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Metal-response element-binding transcription factor 2 (Metal regulatory transcription factor 2) (Metal-response element DNA-binding protein M96) (Polycomb-like protein 2) (mPCl2) (Zinc-regulated factor 1) (ZiRF1)

 MTF2_MOUSE              Reviewed;         593 AA.
Q02395; Q05C61; Q569Z8; Q6PG89; Q8BGP9; Q8BSJ7;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
22-NOV-2005, sequence version 2.
25-OCT-2017, entry version 140.
RecName: Full=Metal-response element-binding transcription factor 2;
AltName: Full=Metal regulatory transcription factor 2;
AltName: Full=Metal-response element DNA-binding protein M96;
AltName: Full=Polycomb-like protein 2;
Short=mPCl2;
AltName: Full=Zinc-regulated factor 1;
Short=ZiRF1;
Name=Mtf2; Synonyms=Pcl2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Egg, Testis, and Wolffian duct;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and NMRI; TISSUE=Head, Mammary tumor, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-476 (ISOFORM 2).
TISSUE=Lymphoma;
PubMed=7772254; DOI=10.1089/dna.1994.13.731;
Inouye C., Remondelli P., Karin M., Elledge S.;
"Isolation of a cDNA encoding a metal response element binding protein
using a novel expression cloning procedure: the one hybrid system.";
DNA Cell Biol. 13:731-742(1994).
[4]
FUNCTION.
PubMed=9173905; DOI=10.1042/bj3230079;
Remondelli P., Leone A.;
"Interactions of the zinc-regulated factor (ZiRF1) with the mouse
metallothionein Ia promoter.";
Biochem. J. 323:79-85(1997).
[5]
FUNCTION, AND ASSOCIATION WITH THE PRC2 COMPLEX.
PubMed=20144788; DOI=10.1016/j.stem.2009.12.014;
Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K.,
Torchia J., Krogan N.J., Reiter J.F., Stanford W.L.;
"Polycomb-like 2 associates with PRC2 and regulates transcriptional
networks during mouse embryonic stem cell self-renewal and
differentiation.";
Cell Stem Cell 6:153-166(2010).
[6]
FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX, AND SUBCELLULAR LOCATION.
PubMed=21367819; DOI=10.1242/dev.053652;
Casanova M., Preissner T., Cerase A., Poot R., Yamada D., Li X.,
Appanah R., Bezstarosti K., Demmers J., Koseki H., Brockdorff N.;
"Polycomblike 2 facilitates the recruitment of PRC2 Polycomb group
complexes to the inactive X chromosome and to target loci in embryonic
stem cells.";
Development 138:1471-1482(2011).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21059868; DOI=10.1128/MCB.00259-10;
Li X., Isono K., Yamada D., Endo T.A., Endoh M., Shinga J.,
Mizutani-Koseki Y., Otte A.P., Casanova M., Kitamura H., Kamijo T.,
Sharif J., Ohara O., Toyada T., Bernstein B.E., Brockdorff N.,
Koseki H.;
"Mammalian polycomb-like Pcl2/Mtf2 is a novel regulatory component of
PRC2 that can differentially modulate polycomb activity both at the
Hox gene cluster and at Cdkn2a genes.";
Mol. Cell. Biol. 31:351-364(2011).
[8]
H3K36ME3-BINDING.
PubMed=23104054; DOI=10.1038/nsmb.2434;
Ballare C., Lange M., Lapinaite A., Martin G.M., Morey L., Pascual G.,
Liefke R., Simon B., Shi Y., Gozani O., Carlomagno T., Benitah S.A.,
Di Croce L.;
"Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb
activity.";
Nat. Struct. Mol. Biol. 19:1257-1265(2012).
[9]
ASSOCIATION WITH THE PRC2 COMPLEX.
PubMed=22438827; DOI=10.1371/journal.pgen.1002576;
Hunkapiller J., Shen Y., Diaz A., Cagney G., McCleary D.,
Ramalho-Santos M., Krogan N., Ren B., Song J.S., Reiter J.F.;
"Polycomb-like 3 promotes polycomb repressive complex 2 binding to CpG
islands and embryonic stem cell self-renewal.";
PLoS Genet. 8:E1002576-E1002576(2012).
[10]
STRUCTURE BY NMR OF 40-98 AND 104-162.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the tudor domain of metal-response element-
binding transcription factor 2.";
Submitted (FEB-2009) to the PDB data bank.
