ID G1T4I6_RABIT Unreviewed; 575 AA.
AC G1T4I6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 62.
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:ENSOCUP00000011193.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000011193.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000011193.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000011193.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000011193.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000011193.3};
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 EMBL; AAGW02056408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1T4I6; -.
DR PaxDb; 9986-ENSOCUP00000011193; -.
DR Ensembl; ENSOCUT00000013003.3; ENSOCUP00000011193.3; ENSOCUG00000013006.3.
DR eggNOG; KOG4161; Eukaryota.
DR GeneTree; ENSGT00530000063687; -.
DR HOGENOM; CLU_034167_0_0_1; -.
DR TreeFam; TF329176; -.
DR Proteomes; UP000001811; Chromosome 9.
DR Bgee; ENSOCUG00000013006; Expressed in autopod skin and 15 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008263; F:pyrimidine-specific mismatch base pair DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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:UP000001811}.
FT DOMAIN 74..146
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 63833 MW; 61A906A0E59A8E2D CRC64;
GGTAEMESPS LGDGGAAPAV SCSERPAPAQ PCDLGDDAVR LERAGEDEKQ MVVNGSSACN
PLLPEPIASA GCGGTAVTES PKSVPCGWER VVKQRLSGKT AGKFDVYFIS PQGLKFRSRR
SLTNYLHKNG ETSLHPEDFD FTLVPKRGTK SRKKDCSVAD LTSQLQNSRN VSNWNLRTRS
RQEKDECPLP SACSELQGNR GLSNPASIHL PSKEDEGVHD VASGKGRKSK GKETVLKGIH
IKKTKKGFGK NRSGSVQSSR KRNAVCNKAG AEREPVPQEG ELERALCVSD ARAGSQPLGV
TSAEKSLVKE RSSSESSFHL EQLTSGVTNE LGSTKEAEHS QKHEDTSSES EGIRTKGDTG
GRKEHLHADI LRCGAEMDSS CSQTETDLTS EKILQEDTIP RTQIERRKTS LYFSSKYNKA
ALSPPRRKAF KKWTPPRSPF NLVQETLFHD PWKLLIATIF LNRTSGKMAI PVLWEFLEKY
PSAEVARAAD WRDVSELLKP LGLYDLRAKT IIKFSDEYLT KQWKYPIELH GIGKYGNDSY
RIFCVNEWKQ VHPEDHKLNK YHDWLWENHE KLSLS
//
