ID F6PQ23_ORNAN Unreviewed; 1124 AA.
AC F6PQ23;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Zinc finger E-box binding homeobox 1 {ECO:0000313|Ensembl:ENSOANP00000009638.5};
GN Name=ZEB1 {ECO:0000313|Ensembl:ENSOANP00000009638.5};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000009638.5, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000009638.5}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000009638.5};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; F6PQ23; -.
DR STRING; 9258.ENSOANP00000009638; -.
DR Ensembl; ENSOANT00000009640.5; ENSOANP00000009638.5; ENSOANG00000006051.5.
DR eggNOG; KOG3623; Eukaryota.
DR GeneTree; ENSGT00950000183208; -.
DR HOGENOM; CLU_005890_0_1_1; -.
DR TreeFam; TF331759; -.
DR Proteomes; UP000002279; Unplaced.
DR Bgee; ENSOANG00000006051; Expressed in fibroblast and 8 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:UniProt.
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; 4.
DR Pfam; PF05605; zf-Di19; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
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; 7.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
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 185..213
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 215..242
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 255..282
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 283..312
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 920..947
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 948..975
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 976..1004
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 62..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 571..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1004..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..902
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1043..1067
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 123305 MW; 293AD494296D5773 CRC64;
MKDSYGEEGY GEADRRLTVR KVRKLIYMHH LGLLVTNYNN VVETNSDSDD EDKLHIVEEE
SVTDAADCDA SVPEDDLPTD QTVLPESSER DGNANSCWEE DGKEAKEILG PEAQADEAGR
TVKDDECDSD AENEQNHDPN VEEFLQQEDT AVIYPEAPEE DQRQGTPEAS GHDENGTPDA
FSQLLTCPYC DRGYKRFTSL KEHIKYRHEK NEDNFSCSLC SYTFAYRTQL ERHMTSHKAG
RDQRHVTQSG GNRKFKCTEC GKAFKYKHHL KEHLRIHSGE KPYECPNCKK RFSHSGSYSS
HISSKKCIGL MPVNGRARAG LKTSQCSSPS LSASPGSPTR PQIRQKIENK PLQEQLPVNQ
IKTEPVDYEF KPIVVASGIN CSTPLPNGVF SGGSQLQATS SPQGVVQAVV LPTVGLVSPI
SINLSDIQNV LKVAVDGNVI RQVLENNHAN LASKEQETIN SATLPQGGHS LISAISLPLV
DQDGTTKIII NYSLEQPSQL QVVPQNLKKE TPVPANSCKS EKLPEDLTVK SEKEKNFEGG
VNDSTCLLCD DCPGDLNALQ ELKHYDLKQP VQLPQPSGTE AEKSDPPVSS DPTDGNLSPS
QPPLKNLLSL LKAYYALNAQ PSAEELSKIA DSVNLPLDVV KKWFAKMQAG QIPVQSPEPA
SPEPGKVLAP TDNADQPETT STSEAQGSTA NPQSPLKITK SPVLPVGSTL NGSRSSTPSS
SPLNLSSSRN PPGYVYTAEG AQEDLQVEPL DLSLPKQHGE LLERSTITSV YQNSVYSVQE
EPLNLSCAKK EPQKDSCSTD SDPVVNVIPP SANPINIAIP TVTAQLPTIV AIADQNSVPC
LRALAANKQT ILIPQVAYTY STTVSPAALQ EPPSKATQPN GNQDERQDTS SEGVSNVEDQ
NDSDSTPPKK KMRKTENGMY ACDLCDKIFQ KSSSLLRHKY EHTGKRPHEC GICKKAFKHK
HHLIEHMRLH SGEKPYQCDK CGKRFSHSGS YSQHMNHRYS YCKREAEERD SPEQEEAGPE
ALNPELAGAR VSPSQIDSDE RESLTREEEE ESEKEEEEEE DKEMEELQED KESGKPQVGV
EEVEGGGKTA GTKKDEEAPN QASSVEEEIT ENGEQASEEK ASEA
//
