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PATZ1_MOUSE
ID   PATZ1_MOUSE             Reviewed;         687 AA.
AC   Q5NBY9;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=POZ (BTB) and AT hook-containing zinc finger 1 {ECO:0000305};
DE   AltName: Full=BTB/POZ domain zinc finger transcription factor;
DE   AltName: Full=Protein kinase A RI subunit alpha-associated protein;
DE   AltName: Full=Zinc finger and BTB domain-containing protein 19;
DE   AltName: Full=Zinc finger protein 278;
GN   Name=Patz1 {ECO:0000312|MGI:MGI:1891832};
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 [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   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=18241078; DOI=10.1002/path.2323;
RA   Fedele M., Franco R., Salvatore G., Paronetto M.P., Barbagallo F., Pero R.,
RA   Chiariotti L., Sette C., Tramontano D., Chieffi G., Fusco A., Chieffi P.;
RT   "PATZ1 gene has a critical role in the spermatogenesis and testicular
RT   tumours.";
RL   J. Pathol. 215:39-47(2008).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=22886576; DOI=10.1002/jcp.24174;
RA   Valentino T., Palmieri D., Vitiello M., Simeone A., Palma G., Arra C.,
RA   Chieffi P., Chiariotti L., Fusco A., Fedele M.;
RT   "Embryonic defects and growth alteration in mice with homozygous disruption
RT   of the Patz1 gene.";
RL   J. Cell. Physiol. 228:646-653(2013).
RN   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=33898458; DOI=10.3389/fcell.2021.657149;
RA   Mancinelli S., Vitiello M., Donnini M., Mantile F., Palma G., Luciano A.,
RA   Arra C., Cerchia L., Liguori G.L., Fedele M.;
RT   "The Transcription Regulator Patz1 Is Essential for Neural Stem Cell
RT   Maintenance and Proliferation.";
RL   Front. Cell Dev. Biol. 9:657149-657149(2021).
RN   [5] {ECO:0007744|PDB:6GUV}
RP   X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) OF 12-166, AND SUBUNIT.
RX   PubMed=32496219; DOI=10.1107/s2059798320005355;
RA   Piepoli S., Alt A.O., Atilgan C., Mancini E.J., Erman B.;
RT   "Structural analysis of the PATZ1 BTB domain homodimer.";
RL   Acta Crystallogr. D 76:581-593(2020).
CC   -!- FUNCTION: Transcriptional regulator that plays a role in many
CC       biological processes such as embryogenesis, senescence, T-cell
CC       development or neurogenesis (PubMed:18241078, PubMed:22886576,
CC       PubMed:33898458). Interacts with the TP53 protein to control genes that
CC       are important in proliferation and in the DNA-damage response.
CC       Mechanistically, the interaction inhibits the DNA binding and
CC       transcriptional activity of TP53/p53 (By similarity). Part of the
CC       transcriptional network modulating regulatory T-cell development and
CC       controls the generation of the regulatory T-cell pool under homeostatic
CC       conditions (By similarity). {ECO:0000250|UniProtKB:Q9HBE1,
CC       ECO:0000269|PubMed:18241078, ECO:0000269|PubMed:22886576,
CC       ECO:0000269|PubMed:33898458}.
CC   -!- SUBUNIT: Homodimer (PubMed:32496219). Interacts with RNF4. Interacts
CC       (via C-terminus) with TP53; this interaction inhibits TP53 ability to
CC       activate transcription (By similarity). {ECO:0000250|UniProtKB:Q9HBE1,
CC       ECO:0000269|PubMed:32496219}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18241078}.
CC   -!- TISSUE SPECIFICITY: Widely expressed at high levels during
CC       embryogenesis, especially in the central nervous system, especially to
CC       the actively proliferating neuroblasts in the periventricular
CC       neocortical neuroepithelium, in the telencephalic cortical plate and in
CC       the hippocampus (PubMed:22886576). Also expressed in a stage-specific
CC       manner in the mouse germinal epithelium (PubMed:18241078). While
CC       strongly expressed during brain development,m its expression turns down
CC       in adult brain (PubMed:33898458). {ECO:0000269|PubMed:18241078,
CC       ECO:0000269|PubMed:22886576, ECO:0000269|PubMed:33898458}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice mostly die in utero or soon after
CC       birth likely because of developmental defects in the cardiac outflow
CC       tract and/or neural tube closure (PubMed:22886576, PubMed:33898458).
CC       Few mice that reach the adult life, equally distributed between males
CC       and females, show a dwarf phenotype likely due to defects in cell
CC       proliferation (PubMed:22886576). Deletion gene also results in
CC       disruption of the testis cytoarchitecture and block of spermatogenesis
CC       (PubMed:18241078). {ECO:0000269|PubMed:18241078,
CC       ECO:0000269|PubMed:22886576, ECO:0000269|PubMed:33898458}.
