ID   H2A_PARAN               Reviewed;         126 AA.
AC   P69140; P02265;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Histone H2A, gonadal;
OS   Parechinus angulosus (Angulate sea urchin) (Cidaris angulosus).
OC   Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC   Euechinoidea; Echinacea; Camarodonta; Echinidea; Echinidae; Parechinus.
OX   NCBI_TaxID=7658;
RN   [1]
RP   PROTEIN SEQUENCE OF 2-126, AND ACETYLATION AT SER-2.
RX   PubMed=6997045; DOI=10.1111/j.1432-1033.1980.tb04779.x;
RA   Strickland W.N., Strickland M.S., de Groot P.C., von Holt C.;
RT   "The primary structure of histone H2A from the sperm cell of the sea urchin
RT   Parechinus angulosus.";
RL   Eur. J. Biochem. 109:151-158(1980).
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-119 gives a specific tag for epigenetic
CC       transcriptional repression. {ECO:0000250}.
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   PIR; A37574; HSUR9P.
DR   AlphaFoldDB; P69140; -.
DR   SMR; P69140; -.
DR   iPTMnet; P69140; -.
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   1: Evidence at protein level;
KW   Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW   Isopeptide bond; Methylation; Nucleosome core; Nucleus; Phosphoprotein;
KW   Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6997045"
FT   CHAIN           2..126
FT                   /note="Histone H2A, gonadal"
FT                   /id="PRO_0000055261"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:6997045"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         104
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        119
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   126 AA;  13411 MW;  635CB345206DB5DB CRC64;
     MSGRGKGAKA KGKAKSRSSR AGLQFPVGRV HRFLRKGNYA NRVGAGAPVY LAAVLEYLAA
     EILELAGNAA RDNKKTRIIP RHLQLAIRND EELNKLLGGV TIAQGGVLPN IQAVLLPKKT
     GSKSSK