H2AV3_ARATH
ID H2AV3_ARATH Reviewed; 134 AA.
AC Q9C944;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Probable histone H2A variant 3;
DE AltName: Full=H2A.F/Z 3;
DE AltName: Full=HTA9;
GN OrderedLocusNames=At1g52740; ORFNames=F14G24.1;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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).
CC -!- FUNCTION: Variant histones H2A are synthesized throughout the cell
CC cycle and are very different from classical S-phase regulated H2A. May
CC replace conventional H2A in a subset of nucleosomes. Nucleosomes wrap
CC and compact DNA into chromatin, limiting DNA accessibility to the
CC cellular machineries which require DNA as a template. Histones thereby
CC play a central role in transcription regulation, DNA repair, DNA
CC replication and chromosomal stability. DNA accessibility is regulated
CC via a complex set of post-translational modifications of histones, also
CC called histone code, and nucleosome remodeling (By similarity).
CC {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.
CC -!- INTERACTION:
CC Q9C944; Q39016: CPK11; NbExp=9; IntAct=EBI-1537419, EBI-979321;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; AC019018; AAG52265.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE32847.1; -; Genomic_DNA.
DR EMBL; AY054557; AAK96748.1; -; mRNA.
DR EMBL; AY058147; AAL25563.1; -; mRNA.
DR EMBL; AY084390; AAM60967.1; -; mRNA.
DR EMBL; AY064631; AAL47344.1; -; mRNA.
DR PIR; D96568; D96568.
DR RefSeq; NP_175683.1; NM_104152.4.
DR AlphaFoldDB; Q9C944; -.
DR SMR; Q9C944; -.
DR BioGRID; 26932; 3.
DR IntAct; Q9C944; 3.
DR STRING; 3702.AT1G52740.1; -.
DR PaxDb; Q9C944; -.
DR PRIDE; Q9C944; -.
DR ProteomicsDB; 230178; -.
DR EnsemblPlants; AT1G52740.1; AT1G52740.1; AT1G52740.
DR GeneID; 841707; -.
DR Gramene; AT1G52740.1; AT1G52740.1; AT1G52740.
DR KEGG; ath:AT1G52740; -.
DR Araport; AT1G52740; -.
DR TAIR; locus:2011456; AT1G52740.
DR eggNOG; KOG1757; Eukaryota.
DR HOGENOM; CLU_062828_2_4_1; -.
DR InParanoid; Q9C944; -.
DR OMA; TRRWTIA; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; Q9C944; -.
DR PRO; PR:Q9C944; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C944; baseline and differential.
DR Genevisible; Q9C944; AT.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA: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:0044030; P:regulation of DNA methylation; IGI:TAIR.
DR GO; GO:0010468; P:regulation of gene expression; IGI:TAIR.
DR GO; GO:0009266; P:response to temperature stimulus; 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; Reference proteome.
FT CHAIN 1..134
FT /note="Probable histone H2A variant 3"
FT /id="PRO_0000055314"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 134 AA; 14272 MW; BE63E2B00DC3955A CRC64;
MSGKGAKGLI MGKPSGSDKD KDKKKPITRS SRAGLQFPVG RVHRLLKTRS TAHGRVGATA
AVYTAAILEY LTAEVLELAG NASKDLKVKR ISPRHLQLAI RGDEELDTLI KGTIAGGGVI
PHIHKSLINK SAKE
