GenomeNet

Database: UniProt
Entry: F1RWD4_PIG
LinkDB: F1RWD4_PIG
Original site: F1RWD4_PIG 
ID   F1RWD4_PIG              Unreviewed;      1060 AA.
AC   F1RWD4;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 4.
DT   27-MAR-2024, entry version 72.
DE   SubName: Full=Zinc finger E-box binding homeobox 1 {ECO:0000313|Ensembl:ENSSSCP00000011759.4};
GN   Name=ZEB1 {ECO:0000313|Ensembl:ENSSSCP00000011759.4,
GN   ECO:0000313|VGNC:VGNC:95536};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000011759.4, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000011759.4, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000011759.4,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSSSCP00000011759.4}
RP   IDENTIFICATION.
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; F1RWD4; -.
DR   PaxDb; 9823-ENSSSCP00000023082; -.
DR   Ensembl; ENSSSCT00000012067.5; ENSSSCP00000011759.4; ENSSSCG00000011025.6.
DR   VGNC; VGNC:95536; ZEB1.
DR   eggNOG; KOG3623; Eukaryota.
DR   GeneTree; ENSGT00950000183208; -.
DR   ChiTaRS; LOC100520325; pig.
DR   Proteomes; UP000008227; Chromosome 10.
DR   Bgee; ENSSSCG00000011025; Expressed in stomach and 42 other cell types or tissues.
DR   ExpressionAtlas; F1RWD4; baseline and differential.
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; 6.
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:UP000008227};
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          103..131
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          133..160
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          173..200
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          837..864
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          865..892
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          893..921
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..647
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          790..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          923..1060
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..260
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..440
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        441..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..647
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..819
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        959..981
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        990..1015
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1043..1060
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1060 AA;  115974 MW;  4D7BD1BCF011C4FD CRC64;
     MADGPRCKRR KQANPRRNNG KEGQEILGPE ARAEEVGCTV KDDECDSDAE NEQNHDPNVE
     EFLQQQDTAV IYPEAPEEDQ RQGTPEASGH DENGTPDAFS QLLTCPYCDR GYKRFTSLKE
     HIKYRHEKNE DNFSCSLCSY TFAYRTQLER HMTSHKSGRD QRHVTQSGGN RKFKCTECGK
     AFKYKHHLKE HLRIHSGEKP YECPNCKKRF SHSGSYSSHI SSKKCISLMP VNGRPRAGLK
     TSQCSSPSLS ASPGSPTRPQ IRQKLENKPL QEQLSVNQIK TEPVDYEFKP IVVASGINCS
     TPLQNGVFSG GGPLQATNSP QGVVQAVVLP TVGLVSPISI NLSDIQNVLK VAVDGNVIRQ
     VLENNQANLA SKEQETINAS SIQQGGHSVI SAISLPLVDQ DGTTKIIINY SLEQPSQLQV
     VPQNLKKETP VPTNSCKSEK LPEDLTVKSE KDKSFEGGGR NDSTCLLCDD RPGDASALAE
     LKHCDLRQPA QPPPLPAPEA DKPEASDPSG SGEGGLSPSR PPLKNLLSLL KAYYALNAQP
     SAEELSKIAD SVNLPLDVVK KWFEKMQAGQ VSVQPSEPSS PEPGRANLPA KSDDQPPPPD
     ADEPQDSTGH QQSPLKITSS PVLPVGSAVN GSRSSTPPSP LNLSSSRNTQ GYLYTAEGAA
     EEPQVEPLDL SLPKQQGELL ERSTITSVYQ NSVYSVQEEP LNLSCAKKEP QKDSCGTDSE
     PVVNVIPPSA NPINIAIPTV TAQLPTIVAI AGQNSVPCLR ALAANKQAVL IPQVAYTYST
     AVSPAVQDAP LKVIPPNGNQ DERQDTSSEG VSNVEEQNDS DSTPPKKKMR KTENGMYACD
     LCDKIFQKSS SLLRHKYEHT GKRPHECGIC KKAFKHKHHL IEHMRLHSGE KPYQCDKCGK
     RFSHSGSYSQ HMNHRYSYCK REAEERDAGP EDAGPGAWPN EHAGARASPS QGDSDERESS
     TREEDEDSDK EEEEEEREME ELQEEKGSGE PGGEEEEEEE EEEEMEEEEE QETEEQEEGG
     RAKTAGATAE REGAGSPESS LEHKVSEGSE QVSEEKTNEA
//
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