H2AV_DROME
ID H2AV_DROME Reviewed; 141 AA.
AC P08985; A0ANX7; A0ANX8; A0ANY0; A0ANY3; C0MJB2; C0MJB9; Q26252; Q540X2;
AC Q9VBB1;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Histone H2A.v;
DE AltName: Full=H2A.F/Z;
DE Short=H2A.Z;
GN Name=His2Av; Synonyms=H2AvD, His2AvD; ORFNames=CG5499;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=3137528; DOI=10.1093/nar/16.15.7487;
RA van Daal A., White E.M., Gorovsky M.A., Elgin S.C.R.;
RT "Drosophila has a single copy of the gene encoding a highly conserved
RT histone H2A variant of the H2A.F/Z type.";
RL Nucleic Acids Res. 16:7487-7497(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Canton-S;
RX PubMed=2111857; DOI=10.1007/bf02101116;
RA van Daal A., White E.M., Elgin S.C.R., Gorovsky M.A.;
RT "Conservation of intron position indicates separation of major and variant
RT H2As is an early event in the evolution of eukaryotes.";
RL J. Mol. Evol. 30:449-455(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ZBMEL131, ZBMEL186, ZBMEL191, ZBMEL377, ZBMEL384, ZBMEL82, ZBMEL84,
RC and ZBMEL95;
RX PubMed=16951084; DOI=10.1534/genetics.106.058008;
RA Proeschel M., Zhang Z., Parsch J.;
RT "Widespread adaptive evolution of Drosophila genes with sex-biased
RT expression.";
RL Genetics 174:893-900(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-95.
RC STRAIN=MEL01, MEL02, MEL11, MEL12, MEL13, MEL14, MEL15, MEL16, MEL17,
RC MEL18, MEL19, and MEL20;
RX PubMed=19126864; DOI=10.1093/molbev/msn297;
RA Parsch J., Zhang Z., Baines J.F.;
RT "The influence of demography and weak selection on the McDonald-Kreitman
RT test: an empirical study in Drosophila.";
RL Mol. Biol. Evol. 26:691-698(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [6]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-53, FUNCTION, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=1498368; DOI=10.1091/mbc.3.6.593;
RA Van Daal A., Elgin S.C.R.;
RT "A histone variant, H2AvD, is essential in Drosophila melanogaster.";
RL Mol. Biol. Cell 3:593-602(1992).
RN [9]
RP FUNCTION.
RX PubMed=10385122; DOI=10.1038/21436;
RA Clarkson M.J., Wells J.R.E., Gibson F., Saint R., Tremethick D.J.;
RT "Regions of variant histone His2AvD required for Drosophila development.";
RL Nature 399:694-697(1999).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=10801889; DOI=10.1074/jbc.m910206199;
RA Leach T.J., Mazzeo M., Chotkowski H.L., Madigan J.P., Wotring M.G.,
RA Glaser R.L.;
RT "Histone H2A.Z is widely but nonrandomly distributed in chromosomes of
RT Drosophila melanogaster.";
RL J. Biol. Chem. 275:23267-23272(2000).
RN [11]
RP FUNCTION, AND PHOSPHORYLATION AT SER-138.
RX PubMed=12202754; DOI=10.1093/nar/gkf496;
RA Madigan J.P., Chotkowski H.L., Glaser R.L.;
RT "DNA double-strand break-induced phosphorylation of Drosophila histone
RT variant H2Av helps prevent radiation-induced apoptosis.";
RL Nucleic Acids Res. 30:3698-3705(2002).
RN [12]
RP ACETYLATION AT LYS-5.
RX PubMed=15528408; DOI=10.1126/science.1103455;
RA Kusch T., Florens L., Macdonald W.H., Swanson S.K., Glaser R.L.,
RA Yates J.R. III, Abmayr S.M., Washburn M.P., Workman J.L.;
RT "Acetylation by Tip60 is required for selective histone variant exchange at
RT DNA lesions.";
RL Science 306:2084-2087(2004).