-!- FUNCTION: Polycomb group (PcG) that specifically binds histone H3
trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2
complex. Acts by binding to H3K36me3, a mark for transcriptional
activation, and recruiting the PRC2 complex, leading to enhance
PRC2 H3K27me3 methylation activity. Regulates the transcriptional
networks during embryonic stem cell self-renewal and
differentiation. Promotes recruitment of the PRC2 complex to the
inactive X chromosome in differentiating XX ES cells and PRC2
recruitment to target genes in undifferentiated ES cells. Required
to repress Hox genes by enhancing H3K27me3 methylation of the PRC2
complex. In some conditions may act as an inhibitor of PRC2
activity: able to activate the CDKN2A gene and promote cellular
senescence by suppressing the catalytic activity of the PRC2
complex locally. Binds to the metal-regulating-element (MRE) of
MT1A gene promoter. {ECO:0000269|PubMed:20144788,
ECO:0000269|PubMed:21059868, ECO:0000269|PubMed:21367819,
ECO:0000269|PubMed:9173905}.
-!- SUBUNIT: Associated component of the PRC2 complex.
-!- INTERACTION:
Q921E6:Eed; NbExp=3; IntAct=EBI-2531578, EBI-904301;
P70351:Ezh1; NbExp=3; IntAct=EBI-2531578, EBI-2531737;
Q61188:Ezh2; NbExp=4; IntAct=EBI-2531578, EBI-904311;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21367819}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q02395-1; Sequence=Displayed;
Name=2;
IsoId=Q02395-2; Sequence=VSP_016240;
-!- DOMAIN: The Tudor domain recognizes and binds H3K36me3.
{ECO:0000269|PubMed:23104054}.
-!- DISRUPTION PHENOTYPE: Mice survive to birth; however, most of them
die before weaning. Axial skeletal alterations that are
characteristic of posterior transformations are observed: ectopic
ribs that associate with the seventh cervical vertebra (C7) are
frequently observed. Consistent with this malformation, sternums
are shifted anteriorly. The odontoid process, which is normally a
characteristic of the second cervical vertebra (C2), is frequently
associated with the first cervical vertebra (C1).
{ECO:0000269|PubMed:21059868}.
-!- SIMILARITY: Belongs to the Polycomblike family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH24889.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH29076.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AK032798; BAC28027.1; -; mRNA.
EMBL; AK032819; BAC28039.1; -; mRNA.
EMBL; AK031409; BAC27390.1; -; mRNA.
EMBL; AK139685; BAE24103.1; -; mRNA.
EMBL; BC057163; AAH57163.1; -; mRNA.
EMBL; BC092237; AAH92237.1; -; mRNA.
EMBL; BC100340; AAI00341.1; -; mRNA.
EMBL; BC024889; AAH24889.1; ALT_SEQ; mRNA.
EMBL; BC029076; AAH29076.1; ALT_SEQ; mRNA.
EMBL; S78454; AAC34714.1; -; mRNA.
CCDS; CCDS39201.1; -. [Q02395-1]
RefSeq; NP_001240806.1; NM_001253877.1. [Q02395-2]
RefSeq; NP_001240807.1; NM_001253878.1. [Q02395-2]
RefSeq; NP_001240808.1; NM_001253879.1. [Q02395-2]
RefSeq; NP_001240809.1; NM_001253880.1. [Q02395-2]
RefSeq; NP_038855.2; NM_013827.3. [Q02395-1]
RefSeq; XP_011247718.1; XM_011249416.2. [Q02395-2]
RefSeq; XP_017176193.1; XM_017320704.1. [Q02395-2]
RefSeq; XP_017176194.1; XM_017320705.1. [Q02395-2]
UniGene; Mm.257149; -.
PDB; 2EQJ; NMR; -; A=40-98.
PDB; 2YT5; NMR; -; A=104-162.
PDBsum; 2EQJ; -.
PDBsum; 2YT5; -.
ProteinModelPortal; Q02395; -.
SMR; Q02395; -.
BioGrid; 201592; 13.
DIP; DIP-56991N; -.
IntAct; Q02395; 10.
STRING; 10090.ENSMUSP00000080278; -.
iPTMnet; Q02395; -.
PhosphoSitePlus; Q02395; -.
EPD; Q02395; -.
MaxQB; Q02395; -.
PaxDb; Q02395; -.
PeptideAtlas; Q02395; -.
PRIDE; Q02395; -.
Ensembl; ENSMUST00000081567; ENSMUSP00000080278; ENSMUSG00000029267. [Q02395-1]
GeneID; 17765; -.
KEGG; mmu:17765; -.
UCSC; uc008ynj.2; mouse. [Q02395-1]
CTD; 22823; -.
