RCORB_CAEEL
ID RCORB_CAEEL Reviewed; 558 AA.
AC Q18919;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=REST corepressor spr-1;
DE AltName: Full=CoREST;
DE AltName: Full=Suppressor of presenilin 1;
GN Name=spr-1 {ECO:0000312|WormBase:D1014.8};
GN Synonyms=slr-10 {ECO:0000312|WormBase:D1014.8};
GN ORFNames=D1014.8 {ECO:0000312|WormBase:D1014.8};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Larva;
RX PubMed=12381669; DOI=10.1101/gad.1022402;
RA Jarriault S., Greenwald I.;
RT "Suppressors of the egg-laying defective phenotype of sel-12 presenilin
RT mutants implicate the CoREST corepressor complex in LIN-12/Notch signaling
RT in C. elegans.";
RL Genes Dev. 16:2713-2728(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SPR-5, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Bristol N2;
RX PubMed=12411496; DOI=10.1093/emboj/cdf561;
RA Eimer S., Lakowski B., Donhauser R., Baumeister R.;
RT "Loss of spr-5 bypasses the requirement for the C.elegans presenilin sel-12
RT by derepressing hop-1.";
RL EMBO J. 21:5787-5796(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17070797; DOI=10.1016/j.ydbio.2006.09.051;
RA Bender A.M., Kirienko N.V., Olson S.K., Esko J.D., Fay D.S.;
RT "lin-35/Rb and the CoREST ortholog spr-1 coordinately regulate vulval
RT morphogenesis and gonad development in C. elegans.";
RL Dev. Biol. 302:448-462(2007).
CC -!- FUNCTION: Probable corepressor protein, which probably participates in
CC the transcriptional repression of the presenilin protein hop-1
CC (PubMed:12381669). Probably acts via the formation of a multiprotein
CC complex that deacetylates and demethylates specific sites on histones
CC (PubMed:12381669). Acts redundantly with the transcriptional repressor
CC lin-35 to play a role in vulval morphogenesis and promote germline
CC proliferation (PubMed:17070797). {ECO:0000269|PubMed:12381669,
CC ECO:0000269|PubMed:17070797}.
CC -!- SUBUNIT: Probably part of a large repressor complex. Interacts with
CC histone demethylase spr-5/lsd-1. {ECO:0000269|PubMed:12411496}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:12381669}.
CC -!- DISRUPTION PHENOTYPE: Loss of function results in a suppression of sel-
CC 12 mutant phenotypes, possibly by up-regulating hop-1 expression
CC (PubMed:12411496). Double knockout with lin-35 results in defects in
CC growth, vulval morphogenesis, somatic gonad development and fertility
CC (PubMed:17070797). {ECO:0000269|PubMed:12411496,
CC ECO:0000269|PubMed:17070797}.
CC -!- SIMILARITY: Belongs to the CoREST family. {ECO:0000305}.
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DR EMBL; AF548624; AAN59932.1; -; mRNA.
DR EMBL; AY160228; AAN62581.1; -; mRNA.
DR EMBL; FO080993; CCD68316.1; -; Genomic_DNA.
DR PIR; T29613; T29613.
DR PIR; T29614; T29614.
DR RefSeq; NP_505098.1; NM_072697.4.
DR AlphaFoldDB; Q18919; -.
DR BioGRID; 44234; 4.
DR DIP; DIP-26333N; -.
DR IntAct; Q18919; 2.
DR STRING; 6239.D1014.8; -.
DR EPD; Q18919; -.
DR PaxDb; Q18919; -.
DR PeptideAtlas; Q18919; -.
DR PRIDE; Q18919; -.
DR EnsemblMetazoa; D1014.8.1; D1014.8.1; WBGene00005006.
DR GeneID; 179192; -.
DR KEGG; cel:CELE_D1014.8; -.
DR UCSC; D1014.8; c. elegans.
DR CTD; 179192; -.
DR WormBase; D1014.8; CE27749; WBGene00005006; spr-1.
DR eggNOG; KOG1194; Eukaryota.
DR GeneTree; ENSGT00970000196447; -.
DR HOGENOM; CLU_019480_0_0_1; -.
DR InParanoid; Q18919; -.
DR OMA; MCENCGE; -.
DR OrthoDB; 641792at2759; -.
DR PhylomeDB; Q18919; -.
DR Reactome; R-CEL-3214815; HDACs deacetylate histones.
DR Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q18919; -.
DR PRO; PR:Q18919; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00005006; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
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; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR000679; Znf_GATA.
DR Pfam; PF01448; ELM2; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
DR PROSITE; PS51293; SANT; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..558
FT /note="REST corepressor spr-1"
FT /id="PRO_0000083507"
FT DOMAIN 107..192
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 193..244
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 481..532
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 271..325
FT /note="GATA-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..53
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 558 AA; 63755 MW; 874893575D3B1A70 CRC64;
MDLYDDDGES AQSEKVDVPS EESTIAGPET DIPAETIEEN VPEVEENTLL EEDSLVDVDS
PRPSQQRSKP SKSKRKRKRS SSGESSAAEP EIDAGAKVKG PLSNTNKEIN VGTEFQAKIA
DLNLNDKACN EDRDDQDELI WNTPETIDDE KLEAFIRESS DRYLIPIDRA LYILTINNFN
FDSAIAEVAR RNELKDVWTD QEITLFENCY QIFGKNFSQI RSALCHRSLQ SIVQFYYESK
KRVKYLNFVN SKCDDSSSSE ETETPSPYPE AIFESMCDNC GEKAENMQIN NAMNRPECRA
CLIYFNQTGV PRPTSLRLVL AERIRNQVSC PDNMKEYMKD FDKLSAQATG STFQKRIIVK
DQCVEYIIDV DKIPSSSCTE NGNVGETSSP SAQKTEIQSE SDGSGPLIWR HKKTVCMEEI
EVLADDSRRK MFEACQHGSK VDIKLVASWK NDMTNLRKRV EQTYYDPDLN PTYLFSHDRV
HYSQDWTQLE RSQVIRCFNM YGAHFEHIAD VIGTKTPDQV YQFYLENQKA IDAADEEFLA
DMKNPERLAD MEEEEDSI