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DR   EMBL; AL671968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PDB; 6GUV; X-ray; 2.29 A; A=12-166.
DR   PDBsum; 6GUV; -.
DR   AlphaFoldDB; Q5NBY9; -.
DR   SMR; Q5NBY9; -.
DR   MaxQB; Q5NBY9; -.
DR   PeptideAtlas; Q5NBY9; -.
DR   PRIDE; Q5NBY9; -.
DR   ProteomicsDB; 348899; -.
DR   Antibodypedia; 25019; 175 antibodies from 24 providers.
DR   Ensembl; ENSMUST00000110043; ENSMUSP00000105670; ENSMUSG00000020453.
DR   MGI; MGI:1891832; Patz1.
DR   VEuPathDB; HostDB:ENSMUSG00000020453; -.
DR   GeneTree; ENSGT00940000159296; -.
DR   InParanoid; Q5NBY9; -.
DR   OMA; KFACGEC; -.
DR   PhylomeDB; Q5NBY9; -.
DR   ChiTaRS; Patz1; mouse.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5NBY9; protein.
DR   Bgee; ENSMUSG00000020453; Expressed in dorsal pancreas and 197 other tissues.
DR   ExpressionAtlas; Q5NBY9; baseline and differential.
DR   GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central.
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:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR   GO; GO:0008584; P:male gonad development; IMP:MGI.
DR   GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IPI:MGI.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0030217; P:T cell differentiation; IDA:MGI.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF57667; SSF57667; 4.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00354; HMGI_Y; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE   1: Evidence at protein level;
KW   3D-structure; Metal-binding; Nucleus; Reference proteome; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..687
FT                   /note="POZ (BTB) and AT hook-containing zinc finger 1"
FT                   /id="PRO_0000453933"
FT   DOMAIN          41..130
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         292..314
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         355..377
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         383..405
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         413..436
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         442..464
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         495..517
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         605..628
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          250..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          564..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   STRAND          16..19
FT                   /evidence="ECO:0007829|PDB:6GUV"
FT   HELIX           22..35
FT                   /evidence="ECO:0007829|PDB:6GUV"
FT   STRAND          43..47
FT                   /evidence="ECO:0007829|PDB:6GUV"
FT   STRAND          50..54
FT                   /evidence="ECO:0007829|PDB:6GUV"
FT   HELIX           56..62
FT                   /evidence="ECO:0007829|PDB:6GUV"
FT   HELIX           64..72
FT                   /evidence="ECO:0007829|PDB:6GUV"
FT   HELIX           111..123
FT                   /evidence="ECO:0007829|PDB:6GUV"
FT   HELIX           133..143
FT                   /evidence="ECO:0007829|PDB:6GUV"
FT   HELIX           146..158
FT                   /evidence="ECO:0007829|PDB:6GUV"
SQ   SEQUENCE   687 AA;  74119 MW;  75145E415EC27D50 CRC64;
     MERVNDASCG PSGCYTYQVS RHSTEMLHNL NQQRKNGGRF CDVLLRVGDE SFPAHRAVLA
     ACSEYFESVF SAQLGDGGAA DGGPADVGGA AAAPGGGAGG SRELEMHTIS SKVFGDILDF
     AYTSRIVVRL ESFPELMTAA KFLLMRSVIE ICQEVIKQSN VQILVPPARA DIMLFRPPGT
     SDLGFPLDMT NGAAMAANSN GIAGSMQPEE EAARATGAAI AGQASLPVLP GVDRLPMVAG
     PLSPQLLTSP FPNVASSAPP LTSKRGRGRP RKANLLDSMF GSPGGLREAG ILPCGLCGKV
     FTDANRLRQH EAQHGVTSLQ LGYIDLPPPR LGENGLPISE DPDGPRKRSR TRKQVACEIC
     GKIFRDVYHL NRHKLSHSGE KPYSCPVCGL RFKRKDRMSY HVRSHDGSVG KPYICQSCGK
     GFSRPDHLNG HIKQVHTSER PHKCQTCNAS FATRDRLRSH LACHEDKVPC QVCGKYLRAA
     YMADHLKKHS EGPSNFCSIC NRGFSSASYL KVHVKTHHGV PLPQVSRHQE PILNGGAAFH
     CARTYGNKEG QKCSHQDLIE SSDSYGDLSD ASDLKTPEKQ SANGSFSCDV AVPKNKMESD
     GEKKYPCPEC GSFFRSKSYL NKHIQKVHVR ALGGPLGDLG PALGSPFSPQ QNMSLLESFG
     FQIVQSAFAS SLVDPEVDQQ PMGPEGK
 
 
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