ID J9PB22_CANLF Unreviewed; 136 AA.
AC J9PB22;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Histone H3 {ECO:0000256|RuleBase:RU004471};
GN Name=H3C8 {ECO:0000313|Ensembl:ENSCAFP00845036234.1};
GN Synonyms=H3C11 {ECO:0000313|Ensembl:ENSCAFP00845022267.1},
GN LOC119867688 {ECO:0000313|Ensembl:ENSCAFP00845035205.1}, LOC119867704
GN {ECO:0000313|Ensembl:ENSCAFP00845022002.1};
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00845036234.1, ECO:0000313|Proteomes:UP000805418};
RN [1] {ECO:0000313|Ensembl:ENSCAFP00845036234.1}
RP IDENTIFICATION.
RC STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00845036234.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 {ECO:0000256|ARBA:ARBA00002001}.
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. {ECO:0000256|RuleBase:RU004471}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the histone H3 family.
CC {ECO:0000256|ARBA:ARBA00010343, ECO:0000256|RuleBase:RU004471}.
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DR RefSeq; XP_005640158.1; XM_005640101.2.
DR RefSeq; XP_013965998.1; XM_014110523.1.
DR RefSeq; XP_013966077.1; XM_014110602.1.
DR RefSeq; XP_013966115.1; XM_014110640.1.
DR RefSeq; XP_854287.2; XM_849194.4.
DR STRING; 9615.ENSCAFP00000043669; -.
DR PaxDb; 9615-ENSCAFP00000043669; -.
DR Ensembl; ENSCAFT00845027953.1; ENSCAFP00845022002.1; ENSCAFG00845015682.1.
DR Ensembl; ENSCAFT00845028301.1; ENSCAFP00845022267.1; ENSCAFG00845015914.1.
DR Ensembl; ENSCAFT00845028387.1; ENSCAFP00845022331.1; ENSCAFG00845015962.1.
DR Ensembl; ENSCAFT00845044837.1; ENSCAFP00845035137.1; ENSCAFG00845025410.1.
DR Ensembl; ENSCAFT00845044925.1; ENSCAFP00845035205.1; ENSCAFG00845025460.1.
DR Ensembl; ENSCAFT00845045048.1; ENSCAFP00845035310.1; ENSCAFG00845025523.1.
DR Ensembl; ENSCAFT00845046147.1; ENSCAFP00845036234.1; ENSCAFG00845026157.1.
DR Ensembl; ENSCAFT00845046307.1; ENSCAFP00845036367.1; ENSCAFG00845026258.1.
DR GeneID; 106558266; -.
DR GeneID; 488263; -.
DR KEGG; cfa:106558266; -.
DR KEGG; cfa:488263; -.
DR CTD; 8350; -.
DR CTD; 8968; -.
DR VEuPathDB; HostDB:ENSCAFG00845015682; -.
DR VEuPathDB; HostDB:ENSCAFG00845015914; -.
DR VEuPathDB; HostDB:ENSCAFG00845015962; -.
DR VEuPathDB; HostDB:ENSCAFG00845025410; -.
DR VEuPathDB; HostDB:ENSCAFG00845025460; -.
DR VEuPathDB; HostDB:ENSCAFG00845025523; -.
DR VEuPathDB; HostDB:ENSCAFG00845026157; -.
DR VEuPathDB; HostDB:ENSCAFG00845026258; -.
DR GeneTree; ENSGT01100000263514; -.
DR OMA; ASHPKKN; -.
DR OrthoDB; 5319100at2759; -.
DR Reactome; R-CFA-1266695; Interleukin-7 signaling.
DR Reactome; R-CFA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-CFA-212300; PRC2 methylates histones and DNA.
DR Reactome; R-CFA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-CFA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-CFA-3214815; HDACs deacetylate histones.
DR Reactome; R-CFA-3214841; PKMTs methylate histone lysines.
DR Reactome; R-CFA-3214842; HDMs demethylate histones.
DR Reactome; R-CFA-3214847; HATs acetylate histones.
DR Reactome; R-CFA-3214858; RMTs methylate histone arginines.
DR Reactome; R-CFA-3247509; Chromatin modifying enzymes.
DR Reactome; R-CFA-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-CFA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-CFA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-CFA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR Reactome; R-CFA-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-CFA-73728; RNA Polymerase I Promoter Opening.
DR Reactome; R-CFA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-CFA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-CFA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-CFA-983231; Factors involved in megakaryocyte development and platelet production.
DR Proteomes; UP000805418; Chromosome 35.
DR Bgee; ENSCAFG00000040996; Expressed in ovary and 31 other cell types or tissues.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
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; Histone, subunit A; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000164; Histone_H3/CENP-A.
DR PANTHER; PTHR11426; HISTONE H3; 1.
DR PANTHER; PTHR11426:SF242; HISTONE H3.1; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00622; HISTONEH3.
DR SMART; SM00428; H3; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR PROSITE; PS00322; HISTONE_H3_1; 1.
DR PROSITE; PS00959; HISTONE_H3_2; 1.
PE 3: Inferred from homology;
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Nucleosome core {ECO:0000256|RuleBase:RU004471};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU004471};
KW Reference proteome {ECO:0000313|Proteomes:UP000805418}.
FT DOMAIN 1..132
FT /note="Histone H2A/H2B/H3"
FT /evidence="ECO:0000259|Pfam:PF00125"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 136 AA; 15404 MW; 9B89008EA50A0EF6 CRC64;
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE
LLIRKLPFQR LVREIAQDFK TDLRFQSSAV MALQEACEAY LVGLFEDTNL CAIHAKRVTI
MPKDIQLARR IRGERA
//