MAZ_MESAU
ID MAZ_MESAU Reviewed; 331 AA.
AC P56670;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Myc-associated zinc finger protein;
DE Short=MAZI;
DE AltName: Full=Pur-1;
DE AltName: Full=Purine-binding transcription factor;
DE Flags: Fragment;
GN Name=MAZ;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Pancreas;
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).
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 -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
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DR EMBL; L06008; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; B47236; B47236.
DR AlphaFoldDB; P56670; -.
DR STRING; 10036.XP_005064433.1; -.
DR eggNOG; KOG1721; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 2: Evidence at transcript level;
KW Activator; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN <1..>331
FT /note="Myc-associated zinc finger protein"
FT /id="PRO_0000047216"
FT ZN_FING 177..199
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 266..288
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..316
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 324..>331
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 46..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..131
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT NON_TER 331
SQ SEQUENCE 331 AA; 33374 MW; 0482F1AF43264B32 CRC64;
FPVLGLDSRG VGGLMNSFPP PQGHAQNPLQ VGAELQSRFF ASQGCAQSPF QAAPAPPPTP
QAPAAEPLQV DLLPVLAAAQ ESAAAAAAAA AAAAAVVTAP PAPAAASTVD TAALKQPPAP
PPPPPAVSAP AAEAAPPAAA ATIAAAAATA VVAPTSTVAV APVASVLEKK TKSKGPYICA
LCAKEFKNGY NLRRHEAIHT GAKAGRVPSG AMKMPTMVPL SLLSVPQLSG ASGGGGEAGA
GGGTTAVAAG GVVTTTASGK RIRKNHACEM CGKAFRDVYH LNRHKLSHSD EKPYQCPVCQ
QRFKRKDRMS YHVRSHDGAV HKPYNCSHCG K