ID A0A218UZR2_9PASE Unreviewed; 716 AA.
AC A0A218UZR2;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Lethal(3)malignant brain tumor-like protein 2 {ECO:0000256|ARBA:ARBA00015504};
GN Name=L3MBTL2 {ECO:0000313|EMBL:OWK59274.1};
GN ORFNames=RLOC_00007942 {ECO:0000313|EMBL:OWK59274.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK59274.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK59274.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK59274.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Putative Polycomb group (PcG) protein. PcG proteins maintain
CC the transcriptionally repressive state of genes, probably via a
CC modification of chromatin, rendering it heritably changed in its
CC expressibility. Its association with a chromatin-remodeling complex
CC suggests that it may contribute to prevent expression of genes that
CC trigger the cell into mitosis. Binds to monomethylated and dimethylated
CC 'Lys-20' on histone H4. Binds histone H3 peptides that are
CC monomethylated or dimethylated on 'Lys-4', 'Lys-9' or 'Lys-27'.
CC {ECO:0000256|ARBA:ARBA00025314}.
CC -!- SUBUNIT: Part of the E2F6.com-1 complex in G0 phase composed of E2F6,
CC MGA, MAX, TFDP1, CBX3, BAT8, EUHMTASE1, RING1, RNF2, MBLR, BAT8 and
CC YAF2. {ECO:0000256|ARBA:ARBA00011444}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK59274.1}.
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DR EMBL; MUZQ01000080; OWK59274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218UZR2; -.
DR STRING; 299123.ENSLSDP00000003351; -.
DR OrthoDB; 5405166at2759; -.
DR Proteomes; UP000197619; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd20100; MBT_dSfmbt-like_rpt4; 1.
DR CDD; cd20121; MBT_L3MBTL2_rpt1; 1.
DR CDD; cd20124; MBT_L3MBTL2_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 4.
DR Gene3D; 3.30.60.160; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR047356; MBT_L3MBTL2_rpt1.
DR InterPro; IPR047357; MBT_L3MBTL2_rpt2.
DR InterPro; IPR012313; Znf_FCS.
DR InterPro; IPR038603; Znf_FCS_sf.
DR PANTHER; PTHR12247:SF64; LETHAL(3)MALIGNANT BRAIN TUMOR-LIKE PROTEIN 2; 1.
DR PANTHER; PTHR12247; POLYCOMB GROUP PROTEIN; 1.
DR Pfam; PF02820; MBT; 4.
DR Pfam; PF21319; zf-FCS_1; 1.
DR SMART; SM00561; MBT; 4.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 4.
DR PROSITE; PS51079; MBT; 4.
DR PROSITE; PS51024; ZF_FCS; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Isopeptide bond {ECO:0000256|ARBA:ARBA00022499};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00367}.
FT DOMAIN 90..125
FT /note="FCS-type"
FT /evidence="ECO:0000259|PROSITE:PS51024"
FT REPEAT 188..292
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 300..400
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 407..510
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REPEAT 518..614
FT /note="MBT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00459"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 612..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..649
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 80357 MW; CC9B5341C339645A CRC64;
MERDRREMVS AFGHKTSSLE RVEEEGDADE EDDELDIFGG YDSLTCYNSS MGSDSSSCLE
ESSDDEVADR EAGELSTSPM HQPSTGRLTE DNGSEPAVCE MCGIVGTREA FFSKTKRFCS
VSCSRSYSSN SKKASILARL QGKPPTKKAK VLHKASWSAK IGAFLHSQGT GQLADGTLTG
QDALVLGFDW GKYLQEHGYK AAPVSCFKHV PLFDQWDDVL KGMKVEVLNS DAVLPSRVYW
IASVIQIVGY RALLRYEGFE NDAGHDFWCN LGTVDIHPIG WCAINSKILV PPQTIHAKYT
DWRSYLMKKL VGARTIPVDF HIKMAESMKY PFRQGMRVEV VDKNHVSQTR MAVVDTVIGG
RLRLLYEDGD SDDDFWCHMW SPLIHPVGWS RRVGHDIKKT EEKRNDMANH PTFRKIYCDA
VPYLFKKVRA VYSEGGWFER GMKLEAIDPL NLGNICVATV CKVLLDGYLM ISIDGATSDD
GSDWFCYHAS SHAIFPANFC KRNSIELTPP KGHEAKTFSW ERYLEETKSR PAPSRLFNTD
CPNHGFKAGM KVEAVDLMEP RLICVATVKR VVQRLLSIHF DGWDNEYDQW VDCESPDIYP
VGWCELTGYQ LQPPVTPEPT TPAKAKEVPK KRKKPYGKKR KKLPAKARSV KQTAKKPSAM
NSKREAKAAS QTLPEPAPDE IIAVRVKEET IDPSDAEFGE TELPVPISSI KQEDTD
//
