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