MAZ_MOUSE
ID MAZ_MOUSE Reviewed; 477 AA.
AC P56671; Q9R1W0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Myc-associated zinc finger protein;
DE Short=MAZI;
DE AltName: Full=Pur-1;
DE AltName: Full=Purine-binding transcription factor;
GN Name=Maz;
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], AND FUNCTION.
RC TISSUE=Pancreatic tumor;
RX PubMed=1454839; DOI=10.1073/pnas.89.23.11498;
RA Kennedy G.C., Rutter W.J.;
RT "Pur-1, a zinc-finger protein which binds to purine-rich sequences,
RT activates an insulin promoter in heterologous cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11498-11502(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129; TISSUE=Liver;
RX PubMed=10092852; DOI=10.1046/j.1432-1327.1999.00081.x;
RA Song J., Murakami H., Tsutsui H., Ugai H., Geltinger C., Murata T.,
RA Matsumura M., Itakura K., Kanazawa I., Sun K., Yokoyama K.K.;
RT "Structural organization and expression of the mouse gene for Pur-1, a
RT highly conserved homolog of the human MAZ gene.";
RL Eur. J. Biochem. 259:676-683(1999).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26089202; DOI=10.1093/hmg/ddv231;
RA Ning Z., McLellan A.S., Ball M., Wynne F., O'Neill C., Mills W.,
RA Quinn J.P., Kleinjan D.A., Anney R.J., Carmody R.J., O'Keeffe G., Moore T.;
RT "Regulation of SPRY3 by X chromosome and PAR2-linked promoters in an autism
RT susceptibility region.";
RL Hum. Mol. Genet. 24:5126-5141(2015).
CC -!- FUNCTION: Transcriptional regulator (By similarity). Acts as a
CC transcriptional activator that binds to purine-rich GAGA sites found in
CC the promoter of many genes including insulin I and II and islet amyloid
CC polypeptide (PubMed:1454839). {ECO:0000250|UniProtKB:P56270,
CC ECO:0000269|PubMed:1454839}.
CC -!- SUBUNIT: Interacts with BPTF. {ECO:0000250}.
CC -!- INTERACTION:
CC P56671; P70211: Dcc; NbExp=3; IntAct=EBI-1809712, EBI-1798863;
CC P56671; P01100: FOS; Xeno; NbExp=2; IntAct=EBI-1809712, EBI-852851;
CC P56671; P05412: JUN; Xeno; NbExp=2; IntAct=EBI-1809712, EBI-852823;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26089202}.
CC -!- TISSUE SPECIFICITY: Expressed in Purkinje cells in the brain (at
CC protein level). {ECO:0000269|PubMed:26089202}.
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DR EMBL; L04649; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB006360; BAA76280.1; -; Genomic_DNA.
DR CCDS; CCDS40137.1; -.
DR PIR; A47236; A47236.
DR AlphaFoldDB; P56671; -.
DR SMR; P56671; -.
DR IntAct; P56671; 3.
DR STRING; 10090.ENSMUSP00000032916; -.
DR iPTMnet; P56671; -.
DR PhosphoSitePlus; P56671; -.
DR EPD; P56671; -.
DR MaxQB; P56671; -.
DR PaxDb; P56671; -.
DR PRIDE; P56671; -.
DR ProteomicsDB; 295962; -.
DR MGI; MGI:1338823; Maz.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; P56671; -.
DR PhylomeDB; P56671; -.
DR ChiTaRS; Maz; mouse.
DR PRO; PR:P56671; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P56671; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA: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:2001234; P:negative regulation of apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISO:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; ISO:MGI.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 6.
DR SUPFAM; SSF57667; SSF57667; 3.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..477
FT /note="Myc-associated zinc finger protein"
FT /id="PRO_0000047217"
FT ZN_FING 190..212
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 279..301
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 307..329
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 337..360
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..388
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..413
FT /note="C2H2-type 6; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..144
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56270"
FT CONFLICT 64
FT /note="Q -> QQ (in Ref. 2; BAA76280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 48770 MW; F2276C4C7538D2EF CRC64;
MFPVFPCTLL APPFPVLGLD SRGVGGLMNS FPPPQGHAQN PLQVGAELQS RFFASQGCAQ
SPFQAAPAPP PTPQAPAAEP LQVDLLPVLA AAQESAAAAA AAAAAAAAVV TAPPAPAAAS
TVDTAALKQP PAPPPPPPAV SAPAAEAAPP AAAATIAAAA ATAVVAPTST VAVAPVASVL
EKKTKSKGPY ICALCAKEFK NGYNLRRHEA IHTGAKAGRV PSGAMKMPTM VPLSLLSVPQ
LSGASGGGGE AGAGGGTTAV AAGGVVTTTA SGKRIRKNHA CEMCGKAFRD VYHLNRHKLS
HSDEKPYQCP VCQQRFKRKD RMSYHVRSHD GAVHKPYNCS HCGKSFSRPD HLNSHVRQVH
STERPFKCEK CEAAFATKDR LRAHTVRHEE KVPCHVCGKM LSSAYISDHM KVHSQGPHHV
CELCNKGTGE VCPMAAAAAA AAAAAAAVVA APPTAVGSLS GAEGVPVSSQ PLPSQPW
