ID   RESTA_XENLA             Reviewed;        1501 AA.
AC   Q2EI21;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=RE1-silencing transcription factor A;
DE   AltName: Full=Neural-restrictive silencer factor A;
GN   Name=rest-a; Synonyms=nrsf-a;
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], FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=16525062; DOI=10.1523/jneurosci.5037-05.2006;
RA   Olguin P., Oteiza P., Gamboa E., Gomez-Skarmeta J.L., Kukuljan M.;
RT   "RE-1 silencer of transcription/neural restrictive silencer factor
RT   modulates ectodermal patterning during Xenopus development.";
RL   J. Neurosci. 26:2820-2829(2006).
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. {ECO:0000250|UniProtKB:Q13127,
CC       ECO:0000269|PubMed:16525062}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13127}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q13127}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in whole ectoderm at early gastrula
CC       stage. During the early neurula stage, it is restricted to the anterior
CC       and lateral neural ridge areas. At the neural tube stage, it is
CC       expressed in the presomitic mesoderm. Later, it is detected surrounding
CC       the anterior nervous system and the developing eye and slightly in the
CC       migratory neural crests. {ECO:0000269|PubMed:16525062}.
CC   -!- DOMAIN: The C2H2-type zinc finger 5 is required for nuclear
CC       localization. {ECO:0000250|UniProtKB:Q13127}.
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DR   EMBL; DQ377343; ABD32117.1; -; mRNA.
DR   Proteomes; UP000186698; Genome assembly.
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   SMART; SM00355; ZnF_C2H2; 9.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Developmental protein; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1501
FT                   /note="RE1-silencing transcription factor A"
FT                   /id="PRO_0000269551"
FT   ZN_FING         158..180
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         214..236
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         246..268
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         274..296
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         302..324
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         330..353
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         359..381
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         387..410
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         1463..1485
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          112..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          186..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          886..929
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1031..1081
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1414..1436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        186..205
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        575..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..606
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1063..1081
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1501 AA;  166204 MW;  6E2ECB59891C5DE8 CRC64;
     MATQMVNQAT GNSLFCTSTY SSISLDNDMY GLHDLSKADM AAPRLIMLAN VALTGELNSG
     GCDYTLEGER QMAELTTVND NSFSDSEGDR LEDSPTMDIQ SRNFTMDIEP AECSKEGTSE
     NDGTLLSNTL EEEVQKDKKA QAPSTTDDKI KCVKSKPFRC KPCQYKAESE EEFVHHIKIH
     SAKIYVDNDS KKNPQGKEAD SSIPEESDIS KGPIQCDGCG YNTNRFDHYL AHLKHHNKAG
     ENERVYKCTI CTYSTVSEYH WKKHLRNHYP RILYTCSQCS YFSDRKNNYI QHIRTHTGER
     PYQCIICLYS SSQKTHLTRH MRTHSGEKPF KCEQCSYVAS NQHEVTRHAR QVHNGPKPLT
     CPHCDYKTAD RSNFKKHVEL HVNPRQFLCP VCDYAASKKC NLQYHIKSRH SGCTNITMNV
     SKVKLRTKKG EVGDEDADTN KPMENGNIIN RSVGKKLEET VKAEKRESCV KAKKRIVGMV
     DGQVAKKSRL SSTQKKIKAS EVRPEKIVDK SRKSSFVKRK TDVLENPNDT QTSTLKKKKL
     KNARIVNTSE IKYDITKKLT GSVNKKENSF VKNMHKKKTG AQSSNGKKNM PNKITEKKEK
     GKQLDSKTSV ASDITEEQTI VGKVANENYS EQVAASEVAS SNVNSDSSES CCLLNDVMQT
     DLSINTTLET EVSTDHDTKS EHVSKAVMAL VMQRDTQMDL SMLVDLKANF SKQEKTQDNL
     LMDIETISSD LLLQREEPNQ VLYQNGIPNK LLREKCGAIA DLPVDGAKTT VNLQIGKANF
     CFQNDCCQPD NLLVDGCKPM ELREPSADLL MDHGHPSSDH LVGRGRPPYD HLINCGKSSR
     DPCVLTWDGE EPTCNKLVEV DEPTSNKLVY SNKSICIQLV GGAEPTKVQP ARDEPTSVQP
     AAAGDEPTRV QPVVPGDEPT SVQPVVPGDE PTSVQLVVTR DKPTSIQTVT VRDEPSIIKT
     VVAGDEPYIV QTVGDEPSIA QTVEDEQSIV QTVAAKDEPS IAXTAAEDEP SIVQTVXAMD
     EPAIVQTVAA GDEPTSVQTV AAGDEPTSVQ PLSREDPKSV QPIGEDQPTS VQPPGGDEQT
     NLLINSKTAY LPVCTKEAIG LSVARQDETE LLVRRENRSV LSTVWDEPTD LSFERNVQSM
     NIPIDLSTTN QNPICMSKGM GCPLHLPVEW SEPFNLSMDM DWHKPANLSL VEPSDLSVRK
     GDSADLSLNN KKPADLSVVW GEPVDLSLGR SEPADLSVGM NQPAELKMGI PDTIGLLVEG
     RQLSVLTMGR GVESFDLLMG RVDHIDLSVE RCEPIDLSVE KGIPRNLEIS EGKHFGKLDN
     CYNLNCAAFQ IKDQAKCNII PENTSQSNTK LSVEIAEPHN HLQSMCVPSE LHGNLDTTVQ
     QSKHNECNNG TKEVGTSQLP CAVSRCVSXD EDEGIHSHDG SDISDNVSEM SYDSGLNGVP
     SVQKTLSSEP KVVINSSETK ESFVCIFCDR TFRKEEEYTK HLRRHLVNVY YLKKAAKDID
     N