ID   Q3T921_RAT              Unreviewed;      1215 AA.
AC   Q3T921;
DT   11-OCT-2005, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2005, sequence version 1.
DT   27-MAR-2024, entry version 121.
DE   SubName: Full=Zfhx1b zinc finger homeobox 1b {ECO:0000313|EMBL:CAJ29798.1};
GN   Name=Zeb2 {ECO:0000313|RGD:1307272};
GN   Synonyms=Zfhx1b {ECO:0000313|RGD:1307272}, Zfhxib
GN   {ECO:0000313|EMBL:CAJ29798.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:CAJ29798.1};
RN   [1] {ECO:0000313|EMBL:CAJ29798.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Sprague Dawley {ECO:0000313|EMBL:CAJ29798.1};
RC   TISSUE=Retina {ECO:0000313|EMBL:CAJ29798.1};
RA   Carter D.A.;
RT   "Role of Zfhx1b in rat development.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC       family. {ECO:0000256|ARBA:ARBA00009867}.
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DR   EMBL; AM084708; CAJ29798.1; -; mRNA.
DR   RefSeq; NP_001028873.1; NM_001033701.1.
DR   AlphaFoldDB; Q3T921; -.
DR   SMR; Q3T921; -.
DR   iPTMnet; Q3T921; -.
DR   PhosphoSitePlus; Q3T921; -.
DR   GeneID; 311071; -.
DR   KEGG; rno:311071; -.
DR   UCSC; RGD:1307272; rat.
DR   AGR; RGD:1307272; -.
DR   CTD; 9839; -.
DR   RGD; 1307272; Zeb2.
DR   OrthoDB; 4266655at2759; -.
DR   PhylomeDB; Q3T921; -.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070412; F:R-SMAD binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR   GO; GO:0048143; P:astrocyte activation; IDA:RGD.
DR   GO; GO:0021846; P:cell proliferation in forebrain; ISO:RGD.
DR   GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR   GO; GO:0048668; P:collateral sprouting; ISO:RGD.
DR   GO; GO:0021540; P:corpus callosum morphogenesis; ISO:RGD.
DR   GO; GO:0021957; P:corticospinal tract morphogenesis; ISO:RGD.
DR   GO; GO:0048066; P:developmental pigmentation; ISO:RGD.
DR   GO; GO:0048598; P:embryonic morphogenesis; ISO:RGD.
DR   GO; GO:0043542; P:endothelial cell migration; IMP:RGD.
DR   GO; GO:0001935; P:endothelial cell proliferation; IMP:RGD.
DR   GO; GO:0072537; P:fibroblast activation; IDA:RGD.
DR   GO; GO:0021766; P:hippocampus development; ISO:RGD.
DR   GO; GO:0061373; P:mammillary axonal complex development; ISO:RGD.
DR   GO; GO:0097324; P:melanocyte migration; ISO:RGD.
DR   GO; GO:0036446; P:myofibroblast differentiation; IEP:RGD.
DR   GO; GO:0010764; P:negative regulation of fibroblast migration; IDA:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0001755; P:neural crest cell migration; ISO:RGD.
DR   GO; GO:0001843; P:neural tube closure; ISO:RGD.
DR   GO; GO:0050772; P:positive regulation of axonogenesis; ISO:RGD.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
DR   GO; GO:1902748; P:positive regulation of lens fiber cell differentiation; ISO:RGD.
DR   GO; GO:0045636; P:positive regulation of melanocyte differentiation; ISO:RGD.
DR   GO; GO:1904330; P:positive regulation of myofibroblast contraction; IDA:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISO:RGD.
DR   GO; GO:0070269; P:pyroptosis; IDA:RGD.
DR   GO; GO:1905603; P:regulation of blood-brain barrier permeability; IMP:RGD.
DR   GO; GO:1903056; P:regulation of melanosome organization; ISO:RGD.
DR   GO; GO:1904520; P:regulation of myofibroblast cell apoptotic process; IMP:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0090649; P:response to oxygen-glucose deprivation; IMP:RGD.
DR   GO; GO:0001756; P:somitogenesis; ISO:RGD.
