MTF1_MOUSE
ID MTF1_MOUSE Reviewed; 675 AA.
AC Q07243; Q9JJW8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Metal regulatory transcription factor 1;
DE AltName: Full=MRE-binding transcription factor;
DE AltName: Full=Transcription factor MTF-1;
GN Name=Mtf1; Synonyms=Mtf-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8467794; DOI=10.1002/j.1460-2075.1993.tb05780.x;
RA Radtke F., Heuchel R., Georgiev O., Hergersberg M., Gariglio M., Dembic Z.,
RA Schaffner W.;
RT "Cloned transcription factor MTF-1 activates the mouse metallothionein I
RT promoter.";
RL EMBO J. 12:1355-1362(1993).
RN [2]
RP SEQUENCE REVISION.
RA Radtke F.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=11005378; DOI=10.1379/1466-1268(2000)005<0196:cotmgf>2.0.co;2;
RA Auf der Maur A., Belser T., Wang Y., Gunes C., Lichtlen P., Georgiev O.,
RA Schaffner W.;
RT "Characterization of the mouse gene for the heavy metal-responsive
RT transcription factor MTF-1.";
RL Cell Stress Chaperones 5:196-206(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-5, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24529376; DOI=10.1016/j.cell.2014.01.007;
RA Kim J.H., Jeon J., Shin M., Won Y., Lee M., Kwak J.S., Lee G., Rhee J.,
RA Ryu J.H., Chun C.H., Chun J.S.;
RT "Regulation of the catabolic cascade in osteoarthritis by the zinc-ZIP8-
RT MTF1 axis.";
RL Cell 156:730-743(2014).
CC -!- FUNCTION: Zinc-dependent transcriptional regulator of cellular adaption
CC to conditions of exposure to heavy metals (PubMed:24529376). Binds to
CC metal responsive elements (MRE) in promoters and activates the
CC transcription of metallothionein genes like metallothionein-2/MT2A (By
CC similarity). Also regulates the expression of metalloproteases in
CC response to intracellular zinc and functions as a catabolic regulator
CC of cartilages (PubMed:24529376). {ECO:0000250|UniProtKB:Q14872,
CC ECO:0000269|PubMed:24529376}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24529376}. Cytoplasm
CC {ECO:0000269|PubMed:24529376}. Note=Translocation to the nucleus is
CC induced by metals. {ECO:0000269|PubMed:24529376}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11005378}.
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DR EMBL; X71327; CAA50470.1; -; mRNA.
DR EMBL; AJ251880; CAB71344.1; -; Genomic_DNA.
DR EMBL; AL606933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30350.1; -; Genomic_DNA.
DR EMBL; BC017679; AAH17679.1; -; mRNA.
DR CCDS; CCDS18627.1; -.
DR PIR; S35335; S35335.
DR RefSeq; NP_032662.3; NM_008636.4.
DR AlphaFoldDB; Q07243; -.
DR SMR; Q07243; -.
DR BioGRID; 201591; 4.
DR IntAct; Q07243; 3.
DR STRING; 10090.ENSMUSP00000030723; -.
DR iPTMnet; Q07243; -.
DR PhosphoSitePlus; Q07243; -.
DR MaxQB; Q07243; -.
DR PaxDb; Q07243; -.
DR PRIDE; Q07243; -.
DR ProteomicsDB; 287632; -.
DR Antibodypedia; 17617; 231 antibodies from 29 providers.
DR DNASU; 17764; -.
DR Ensembl; ENSMUST00000030723; ENSMUSP00000030723; ENSMUSG00000028890.
DR Ensembl; ENSMUST00000106193; ENSMUSP00000101799; ENSMUSG00000028890.
DR GeneID; 17764; -.
DR KEGG; mmu:17764; -.
DR UCSC; uc008urb.2; mouse.
DR CTD; 4520; -.
DR MGI; MGI:101786; Mtf1.
DR VEuPathDB; HostDB:ENSMUSG00000028890; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157291; -.
DR HOGENOM; CLU_026685_0_0_1; -.
DR InParanoid; Q07243; -.
DR OMA; SMFQSPD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q07243; -.
DR TreeFam; TF106493; -.
DR BioGRID-ORCS; 17764; 11 hits in 72 CRISPR screens.
DR ChiTaRS; Mtf1; mouse.
DR PRO; PR:Q07243; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q07243; protein.
DR Bgee; ENSMUSG00000028890; Expressed in spermatid and 253 other tissues.
DR ExpressionAtlas; Q07243; baseline and differential.
DR Genevisible; Q07243; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:1990079; P:cartilage homeostasis; IMP:UniProtKB.
DR GO; GO:0071294; P:cellular response to zinc ion; IDA:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0046686; P:response to cadmium ion; IMP:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR InterPro; IPR029796; Metal_TF1.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR19818:SF131; PTHR19818:SF131; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17242355"
FT CHAIN 2..675
FT /note="Metal regulatory transcription factor 1"
FT /id="PRO_0000047221"
FT ZN_FING 139..163
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 169..193
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 199..223
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 228..252
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 258..282
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 288..312
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 427..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 132..137
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 432..450
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..675
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14872"
FT CONFLICT 603
FT /note="A -> T (in Ref. 1; CAA50470)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 675 AA; 72603 MW; 3FD37F1736D07FC6 CRC64;
MGEHSPDDNI IFFKGEEDDL TPHDKMLRFV DDNGLVPSSS GTVYDRTTVL IEQDPGTLED
DEDDGQCGEP LPFLVEGEEG FLIDQEAMSQ GYVQHIISPD QIHLTINPGS TPMPRNIEGA
TLTLQSECPE TKRKEVKRYQ CTFEGCPRTY STAGNLRTHQ KTHRGEYTFV CNQEGCGKAF
LTSYSLRIHV RVHTKEKPFE CDVQGCEKAF NTLYRLKAHQ RLHTGKTFNC ESQGCSKYFT
TLSDLRKHIR THTGEKPFRC DHDGCGKAFA ASHHLKTHVR THTGERPFFC PSNGCEKTFS
TQYSLKSHMK GHDNKGTAYS ALPQHNGSED TNHSLYLSEL GLLSTDSELQ ENSSSTQDQD
LSTISPAIIF ESMFQNSDDP GIQDDPLQTA ALIDSFNGDA ESVIDVPPPA GNSASLSLPL
VLQSGISEPP QPLLPATAPS APPPAPSLGP GSQPAAFGSP PALLQPPEVP VPHSTQFAAN
HQEFLPHPQA PPQTIVPGLS VVAGAPASAA TVASAVAAPA PPQSTTEPLP AMVQTLPLGA
NSVLTNNPTI TITPTPNTAI LQSSLVMGEQ NLQWILNGAT SSPQNQEQIQ QASKVEQVYF
ATAVPVASGT GSSVQQIGLS VPVIIIKQEE ACQCQCACRD SAKERAAGRR KGCSSPPPPE
PNPQPPDGPS LQLPP
