ID   H33_SPISO               Reviewed;         136 AA.
AC   P84248; P06351; P33155; Q9V3W4;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Histone H3.3;
OS   Spisula solidissima (Atlantic surf-clam).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC   Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei;
OC   Venerida; Mactroidea; Mactridae; Spisula.
OX   NCBI_TaxID=6584;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3040499; DOI=10.1016/0012-1606(87)90421-0;
RA   Swenson K.I., Borgese N., Pietrini G., Ruderman J.V.;
RT   "Three translationally regulated mRNAs are stored in the cytoplasm of clam
RT   oocytes.";
RL   Dev. Biol. 123:10-16(1987).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC       DNA into chromatin, limiting DNA accessibility to the cellular
CC       machineries which require DNA as a template. Histones thereby play a
CC       central role in transcription regulation, DNA repair, DNA replication
CC       and chromosomal stability. DNA accessibility is regulated via a complex
CC       set of post-translational modifications of histones, also called
CC       histone code, and nucleosome remodeling.
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   -!- 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   -!- MISCELLANEOUS: This histone is the predominant form in non-dividing
CC       cells.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR   EMBL; M17876; AAA29965.1; -; mRNA.
DR   PIR; A45941; A45941.
DR   AlphaFoldDB; P84248; -.
DR   SMR; P84248; -.
DR   SWISS-2DPAGE; P99061; -.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW   Nucleus; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..136
FT                   /note="Histone H3.3"
FT                   /id="PRO_0000221307"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="N6-methylated lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         10
FT                   /note="N6-methylated lysine; 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-methylated lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="N6-methylated lysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         80
FT                   /note="N6-methylated lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   136 AA;  15328 MW;  5158ED279E6F9E1C CRC64;
     MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE
     LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI
     MPKDIQLARR IRGERA