ID A0A1L8FQP4_XENLA Unreviewed; 1089 AA.
AC A0A1L8FQP4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Zinc finger E-box-binding homeobox 1 {ECO:0000256|ARBA:ARBA00039204};
DE AltName: Full=Transcription factor 8 {ECO:0000256|ARBA:ARBA00041235};
GN Name=zeb1.S {ECO:0000313|RefSeq:XP_041423157.1};
GN Synonyms=areb6 {ECO:0000313|RefSeq:XP_041423157.1}, bzp
GN {ECO:0000313|RefSeq:XP_041423157.1}, deltaef1
GN {ECO:0000313|RefSeq:XP_041423157.1}, fecd6
GN {ECO:0000313|RefSeq:XP_041423157.1}, nil-2a
GN {ECO:0000313|RefSeq:XP_041423157.1}, nil2a
GN {ECO:0000313|RefSeq:XP_041423157.1}, tcf8
GN {ECO:0000313|RefSeq:XP_041423157.1}, zeb
GN {ECO:0000313|RefSeq:XP_041423157.1}, zfhep
GN {ECO:0000313|RefSeq:XP_041423157.1}, zfhx1
GN {ECO:0000313|RefSeq:XP_041423157.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_041423157.1};
RN [1] {ECO:0000313|RefSeq:XP_041423157.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_041423157.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_041423157.1};
RG RefSeq;
RL Submitted (SEP-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 RefSeq; XP_041423157.1; XM_041567223.1.
DR AlphaFoldDB; A0A1L8FQP4; -.
DR STRING; 8355.A0A1L8FQP4; -.
DR PaxDb; 8355-A0A1L8FQP4; -.
DR OMA; ANYINFP; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR GO; GO:0003677; F:DNA 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:SF17; ZINC FINGER E-BOX-BINDING HOMEOBOX 1; 1.
DR Pfam; PF00096; zf-C2H2; 3.
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 ECO:0000313|RefSeq:XP_041423157.1};
KW Homeobox {ECO:0000313|RefSeq:XP_041423157.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
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}.
FT DOMAIN 171..199
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 201..228
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 241..268
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 893..920
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 921..948
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 949..977
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
SQ SEQUENCE 1089 AA; 119214 MW; 5D899206118530E2 CRC64;
MADGPRCKRR KQANPKRNDV TNYNSVLEAN SDSDDEDKLH IVEEESVTDA ADGEGSVPED
DLPTDQTVLP EGSESGKGST KTCWEDEEGA DCCDEILGPE AEADELGVKD EECDSDLENE
QNHDPNVEEF LQQSDTAVIY PEAPDDEQRQ GTPEAVGQDE NGTPDAFSQL LTCPYCERGY
KRFTSLKEHI KYRHEKNEDN FSCSMCSYTF AYRTQLDRHM TSHKSGKDQR HVTQSGGNRK
FKCPECGKAF KYKHHLKEHL RIHSGEKPYE CSNCKKRFSH SGSYSSHISS KKCISVAPVN
GRVRSGLKTP QCSSPSLSAS PGSPARPQIR QKIENKPLQE QLPVNQIKTE PVDYEIKPIV
VASGINCSAP LQNGVFTSGS LLQATNSPQG VVQAVVLPTM GLVSPISINL SDIQNVLKMA
VDGNIIRQVL ENNHASLASK EQGTLTSATI QQAGHSVISA ISLPLVDQDG TTKIIINYSL
EQPTQLPVVA QNLKKEVTAP AEVCKTEKLP EDLTIKTEKD TKFTDKSTCL LGADHPGDTN
ALQEPKHYDP KKNSLLPESS KAEVIKSEPS SANSEDGNLT PSQPPLKNLL SLLKAYYALN
AQPSAEELSK IADSVNLPLD VVKKWFEKMQ SGEIPVDSSQ PSSPKPSQNS VTENSVKSKT
ESGLNDGTSV PLKSPKQEAE EPLAVNGSES GTASPTPLNL SSLENSDGAA CTDGTPDGEQ
QAEPLDLSLP KPQGNVPERP SITSVYQSSS YSVQEEPLNL SCVKKEPMQV DNAAKAETTL
IINPSANPIN IAIPTVTAQL PTIVAIADQN GVPCLRALAA NKQTILIPQV TYTYSTTASP
AVPEPQVKNI QPNGNQDERQ DTSSEGVSNV EDQNDSDSTP PKKKLKKTEN GLYACDLCDK
IFQKSSSLLR HKYEHTGKRP HECGICAKAF KHKHHLIEHM RLHSGEKPYQ CDKCGKRFSH
SGSYSQHMNH RYSYCKKEAE ERDGMEQEES AQENLSNEHV DSQVSPSQID SDEQESITRE
EDSEKEEEDE KDADDGQEEK ERVGDGDVEE GEAEPLAGTL KDEECAAEDK CLEEEVTEEN
VSDEDLTQP
//