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 10-APR-2019, entry version 139. 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 RP HDA-1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION RP PHENOTYPE, AND 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 RT pathway, encode proteins similar to Rb and its binding protein RT 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 RT investigating 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 RP WITH 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 RT conserved LIN-35 Rb-containing complex distinct from a NuRD-like RT 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 RT protein to promote programmed cell death in Caenorhabditis elegans."; RL Genetics 175:1719-1733(2007). RN [6] 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 CC deacetylases to their histone substrates in a manner that is CC regulated by nucleosomal DNA (By similarity). Required for hcp-3 CC and his-1 stabilization, localization of hcp-3 to centromeres and CC for proper chromosome segregation (PubMed:26904949). Synthetic CC multivulva class B (synMuvB) protein (PubMed:9875852). SynMuvB CC proteins are required to repress the induction of vulval CC development by Ras signaling and probably act by forming the CC multiprotein DRM complex that represses transcription CC (PubMed:9875852, PubMed:10704416, PubMed:17075059). CC {ECO:0000250|UniProtKB:Q09028, ECO:0000269|PubMed:10704416, CC ECO:0000269|PubMed:17075059, ECO:0000269|PubMed:26904949, CC ECO:0000269|PubMed:9875852}. CC -!- SUBUNIT: Binds directly to helix 1 of the histone fold of histone CC H4, a region that is not accessible when H4 is in chromatin (By CC similarity). Probable component of a NuRD-like complex, composed CC of at least lin-53 and hda-1 (PubMed:17075059). Interacts with CC lin-35 (PubMed:9875852). Interacts with hda-1; the interaction is CC direct (PubMed:9875852, PubMed:17075059). Component of the DRM CC complex, at least composed of lin-9, lin-35, lin-37, lin-52, lin- CC 53, lin-54- dpl-1 and efl-1 (PubMed:17075059). Interacts with hcp- CC 3 (PubMed:26904949). {ECO:0000250|UniProtKB:Q24572, CC ECO:0000269|PubMed:17075059, ECO:0000269|PubMed:26904949, CC ECO:0000269|PubMed:9875852, ECO:0000305}. CC -!- INTERACTION: CC Q23482:lin-37; NbExp=5; IntAct=EBI-324314, EBI-324325; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9875852}. CC Chromosome, centromere {ECO:0000269|PubMed:26904949}. CC Note=Localizes to centromeres during metaphase. Requires hcp-3 and CC knl-2 for nuclear and centromere localization. CC {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 CC at the time of vulval induction and until after all cell divisions CC and vulval morphogenesis are complete. CC {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). CC RNAi-mediated knockdown results in embryonic lethality CC (PubMed:9875852). RNAi-mediated knockdown leads to a reduction of CC hcp-3 and his-1 protein levels and to a depletion of hcp-3 on CC centromeres, a reduction of H3K27me3 levels on metaphase CC chromosomes and to chromosome segregation defects CC (PubMed:26904949). {ECO:0000269|PubMed:17075059, CC ECO:0000269|PubMed:17237514, 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 UniGene; Cel.19610; -. DR ProteinModelPortal; P90916; -. DR SMR; P90916; -. DR BioGrid; 38227; 6. 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; K07A1.12; 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 eggNOG; ENOG410XNU9; LUCA. DR GeneTree; ENSGT00940000154748; -. DR HOGENOM; HOG000160330; -. DR InParanoid; P90916; -. DR KO; K10752; -. DR OMA; SEDRVAN; -. DR OrthoDB; 831322at2759; -. DR PhylomeDB; P90916; -. DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence. 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 Reactome; R-CEL-8953750; Transcriptional Regulation by E2F6. DR SignaLink; P90916; -. DR PRO; PR:P90916; -. DR Proteomes; UP000001940; Chromosome I. DR Bgee; WBGene00003036; Expressed in 5 organ(s), highest expression level in multi-cellular organism. 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:transcriptional 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; Complete proteome; KW Developmental protein; Nucleus; Reference proteome; Repeat; Repressor; KW Transcription; Transcription regulation; WD repeat. FT CHAIN 1 417 Probable histone-binding protein lin-53. FT /FTId=PRO_0000051059. FT REPEAT 118 158 WD 1. FT REPEAT 170 210 WD 2. FT REPEAT 220 260 WD 3. FT REPEAT 263 303 WD 4. FT REPEAT 307 347 WD 5. FT REPEAT 364 404 WD 6. FT MUTAGEN 292 292 L->F: In semidominant alleles n883 and FT n2978; causes development of multiple FT vulvas. {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 //