ID   H2A7_ARATH              Reviewed;         150 AA.
AC   Q9FJE8;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Probable histone H2A.7;
DE   AltName: Full=HTA6;
GN   OrderedLocusNames=At5g59870; ORFNames=MMN10.22, MMN10_90;
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=9872454; DOI=10.1093/dnares/5.5.297;
RA   Nakamura Y., Sato S., Asamizu E., Kaneko T., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VII. Sequence
RT   features of the regions of 1,013,767 bp covered by sixteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:297-308(1998).
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].
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [5]
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   [6]
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   [7]
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).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
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: Strong expression through-out the roots and leaves.
CC       Also found in meristems and dividing cells.
CC       {ECO:0000269|PubMed:16751347}.
CC   -!- DOMAIN: Contains one SPKK motif which may interact with the minor
CC       groove of A/T-rich DNA sites. Phosphorylation of this motif may
CC       regulate DNA binding. This motif is reiterated in both termini of
CC       histone H1 and in the N-terminus of sea urchin histones H2B, but its
CC       presence in the C-terminus seems to be unique to plant H2A.
CC   -!- PTM: Not ubiquitinated.
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR   EMBL; AB015475; BAB08355.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED97244.1; -; Genomic_DNA.
DR   EMBL; AY085948; AAM63158.1; -; mRNA.
DR   EMBL; AK117890; BAC42529.1; -; mRNA.
DR   EMBL; BT003669; AAO39897.1; -; mRNA.
DR   RefSeq; NP_200795.1; NM_125380.4.
DR   AlphaFoldDB; Q9FJE8; -.
DR   SMR; Q9FJE8; -.
DR   BioGRID; 21353; 5.
DR   IntAct; Q9FJE8; 1.
DR   STRING; 3702.AT5G59870.1; -.
DR   iPTMnet; Q9FJE8; -.
DR   PaxDb; Q9FJE8; -.
DR   PRIDE; Q9FJE8; -.
DR   ProteomicsDB; 230123; -.
DR   EnsemblPlants; AT5G59870.1; AT5G59870.1; AT5G59870.
DR   GeneID; 836109; -.
DR   Gramene; AT5G59870.1; AT5G59870.1; AT5G59870.
DR   KEGG; ath:AT5G59870; -.
DR   Araport; AT5G59870; -.
DR   TAIR; locus:2168148; AT5G59870.
DR   eggNOG; KOG1756; Eukaryota.
DR   HOGENOM; CLU_062828_3_1_1; -.
DR   InParanoid; Q9FJE8; -.
DR   OMA; HRHKAQS; -.
DR   OrthoDB; 1504122at2759; -.
DR   PhylomeDB; Q9FJE8; -.
DR   PRO; PR:Q9FJE8; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FJE8; baseline and differential.
DR   Genevisible; Q9FJE8; AT.
DR   GO; GO:0000792; C:heterochromatin; IDA:TAIR.
DR   GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005721; C:pericentric heterochromatin; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0003682; F:chromatin binding; IDA:TAIR.
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:0070828; P:heterochromatin organization; IGI:TAIR.
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; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..150
FT                   /note="Probable histone H2A.7"
FT                   /id="PRO_0000055204"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           146..149
FT                   /note="SPKK motif"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19376835"
SQ   SEQUENCE   150 AA;  15966 MW;  7CFEB84C42D6EB5C CRC64;
     MESTGKVKKA FGGRKPPGAP KTKSVSKSMK AGLQFPVGRI TRFLKKGRYA QRLGGGAPVY
     MAAVLEYLAA EVLELAGNAA RDNKKSRIIP RHLLLAIRND EELGKLLSGV TIAHGGVLPN
     INSVLLPKKS ATKPAEEKAT KSPVKSPKKA