RN [13]
RP FUNCTION.
RX PubMed=15630020; DOI=10.1101/gad.1259105;
RA Swaminathan J., Baxter E.M., Corces V.G.;
RT "The role of histone H2Av variant replacement and histone H4 acetylation in
RT the establishment of Drosophila heterochromatin.";
RL Genes Dev. 19:65-76(2005).
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. Acts as a Polycomb group (PcG) protein required
CC to maintain the transcriptionally repressive state of homeotic genes of
CC the animal throughout development. Required for histone H3 'Lys-9'
CC methylation and histone H4 'Lys-12' acetylation, two modifications that
CC are essential for heterochromatin formation. Also involved in DNA
CC double strand break (DSB) repair. Essential for early development.
CC {ECO:0000269|PubMed:10385122, ECO:0000269|PubMed:12202754,
CC ECO:0000269|PubMed:1498368, ECO:0000269|PubMed:15630020}.
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 His2Av forms a heterodimer with H2B.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10801889}. Chromosome
CC {ECO:0000269|PubMed:10801889}. Note=Widely distributed in the genome,
CC irrespective of the transcriptional status or coding capacity of the
CC sequence.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed in embryos and adults (females only).
CC {ECO:0000269|PubMed:1498368}.
CC -!- DOMAIN: The [ST]-Q motif constitutes a recognition sequence for kinases
CC from the PI3/PI4-kinase family.
CC -!- PTM: Phosphorylated. Phosphorylation of Ser-138 occurs in response to
CC DNA double strand breaks (DSBs) generated by exogenous genotoxic
CC agents. Phosphorylation is dependent on the DNA damage checkpoint
CC kinases ATR and ATM, spreads on either side of a detected DSB site and
CC may mark the surrounding chromatin for recruitment of proteins required
CC for DNA damage signaling and repair. {ECO:0000269|PubMed:12202754}.
CC -!- PTM: Acetylated on Lys-5 by Tip60. Acetylation is enhanced by Ser-138
CC phosphorylation and promotes the exchange of the phosphorylated form
CC with the unmodified form of H2AV. {ECO:0000269|PubMed:12202754,
CC ECO:0000269|PubMed:15528408}.
CC -!- PTM: Monoubiquitination of Lys-121 by sce/dRING gives a specific tag
CC for epigenetic transcriptional repression. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; X07485; CAA30370.1; -; mRNA.
DR EMBL; X15549; CAA33555.1; -; Genomic_DNA.
DR EMBL; AM294365; CAL26295.1; -; Genomic_DNA.
DR EMBL; AM294366; CAL26296.1; -; Genomic_DNA.
DR EMBL; AM294367; CAL26297.1; -; Genomic_DNA.
DR EMBL; AM294368; CAL26298.1; -; Genomic_DNA.
DR EMBL; AM294369; CAL26299.1; -; Genomic_DNA.
DR EMBL; AM294370; CAL26300.1; -; Genomic_DNA.
DR EMBL; AM294371; CAL26301.1; -; Genomic_DNA.
DR EMBL; AM294372; CAL26302.1; -; Genomic_DNA.
DR EMBL; FM245434; CAR93360.1; -; Genomic_DNA.
DR EMBL; FM245435; CAR93361.1; -; Genomic_DNA.
DR EMBL; FM245436; CAR93362.1; -; Genomic_DNA.
DR EMBL; FM245437; CAR93363.1; -; Genomic_DNA.
DR EMBL; FM245438; CAR93364.1; -; Genomic_DNA.
DR EMBL; FM245439; CAR93365.1; -; Genomic_DNA.
DR EMBL; FM245440; CAR93366.1; -; Genomic_DNA.
DR EMBL; FM245441; CAR93367.1; -; Genomic_DNA.
DR EMBL; FM245442; CAR93368.1; -; Genomic_DNA.
