MTF2_PONAB
ID MTF2_PONAB Reviewed; 593 AA.
AC Q5R7T9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Metal-response element-binding transcription factor 2;
DE AltName: Full=Metal regulatory transcription factor 2;
GN Name=MTF2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Polycomb group (PcG) protein that specifically binds histone
CC H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex,
CC thus enhancing PRC2 H3K27me3 methylation activity (By similarity).
CC Regulates the transcriptional networks during embryonic stem cell self-
CC renewal and differentiation. Promotes recruitment of the PRC2 complex
CC to the inactive X chromosome in differentiating XX ES cells and PRC2
CC recruitment to target genes in undifferentiated ES cells. Required to
CC repress Hox genes by enhancing H3K27me3 methylation of the PRC2
CC complex. In some conditions may act as an inhibitor of PRC2 activity:
CC able to activate the CDKN2A gene and promote cellular senescence by
CC suppressing the catalytic activity of the PRC2 complex locally. Binds
CC to the metal-regulating-element (MRE) of MT1A gene promoter (By
CC similarity). {ECO:0000250|UniProtKB:Q02395,
CC ECO:0000250|UniProtKB:Q9Y483}.
CC -!- SUBUNIT: Associates with the PRC2 complex, which consists of the core
CC components EED, EZH1 or EZH2, SUZ12, and RBBP4, and various
CC combinations of accessory subunits including AEBP2, JARID2, PHF19, MTF2
CC and EPOP. Forms a dimeric PRC2.1 (class 1, PRC-PCL) complex consisting
CC of at least SUZ12, RBBP4, and PHF19 or MTF2; PHF19 and MTF2 stabilize
CC the dimeric structure which enhances PRC2 interaction with chromatin.
CC {ECO:0000250|UniProtKB:Q9Y483}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y483}.
CC Note=Localizes to chromatin as part of the PRC2 complex.
CC {ECO:0000250|UniProtKB:Q9Y483}.
CC -!- DOMAIN: The Tudor domain recognizes and binds H3K36me3. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Polycomblike family. {ECO:0000305}.
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DR EMBL; CR860020; CAH92171.1; -; mRNA.
DR RefSeq; NP_001126272.1; NM_001132800.1.
DR AlphaFoldDB; Q5R7T9; -.
DR SMR; Q5R7T9; -.
DR STRING; 9601.ENSPPYP00000001332; -.
DR DNASU; 100173244; -.
DR Ensembl; ENSPPYT00000061487; ENSPPYP00000033334; ENSPPYG00000001150.
DR GeneID; 100173244; -.
DR KEGG; pon:100173244; -.
DR CTD; 22823; -.
DR eggNOG; KOG4323; Eukaryota.
DR GeneTree; ENSGT00950000183180; -.
DR HOGENOM; CLU_032773_1_0_1; -.
DR InParanoid; Q5R7T9; -.
DR OrthoDB; 281828at2759; -.
DR TreeFam; TF106420; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0007379; P:segment specification; ISS:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; ISS:UniProtKB.
DR CDD; cd15578; PHD1_MTF2; 1.
DR CDD; cd15580; PHD2_MTF2; 1.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR040477; KDM4_Tudor_2.
DR InterPro; IPR025894; Mtf2_C_dom.
DR InterPro; IPR042014; MTF2_PHD1.
DR InterPro; IPR042015; MTF2_PHD2.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF14061; Mtf2_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF18104; Tudor_2; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..593
FT /note="Metal-response element-binding transcription factor
FT 2"
FT /id="PRO_0000059319"
FT DOMAIN 44..101
FT /note="Tudor"
FT ZN_FING 102..157
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 201..255
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 442..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y483"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y483"
FT CROSSLNK 360
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y483"
FT CROSSLNK 522
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y483"
SQ SEQUENCE 593 AA; 67090 MW; 4517B5DD61BB1AF4 CRC64;
MRDSTGAGNS LVHKRSPLRR NQKTPTSLTK LSLQDGHKAK KPACKFEEGQ DVLARWSDGL
FYLGTIKKIN ILKQSCFIIF EDSSKSWVLW KDIQTGATGS GEMVCTICQE EYSEAPNEMV
ICDKCGQGYH QLCHTPHIDS SVIDSDEKWL CRQCVFATTT KRGGALKKGP NAKALQVMKQ
TLPYSVADLE WDAGHKTNVQ QCYCYCGGPG DWYLKMLQCC KCKQWFHEAC VQCLQKPMLF
GDRFYTFICS VCSSGPEYLK RLPLQWVDIA HLCLYNLSVI HKKKYFDSEL ELMTYINENW
DRLHPGELAD TPKSERYEHV LEALNDYKTM FMSGKEIKKK KHLFGLRIRV PPVPPNVAFK
AEKEPEGTSH EFKIKGRKAS KPISDSREVS NGIEKKGKKK SVGRPPGPYT RKMIQKTAEP
LLDKESISEN PTLDLPCSIG RTEGTAHSSN TSDVDFTGAS SAKETTSSSI SRHYGLSDSR
KRTRTGRSWP AAIPHLRRRR GRLPRRALQT QNSEIVKDDE GKEDYQFDEL NTEILNNLAD
QELQLNHLKN SITSYFGAAG RIACGEKYRV LARRVTLDGK VQYLVEWEGA TAS
