ID   H2A3_LYTPI              Reviewed;         112 AA.
AC   P09589;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Histone H2A, sperm;
DE   Flags: Fragment;
OS   Lytechinus pictus (Painted sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Temnopleuroida; Toxopneustidae; Lytechinus.
OX   NCBI_TaxID=7653;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=3785204; DOI=10.1128/mcb.6.7.2602-2612.1986;
RA   Lieber T., Weisser K., Childs G.;
RT   "Analysis of histone gene expression in adult tissues of the sea urchins
RT   Strongylocentrotus purpuratus and Lytechinus pictus: tissue-specific
RT   expression of sperm histone genes.";
RL   Mol. Cell. Biol. 6:2602-2612(1986).
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. Chromosome.
CC   -!- PTM: Monoubiquitination gives a specific tag for epigenetic
CC       transcriptional repression. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; M13637; AAA30000.1; -; mRNA.
DR   PIR; D25381; HSURA2.
DR   AlphaFoldDB; P09589; -.
DR   SMR; P09589; -.
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   CDD; cd00074; H2A; 1.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR032454; Histone_H2A_C.
DR   InterPro; IPR032458; Histone_H2A_CS.
DR   PANTHER; PTHR23430; PTHR23430; 1.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF16211; Histone_H2A_C; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
DR   PROSITE; PS00046; HISTONE_H2A; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Isopeptide bond; Methylation; Nucleosome core;
KW   Nucleus; Ubl conjugation.
FT   CHAIN           <1..112
FT                   /note="Histone H2A, sperm"
FT                   /id="PRO_0000055249"
FT   MOD_RES         91
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        106
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   112 AA;  12069 MW;  0AFBE3A04EC65357 CRC64;
     AKSRSSRAGL QFPVGRVHRF LRKGNYAQRV GAGAPVYLAA VFEYLAAEIL ELAGNAAPDN
     KKTRIIPRHL QLAIRNDEEL NKLLGGVTIA QGGVLPNIQA VLLPKKTAKS SK