ID   H3L3_LILLO              Reviewed;         155 AA.
AC   Q2Z2F6; Q2Z2F5;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 51.
DE   RecName: Full=Histone H3-like 3;
DE   AltName: Full=Histone leH3;
DE   AltName: Full=Late embryonic-like histone H3;
GN   Name=leH3;
OS   Lilium longiflorum (Trumpet lily).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Liliales; Liliaceae; Lilium.
OX   NCBI_TaxID=4690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE, AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=cv. White Fox;
RX   PubMed=16915513; DOI=10.1007/s11103-006-9036-8;
RA   Okada T., Singh M.B., Bhalla P.L.;
RT   "Histone H3 variants in male gametic cells of lily and H3 methylation in
RT   mature pollen.";
RL   Plant Mol. Biol. 62:503-512(2006).
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. Chromosome.
CC   -!- TISSUE SPECIFICITY: Pollen specific. {ECO:0000269|PubMed:16915513}.
CC   -!- DEVELOPMENTAL STAGE: Detected in the generative cell of bicellular
CC       pollen. Also expressed in uninucleate microspores.
CC       {ECO:0000269|PubMed:16915513}.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR   EMBL; AB195648; BAE48431.1; -; mRNA.
DR   EMBL; AB195649; BAE48432.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2Z2F6; -.
DR   SMR; Q2Z2F6; -.
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; 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; -; 2.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR000164; Histone_H3/CENP-A.
DR   PANTHER; PTHR11426; PTHR11426; 2.
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.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA-binding; Nucleosome core; Nucleus.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..155
FT                   /note="Histone H3-like 3"
FT                   /id="PRO_0000263050"
FT   REGION          34..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        32
FT                   /note="P -> Q (in Ref. 1; BAE48432)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="E -> G (in Ref. 1; BAE48432)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   155 AA;  17442 MW;  2F051F636F2D712F CRC64;
     MARMKLNARM STGGKAPRKQ LAYKAVRKAA PPTIGVKLPN SYRPGDQTVC KPAPPTDGVK
     EPHRYRPGKM GLREIRKYKK NARFFISKLP FHRLVRKITQ NLKAHLRFQS TAMPAPEEVS
     EAYLVKLFED AIHAKRVTLV PKDIQLARCI GGVLA