ID   H2AV_STRPU              Reviewed;         125 AA.
AC   P08991;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Histone H2A.V;
DE   AltName: Full=H2A.F/Z;
DE   Flags: Fragment;
GN   Name=H2A.F/Z;
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 [MRNA].
RX   PubMed=2438657; DOI=10.1093/nar/15.11.4629;
RA   Ernst S.G., Miller H., Brenner C.A., Nocente-Mcgrath C., Francis S.,
RA   McIsaac R.;
RT   "Characterization of a cDNA clone coding for a sea urchin histone H2A
RT   variant related to the H2A.F/Z histone protein in vertebrates.";
RL   Nucleic Acids Res. 15:4629-4644(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: Variant histone H2A which replaces conventional H2A in a
CC       subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin,
CC       limiting DNA accessibility to the cellular machineries which require
CC       DNA as a template. Histones thereby play a central role in
CC       transcription regulation, DNA repair, DNA replication and chromosomal
CC       stability. DNA accessibility is regulated via a complex set of post-
CC       translational modifications of histones, also called histone code, and
CC       nucleosome remodeling. May be involved in the formation of constitutive
CC       heterochromatin. May be required for chromosome segregation during cell
CC       division (By similarity). {ECO:0000250}.
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. H2A or its variant H2AF/Z forms a heterodimer with H2B (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC   -!- PTM: Monoubiquitination of Lys-119 gives a specific tag for epigenetic
CC       transcriptional repression. {ECO:0000305}.
CC   -!- PTM: May be acetylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; X05547; CAA29061.1; -; mRNA.
DR   PIR; S07392; S07392.
DR   AlphaFoldDB; P08991; -.
DR   SMR; P08991; -.
DR   STRING; 7668.SPU_024890-tr; -.
DR   iPTMnet; P08991; -.
DR   eggNOG; KOG1757; Eukaryota.
DR   HOGENOM; CLU_1965151_0_0_1; -.
DR   InParanoid; P08991; -.
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; Nucleosome core;
KW   Nucleus; Reference proteome; Ubl conjugation.
FT   CHAIN           <1..125
FT                   /note="Histone H2A.V"
FT                   /id="PRO_0000055310"
FT   CROSSLNK        119
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000305|PubMed:7796537"
FT   NON_TER         1
SQ   SEQUENCE   125 AA;  13164 MW;  F65A17FDF263823F CRC64;
     GKAGKDSGKA KAKAVSRSAR AGLQFPVGRI HRHLKNRTTS HGRVGATAAV YSAAILEYLT
     AEVLELAGNA SKDLKVKRIT PRHLQLAIRG DEELDSLIKA TIAGGGVIPH IHKSLIGKKG
     SQKAT