ID LIN53_CAEEL Reviewed; 417 AA. AC P90916; A2JDY3; O62411; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 2. DT 12-AUG-2020, entry version 148. DE RecName: Full=Probable histone-binding protein lin-53; DE AltName: Full=Abnormal cell lineage protein 53; DE AltName: Full=Synthetic multivulva protein p48; GN Name=lin-53 {ECO:0000312|WormBase:K07A1.12}; GN Synonyms=rba-2 {ECO:0000312|WormBase:K07A1.12}; GN ORFNames=K07A1.12 {ECO:0000312|WormBase:K07A1.12}; 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, INTERACTION WITH LIN-35 AND HDA-1, RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, AND RP MUTAGENESIS OF LEU-292. RX PubMed=9875852; DOI=10.1016/s0092-8674(00)81722-5; RA Lu X., Horvitz H.R.; RT "lin-35 and lin-53, two genes that antagonize a C. elegans Ras pathway, RT encode proteins similar to Rb and its binding protein RbAp48."; RL Cell 95:981-991(1998). RN [2] 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 [3] RP FUNCTION. RX PubMed=10704416; DOI=10.1016/s0960-9822(00)00343-2; RA Solari F., Ahringer J.; RT "NURD-complex genes antagonise Ras-induced vulval development in RT Caenorhabditis elegans."; RL Curr. Biol. 10:223-226(2000). RN [4] RP FUNCTION, IDENTIFICATION IN THE DRM COMPLEX, IDENTIFICATION IN COMPLEX WITH RP HDA-1, AND DISRUPTION PHENOTYPE. RX PubMed=17075059; DOI=10.1073/pnas.0608461103; RA Harrison M.M., Ceol C.J., Lu X., Horvitz H.R.; RT "Some C. elegans class B synthetic multivulva proteins encode a conserved RT LIN-35 Rb-containing complex distinct from a NuRD-like complex."; RL Proc. Natl. Acad. Sci. U.S.A. 103:16782-16787(2006). RN [5] RP DISRUPTION PHENOTYPE. RX PubMed=17237514; DOI=10.1534/genetics.106.068148; RA Reddien P.W., Andersen E.C., Huang M.C., Horvitz H.R.; RT "DPL-1 DP, LIN-35 Rb and EFL-1 E2F act with the MCD-1 zinc-finger protein RT to promote programmed cell death in Caenorhabditis elegans."; RL Genetics 175:1719-1733(2007). RN [6] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=25446273; DOI=10.1016/j.ydbio.2014.10.014; RA Krueger A.V., Jelier R., Dzyubachyk O., Zimmerman T., Meijering E., RA Lehner B.; RT "Comprehensive single cell-resolution analysis of the role of chromatin RT regulators in early C. elegans embryogenesis."; RL Dev. Biol. 398:153-162(2015). RN [7] RP FUNCTION, INTERACTION WITH HCP-3, SUBCELLULAR LOCATION, AND DISRUPTION RP PHENOTYPE. RX PubMed=26904949; DOI=10.1016/j.celrep.2016.01.065; RA Lee B.C., Lin Z., Yuen K.W.; RT "RbAp46/48(LIN-53) is required for holocentromere assembly in RT Caenorhabditis elegans."; RL Cell Rep. 14:1819-1828(2016). CC -!- FUNCTION: Core histone-binding subunit that may target chromatin CC assembly factors, chromatin remodeling factors and histone deacetylases CC to their histone substrates in a manner that is regulated by CC nucleosomal DNA (By similarity). Required for hcp-3 and his-1 CC stabilization, localization of hcp-3 to centromeres and for proper CC chromosome segregation (PubMed:25446273, PubMed:26904949). Synthetic CC multivulva class B (synMuvB) protein (PubMed:9875852). SynMuvB proteins CC are required to repress the induction of vulval development by Ras CC signaling and probably act by forming the multiprotein DRM complex that CC represses transcription (PubMed:10704416, PubMed:17075059, CC PubMed:9875852). {ECO:0000250|UniProtKB:Q09028, CC ECO:0000269|PubMed:10704416, ECO:0000269|PubMed:17075059, CC ECO:0000269|PubMed:25446273, ECO:0000269|PubMed:26904949, CC ECO:0000269|PubMed:9875852}. CC -!- SUBUNIT: Binds directly to helix 1 of the histone fold of histone H4, a CC region that is not accessible when H4 is in chromatin (By similarity). CC Probable component of a NuRD-like complex, composed of at least lin-53 CC and hda-1 (PubMed:17075059). Interacts with lin-35 (PubMed:9875852). CC Interacts with hda-1; the interaction is direct (PubMed:9875852, CC PubMed:17075059). Component of the DRM complex, at least composed of CC lin-9, lin-35, lin-37, lin-52, lin-53, lin-54- dpl-1 and efl-1 CC (PubMed:17075059). Interacts with hcp-3 (PubMed:26904949). CC {ECO:0000250|UniProtKB:Q24572, ECO:0000269|PubMed:17075059, CC ECO:0000269|PubMed:26904949, ECO:0000269|PubMed:9875852, ECO:0000305}. CC -!- INTERACTION: CC P90916; Q23482: lin-37; NbExp=5; IntAct=EBI-324314, EBI-324325; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9875852}. Chromosome, CC centromere {ECO:0000269|PubMed:26904949}. Note=Localizes to centromeres CC during metaphase. Requires hcp-3 and knl-2 for nuclear and centromere CC localization. {ECO:0000269|PubMed:26904949}. CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in embryos and newly CC hatched larvae. Expressed in all P(3-8).p vulval precursor cells at the CC time of vulval induction and until after all cell divisions and vulval CC morphogenesis are complete. {ECO:0000269|PubMed:9875852}. CC -!