ZBT32_MOUSE
ID ZBT32_MOUSE Reviewed; 465 AA.
AC Q9JKD9; Q9D523;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Zinc finger and BTB domain-containing protein 32;
DE AltName: Full=Repressor of GATA;
DE AltName: Full=Testis zinc finger protein;
GN Name=Zbtb32; Synonyms=Rog, Tzfp;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION
RP WITH GATA3.
RX PubMed=10755619; DOI=10.1016/s1074-7613(00)80185-5;
RA Miaw S.-C., Choi A., Yu E., Kishikawa H., Ho I.-C.;
RT "ROG, repressor of GATA, regulates the expression of cytokine genes.";
RL Immunity 12:323-333(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND FUNCTION.
RC STRAIN=129/SvJ; TISSUE=Testis;
RX PubMed=11279021; DOI=10.1074/jbc.m100170200;
RA Tang C.J., Chuang C.K., Hu H.M., Tang T.K.;
RT "The zinc finger domain of Tzfp binds to the tbs motif located at the
RT upstream flanking region of the Aie1 (aurora-C) kinase gene.";
RL J. Biol. Chem. 276:19631-19639(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP STRUCTURE BY NMR OF 348-428, DNA-BINDING, AND ZINC-BINDING.
RX PubMed=20544958; DOI=10.1002/prot.22732;
RA Chou C.C., Lou Y.C., Tang T.K., Chen C.;
RT "Structure and DNA binding characteristics of the three-Cys2His2 domain of
RT mouse testis zinc finger protein.";
RL Proteins 78:2202-2212(2010).
CC -!- FUNCTION: DNA-binding protein that binds to the to a 5'-TGTACAGTGT-3'
CC core sequence. May function as a transcriptional transactivator and
CC transcriptional repressor (By similarity). Probably exerts its
CC repressor effect by preventing GATA3 from binding to DNA. May play a
CC role in regulating the differentiation and activation of helper T-
CC cells. {ECO:0000250, ECO:0000269|PubMed:11279021}.
CC -!- SUBUNIT: Homodimer (via PTB domain). Interacts with the N-terminal of
CC FANCC. Interacts with ZBTB16 (By similarity). Interacts with GATA3.
CC {ECO:0000250, ECO:0000269|PubMed:10755619}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Located in nuclear speckles.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JKD9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JKD9-2; Sequence=VSP_022552;
CC -!- TISSUE SPECIFICITY: Isoform 1 is testis-specific and is not expressed
CC in lymphoid organs such as thymus or spleen. Isoform 2 is expressed in
CC both B- and T-lymphoid cells. {ECO:0000269|PubMed:10755619}.
CC -!- DOMAIN: The C-terminal zinc finger domain functions as a
CC transcriptional transactivator.
CC -!- DOMAIN: The BTB (POZ) domain possesses repressor activity.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF241232; AAF61244.1; -; mRNA.
DR EMBL; AY015272; AAK13198.1; -; Genomic_DNA.
DR EMBL; AK015881; BAB30015.1; -; mRNA.
DR CCDS; CCDS21102.1; -. [Q9JKD9-1]
DR RefSeq; NP_067372.2; NM_021397.2.
DR PDB; 2KVF; NMR; -; A=348-374.
DR PDB; 2KVG; NMR; -; A=402-428.
DR PDB; 2KVH; NMR; -; A=375-401.
DR PDBsum; 2KVF; -.
DR PDBsum; 2KVG; -.
DR PDBsum; 2KVH; -.
DR AlphaFoldDB; Q9JKD9; -.
DR BMRB; Q9JKD9; -.
DR SMR; Q9JKD9; -.
DR BioGRID; 208389; 1.
DR STRING; 10090.ENSMUSP00000103786; -.
DR iPTMnet; Q9JKD9; -.
DR PhosphoSitePlus; Q9JKD9; -.
DR EPD; Q9JKD9; -.
DR MaxQB; Q9JKD9; -.
DR PaxDb; Q9JKD9; -.
DR PRIDE; Q9JKD9; -.
DR ProteomicsDB; 275053; -. [Q9JKD9-1]
DR ProteomicsDB; 275054; -. [Q9JKD9-2]
DR Antibodypedia; 35117; 183 antibodies from 25 providers.
DR DNASU; 58206; -.
DR Ensembl; ENSMUST00000108150; ENSMUSP00000103785; ENSMUSG00000006310. [Q9JKD9-2]
DR GeneID; 58206; -.
DR KEGG; mmu:58206; -.
DR UCSC; uc009gfi.1; mouse. [Q9JKD9-2]
DR CTD; 27033; -.
DR MGI; MGI:1891838; Zbtb32.
DR VEuPathDB; HostDB:ENSMUSG00000006310; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000162716; -.
DR HOGENOM; CLU_002678_42_18_1; -.
DR InParanoid; Q9JKD9; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9JKD9; -.
DR BioGRID-ORCS; 58206; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Zbtb32; mouse.
DR EvolutionaryTrace; Q9JKD9; -.
DR PRO; PR:Q9JKD9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JKD9; protein.
DR Bgee; ENSMUSG00000006310; Expressed in spermatocyte and 62 other tissues.
DR ExpressionAtlas; Q9JKD9; baseline and differential.
DR Genevisible; Q9JKD9; MM.
DR GO; GO:0000228; C:nuclear chromosome; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0001817; P:regulation of cytokine production; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
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; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF54695; SSF54695; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS50097; BTB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..465
FT /note="Zinc finger and BTB domain-containing protein 32"
FT /id="PRO_0000273418"
FT DOMAIN 29..87
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT ZN_FING 350..372
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 378..400
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..427
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 111..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..364
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022552"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:2KVF"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:2KVF"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:2KVF"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:2KVF"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:2KVH"
FT STRAND 386..389
FT /evidence="ECO:0007829|PDB:2KVH"
FT HELIX 390..399
FT /evidence="ECO:0007829|PDB:2KVH"
FT STRAND 405..407
FT /evidence="ECO:0007829|PDB:2KVG"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:2KVG"
FT STRAND 412..415
FT /evidence="ECO:0007829|PDB:2KVG"
FT HELIX 417..424
FT /evidence="ECO:0007829|PDB:2KVG"
SQ SEQUENCE 465 AA; 50828 MW; D72E83AB3661F403 CRC64;
MPQTPTRLVS PYGSDRLVQL AARLRPALCD TLITVGGLEF PAHSLVLAGA SPRLGCRGRW
ALVEDISPST FAQILTFVYG ESIELQPGEL GDLEEAAKAL GVQALEEACQ RAQKGKDEDE
LDPGLKRHQQ SEDFMRGSER GLGSPGEKQK PEKDFRSNGR EQEMSHKHKA PGERPEMAGA
TRMMSSEEVM RGIESHKGSE ESLRGCPDPL SPPGSLLTSL IPRPWWAEVP RLGEGQSALW
SILLWPSRYG APFSHSTPIT AAWQVRPQDQ RIPLTLNHSK ALWSQNQLAS SSPTPGSFPQ
GTESLSPWQI ETSGQGFTGT LATCVSQERT LNCPSHQHPP LPSPARSRPY SCSVCGKRFS
LKHQMETHYR VHTGEKPFSC SLCPQRSRDF SAMTKHLRTH GAAPYRCPLC RAGCPSLASM
QAHMRGHSPS RLPPGWTIRS TFLYSSSRPT RASSSPGSPT SSAAT
