H33L3_CAEEL
ID H33L3_CAEEL Reviewed; 127 AA.
AC Q27489;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Putative histone H3.3-like type 3;
GN Name=his-69; ORFNames=E03A3.3;
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 [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 [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=14551910; DOI=10.1371/journal.pbio.0000012;
RA Simmer F., Moorman C., van der Linden A.M., Kuijk E.,
RA van den Berghe P.V.E., Kamath R.S., Fraser A.G., Ahringer J.,
RA Plasterk R.H.A.;
RT "Genome-wide RNAi of C. elegans using the hypersensitive rrf-3 strain
RT reveals novel gene functions.";
RL PLoS Biol. 1:E12-E12(2003).
RN [3]
RP IDENTIFICATION.
RX PubMed=16846252; DOI=10.1371/journal.pgen.0020097;
RA Ooi S.L., Priess J.R., Henikoff S.;
RT "Histone H3.3 variant dynamics in the germline of Caenorhabditis elegans.";
RL PLoS Genet. 2:883-895(2006).
CC -!- FUNCTION: Putative variant histone H3 which may replace conventional H3
CC in a subset of nucleosomes. Nucleosomes wrap and compact DNA into
CC chromatin, limiting DNA accessibility to the cellular machineries which
CC require DNA as a template. Histones thereby play a central role in
CC transcription regulation, DNA repair, DNA replication and chromosomal
CC stability. DNA accessibility is regulated via a complex set of post-
CC translational modifications of histones, also called histone code, and
CC nucleosome remodeling (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Acetylation is generally linked to gene activation. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Worms exhibit slow postembryonic growth.
CC {ECO:0000269|PubMed:14551910}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC -!- CAUTION: Could be the product of a pseudogene. {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; Z38112; CAA86228.1; -; Genomic_DNA.
DR PIR; T20426; T20426.
DR RefSeq; NP_497811.1; NM_065410.1.
DR AlphaFoldDB; Q27489; -.
DR SMR; Q27489; -.
DR BioGRID; 48808; 2.
DR STRING; 6239.E03A3.3; -.
DR PaxDb; Q27489; -.
DR PeptideAtlas; Q27489; -.
DR EnsemblMetazoa; E03A3.3.1; E03A3.3.1; WBGene00001943.
DR GeneID; 184005; -.
DR KEGG; cel:CELE_E03A3.3; -.
DR UCSC; E03A3.3; c. elegans.
DR CTD; 184005; -.
DR WormBase; E03A3.3; CE00942; WBGene00001943; his-69.
DR eggNOG; KOG1745; Eukaryota.
DR GeneTree; ENSGT01050000244889; -.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; Q27489; -.
DR OMA; KAPRMGE; -.
DR OrthoDB; 278624at2759; -.
DR PhylomeDB; Q27489; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00001943; Expressed in anatomical system and 3 other tissues.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 5: Uncertain;
KW Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW Nucleus; Reference proteome.
FT CHAIN 1..127
FT /note="Putative histone H3.3-like type 3"
FT /id="PRO_0000268635"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 19
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 71
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 127 AA; 14523 MW; C432C3D4C35CDCA4 CRC64;
MCPGGKAPRK QLATKAARKN AIVVGAVKKP HRFRPGTVAL REIRRYQKST DLLLRKLPFQ
RLVREIAQDV KQDLRFQSAA IQALQEASEY FLVGLFEDTN LCAIHAKRVT IMPKDMQLAR
RIRGERN