ID   H3_URECA                Reviewed;         136 AA.
AC   P84239; P02295; P02297; P16105; P17269; P17320;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Histone H3;
OS   Urechis caupo (Innkeeper worm) (Spoonworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Polychaeta;
OC   Echiura; Xenopneusta; Urechidae; Urechis.
OX   NCBI_TaxID=6431;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Sperm;
RX   PubMed=1339330; DOI=10.3109/10425179209020810;
RA   Davis F.C., Shelton J.C., Ingham L.D.;
RT   "Nucleotide sequence of the Urechis caupo core histone gene tandem
RT   repeat.";
RL   DNA Seq. 2:247-256(1992).
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   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR   EMBL; X58895; CAA41696.1; -; Genomic_DNA.
DR   PDB; 2P5B; X-ray; 1.99 A; I/J=27-47.
DR   PDBsum; 2P5B; -.
DR   AlphaFoldDB; P84239; -.
DR   SMR; P84239; -.
DR   EvolutionaryTrace; P84239; -.
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   1: Evidence at protein level;
KW   3D-structure; Acetylation; Chromosome; DNA-binding; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..136
FT                   /note="Histone H3"
FT                   /id="PRO_0000221310"
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"
FT   STRAND          32..34
FT                   /evidence="ECO:0007829|PDB:2P5B"
SQ   SEQUENCE   136 AA;  15388 MW;  6FD8508EA50A0EEC CRC64;
     MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
     LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI
     MPKDIQLARR IRGERA