ID   H331_CAEEL              Reviewed;         136 AA.
AC   Q10453;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Histone H3.3 type 1;
GN   Name=his-71; ORFNames=F45E1.6;
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   TISSUE SPECIFICITY, AND FUNCTION.
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: Variant histone H3 which replaces conventional H3 in a wide
CC       range of nucleosomes in active genes. Constitutes the predominant form
CC       of histone H3 in non-dividing cells and is incorporated into chromatin
CC       independently of DNA synthesis. Deposited at sites of nucleosomal
CC       displacement throughout transcribed genes, suggesting that it
CC       represents an epigenetic imprint of transcriptionally active chromatin.
CC       Nucleosomes wrap and compact DNA into chromatin, limiting DNA
CC       accessibility to the cellular machineries which require DNA as a
CC       template. Histones thereby play a central role in transcription
CC       regulation, DNA repair, DNA replication and chromosomal stability. DNA
CC       accessibility is regulated via a complex set of post-translational
CC       modifications of histones, also called histone code, and nucleosome
CC       remodeling. {ECO:0000269|PubMed:16846252}.
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
CC       DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in all adult nuclei.
CC       {ECO:0000269|PubMed:16846252}.
CC   -!- PTM: Acetylation is generally linked to gene activation. {ECO:0000250}.
CC   -!- PTM: Methylation at Lys-5 is linked to gene activation. Methylation at
CC       Lys-10 is linked to gene repression (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR   EMBL; FO080773; CCD66641.1; -; Genomic_DNA.
DR   PIR; T16361; T16361.
DR   RefSeq; NP_509344.1; NM_076943.4.
DR   PDB; 4ZBJ; X-ray; 2.25 A; B=62-136.
DR   PDBsum; 4ZBJ; -.
DR   AlphaFoldDB; Q10453; -.
DR   SMR; Q10453; -.
DR   BioGRID; 45980; 3.
DR   DIP; DIP-26634N; -.
DR   STRING; 6239.F45E1.6.1; -.
DR   EPD; Q10453; -.
DR   PaxDb; 6239-F45E1-6; -.
DR   PeptideAtlas; Q10453; -.
DR   EnsemblMetazoa; F45E1.6.1; F45E1.6.1; WBGene00001945.
DR   GeneID; 181057; -.
DR   KEGG; cel:CELE_F45E1.6; -.
DR   UCSC; F45E1.6.2; c. elegans.
DR   AGR; WB:WBGene00001945; -.
DR   WormBase; F45E1.6; CE01943; WBGene00001945; his-71.
DR   eggNOG; KOG1745; Eukaryota.
DR   GeneTree; ENSGT01100000263504; -.
DR   HOGENOM; CLU_078295_4_0_1; -.
DR   InParanoid; Q10453; -.
DR   OMA; HFAMART; -.
DR   OrthoDB; 2873654at2759; -.
DR   PhylomeDB; Q10453; -.
DR   Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-CEL-983231; Factors involved in megakaryocyte development and platelet production.
DR   PRO; PR:Q10453; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00001945; Expressed in pharyngeal muscle cell (C elegans) and 3 other cell types or 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; Histone, subunit A; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000164; Histone_H3/CENP-A.
DR   PANTHER; PTHR11426; HISTONE H3; 1.
DR   PANTHER; PTHR11426:SF277; HISTONE H3.3; 1.
DR   Pfam; PF00125; Histone; 1.
DR   PRINTS; PR00622; HISTONEH3.
DR   SMART; SM00428; H3; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00322; HISTONE_H3_1; 1.
DR   PROSITE; PS00959; HISTONE_H3_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chromosome; DNA-binding; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..136
FT                   /note="Histone H3.3 type 1"
FT                   /id="PRO_0000221298"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         5
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         5
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         24
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         28
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         80
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   136 AA;  15342 MW;  57E8809145022E77 CRC64;
     MARTKQTARK STGGKAPRKQ LATKAARKSA PTTGGVKKPH RYRPGTVALR EIRRYQKSTE
     LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
     MPKDIQLARR IRGERA
//