ID A0A2R9AX52_PANPA Unreviewed; 493 AA.
AC A0A2R9AX52;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
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:ENSPPAP00000021757.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000021757.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000021757.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000021757.1}
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; AJFE02011992; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02011993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02011994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02011995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJFE02011996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R9AX52; -.
DR Ensembl; ENSPPAT00000044560.1; ENSPPAP00000021757.1; ENSPPAG00000034020.1.
DR GeneTree; ENSGT00530000063687; -.
DR Proteomes; UP000240080; Chromosome X.
DR Bgee; ENSPPAG00000034020; Expressed in placenta and 6 other cell types or tissues.
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:UP000240080};
KW Repressor {ECO:0000256|PIRNR:PIRNR038006};
KW Transcription {ECO:0000256|PIRNR:PIRNR038006};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR038006}.
FT DOMAIN 97..169
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..407
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 493 AA; 53180 MW; 0F11C121F2A60D60 CRC64;
LRQENNLNPA GGGCDEEEKS EDQDLQGLKD KPLKFKKVKK DKKEEKEGKH EPVQPSAHHS
AEPAEAGKAE TSEGSGSAPA VPEASASPKQ RRSIIRDRGP MYDDPTLPEG WTRKLKQRKS
GRSAGKYDVY LINPQGKAFR SKVELIAYFE KVGDTSLDPN DFDFTVTGRG SPSRREQKPP
KKPKSPKAPG TGRGRGRPKG SGTTRPKAAT SEGVQVKRVL EKSPGKLLVK MPFQTSPGGK
AEGGGATTST QVMVIKRPGR KRKAEADPQA IPKKRGRKPG SVVAAAAAEA KKKAVKESSI
RSVQETVLPI KKRKTRETVS IEVKEVVKPL LVSTLGEKSG KGLKTCKSPG RKSKESSPKG
RSSSASSPPK KEHHHHHHHS ESPKAPVPLL PPLPPPPPEP ESSEDPTSPP EPQDLSSSVC
KEEKMPRGGS LESDGCPKEP AKTQPAVATA ATAAEKYKHR GEGERKDIVS SSMPRPNREE
PVDSRTPVTE RVS
//