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H3L2_ARATH
ID   H3L2_ARATH              Reviewed;         137 AA.
AC   Q9FXI7; A6QRD3;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Histone H3-like 2;
DE   AltName: Full=Male gamete-specific histone H3;
GN   Name=MGH3; OrderedLocusNames=At1g19890; ORFNames=F6F9.5;
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;
RA   Bautista V.R., Kim C.J., Chen H., Quan R., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
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. Chromosome.
CC   -!- TISSUE SPECIFICITY: Pollen specific. {ECO:0000269|PubMed:16262706}.
CC   -!- DEVELOPMENTAL STAGE: Detected only in the generative cell and the
CC       sperm-cell of late bicellular and tricellular pollen. Not detected in
CC       pollen vegetative cells. Replication-independent expression.
CC       {ECO:0000269|PubMed:16262706}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. The high redundancy of
CC       histones H3 might compensate for this mutation.
CC       {ECO:0000269|PubMed:16262706}.
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
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DR   EMBL; AC007797; AAG12563.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE29910.1; -; Genomic_DNA.
DR   EMBL; BT030656; ABR46236.1; -; mRNA.
DR   PIR; C86332; C86332.
DR   RefSeq; NP_173418.1; NM_101844.2.
DR   AlphaFoldDB; Q9FXI7; -.
DR   SMR; Q9FXI7; -.
DR   BioGRID; 23816; 8.
DR   STRING; 3702.AT1G19890.1; -.
DR   PaxDb; Q9FXI7; -.
DR   PRIDE; Q9FXI7; -.
DR   ProteomicsDB; 247250; -.
DR   EnsemblPlants; AT1G19890.1; AT1G19890.1; AT1G19890.
DR   GeneID; 838577; -.
DR   Gramene; AT1G19890.1; AT1G19890.1; AT1G19890.
DR   KEGG; ath:AT1G19890; -.
DR   Araport; AT1G19890; -.
DR   TAIR; locus:2035415; AT1G19890.
DR   eggNOG; KOG1745; Eukaryota.
DR   HOGENOM; CLU_078295_4_0_1; -.
DR   InParanoid; Q9FXI7; -.
DR   OMA; KTRRPYR; -.
DR   OrthoDB; 1564596at2759; -.
DR   PhylomeDB; Q9FXI7; -.
DR   PRO; PR:Q9FXI7; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9FXI7; baseline and differential.
DR   Genevisible; Q9FXI7; AT.
DR   GO; GO:0048555; C:generative cell nucleus; IDA:TAIR.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IDA: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   GO; GO:0009567; P:double fertilization forming a zygote and endosperm; IEP:TAIR.
DR   GO; GO:0048235; P:pollen sperm cell differentiation; IEP:TAIR.
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; 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..137
FT                   /note="Histone H3-like 2"
FT                   /id="PRO_0000264606"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..27
FT                   /note="Basic and acidic residues"
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         10
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P59226"
FT   MOD_RES         10
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P59226"
FT   MOD_RES         10
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P59226"
FT   MOD_RES         10
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         28
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P59226"
FT   MOD_RES         28
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P59226"
FT   MOD_RES         28
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P59226"
FT   MOD_RES         38
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P59226"
FT   MOD_RES         38
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P59226"
FT   MOD_RES         38
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P59226"
SQ   SEQUENCE   137 AA;  15725 MW;  1D1B455A074F5254 CRC64;
     MARTKQTARK STGGKGPRKE LATKAARKTR RPYRGGVKRA HRFRPGTVAL REIRKYQKST
     DLLIRKLPFQ RLVREIAQDF KVDLRFQSHA VLALQEAAEA YLVGLFEDTN LCAIHAKRVT
     IMSKDIQLAR RIRGERA
 
 
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