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H3L2_LILLO
ID   H3L2_LILLO              Reviewed;         100 AA.
AC   Q9XG57; Q2Z2F9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Histone H3-like 2;
DE   AltName: Full=Generative cell-specific histone H3;
DE   AltName: Full=Histone gcH3;
GN   Name=gcH3;
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=10092186; DOI=10.1023/a:1006162120037;
RA   Xu H., Swoboda I., Bhalla P.L., Singh M.B.;
RT   "Male gametic cell-specific expression of H2A and H3 histone genes.";
RL   Plant Mol. Biol. 39:607-614(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-84, 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:10092186,
CC       ECO:0000269|PubMed:16915513}.
CC   -!- DEVELOPMENTAL STAGE: Detected only in the generative cell of late
CC       bicellular pollen and not in early bicellular pollen. Also expressed in
CC       uninucleate microspores. {ECO:0000269|PubMed:10092186,
CC       ECO:0000269|PubMed:16915513}.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD55814.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAE48428.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAB40357.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ010975; CAB40357.1; ALT_INIT; mRNA.
DR   EMBL; AF090827; AAD55814.1; ALT_INIT; mRNA.
DR   EMBL; AB195645; BAE48428.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; Q9XG57; -.
DR   SMR; Q9XG57; -.
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; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR000164; Histone_H3/CENP-A.
DR   PANTHER; PTHR11426; PTHR11426; 1.
DR   PRINTS; PR00622; HISTONEH3.
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..100
FT                   /note="Histone H3-like 2"
FT                   /id="PRO_0000263049"
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        61
FT                   /note="G -> R (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="Q -> R (in Ref. 2)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        75..77
FT                   /note="RFK -> GFQ (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   100 AA;  11396 MW;  EFA2AC86BB6E0EBC CRC64;
     MARMKHTARM STGGKAPRKQ LASKALRKAP PPPTKGVKQP TTTTSGKWRF ARFHRKLPFQ
     GLVRKIWQDL KTHLRFKNHS VPPLEEVTEV YPCQTIGGCY
 
 
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