ID   H2AV_RABIT              Reviewed;         128 AA.
AC   O62695;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Histone H2A.V;
DE   AltName: Full=H2A.F/Z;
GN   Name=H2AZ2 {ECO:0000250|UniProtKB:Q71UI9}; Synonyms=H2AV;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=New England white; TISSUE=Urinary bladder;
RX   PubMed=9571203; DOI=10.1006/bbrc.1998.8495;
RA   Jiang W., Guo X., Bhavanandan V.P.;
RT   "Histone H2A.F/Z subfamily: the smallest member and the signature
RT   sequence.";
RL   Biochem. Biophys. Res. Commun. 245:613-617(1998).
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 H2AZ2 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 during interphase.
CC       Acetylation disappears at mitosis (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC39253.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF030235; AAC39253.1; ALT_SEQ; mRNA.
DR   PIR; JE0093; JE0093.
DR   RefSeq; NP_001164412.1; NM_001170941.1.
DR   AlphaFoldDB; O62695; -.
DR   SMR; O62695; -.
DR   STRING; 9986.ENSOCUP00000007030; -.
DR   PRIDE; O62695; -.
DR   GeneID; 100328558; -.
DR   KEGG; ocu:100328558; -.
DR   CTD; 94239; -.
DR   eggNOG; KOG1757; Eukaryota.
DR   InParanoid; O62695; -.
DR   OrthoDB; 1504122at2759; -.
DR   Proteomes; UP000001811; Unplaced.
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; Nucleosome core; Nucleus;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000305"
FT   CHAIN           2..128
FT                   /note="Histone H2A.V"
FT                   /id="PRO_0000239070"
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|UniProtKB:Q3THW5"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3THW5"
FT   MOD_RES         12
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3THW5"
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"
SQ   SEQUENCE   128 AA;  13481 MW;  1F3C20383854041C CRC64;
     MAGGKAGKDS GKAKAKAVSR SQRAGLQFPV GRIHRHLKTR TTSHGRVGAT AAVYSAAILE
     YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGA IPHIHKSLIG
     KKGQQKTA