MGI; MGI:105050; Mtf2.
eggNOG; KOG4323; Eukaryota.
eggNOG; ENOG410XQ6E; LUCA.
GeneTree; ENSGT00390000009222; -.
HOGENOM; HOG000010307; -.
HOVERGEN; HBG004755; -.
InParanoid; Q02395; -.
KO; K11485; -.
OMA; SDDKWLC; -.
OrthoDB; EOG091G01JL; -.
PhylomeDB; Q02395; -.
TreeFam; TF106420; -.
Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
ChiTaRS; Mtf2; mouse.
EvolutionaryTrace; Q02395; -.
PRO; PR:Q02395; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029267; -.
ExpressionAtlas; Q02395; baseline and differential.
Genevisible; Q02395; MM.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0007379; P:segment specification; IMP:UniProtKB.
GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
Gene3D; 3.30.40.10; -; 2.
InterPro; IPR025894; Mtf2_C_dom.
InterPro; IPR002999; Tudor.
InterPro; IPR019786; Zinc_finger_PHD-type_CS.
InterPro; IPR011011; Znf_FYVE_PHD.
InterPro; IPR001965; Znf_PHD.
InterPro; IPR019787; Znf_PHD-finger.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF14061; Mtf2_C; 1.
Pfam; PF00628; PHD; 1.
SMART; SM00249; PHD; 2.
SMART; SM00333; TUDOR; 1.
SUPFAM; SSF57903; SSF57903; 2.
PROSITE; PS01359; ZF_PHD_1; 2.
PROSITE; PS50016; ZF_PHD_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromatin regulator;
Complete proteome; DNA-binding; Isopeptide bond; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation;
Zinc; Zinc-finger.
CHAIN 1 593 Metal-response element-binding
transcription factor 2.
/FTId=PRO_0000059318.
DOMAIN 44 101 Tudor.
ZN_FING 102 157 PHD-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
ZN_FING 201 255 PHD-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00146}.
COMPBIAS 338 341 Poly-Lys.
COMPBIAS 497 502 Poly-Arg.
MOD_RES 24 24 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9Y483}.
MOD_RES 452 452 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Y483}.
CROSSLNK 360 360 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y483}.
CROSSLNK 522 522 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q9Y483}.
VAR_SEQ 1 102 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:7772254}.
/FTId=VSP_016240.
CONFLICT 200 201 QQ -> PE (in Ref. 3; AAC34714).
{ECO:0000305}.
CONFLICT 282 282 Missing (in Ref. 3; AAC34714).
{ECO:0000305}.
CONFLICT 394 394 E -> K (in Ref. 2; AAH57163).
{ECO:0000305}.
CONFLICT 397 397 G -> K (in Ref. 2; AAH57163).
{ECO:0000305}.
CONFLICT 519 519 D -> G (in Ref. 1; BAC28027).
{ECO:0000305}.
STRAND 51 55 {ECO:0000244|PDB:2EQJ}.
STRAND 61 70 {ECO:0000244|PDB:2EQJ}.
TURN 71 74 {ECO:0000244|PDB:2EQJ}.
STRAND 75 80 {ECO:0000244|PDB:2EQJ}.
TURN 81 83 {ECO:0000244|PDB:2EQJ}.
STRAND 84 89 {ECO:0000244|PDB:2EQJ}.
TURN 90 92 {ECO:0000244|PDB:2EQJ}.
STRAND 105 108 {ECO:0000244|PDB:2YT5}.
STRAND 119 121 {ECO:0000244|PDB:2YT5}.
STRAND 123 125 {ECO:0000244|PDB:2YT5}.
STRAND 128 130 {ECO:0000244|PDB:2YT5}.
TURN 131 133 {ECO:0000244|PDB:2YT5}.
STRAND 134 136 {ECO:0000244|PDB:2YT5}.
HELIX 140 144 {ECO:0000244|PDB:2YT5}.
HELIX 152 156 {ECO:0000244|PDB:2YT5}.
SEQUENCE 593 AA; 66924 MW; C595438196DC3E0F CRC64;
MRDSTGAGNS LVHKRSPLRR NQKTSASLNK 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 KPTSDSREVS NGIEKKGKKK SVGRPPGPYT RKMIQKTAEL
PLDKESVSEN PTLDLPCSIG RTEGIAHSSN TSDVDLTGAS SANETTSASI SRHCGLSDSR
KRTRTGRSWP AAIPHLRRRR GRLPRRALQT QNSEVVKDDE GKEDYQFEEL NTEILNNLAD
QELQLNHLKN SITSYFGAAG RIACGEKYRV LARRVTLDGK VQYLVEWEGA TAS


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