ID   H3_PENVA                Reviewed;          43 AA.
AC   P83864;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=Histone H3;
DE   Flags: Fragments;
OS   Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC   Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC   Penaeoidea; Penaeidae; Penaeus.
OX   NCBI_TaxID=6689;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Hemocyte {ECO:0000269|PubMed:15606770};
RX   PubMed=15606770; DOI=10.1111/j.1432-1033.2004.04448.x;
RA   Patat S.A., Carnegie R.B., Kingsbury C., Gross P.S., Chapman R.,
RA   Schey K.L.;
RT   "Antimicrobial activity of histones from hemocytes of the Pacific white
RT   shrimp.";
RL   Eur. J. Biochem. 271:4825-4833(2004).
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 {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- MASS SPECTROMETRY: Mass=15330; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15606770};
CC   -!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000255}.
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DR   AlphaFoldDB; P83864; -.
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   SUPFAM; SSF47113; SSF47113; 1.
PE   1: Evidence at protein level;
KW   Chromosome; Direct protein sequencing; DNA-binding; Nucleosome core;
KW   Nucleus.
FT   CHAIN           <1..>43
FT                   /note="Histone H3"
FT                   /id="PRO_0000221308"
FT   NON_CONS        13..14
FT                   /evidence="ECO:0000303|PubMed:15606770"
FT   NON_CONS        26..27
FT                   /evidence="ECO:0000303|PubMed:15606770"
FT   NON_CONS        37..38
FT                   /evidence="ECO:0000303|PubMed:15606770"
FT   NON_TER         1
FT                   /evidence="ECO:0000303|PubMed:15606770"
FT   NON_TER         43
FT                   /evidence="ECO:0000303|PubMed:15606770"
SQ   SEQUENCE   43 AA;  5148 MW;  E2879B6557829DD1 CRC64;
     KPHRYRPGTV ALRSTELLIR KLPFQREIAQ DFKTDLRDIQ LAR