSMPRPN REEPVDSRTP
VTERVS
