RCOR2_RAT
ID RCOR2_RAT Reviewed; 523 AA.
AC Q5FWT8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=REST corepressor 2;
GN Name=Rcor2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: May act as a component of a corepressor complex that
CC represses transcription. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- SIMILARITY: Belongs to the CoREST family. {ECO:0000305}.
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DR EMBL; BC089209; AAH89209.1; -; mRNA.
DR RefSeq; NP_001014016.1; NM_001013994.1.
DR RefSeq; XP_001061203.1; XM_001061203.6.
DR RefSeq; XP_008758336.1; XM_008760114.2.
DR RefSeq; XP_008758337.1; XM_008760115.2.
DR RefSeq; XP_008768833.1; XM_008770611.1.
DR AlphaFoldDB; Q5FWT8; -.
DR SMR; Q5FWT8; -.
DR STRING; 10116.ENSRNOP00000035978; -.
DR iPTMnet; Q5FWT8; -.
DR PhosphoSitePlus; Q5FWT8; -.
DR PaxDb; Q5FWT8; -.
DR PRIDE; Q5FWT8; -.
DR GeneID; 305811; -.
DR KEGG; rno:305811; -.
DR UCSC; RGD:1359467; rat.
DR CTD; 283248; -.
DR RGD; 1359467; Rcor2.
DR VEuPathDB; HostDB:ENSRNOG00000060849; -.
DR eggNOG; KOG1194; Eukaryota.
DR HOGENOM; CLU_026741_3_1_1; -.
DR InParanoid; Q5FWT8; -.
DR OMA; ASQYRHH; -.
DR OrthoDB; 641792at2759; -.
DR PhylomeDB; Q5FWT8; -.
DR TreeFam; TF106450; -.
DR PRO; PR:Q5FWT8; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021183; Expressed in heart and 18 other tissues.
DR Genevisible; Q5FWT8; RN.
DR GO; GO:0000785; C:chromatin; IDA:RGD.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:RGD.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 1: Evidence at protein level;
KW Coiled coil; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..523
FT /note="REST corepressor 2"
FT /id="PRO_0000226778"
FT DOMAIN 44..129
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 130..181
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..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 283..314
FT /evidence="ECO:0000255"
FT COMPBIAS 15..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..465
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..523
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ40"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ40"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ40"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ40"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 479
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8C796"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IZ40"
SQ SEQUENCE 523 AA; 57981 MW; 89F8DA438C925D1E CRC64;
MPSVMEKPSA GSGILSRSRA KTAPNGGQPH SEDDSSEEEH SHDSMIRVGT NYQAVIPECK
PESPARYSNK ELKGMLVWSP NHCVSDAKLD KYIAMAKEKH GYNIEQALGM LLWHKHDVEK
SLADLANFTP FPDEWTVEDK VLFEQAFGFH GKCFQRIQQM LPDKLIPSLV KYYYSWKKTR
SRTSVMDRQA RRLGGRKDKE DSDELEEGRG AVSEGEPDTG DPKREPLPSR PLNARPGPGK
KEIQVSQYRH HPLRTRRRPP KGMYLSPEGL TAVSGSPDLA NLTLRGLDSQ LISLKRQVQS
MKQTNSSLRQ ALEGGIDPLR PPEANTKFNS RWTTDEQLLA VQAIRRYGKD FGAIAEVIGN
KTLTQVKTFF VSYRRRFNLE EVLQEWEAEQ DGAPTAPVPV EEARRGAPVP ATALEEDDEV
QITSVSTSVP RSVPPAPPPP PPPTSLSQPP PLLRPPLPTA PTLLRQPPPL QQGRFLQPRL
APNQPPPPLI RPALAASRHS ARPGPQPPPT LVGAQLEPPA PSL
