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-APR-2017, entry version 122. 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; Synonyms=rba-2; ORFNames=K07A1.12; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH LIN-35 AND RP HDA-1, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF RP 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, AND IDENTIFICATION IN THE DRM COMPLEX. 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 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 the NuRD complex, composed of CC at least lin-35, lin-53 and hda-1. Component of the DRM complex, CC at least composed of lin-9, lin-35, lin-37, lin-52, lin-53, lin- CC 54- dpl-1 and efl-1. Interacts with hcp-3 (PubMed:26904949). CC {ECO:0000250|UniProtKB:Q24572, ECO:0000269|PubMed:17075059, CC ECO:0000269|PubMed:26904949}. 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 cells at the time of CC vulval induction. {ECO:0000269|PubMed:9875852}. CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown leads to a reduction CC of 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 {ECO:0000269|PubMed:26904949}. 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 DIP; DIP-24440N; -. DR IntAct; P90916; 6. DR MINT; MINT-114323; -. DR STRING; 6239.K07A1.12.2; -. 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; ENSGT00570000079069; -. DR HOGENOM; HOG000160330; -. DR InParanoid; P90916; -. DR KO; K10752; -. DR OMA; PDIRINH; -. DR OrthoDB; EOG091G0A20; -. DR PhylomeDB; P90916; -. DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence. DR Reactome; R-CEL-3214847; HATs acetylate histones. DR SignaLink; P90916; -. DR PRO; PR:P90916; -. DR Proteomes; UP000001940; Chromosome I. DR Bgee; WBGene00003036; -. 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:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0009790; P:embryo development; IMP:UniProtKB. 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 GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. 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. DR InterPro; IPR001680; WD40_repeat. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR017986; WD40_repeat_dom. 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 //