DR   GO; GO:0043149; P:stress fiber assembly; IMP:RGD.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 6.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR   InterPro; IPR008598; Di19_Zn-bd.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24391; HISTONE H4 TRANSCRIPTION FACTOR-RELATED; 1.
DR   PANTHER; PTHR24391:SF18; ZINC FINGER PROTEIN 1; 1.
DR   Pfam; PF00096; zf-C2H2; 3.
DR   Pfam; PF05605; zf-Di19; 1.
DR   Pfam; PF12874; zf-met; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM00355; ZnF_C2H2; 8.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
DR   Genevisible; Q3T921; RN.
PE   2: Evidence at transcript level;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000313|EMBL:CAJ29798.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00042}.
FT   DOMAIN          211..239
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          241..263
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          282..309
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          999..1026
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1027..1054
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          1055..1083
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          1..111
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..740
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          769..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          831..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1117..1215
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..52
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..96
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        702..727
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        778..810
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..857
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1125..1157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1172..1209
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1215 AA;  136498 MW;  C18AFA412EF4C506 CRC64;
     MKQPIMADGP RCKRRKQANP RRKNVVNYDN VVDAGSETDE EDKLHIAEDD GIANPLDQET
     SPASMPNHES SPHMSQGLLP REEEEDEIRE SVVEHSWHSG EILQASVDGP EEMKEDYDAL
     GPEATIQTTI NNGTVKNANC TSDFEEYFAK RKLEERDGHA VSIEEYLQRS DTAIIYPEAP
     EELSRLGTPE ANGQEENDLP PGTPDAFAQL LTCPYCDRGY KRLTSLKEHI KYRHEKNEEN
     FSCPLCSYTF AYRTQLERHM VTHKPGTDQH QMLTQGAGNR KFKCTECGKA FKYKHHLKEH
     LRIHSGEKPY ECPNCKKRFS HSGSYSSHIS SKKCIGLISV NGRMRNNIKT GSSPNSVSSS
     PTNSAITQLR NKLENGKPLS MSEQTGLLKI KTEPLDFNDY KVLMATHGFS GTSPFMNGGL
     GATSPLGVHP SAQSPMQHLG VGLEAPLLGF PTMNSNLSEV QKVLQIVDNT VSRQKMDCKT
     EDISKLKGYH MKDPCSQPEE QGVTSPSIPA VGLPVVSHNG ATKSIIDYTL EKVNEAKACL
     QSLTTDSRRQ ISNIKKEKLR TLIDLVTDDK MIENHSIPTP FSCQFCKESF PGPIPLHQHE
     RYLCKMNEEI KAVLQPHENI VPNKAGVFVD NKALLLSSVL SEKGLTSPIN PYKDHMSVLK
     AYYAMNMEPN SDELLKISIA VGLPQEFVKE WFEQRKVYQY SSSRSPSLER NSKPLAPNSN
     PTTKDSLLPR SPVKPMDSIT SPSIAELHNS VTSCDPPLRL TKSSHFTNTK AVDKLDHSRS
     NTPSPLNLSS TSSKNSHSSS YTPNSFSSEE LQAEPLDLSL PKQMREPKSI IATKNKTKAT
     SISLDHNSVS SSSENSDEPL NLTFIKKEFS NSNNLDNKST NPVFGMNPFS AKPLYTALPP
     QSAFPPATFM PPVQTSIPGL RPYPGLDQMS FLPHMAYTYP TGAATFADMQ QRRKYQRKQG
     FQGELLDGAQ DYMSGLDDLT DSDSCLSRKK IKKTESGMYA CDLCDKTFQK SSSLLRHKYE
     HTGKRPHQCQ ICKKAFKHKH HLIEHSRLHS GEKPYQCDKC GKRFSHSGSY SQHMNHRYSY
     CKREAEEREA AEREAREKGH LEPTELLMNR AYLQSITPQG YSDSEERESM PRDGESEKEH
     EKEGEEGYGK LRRRDGDEEE EEEEEESENK SMDTDPETIR DEEETGDHSM DDSSEDGKME
     TKSDHEEDNM EDGME
//