H2A3_PSAMI
ID H2A3_PSAMI Reviewed; 126 AA.
AC P69139; P02265;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Late histone H2A.3, gonadal;
OS Psammechinus miliaris (Green sea urchin) (Echinus miliaris).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Camarodonta; Echinidea; Parechinidae;
OC Psammechinus.
OX NCBI_TaxID=7660;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2412222; DOI=10.1073/pnas.82.17.5676;
RA Busslinger M., Barberis A.;
RT "Synthesis of sperm and late histone cDNAs of the sea urchin with a primer
RT complementary to the conserved 3' terminal palindrome: evidence for tissue-
RT specific and more general histone gene variants.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5676-5680(1985).
RN [2]
RP PROTEIN SEQUENCE OF 2-126, AND ACETYLATION AT SER-2.
RX PubMed=710427; DOI=10.1111/j.1432-1033.1978.tb12595.x;
RA Wouters D., Sautiere P., Biserte G.;
RT "Primary structure of histone H2A from gonad of the sea urchin Psammechinus
RT miliaris.";
RL Eur. J. Biochem. 90:231-239(1978).
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 -!- DEVELOPMENTAL STAGE: The different late H2A and H2B mRNAs are present
CC in as few as 200 copies in the egg and each accumulate to 3-5 x 100000
CC molecules in the gastrula embryo. The H2A-3 mRNA is also abundant in
CC testis RNA and codes for the H2A variant present in sperm chromatin.
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 EMBL; M11083; AAA30019.1; -; mRNA.
DR PIR; A38054; HSUR9M.
DR AlphaFoldDB; P69139; -.
DR SMR; P69139; -.
DR iPTMnet; P69139; -.
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:710427"
FT CHAIN 2..126
FT /note="Late histone H2A.3, gonadal"
FT /id="PRO_0000055272"
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:710427"
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"
FT CONFLICT 10..12
FT /note="AKG -> GKA (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 126 AA; 13411 MW; 635CB345206DB5DB CRC64;
MSGRGKGAKA KGKAKSRSSR AGLQFPVGRV HRFLRKGNYA NRVGAGAPVY LAAVLEYLAA
EILELAGNAA RDNKKTRIIP RHLQLAIRND EELNKLLGGV TIAQGGVLPN IQAVLLPKKT
GSKSSK
