ZEB1_RAT
ID ZEB1_RAT Reviewed; 1109 AA.
AC Q62947; Q62948;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2001, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc finger E-box-binding homeobox 1;
DE AltName: Full=Transcription factor 8;
DE Short=TCF-8;
DE AltName: Full=Zinc finger homeodomain enhancer-binding protein;
DE Short=Zfhep;
GN Name=Zeb1; Synonyms=Tcf8;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-1109, AND ALTERNATIVE SPLICING.
RX PubMed=8769566; DOI=10.1089/dna.1996.15.643;
RA Cabanillas A.M., Darling D.S.;
RT "Alternative splicing gives rise to two isoforms of Zfhep, a zinc
RT finger/homeodomain protein that binds T3-response elements.";
RL DNA Cell Biol. 15:643-651(1996).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-33 AND SER-678, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts as a transcriptional repressor. Binds to E-box sequences
CC in the immunoglobulin heavy chain enhancer as well as in the regulatory
CC regions of many other tissue-specific genes. Represses E-cadherin
CC promoter and induces an epithelial-mesenchymal transition (EMT) by
CC recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence
CC of the corepressor CTBP1. Positively regulates neuronal
CC differentiation. Represses RCOR1 transcription activation during
CC neurogenesis. Represses transcription by binding to the E box (5'-
CC CANNTG-3'). Promotes tumorigenicity by repressing stemness-inhibiting
CC microRNAs (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via N-terminus) with SMARCA4/BRG1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Zfhep-1;
CC IsoId=Q62947-1; Sequence=Displayed;
CC Name=2; Synonyms=Zfhep-2;
CC IsoId=Q62947-2; Sequence=VSP_006881;
CC -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC family. {ECO:0000305}.
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DR EMBL; U51583; AAB17130.1; -; mRNA.
DR EMBL; U51584; AAB17131.1; -; mRNA.
DR RefSeq; NP_001295194.1; NM_001308265.1. [Q62947-1]
DR AlphaFoldDB; Q62947; -.
DR STRING; 10116.ENSRNOP00000024336; -.
DR iPTMnet; Q62947; -.
DR PhosphoSitePlus; Q62947; -.
DR PaxDb; Q62947; -.
DR PRIDE; Q62947; -.
DR Ensembl; ENSRNOT00000024336; ENSRNOP00000024336; ENSRNOG00000017863. [Q62947-1]
DR GeneID; 25705; -.
DR KEGG; rno:25705; -.
DR UCSC; RGD:3831; rat. [Q62947-1]
DR CTD; 6935; -.
DR RGD; 3831; Zeb1.
DR eggNOG; KOG3623; Eukaryota.
DR GeneTree; ENSGT00950000183208; -.
DR InParanoid; Q62947; -.
DR OrthoDB; 890458at2759; -.
DR PhylomeDB; Q62947; -.
DR PRO; PR:Q62947; -.
DR Proteomes; UP000002494; Chromosome 17.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003682; F:chromatin binding; IDA:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS: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:0003690; F:double-stranded DNA binding; IDA:RGD.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0008270; F:zinc ion binding; TAS:RGD.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0048513; P:animal organ development; ISO:RGD.
DR GO; GO:0051216; P:cartilage development; ISO:RGD.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; ISO:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEP:RGD.
DR GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR GO; GO:0090103; P:cochlea morphogenesis; ISO:RGD.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; ISO:RGD.
DR GO; GO:0048598; P:embryonic morphogenesis; ISO:RGD.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; ISO:RGD.
DR GO; GO:0030900; P:forebrain development; IEP:RGD.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:RGD.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; ISO:RGD.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0010464; P:regulation of mesenchymal cell proliferation; ISO:RGD.
DR GO; GO:0051150; P:regulation of smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0048752; P:semicircular canal morphogenesis; ISO:RGD.
DR CDD; cd00086; homeodomain; 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 Pfam; PF00096; zf-C2H2; 4.
DR Pfam; PF05605; zf-Di19; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Homeobox; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1109
FT /note="Zinc finger E-box-binding homeobox 1"
FT /id="PRO_0000047234"
FT ZN_FING 150..173
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 180..202
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 220..242
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 248..272
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 559..618
FT /note="Homeobox; atypical"
FT ZN_FING 881..903
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 909..931
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 937..958
FT /note="C2H2-type 7; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..1109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..307
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..566
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1065
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT MOD_RES 678
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 680
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT MOD_RES 682
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 311
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 473
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 484
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 495
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 528
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 752
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 752
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT VAR_SEQ 1..198
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_006881"
SQ SEQUENCE 1109 AA; 121627 MW; BEFE291C8795DDA6 CRC64;
MADGPRCKRR KQANPRRNNV TNYNTVVEAN SDSDDEDKLH IVEEESVTDA ADCEGGVPDD
ELPTDQTVLP GGSDRAGSAK NCWQDDVKDD ECDSDAENEQ NHDPNVEEFL QQQDTAVIYP
EAPEEDQRQG TPEASGHDDN GTPDAFSQLL TCPYCDRGYK RFTSLKEHIK YRHEKNEDNF
SCSLCSYTFA YRTQLERHMT SHKSGREQRH VTQSGGNRKF KCTECGKAFK YKHHLKEHLR
IHSGEKPYEC PNCKKRFSHS GSYSSHISSK KCISLMPVNG RPRSGLKTSQ CSSPSLSTSP
GSPTRPQIRQ KIENKPLQEP LSVNQIKTEP VDYEFKPIVV ASGINCSTPL QNGVFSGGGQ
LQATSSPQGV VQAVVLPTVG LVSPISINLS DIQNVLKVAV DGNIIRQVLE NNQASLASKE
QEAVSASSIQ QGGHSVISAI SLPLVDQDGT TKIIINYSLE QPGQLQVVPQ NLKKENPAPP
KSCKSEKSPE DLTVKSEKDK SFDGAADEST CLLCEDCPGD LNALPELKHY DPEHPAQPPP
PAPATEKPES SASSAGNGDL SPSQPPLKNL LSLLKAYYAL NAQPSTEELT KIADSVNLPL
DVVKKWFEKM QAGQIPGQSL EPPSPGPGSG NIPAKTEEQP QPVDGNEPQE DSTRGQSPLK
MTSSPVLPVG SAINGSRSCT SSPSPLNLSS ARNPQGYSCV SEGTQEEPQV EPLDLSLPKQ
QGELLERSTV SSVYQNSVYS VQEEPLNLSC AKKEPQKDSC VTDSEPVVNV VPPSANPINI
AIPTVTAQLP TIVAIADQNS VPCLRALAAN KQTILIPQVA YTYSATVSPA MQEPPVKVIQ
PNGNQDERQD TSSEGVSVED QNDSDCTPPK KKTRKAENGM YACDLCDKIF QKSSSLLRHK
YEHTGKRPHE CGICRKAFKH KHHLIEHMRL HSGEKPYQCD KCGKRFSHSG SYSQHMNHRY
SYCKRGAEDR DAMEQEDTGP EALPEVLPTE LVGARASPSQ ADSDERESLT REEDEDSEKE
EEEEDKEMEE LQEDKECENP QEEEEEEEEE EEEEEEEEEE EAEEAEHEAA AAKTGGAVEE
EAAQQAGSFQ QKASGSESKR LSEEKTNEA
