ID H2PX75_PONAB Unreviewed; 486 AA.
AC H2PX75; A0A2J8RLQ6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 3.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Methyl-CpG-binding protein 2 {ECO:0000256|PIRNR:PIRNR038006};
DE Short=MeCp-2 protein {ECO:0000256|PIRNR:PIRNR038006};
DE Short=MeCp2 {ECO:0000256|PIRNR:PIRNR038006};
GN Name=MECP2 {ECO:0000313|Ensembl:ENSPPYP00000023354.3};
GN ORFNames=CR201_G0049923 {ECO:0000313|EMBL:PNJ09456.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000023354.3, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000023354.3, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ09456.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ09456.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000023354.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. Binds both 5-methylcytosine (5mC)
CC and 5-hydroxymethylcytosine (5hmC)-containing DNA, with a preference
CC for 5-methylcytosine (5mC). {ECO:0000256|PIRNR:PIRNR038006}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR038006}.
CC Note=Colocalized with methyl-CpG in the genome.
CC {ECO:0000256|PIRNR:PIRNR038006}.
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DR EMBL; NDHI03003672; PNJ09456.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000023354; -.
DR Ensembl; ENSPPYT00000024331.3; ENSPPYP00000023354.3; ENSPPYG00000020866.3.
DR eggNOG; KOG4161; Eukaryota.
DR GeneTree; ENSGT00530000063687; -.
DR HOGENOM; CLU_045066_0_0_1; -.
DR OrthoDB; 5262043at2759; -.
DR TreeFam; TF332974; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:UniProtKB-UniRule.
DR CDD; cd01396; MeCP2_MBD; 1.
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; METHYL-CPG-BINDING PROTEIN; 1.
DR PANTHER; PTHR15074:SF6; METHYL-CPG-BINDING PROTEIN 2; 1.
DR Pfam; PF01429; MBD; 1.
DR PIRSF; PIRSF038006; Methyl_CpG_bd_MeCP2; 1.
DR SMART; SM00391; MBD; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR PROSITE; PS50982; MBD; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|PIRNR:PIRNR038006};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR038006};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Repressor {ECO:0000256|PIRNR:PIRNR038006};
KW Transcription {ECO:0000256|PIRNR:PIRNR038006};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR038006}.
FT DOMAIN 90..162
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT REGION 1..119
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 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"
SQ SEQUENCE 486 AA; 52441 MW; EB6A33233AEDA566 CRC64;
MVAGMLGLRE EKSEDQDLQG LKDKPLKFKK VKKDKKEEKE 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
//
