ID   RCOR1_XENLA             Reviewed;         431 AA.
AC   Q90WN5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=REST corepressor 1;
DE   AltName: Full=Protein CoREST;
DE            Short=xCoREST;
GN   Name=rcor1; Synonyms=corest;
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], AND TISSUE SPECIFICITY.
RX   PubMed=11744385; DOI=10.1016/s0925-4773(01)00565-2;
RA   de la Calle-Mustienes E., Modolell J., Gomez-Skarmeta J.L.;
RT   "The Xiro-repressed gene CoREST is expressed in Xenopus neural
RT   territories.";
RL   Mech. Dev. 110:209-211(2002).
CC   -!- FUNCTION: Essential component of the BHC complex, a corepressor complex
CC       that represses transcription of neuron-specific genes in non-neuronal
CC       cells. The BHC complex is recruited at RE1/NRSE sites by REST and acts
CC       by deacetylating and demethylating specific sites on histones, thereby
CC       acting as a chromatin modifier. In the BHC complex, it serves as a
CC       molecular beacon for the recruitment of molecular machinery that
CC       imposes silencing across a chromosomal interval. Plays a central role
CC       in demethylation of Lys-4 of histone H3 by promoting demethylase
CC       activity of KDM1A on core histones and nucleosomal substrates (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of a BHC histone deacetylase complex that contains
CC       KDM1A. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC       ECO:0000255|PROSITE-ProRule:PRU00624}.
CC   -!- TISSUE SPECIFICITY: Expressed in territories in which neurogenesis
CC       takes place. {ECO:0000269|PubMed:11744385}.
CC   -!- SIMILARITY: Belongs to the CoREST family. {ECO:0000305}.
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DR   EMBL; AJ311849; CAC67558.1; -; mRNA.
DR   RefSeq; NP_001082141.1; NM_001088672.1.
DR   AlphaFoldDB; Q90WN5; -.
DR   SMR; Q90WN5; -.
DR   GeneID; 398247; -.
DR   KEGG; xla:398247; -.
DR   CTD; 398247; -.
DR   Xenbase; XB-GENE-5727224; rcor1.L.
DR   OMA; WHKHDLN; -.
DR   OrthoDB; 641792at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 398247; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   CDD; cd00167; SANT; 1.
DR   InterPro; IPR000949; ELM2_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   Pfam; PF01448; ELM2; 1.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   SMART; SM01189; ELM2; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS51156; ELM2; 1.
DR   PROSITE; PS51293; SANT; 2.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Coiled coil; Nucleus; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..431
FT                   /note="REST corepressor 1"
FT                   /id="PRO_0000226775"
FT   DOMAIN          50..135
FT                   /note="ELM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT   DOMAIN          136..187
FT                   /note="SANT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   DOMAIN          327..378
FT                   /note="SANT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          190..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          267..314
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        14..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   431 AA;  49022 MW;  2CE43E73388002DC CRC64;
     MIEKGAEISG KRRGRNNAAN SKSLGTNVNG SNSWEEGSSS SSSDDEPGGG GMRVGLQYQA
     VVPEFDQEVA KNCQERENLG MLVWSPNQNI SEAKLDEYIS VAKEKHGYNM EQALGMLFWH
     KHNIEKSLAD LLNFTPFPDE WTVEDRVLFE QAFSFHGKTF HRIQQMLPDK SIASLVKFYY
     SWKKTRSKTS VMDRHARKQK REREGSGDEI EETNGANPVD IEIEQPKEAK KEVPKNDTVP
     HIKKEKHPSQ AKNRAKRKPP NGMFLSQEDV EAVSANANAA TTVLRQLDME LVSIKRQIQN
     IKQTNSAFKE KLQGGIEDYR IQEVSQKFNA RWTTEEQLLA VQAIRMYGRD FQAISDVIGN
     KSVVQVKNFF VNYRRRFNID QVLQEWEAEH GKTEENGDCT EKAVKLPETA IKMSDEEEEA
     SLLDITYPSA S