RESTB_XENLA
ID RESTB_XENLA Reviewed; 529 AA.
AC Q9PVG3; Q9PVG2;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=RE1-silencing transcription factor B;
DE AltName: Full=Neural-restrictive silencer factor B;
DE Flags: Fragment;
GN Name=rest-b; Synonyms=nrsf-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 [MRNA] (ISOFORMS 1 AND 2).
RA Eggen B.J.L., Toledo-Aral J.J., Mandel G., Hemmati-Brivanlou A.;
RT "Cloning and expression pattern of Xenopus laevis REST.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional repressor which binds neuron-restrictive
CC silencer element (NRSE) and represses neuronal gene transcription in
CC non-neuronal cells (By similarity). Plays a role in the early
CC development of the nervous system and is required for proper patterning
CC of the neuroectoderm during gastrulation. This involves the correct
CC speciation of the neuroepithelial domain and adequate development of
CC the non-neural ectoderm (By similarity). {ECO:0000250|UniProtKB:Q13127,
CC ECO:0000250|UniProtKB:Q2EI21}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13127}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q13127}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9PVG3-1; Sequence=Displayed;
CC Name=2; Synonyms=rest-T4;
CC IsoId=Q9PVG3-2; Sequence=VSP_022084, VSP_022085;
CC -!- DOMAIN: The C2H2-type zinc finger 5 is required for nuclear
CC localization. {ECO:0000250|UniProtKB:Q13127}.
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DR EMBL; AF096301; AAF06720.1; -; mRNA.
DR EMBL; AF096302; AAF06721.1; -; mRNA.
DR RefSeq; NP_001165645.1; NM_001172174.1. [Q9PVG3-2]
DR AlphaFoldDB; Q9PVG3; -.
DR SMR; Q9PVG3; -.
DR GeneID; 373614; -.
DR KEGG; xla:373614; -.
DR CTD; 373614; -.
DR Xenbase; XB-GENE-955471; rest.S.
DR OrthoDB; 1185468at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 373614; Expressed in egg cell and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 1.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 5.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Developmental protein; Metal-binding;
KW Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..>529
FT /note="RE1-silencing transcription factor B"
FT /id="PRO_0000269552"
FT ZN_FING 156..178
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 212..234
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 244..266
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 272..294
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 300..322
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..351
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 357..379
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 385..408
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 188..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 297..303
FT /note="ERPYQCI -> KTFSFYY (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_022084"
FT VAR_SEQ 304..529
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_022085"
FT NON_TER 529
SQ SEQUENCE 529 AA; 60019 MW; 8AB56219C0F06CC3 CRC64;
MATQMVNQST GNSLFCTSTY SNISLDNDMY GLHDLSKADM AAPRLIMLAN VALTGELSSG
CCDYTPEGER QMAELTTVND NSFSDSEGDR LEDSPSMDIQ SHNFIMEMEP AECSKEGTSE
NDGTLLSNTL EVEVQKDKRT PSPTDDKYKC VKSKPFRCKP CQYKAESEEE FVHHIKIHSA
KIYVDNDSNK KAQGNEADSS ISEESDVSKG PIQCDRCGYN TNRFDHYLAH LKHHNKAGEN
ERVYKCTICT YTTVSEYHWK KHLRNHYPRI LYTCSQCSYF SDRKNNYIQH IRTHTGERPY
QCILCPYSSS QKTHLTRHMR THSGEKPFKC EQCSYVASNQ HEVTRHARQV HNGPKPLTCP
HCDYKTADRS NFKKHVELHV NPRQFLCPVC DYAASKKCNL QYHIKSRHSG CTNITMDVSK
VKLRTKKGDI GVADVDANKQ TENGNIIDKS VEETVKAEKR ESCGKAKKSI VNLVDGQVAK
KRRLSSTQKK IKTSDARPEK ILDKSRKSSC VKRKSDLLEN SNDTQTSTV
