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Database: UniProt
Entry: A0A2R9AX52_PANPA
LinkDB: A0A2R9AX52_PANPA
Original site: A0A2R9AX52_PANPA 
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
//
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