H2AV_CAEEL
ID H2AV_CAEEL Reviewed; 140 AA.
AC Q27511;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Histone H2A.V;
DE AltName: Full=H2A.F/Z;
GN Name=htz-1 {ECO:0000312|WormBase:R08C7.3};
GN ORFNames=R08C7.3 {ECO:0000312|WormBase:R08C7.3};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP DISRUPTION PHENOTYPE.
RX PubMed=16710447; DOI=10.1371/journal.pgen.0020074;
RA Cui M., Kim E.B., Han M.;
RT "Diverse chromatin remodeling genes antagonize the Rb-involved SynMuv
RT pathways in C. elegans.";
RL PLoS Genet. 2:E74-E74(2006).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24346701; DOI=10.1242/dev.090746;
RA Shibata Y., Sawa H., Nishiwaki K.;
RT "HTZ-1/H2A.z and MYS-1/MYST HAT act redundantly to maintain cell fates in
RT somatic gonadal cells through repression of ceh-22 in C. elegans.";
RL Development 141:209-218(2014).
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 (By similarity). Required to maintain non-distal
CC tip cell (DTC) fate of somatic gonadal cells through the repression of
CC transcription factor ceh-22 (PubMed:24346701).
CC {ECO:0000250|UniProtKB:P27661, ECO:0000269|PubMed:24346701}.
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 H2AV forms a heterodimer with H2B (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24346701}. Chromosome
CC {ECO:0000250|UniProtKB:P27661}. Note=Localizes in punctate structures
CC in the nucleus. {ECO:0000269|PubMed:24346701}.
CC -!- TISSUE SPECIFICITY: Expressed in somatic gonadal cells.
CC {ECO:0000269|PubMed:24346701}.
CC -!- PTM: Monoubiquitination of Lys-124 gives a specific tag for epigenetic
CC transcriptional repression. {ECO:0000250}.
CC -!- PTM: May be acetylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in sterility.
CC {ECO:0000269|PubMed:16710447}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; BX284604; CCD73086.1; -; Genomic_DNA.
DR PIR; T29662; T29662.
DR RefSeq; NP_500569.1; NM_068168.6.
DR PDB; 6K0C; X-ray; 2.28 A; D=17-124.
DR PDBsum; 6K0C; -.
DR AlphaFoldDB; Q27511; -.
DR SMR; Q27511; -.
DR BioGRID; 42342; 10.
DR STRING; 6239.R08C7.3.2; -.
DR EPD; Q27511; -.
DR PaxDb; Q27511; -.
DR PeptideAtlas; Q27511; -.
DR PRIDE; Q27511; -.
DR EnsemblMetazoa; R08C7.3.1; R08C7.3.1; WBGene00019947.
DR GeneID; 177212; -.
DR KEGG; cel:CELE_R08C7.3; -.
DR UCSC; R08C7.3.1; c. elegans.
DR CTD; 177212; -.
DR WormBase; R08C7.3; CE07426; WBGene00019947; htz-1.
DR eggNOG; KOG1757; Eukaryota.
DR GeneTree; ENSGT00940000174660; -.
DR HOGENOM; CLU_062828_2_2_1; -.
DR InParanoid; Q27511; -.
DR OMA; FPCGRIK; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; Q27511; -.
DR Reactome; R-CEL-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-CEL-212300; PRC2 methylates histones and DNA.
DR Reactome; R-CEL-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-CEL-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-CEL-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-CEL-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-CEL-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-CEL-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-CEL-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-CEL-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-CEL-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-CEL-9018519; Estrogen-dependent gene expression.
DR PRO; PR:Q27511; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00019947; Expressed in embryo and 4 other tissues.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0000793; C:condensed chromosome; IDA:WormBase.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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 GO; GO:0009996; P:negative regulation of cell fate specification; IGI:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:UniProtKB.
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 3D-structure; Acetylation; Chromosome; DNA-binding; Isopeptide bond;
KW Nucleosome core; Nucleus; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..140
FT /note="Histone H2A.V"
FT /id="PRO_0000239071"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT HELIX 22..25
FT /evidence="ECO:0007829|PDB:6K0C"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:6K0C"
FT HELIX 51..78
FT /evidence="ECO:0007829|PDB:6K0C"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:6K0C"
FT HELIX 86..94
FT /evidence="ECO:0007829|PDB:6K0C"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:6K0C"
SQ SEQUENCE 140 AA; 14669 MW; 3E3435A8FAE6D821 CRC64;
MAGGKGKAGK DSGKSKSKVV SRSARAGLQF PVGRIHRFLK QRTTSSGRVG ATAAVYSAAI
LEYLTAEVLE LAGNASKDLK VKRITPRHLH LAIRGDEELD TLIKATIAGG GVIPHIHRYL
MNKKGAPVPG KPGAPGQGPQ
