ID   H3_PARLI                Reviewed;         136 AA.
AC   P69073; P02298; P05320; P05321; P05322;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Histone H3, embryonic;
OS   Paracentrotus lividus (Common sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinidae; Paracentrotus.
OX   NCBI_TaxID=7656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Spinelli G.;
RL   Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16453405; DOI=10.1002/j.1460-2075.1982.tb01119.x;
RA   Busslinger M., Rusconi S., Birnstiel M.L.;
RT   "An unusual evolutionary behaviour of a sea urchin histone gene cluster.";
RL   EMBO J. 1:27-33(1982).
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   -!- DEVELOPMENTAL STAGE: This histone is expressed during late embryonic
CC       development.
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; M25281; AAA65843.1; -; Genomic_DNA.
DR   EMBL; M36919; AAA75395.1; -; Genomic_DNA.
DR   EMBL; M36920; AAA29441.1; -; Genomic_DNA.
DR   AlphaFoldDB; P69073; -.
DR   SMR; P69073; -.
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, embryonic"
FT                   /id="PRO_0000221313"
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;  15402 MW;  CFD9518EA50A0F2A CRC64;
     MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
     LLIRKLPFQR LVREIAQDFK TELRFQSSAV MALQEASEAY LVGLFEDTNL CAIHAKRVTI
     MPKDIQLARR IRGERA