- DISRUPTION PHENOTYPE: Decreased protein levels of DRM complex CC components including lin-9, lin-37, lin-52 and lin-54 CC (PubMed:17075059). Double knockout with the programmed cell death CC regulator mcd-1 results slow larval growth (PubMed:17237514). RNAi- CC mediated knockdown results in embryonic lethality (PubMed:9875852, CC PubMed:26904949). RNAi-mediated knockdown leads to a reduction of hcp-3 CC and his-1 protein levels and to a depletion of hcp-3 on centromeres and CC a reduction of H3K27me3 levels on metaphase chromosomes CC (PubMed:26904949). RNAi-mediated knockdown results in chromosome CC segregation defects during mitosis (PubMed:25446273, PubMed:26904949). CC {ECO:0000269|PubMed:17075059, ECO:0000269|PubMed:17237514, CC ECO:0000269|PubMed:25446273, ECO:0000269|PubMed:26904949, CC ECO:0000269|PubMed:9875852}. CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF116530; AAD05571.1; -; mRNA. DR EMBL; Z81097; CAB03178.1; -; Genomic_DNA. DR EMBL; AL023833; CAB03178.1; JOINED; Genomic_DNA. DR PIR; T23391; T23391. DR RefSeq; NP_492552.1; NM_060151.6. DR SMR; P90916; -. DR BioGRID; 38227; 37. DR ComplexPortal; CPX-1100; DRM complex. DR DIP; DIP-24440N; -. DR IntAct; P90916; 9. DR MINT; P90916; -. DR STRING; 6239.K07A1.12; -. DR EPD; P90916; -. DR PaxDb; P90916; -. DR PeptideAtlas; P90916; -. DR PRIDE; P90916; -. DR EnsemblMetazoa; K07A1.12.1; K07A1.12.1; WBGene00003036. DR GeneID; 172802; -. DR KEGG; cel:CELE_K07A1.12; -. DR UCSC; K07A1.12.1; c. elegans. DR CTD; 172802; -. DR WormBase; K07A1.12; CE16234; WBGene00003036; lin-53. DR eggNOG; KOG0264; Eukaryota. DR GeneTree; ENSGT00940000154748; -. DR HOGENOM; CLU_020445_3_1_1; -. DR InParanoid; P90916; -. DR KO; K10752; -. DR OMA; PITDFNW; -. DR OrthoDB; 831322at2759; -. DR PhylomeDB; P90916; -. DR Reactome; R-CEL-1538133; G0 and Early G1. DR Reactome; R-CEL-212300; PRC2 methylates histones and DNA. DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-CEL-3214815; HDACs deacetylate histones. DR Reactome; R-CEL-3214847; HATs acetylate histones. DR Reactome; R-CEL-3214858; RMTs methylate histone arginines. DR Reactome; R-CEL-8943724; Regulation of PTEN gene transcription. DR Reactome; R-CEL-8951664; Neddylation. DR SignaLink; P90916; -. DR PRO; PR:P90916; -. DR Proteomes; UP000001940; Chromosome I. DR Bgee; WBGene00003036; Expressed in multi-cellular organism and 5 other tissues. DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell. DR GO; GO:0070176; C:DRM complex; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB. DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB. DR GO; GO:0001708; P:cell fate specification; IMP:WormBase. DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW. DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB. DR GO; GO:0048557; P:embryonic digestive tract morphogenesis; IGI:WormBase. DR GO; GO:0040035; P:hermaphrodite genitalia development; IMP:UniProtKB. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB. DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase. DR Gene3D; 2.130.10.10; -; 1. DR InterPro; IPR020472; G-protein_beta_WD-40_rep. DR InterPro; IPR022052; Histone-bd_RBBP4_N. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_dom. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR Pfam; PF12265; CAF1C_H4-bd; 1. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00320; GPROTEINBRPT. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; SSF50978; 1. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. PE 1: Evidence at protein level; KW Centromere; Chromatin regulator; Chromosome; Developmental protein; KW Nucleus; Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; WD repeat. FT CHAIN 1..417 FT /note="Probable histone-binding protein lin-53" FT /id="PRO_0000051059" FT REPEAT 118..158 FT /note="WD 1" FT REPEAT 170..210 FT /note="WD 2" FT REPEAT 220..260 FT /note="WD 3" FT REPEAT 263..303 FT /note="WD 4" FT REPEAT 307..347 FT /note="WD 5" FT REPEAT 364..404 FT /note="WD 6" FT MUTAGEN 292 FT /note="L->F: In semidominant alleles n883 and n2978; causes FT development of multiple vulvas." FT /evidence="ECO:0000269|PubMed:9875852" SQ SEQUENCE 417 AA; 47166 MW; AE388CFB048CE51B CRC64; MATLEDGTSE DRVANDEYKI WKKNTPFLYD LVMTHALEWP SLSVQWLPDV AKDNSDHTIH RLILGTHTSD EQNHLLISKI CMPTDDAQFD ASRYDTERSE YGGFGAVNGK VEPDIRINHE GEVNRARYMP QKSNIIATKS PHADVYIFDY LKHSAVPRDN TFNPLIRLKG HTKEGYGLSW NPNKEGLILS ASDDQTVCHW DINANQNVAG ELQAKDVFKG HESVVEDVAW HVLHDGVFGS VGDDKKLLIW DVRTSTPGHC IDAHSAEVNC LAFNPYSEFI LATGSADKTV ALWDLRNLRM KLHSFESHRD EIFQVQWSPH NETILASSGT DKRLHVWDLS KIGEDQSAED AEDGPPELLF IHGGHTAKIS DFSWNPNEPW VVCSVSEDNI LQVWQMADNI YNEVDEETPA DVVERQQ //