ID A0A2K6QBR0_RHIRO Unreviewed; 1253 AA.
AC A0A2K6QBR0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Zinc finger E-box binding homeobox 2 {ECO:0000313|Ensembl:ENSRROP00000026227.1};
GN Name=ZEB2 {ECO:0000313|Ensembl:ENSRROP00000026227.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000026227.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000026227.1}
RP IDENTIFICATION.
RG Ensembl;
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 AlphaFoldDB; A0A2K6QBR0; -.
DR STRING; 61622.ENSRROP00000026227; -.
DR Ensembl; ENSRROT00000050461.1; ENSRROP00000026227.1; ENSRROG00000036815.1.
DR GeneTree; ENSGT00950000183208; -.
DR OMA; QENMFTP; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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.
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:UP000233200};
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 250..278
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 280..302
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 321..348
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1038..1065
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1066..1093
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1094..1122
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 89..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1156..1253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..896
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1164..1195
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1210
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1253 AA; 140742 MW; 6FBEE5752F6315C9 CRC64;
MTHFEDVILV SLIPSRIEPA CCRSRAPSPC ELPSDPLLSM KQPIMADGPR CKRRKQANPR
RKNVVNYDNV VDTGSETDEE DKLHIAEDDG IANPLDQETS PASVPNHESS PHMSQALLPR
EEEEDEIREG GVEHPWHNNE ILQASVDGPE EMKEDYDTMG PEATIQTTIN NGTVKNANCT
SDFEEYFAKR KLEERDGHAV SIEEYLQRSD TAIIYPEAPE ELSRLGTPEA NGQEENDLPP
GTPDAFAQLL TCPYCDRGYK RLTSLKEHIK YRHEKNEENF SCPLCSYTFA YRTQLERHMV
THKPGTDQHQ MLTQGAGNRK FKCTECGKAF KYKHHLKEHL RIHSGEKPYE CPNCKKRFSH
SGSYSSHISS KKCIGLISVN GRMRNNIKTG SSPNSVSSSP TNSAITQLRN KLENGKPLSM
SEQTGLLKIK TEPLDFNDYK VLMATHGFSG TSPFMNGGLG ATSPLGVHPS AQSPMQHLGV
GMEAPLLGFP TMNSNLSEVQ KVLQIVDNTV SRQKMDCKAE EISKLKGYHM KDPCSQPEEQ
GVTSPNIPPV GLPVVSHNGA TKSIIDYTLE KVNEAKACLQ SLTTDSRRQI SNIKKEKLRT
LIDLVTDDKM IENHNISTPF SCQFCKESFP GPIPLHQHER YLCKMNEEIK AVLQPHENIV
PNKAGVFVDN KALLLSSVLS EKGMTSPINP YKDHMSVLKA YYAMNMEPNS DELLKISIAV
GLPQEFVKEW FEQRKVYQYS NSRSPSLERS SKPLAPNSNP PTKDSLLPRS PVKPMDSITS
PSIAELHNSV TNCDPPLRLT KPSHFTNIKP VEKLDHSRSN TPSPLNLSST SSKNSHSSSY
TPNSFSSEEL QAEPLDLSLP KQMKEPKSII ATKNKTKASS ISLDHNSVSS SSENSDEPLN
LTFIKKEFSN SNNLDNKSTN PVFGMNPFSA KPLYTALPPQ SAFPPATFMP PVQTSIPGLR
PYPGLDQMSF LPHMAYTYPT GAATFADMQQ RRKYQRKQGF QGELLDGAQD YMSGLDDMTD
SDSCLSRKKI KKTESGMYAC DLCDKTFQKS SSLLRHKYEH TGKRPHQCQI CKKAFKHKHH
LIEHSRLHSG EKPYQCDKCG KRFSHSGSYS QHMNHRYSYC KREAEEREAA EREAREKGHL
EPTELLMNRA YLQSITPQGY SDSEERESMP RDGESEKEHE KEGEDGYGKL GRQDGDEEFE
EEEEESENKS MDTDPETIRD EEETGDHSMD DSSEDGKMET KSDHEEDNME DGM
//
