ID   H2AL_STRPU              Reviewed;         126 AA.
AC   P16886;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Late histone H2A.L3;
OS   Strongylocentrotus purpuratus (Purple sea urchin).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Strongylocentrotidae;
OC   Strongylocentrotus.
OX   NCBI_TaxID=7668;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3697096; DOI=10.1093/nar/15.24.10569;
RA   Maxson R., Mohun T., Gormezano G., Kedes L.;
RT   "Evolution of late H2A, H2B, and H4 histone genes of the sea urchin,
RT   Strongylocentrotus purpuratus.";
RL   Nucleic Acids Res. 15:10569-10582(1987).
RN   [2]
RP   UBIQUITINATION.
RX   PubMed=7796537; DOI=10.1002/dvg.1020160308;
RA   Jasinskiene N., Jasinskas A., Langmore J.P.;
RT   "Embryonic regulation of histone ubiquitination in the sea urchin.";
RL   Dev. Genet. 16:278-290(1995).
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 of Lys-120 gives a specific tag for epigenetic
CC       transcriptional repression. {ECO:0000305}.
CC   -!- PTM: Phosphorylation of Ser-2 directly represses transcription.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; X06642; CAA29851.1; -; Genomic_DNA.
DR   PIR; S01622; S01622.
DR   RefSeq; NP_999718.1; NM_214553.1.
DR   AlphaFoldDB; P16886; -.
DR   SMR; P16886; -.
DR   STRING; 7668.SPU_023663-tr; -.
DR   iPTMnet; P16886; -.
DR   EnsemblMetazoa; NM_214553; NP_999718; LOC373348.
DR   GeneID; 373348; -.
DR   KEGG; spu:373348; -.
DR   eggNOG; KOG1756; Eukaryota.
DR   HOGENOM; CLU_062828_3_3_1; -.
DR   InParanoid; P16886; -.
DR   OMA; WSVENDT; -.
DR   OrthoDB; 1504122at2759; -.
DR   PhylomeDB; P16886; -.
DR   Proteomes; UP000007110; Unassembled WGS sequence.
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; IBA:GO_Central.
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   1: Evidence at protein level;
KW   Acetylation; Chromosome; DNA-binding; Isopeptide bond; Methylation;
KW   Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..126
FT                   /note="Late histone H2A.L3"
FT                   /id="PRO_0000055282"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         105
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        120
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000305|PubMed:7796537"
SQ   SEQUENCE   126 AA;  13451 MW;  0C6B6D8D794A06F8 CRC64;
     MSGRGKGAGK ARAKAKSRSA RAGLQFPVGR VHRFLRKGNY AQRVGAGAPV YLAAVLEYLA
     AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLSG VTIAQGGVLP NIQAVLLPKK
     TSKASK