ID   H2A2_ARATH              Reviewed;         132 AA.
AC   Q9LHQ5;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Probable histone H2A.2;
DE   AltName: Full=HTA13;
GN   OrderedLocusNames=At3g20670; ORFNames=F3H11.6;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY, AND NOMENCLATURE.
RX   PubMed=16751347; DOI=10.1105/tpc.105.039719;
RA   Yi H., Sardesai N., Fujinuma T., Chan C.-W., Veena X., Gelvin S.B.;
RT   "Constitutive expression exposes functional redundancy between the
RT   Arabidopsis histone H2A gene HTA1 and other H2A gene family members.";
RL   Plant Cell 18:1575-1589(2006).
RN   [6]
RP   LACK OF UBIQUITINATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17554311; DOI=10.1038/nature05864;
RA   Sridhar V.V., Kapoor A., Zhang K., Zhu J., Zhou T., Hasegawa P.M.,
RA   Bressan R.A., Zhu J.-K.;
RT   "Control of DNA methylation and heterochromatic silencing by histone H2B
RT   deubiquitination.";
RL   Nature 447:735-738(2007).
CC   -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC       DNA into chromatin, limiting DNA accessibility to the cellular
CC       machineries which require DNA as a template. Histones thereby play a
CC       central role in transcription regulation, DNA repair, DNA replication
CC       and chromosomal stability. DNA accessibility is regulated via a complex
CC       set of post-translational modifications of histones, also called
CC       histone code, and nucleosome remodeling.
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.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in non-dividing tissues of the
CC       plant. Also found in meristems and dividing cells.
CC       {ECO:0000269|PubMed:16751347}.
CC   -!- PTM: Not ubiquitinated.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; AP002034; BAB02243.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE76410.1; -; Genomic_DNA.
DR   EMBL; AY045967; AAK76641.1; -; mRNA.
DR   EMBL; AY079320; AAL85051.1; -; mRNA.
DR   EMBL; AY085312; AAM62543.1; -; mRNA.
DR   RefSeq; NP_188703.1; NM_112958.4.
DR   AlphaFoldDB; Q9LHQ5; -.
DR   SMR; Q9LHQ5; -.
DR   BioGRID; 6946; 7.
DR   IntAct; Q9LHQ5; 7.
DR   STRING; 3702.AT3G20670.1; -.
DR   PaxDb; Q9LHQ5; -.
DR   PRIDE; Q9LHQ5; -.
DR   ProteomicsDB; 247209; -.
DR   EnsemblPlants; AT3G20670.1; AT3G20670.1; AT3G20670.
DR   GeneID; 821614; -.
DR   Gramene; AT3G20670.1; AT3G20670.1; AT3G20670.
DR   KEGG; ath:AT3G20670; -.
DR   Araport; AT3G20670; -.
DR   TAIR; locus:2083430; AT3G20670.
DR   eggNOG; KOG1756; Eukaryota.
DR   HOGENOM; CLU_062828_3_0_1; -.
DR   InParanoid; Q9LHQ5; -.
DR   OMA; FRFIMSS; -.
DR   OrthoDB; 1504122at2759; -.
DR   PhylomeDB; Q9LHQ5; -.
DR   PRO; PR:Q9LHQ5; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LHQ5; baseline and differential.
DR   Genevisible; Q9LHQ5; AT.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
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   Chromosome; DNA-binding; Nucleosome core; Nucleus; Reference proteome.
FT   CHAIN           1..132
FT                   /note="Probable histone H2A.2"
FT                   /id="PRO_0000055200"
SQ   SEQUENCE   132 AA;  13849 MW;  0D5ED60734766CE3 CRC64;
     MAGRGKTLGS GVAKKSTSRS SKAGLQFPVG RIARFLKNGK YATRVGAGAP VYLAAVLEYL
     AAEVLELAGN AARDNKKTRI VPRHIQLAVR NDEELSKLLG DVTIANGGVM PNIHSLLLPK
     KAGASKPSAD ED