LMBL1_CHICK
ID LMBL1_CHICK Reviewed; 847 AA.
AC E1C2V1;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Lethal(3)malignant brain tumor-like protein 1;
DE Short=H-l(3)mbt;
DE Short=H-l(3)mbt protein;
DE Short=L(3)mbt-like;
DE AltName: Full=L(3)mbt protein homolog;
GN Name=L3MBTL1; Synonyms=L3MBT, L3MBTL;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
CC -!- FUNCTION: Polycomb group (PcG) protein that specifically recognizes and
CC binds mono- and dimethyllysine residues on target proteins, therey
CC acting as a 'reader' of a network of post-translational modifications.
CC PcG proteins maintain the transcriptionally repressive state of genes:
CC acts as a chromatin compaction factor by recognizing and binding
CC mono- and dimethylated histone H1b/H1-4 at 'Lys-26' (H1bK26me1 and
CC H1bK26me2) and histone H4 at 'Lys-20' (H4K20me1 and H4K20me2), leading
CC to condense chromatin and repress transcription (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: The MBT repeat 2 specifically recognizes and binds
CC monomethylated and dimethylated proteins. In contrast, it does not bind
CC trimethylated proteins. The MBT repeat 1 does not bind methylated
CC peptides but inserts a proline ring in a Pro-Ser-Ser/Thr sequence
CC context (By similarity). {ECO:0000250}.
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DR EMBL; AADN02019575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1C2V1; -.
DR SMR; E1C2V1; -.
DR STRING; 9031.ENSGALP00000001451; -.
DR PaxDb; E1C2V1; -.
DR VEuPathDB; HostDB:geneid_419115; -.
DR eggNOG; KOG3766; Eukaryota.
DR InParanoid; E1C2V1; -.
DR OrthoDB; 63195at2759; -.
DR PhylomeDB; E1C2V1; -.
DR TreeFam; TF316498; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR004092; Mbt.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR002515; Znf_C2H2C.
DR InterPro; IPR036060; Znf_C2H2C_sf.
DR Pfam; PF02820; MBT; 3.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF01530; zf-C2HC; 1.
DR SMART; SM00561; MBT; 3.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF103637; SSF103637; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR PROSITE; PS51079; MBT; 3.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51802; ZF_CCHHC; 1.
PE 3: Inferred from homology;
KW Chromatin regulator; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..847
FT /note="Lethal(3)malignant brain tumor-like protein 1"
FT /id="PRO_0000405833"
FT REPEAT 300..400
FT /note="MBT 1"
FT REPEAT 408..507
FT /note="MBT 2"
FT REPEAT 516..611
FT /note="MBT 3"
FT DOMAIN 778..842
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT ZN_FING 639..682
FT /note="CCHHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT REGION 65..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..480
FT /note="Interaction with monomethylated and dimethylated
FT peptides"
FT /evidence="ECO:0000250"
FT COMPBIAS 142..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 648
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 653
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT BINDING 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT SITE 449
FT /note="Mediates recognition of monomethylated and
FT dimethylated peptides"
FT /evidence="ECO:0000250"
FT SITE 452
FT /note="Positioned at the entrance of MBT 2 and is required
FT for recognition of monomethylated and dimethylated
FT peptides"
FT /evidence="ECO:0000250"
SQ SEQUENCE 847 AA; 94760 MW; 35579453F86E9433 CRC64;
MDGRAEMEVV RTTKGNAAGE VSVHVVTTES TVQSTHLPTT AFIFPSQANA TTINLPTSTL
EIQRFPREPP RNTGAERPEK GVGSEPITAT VIPQISGVQT CNTVRVLEWK DGVATLPGSN
LRFRINEYGT LKVVSADKMP PAEAVKEGHA KKDGDSDVAP TSRDNTIVAQ DVPEQSKLPT
ADSICHCDTC GRRHVSDGAR EGRGFCSEHC HQQFKERSVI VENSASSTSA TEILKPVKKR
KRKDYQSPSE EDYESEQMEE KQEEMKNSVG DSAISNPEAH AWSQHSTEGP GASEEKKEGW
SWASYLEEQK AVAAPLDLFQ DYQVASQHKN GFKVGMKLEG IDPQHPSMYF ILTVAEVCGY
RMRLHFDGYS ECHDFWLNAD SPDIHPAGWF EETGHKLQPP KGYKEEEFSW TNYLKITKAQ
AAPKHLFVIR NTHEAPPGFE VGMKLEAVDR MNPSLICVAT VTDVVDDRFL VHFDNWDDTY
DYWCDPSSPY IHPVGWCQEH GKPLTPPQDY PDPDNFIWEK YLKETGASAV PAWAFKVRPP
HGFLVNMKLE AVDRRTPSFI RVASVEDVED HRIKIHFDGW SHVYDFWIDA DHPDIHPIGW
CSKTGHPLQP PLRPKEPASS AHSGCPTLGC KNIPHTKSSK YSFHHRKCPT PGCDGSGHVT
GRFTAHYCLS GCPLAEKNQG KLKADLSDTE ASTRKRNLIG FPQRKKSRHH GSFRGRPPKY
RKIQQEDFQT ISSDNMHQSL FMSALSAHPD RSLSLCWEQH CKLLPGVAGI TATTVAKWTI
DEVFSFVQTL TGCEDQAKLF KDEMIDGEAF LLLTQADIVK IMSVKLGPAL KIYNAILMFK
NADDTLK
