GenomeNet

Database: UniProt
Entry: D4A9W8_RAT
LinkDB: D4A9W8_RAT
Original site: D4A9W8_RAT 
ID   D4A9W8_RAT              Unreviewed;       549 AA.
AC   D4A9W8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 4.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Methyl-CpG-binding domain protein 4 {ECO:0000256|PIRNR:PIRNR038005};
DE            EC=3.2.2.- {ECO:0000256|PIRNR:PIRNR038005};
GN   Name=Mbd4 {ECO:0000313|Ensembl:ENSRNOP00000014537.7,
GN   ECO:0000313|RGD:1585874};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000014537.7, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000014537.7, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000014537.7,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000014537.7}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000014537.7};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Mismatch-specific DNA N-glycosylase involved in DNA repair.
CC       Has thymine glycosylase activity and is specific for G:T mismatches
CC       within methylated and unmethylated CpG sites. Can also remove uracil or
CC       5-fluorouracil in G:U mismatches. Has no lyase activity. Was first
CC       identified as methyl-CpG-binding protein.
CC       {ECO:0000256|PIRNR:PIRNR038005}.
CC   -!- SUBUNIT: Interacts with MLH1. {ECO:0000256|PIRNR:PIRNR038005}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR038005}.
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DR   AlphaFoldDB; D4A9W8; -.
DR   STRING; 10116.ENSRNOP00000014537; -.
DR   PaxDb; 10116-ENSRNOP00000014537; -.
DR   Ensembl; ENSRNOT00000014537.8; ENSRNOP00000014537.7; ENSRNOG00000010919.9.
DR   AGR; RGD:1585874; -.
DR   RGD; 1585874; Mbd4.
DR   VEuPathDB; HostDB:ENSRNOG00000010919; -.
DR   eggNOG; KOG4161; Eukaryota.
DR   GeneTree; ENSGT00530000063687; -.
DR   HOGENOM; CLU_034167_0_0_1; -.
DR   InParanoid; D4A9W8; -.
DR   OrthoDB; 1451962at2759; -.
DR   TreeFam; TF329176; -.
DR   Reactome; R-RNO-110329; Cleavage of the damaged pyrimidine.
DR   Reactome; R-RNO-110357; Displacement of DNA glycosylase by APEX1.
DR   Proteomes; UP000002494; Chromosome 4.
DR   Bgee; ENSRNOG00000010919; Expressed in testis and 19 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISO:RGD.
DR   GO; GO:0008263; F:pyrimidine-specific mismatch base pair DNA N-glycosylase activity; ISO:RGD.
DR   GO; GO:0006974; P:DNA damage response; ISO:RGD.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; ISO:RGD.
DR   GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; ISO:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0009314; P:response to radiation; ISO:RGD.
DR   CDD; cd01396; MeCP2_MBD; 1.
DR   InterPro; IPR016177; DNA-bd_dom_sf.
DR   InterPro; IPR011257; DNA_glycosylase.
DR   InterPro; IPR017352; MBD4.
DR   InterPro; IPR045138; MeCP2/MBD4.
DR   InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR   PANTHER; PTHR15074:SF7; METHYL-CPG-BINDING DOMAIN PROTEIN 4; 1.
DR   PANTHER; PTHR15074; METHYL-CPG-BINDING PROTEIN; 1.
DR   Pfam; PF01429; MBD; 1.
DR   PIRSF; PIRSF038005; Methyl_CpG_bd_MBD4; 1.
DR   SMART; SM00391; MBD; 1.
DR   SUPFAM; SSF54171; DNA-binding domain; 1.
DR   SUPFAM; SSF48150; DNA-glycosylase; 1.
DR   PROSITE; PS50982; MBD; 1.
PE   4: Predicted;
KW   DNA damage {ECO:0000256|PIRNR:PIRNR038005};
KW   DNA repair {ECO:0000256|PIRNR:PIRNR038005};
KW   DNA-binding {ECO:0000256|PIRNR:PIRNR038005};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR038005};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR038005};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   DOMAIN          51..123
FT                   /note="MBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50982"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          216..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..150
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   549 AA;  61550 MW;  AD6D9AE7820623E8 CRC64;
     SAERAGTQEA EAKEDVAVGL GGVGEDGKDL VISSECGSLL QEPAASTLPS CTTVAECHKP
     VPCGWERVVK QRLSGKTAGR VDVYFISPQG SKFRSKRSLA NYLLKTGETC LKPEDFDFTV
     LSKGGINPGY KHQSLSAPAS QQPNEADISK LNLRTRSKWK TDVLPLPGGN SESPDSNSLS
     NSNSARLLLK EHKGIQDADS GKSRKPKIKV TVLKGIASQR TKQRCRKSPS DSTGRNRKRL
     CTVQKADTDS ELVPQESRLH RTVCPADACA RATVSLVREA KGLGEEKSPS SDLRFTQVTS
     SITNKLYSTE AAGEATREAT REQTFLESEE IRSKGEEEEA HLHIDILQSG SETPSCSQAK
     KHLTSETFRE DSIPRTQVEK RKTSLYFSSK YNKEALSPPR RKAFKKWTPP RSPFNLVQET
     LFHDPWKLLI STIFLNRTSG KMAIPVLWEF LEKYPSAEVA RTADWRDVSE LLKPLGLYDL
     RAKTIIKFSD EYLTKPWRYP IELHGIGKYG NDSYRIFCVN EWKQVHPEDH KLNKYHDWLW
     ENHEKLSLS
//
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