H3L5_ARATH
ID H3L5_ARATH Reviewed; 139 AA.
AC Q9FKQ3;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Histone H3-like 5;
GN OrderedLocusNames=At5g65350; ORFNames=MNA5.8;
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=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(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].
RC STRAIN=cv. Columbia;
RA Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION.
RX PubMed=16262706; DOI=10.1111/j.1365-313x.2005.02554.x;
RA Okada T., Endo M., Singh M.B., Bhalla P.L.;
RT "Analysis of the histone H3 gene family in Arabidopsis and identification
RT of the male-gamete-specific variant AtMGH3.";
RL Plant J. 44:557-568(2005).
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 (By similarity). {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 DNA
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR EMBL; AB011479; BAB11557.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98042.1; -; Genomic_DNA.
DR EMBL; BT029340; ABK32154.1; -; mRNA.
DR RefSeq; NP_201338.1; NM_125933.2.
DR AlphaFoldDB; Q9FKQ3; -.
DR SMR; Q9FKQ3; -.
DR BioGRID; 21902; 8.
DR STRING; 3702.AT5G65350.1; -.
DR PaxDb; Q9FKQ3; -.
DR PRIDE; Q9FKQ3; -.
DR EnsemblPlants; AT5G65350.1; AT5G65350.1; AT5G65350.
DR GeneID; 836660; -.
DR Gramene; AT5G65350.1; AT5G65350.1; AT5G65350.
DR KEGG; ath:AT5G65350; -.
DR Araport; AT5G65350; -.
DR TAIR; locus:2168267; AT5G65350.
DR eggNOG; KOG1745; Eukaryota.
DR HOGENOM; CLU_078295_4_0_1; -.
DR InParanoid; Q9FKQ3; -.
DR OMA; NIFFPPM; -.
DR OrthoDB; 1564596at2759; -.
DR PhylomeDB; Q9FKQ3; -.
DR PRO; PR:Q9FKQ3; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKQ3; baseline and differential.
DR Genevisible; Q9FKQ3; AT.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; PTHR11426; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..139
FT /note="Histone H3-like 5"
FT /id="PRO_0000264609"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 5
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 5
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 15
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 19
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 19
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 24
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 24
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 37
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 37
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
FT MOD_RES 37
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59226"
SQ SEQUENCE 139 AA; 15591 MW; 0F9C36EF54B9D7B8 CRC64;
MARTKQTARI STGGKAPRKQ LAPKAARQSA PATGGVKKPH RFRPGTVALR DIRKYQKSTE
ILIRKLPFQR LVREIAQDFK TDLRFQSSAV AALQEAAEAY LVGLFEDTNL CAIHAKRVTI
MPKEIQLARR IRGERARGE