Z703B_XENLA
ID Z703B_XENLA Reviewed; 531 AA.
AC Q2VPM4;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Zinc finger protein 703-B;
GN Name=znf703-b;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=28716930; DOI=10.1073/pnas.1704194114;
RA Li Y., Zhao D., Horie T., Chen G., Bao H., Chen S., Liu W., Horie R.,
RA Liang T., Dong B., Feng Q., Tao Q., Liu X.;
RT "Conserved gene regulatory module specifies lateral neural borders across
RT bilaterians.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6352-6360(2017).
CC -!- FUNCTION: Transcriptional corepressor which does not bind directly to
CC DNA and may regulate transcription through recruitment of histone
CC deacetylases to gene promoters. Regulates cell adhesion, migration and
CC proliferation (By similarity). Involved in specification of the lateral
CC neural plate border (NPB) (PubMed:28716930). May be required for
CC segmental gene expression during hindbrain development (By similarity).
CC {ECO:0000250|UniProtKB:Q9H7S9, ECO:0000269|PubMed:28716930}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H7S9}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9H7S9}.
CC -!- DEVELOPMENTAL STAGE: Expressed at the posterior ectoderm except for the
CC dorsal midline in gastrulae (PubMed:28716930). During neurulation,
CC expression diminishes so as to become restricted to the lateral neural
CC plate border (NPB) and neural crest (PubMed:28716930).
CC {ECO:0000269|PubMed:28716930}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown blocks differentiation of
CC the neural plate border (NPB). {ECO:0000269|PubMed:28716930}.
CC -!- SIMILARITY: Belongs to the Elbow/Noc family. {ECO:0000305}.
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DR EMBL; BC108592; AAI08593.1; -; mRNA.
DR RefSeq; NP_001084448.1; NM_001090979.1.
DR AlphaFoldDB; Q2VPM4; -.
DR DNASU; 403392; -.
DR GeneID; 403392; -.
DR KEGG; xla:403392; -.
DR CTD; 403392; -.
DR Xenbase; XB-GENE-1217466; znf703.S.
DR OrthoDB; 1163882at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 403392; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034333; P:adherens junction assembly; ISS:UniProtKB.
DR GO; GO:0034111; P:negative regulation of homotypic cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR InterPro; IPR022129; Tscrpt_rep_NocA-like.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF12402; nlz1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Developmental protein; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..531
FT /note="Zinc finger protein 703-B"
FT /id="PRO_0000292210"
FT ZN_FING 404..432
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..200
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 55357 MW; 3B57A3440A669F14 CRC64;
MNCSPPGSCT DTERQRSGTP ATPCATLAPT HPLRQANRLP IRRIKMLTAH TGHLLHPEYL
QPLSSTPISP IELDAKKSPL ALLAQTCSQI GKPDPPPSSK LNSVTSSEKE SGRSSSLKLG
ESPLEDKSSF KPYAKGGETR KESGSSAGGA ADKAGFRVPS GSCQPFPHAP SPSSRVSSPG
QHCESKNNES QEKKEPEVNK SSLETSQANP TLTRASISNS SAESSQSGDV APSSKSDPPS
LGSGHVAPIS PYKPGHSVFP LPPSGIGYHG SIVGAYAGYP SQYVPGLDHT KSSLVGNQLP
GTLGLPGKPP SSSPLTGASP PSFMQGLCRD PYCLSYHNAS HLGSSSCSTC VHDPSALKSG
YPLVYPSHPL HSVHTTLSSS VTPSLSGHPL YTYGFMLQND PVPHICNWVS ASGPCDKRFA
TSEELLAHLR THTALPGADK LLAGYPTGLG SAASCHLHLP PTGPGSPNTL PGSLSLRSPH
TFGLSRYHPY GKGHLTAPNG LPVPSLPAGS YYSPYALYGQ RLTSASALGY Q