ID   H2AV_PAGMA              Reviewed;         128 AA.
AC   Q6Y237;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Histone H2A.V;
DE   AltName: Full=H2A.F/Z;
GN   Name=h2az2;
OS   Pagrus major (Red sea bream) (Chrysophrys major).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Spariformes; Sparidae; Pagrus.
OX   NCBI_TaxID=143350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Spleen;
RX   AGRICOLA=IND43674139; DOI=10.1016/j.aquaculture.2004.07.008;
RA   Chen S.-L., Xu M.-Y., Hu S.-L., Li L.;
RT   "Analysis of immune-relevant genes expressed in red sea bream spleen.";
RL   Aquaculture 240:115-130(2004).
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 H2AZ1 forms a heterodimer with H2B (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic
CC       transcriptional repression. {ECO:0000250}.
CC   -!- PTM: Acetylated on Lys-5, Lys-8 and Lys-12 when associated with the 5'-
CC       end of active genes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; AY190700; AAP20175.1; -; mRNA.
DR   AlphaFoldDB; Q6Y237; -.
DR   SMR; Q6Y237; -.
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   Acetylation; Chromosome; DNA-binding; Isopeptide bond; Nucleosome core;
KW   Nucleus; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..128
FT                   /note="Histone H2A.V"
FT                   /id="PRO_0000055305"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         12
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         14
FT                   /note="N6-lactoyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   MOD_RES         116
FT                   /note="N6-lactoyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT   CROSSLNK        122
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   128 AA;  13509 MW;  1F3C388F6854041C CRC64;
     MAGGKAGKDS GKAKAKAVSR SQRAGLQFPV GRIHRHLKTR TTSHGRVGAT AAVYSAAILE
     YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
     KKGQQKTA