DR EMBL; FM245443; CAR93369.1; -; Genomic_DNA.
DR EMBL; FM245444; CAR93370.1; -; Genomic_DNA.
DR EMBL; FM245445; CAR93371.1; -; Genomic_DNA.
DR EMBL; AE014297; AAF56631.1; -; Genomic_DNA.
DR EMBL; AY118910; AAM50770.1; -; mRNA.
DR EMBL; S42733; AAB22897.1; -; Genomic_DNA.
DR PIR; S08118; S08118.
DR RefSeq; NP_001262997.1; NM_001276068.1.
DR RefSeq; NP_524519.1; NM_079795.3.
DR AlphaFoldDB; P08985; -.
DR SMR; P08985; -.
DR BioGRID; 68120; 31.
DR DIP; DIP-23205N; -.
DR IntAct; P08985; 3.
DR MINT; P08985; -.
DR STRING; 7227.FBpp0084434; -.
DR iPTMnet; P08985; -.
DR PaxDb; P08985; -.
DR PRIDE; P08985; -.
DR DNASU; 43229; -.
DR EnsemblMetazoa; FBtr0085062; FBpp0084434; FBgn0001197.
DR EnsemblMetazoa; FBtr0334311; FBpp0306426; FBgn0001197.
DR GeneID; 43229; -.
DR KEGG; dme:Dmel_CG5499; -.
DR CTD; 43229; -.
DR FlyBase; FBgn0001197; His2Av.
DR VEuPathDB; VectorBase:FBgn0001197; -.
DR eggNOG; KOG1757; Eukaryota.
DR GeneTree; ENSGT00900000140979; -.
DR HOGENOM; CLU_062828_2_2_1; -.
DR InParanoid; P08985; -.
DR OMA; FPCGRIK; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; P08985; -.
DR Reactome; R-DME-212300; PRC2 methylates histones and DNA.
DR Reactome; R-DME-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DME-3214858; RMTs methylate histone arginines.
DR Reactome; R-DME-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-DME-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-DME-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-DME-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-DME-9018519; Estrogen-dependent gene expression.
DR SignaLink; P08985; -.
DR BioGRID-ORCS; 43229; 1 hit in 3 CRISPR screens.
DR ChiTaRS; His2Av; fly.
DR GenomeRNAi; 43229; -.
DR PRO; PR:P08985; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0001197; Expressed in egg cell and 41 other tissues.
DR ExpressionAtlas; P08985; baseline and differential.
DR Genevisible; P08985; DM.
DR GO; GO:0005694; C:chromosome; IDA:FlyBase.
DR GO; GO:0000786; C:nucleosome; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005701; C:polytene chromosome chromocenter; IDA:FlyBase.
DR GO; GO:0035861; C:site of double-strand break; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0036098; P:male germ-line stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IGI:FlyBase.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:FlyBase.
DR GO; GO:0071168; P:protein localization to chromatin; IDA:FlyBase.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:FlyBase.
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; Developmental protein; DNA damage; DNA repair;
KW DNA-binding; Isopeptide bond; Nucleosome core; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..141
FT /note="Histone H2A.v"
FT /id="PRO_0000055309"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..103
FT /note="Essential for function in development"
FT MOTIF 138..139
FT /note="[ST]-Q motif"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15528408"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:12202754"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT VARIANT 25
FT /note="G -> D (in strain: ZBMEL377)"
FT VARIANT 90
FT /note="A -> T (in strain: ZBMEL131)"
FT VARIANT 95
FT /note="E -> K (in strain: MEL16 and ZBMEL84)"
FT /evidence="ECO:0000269|PubMed:19126864"
SQ SEQUENCE 141 AA; 14981 MW; 0DA41C01F831A5B6 CRC64;
MAGGKAGKDS GKAKAKAVSR SARAGLQFPV GRIHRHLKSR TTSHGRVGAT AAVYSAAILE
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
KKEETVQDPQ RKGNVILSQA Y
