H1T_RAT
ID H1T_RAT Reviewed; 208 AA.
AC P06349;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Histone H1t;
GN Name=H1-6 {ECO:0000250|UniProtKB:P22492};
GN Synonyms=H1f6 {ECO:0000312|RGD:2778}, H1ft, H1t;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=2423516; DOI=10.1016/s0021-9258(17)38371-0;
RA Cole K.D., Kandala J.C., Kistler W.S.;
RT "Isolation of the gene for the testis-specific H1 histone variant H1t.";
RL J. Biol. Chem. 261:7178-7183(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=1706721; DOI=10.1016/s0021-9258(18)38164-x;
RA Wolfe S.A., Grimes S.R.;
RT "Protein-DNA interactions within the rat histone H4t promoter.";
RL J. Biol. Chem. 266:6637-6643(1991).
RN [3]
RP PROTEIN SEQUENCE OF 2-109.
RX PubMed=3947637; DOI=10.1016/0167-4838(86)90062-2;
RA Cole K.D., York R.G., Kistler W.S.;
RT "Sequence of the amino terminal half of rat testis-specific histone variant
RT H1t.";
RL Biochim. Biophys. Acta 869:223-229(1986).
RN [4]
RP MUTAGENESIS OF GLN-54.
RX PubMed=17052712; DOI=10.1016/j.febslet.2006.09.061;
RA Ramesh S., Bharath M.M., Chandra N.R., Rao M.R.;
RT "A K52Q substitution in the globular domain of histone H1t modulates its
RT nucleosome binding properties.";
RL FEBS Lett. 580:5999-6006(2006).
RN [5]
RP PHOSPHORYLATION AT SER-9; SER-141; THR-156; SER-178 AND SER-187.
RX PubMed=19043117; DOI=10.1074/jbc.m805925200;
RA Sarg B., Chwatal S., Talasz H., Lindner H.H.;
RT "Testis-specific linker histone H1t is multiply phosphorylated during
RT spermatogenesis. Identification of phosphorylation sites.";
RL J. Biol. Chem. 284:3610-3618(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Testis-specific histone H1 that forms less compacted
CC chromatin compared to other H1 histone subtypes. Formation of more
CC relaxed chromatin may be required to promote chromatin architecture
CC required for proper chromosome regulation during meiosis, such as
CC homologous recombination. Histones H1 act as linkers that bind to
CC nucleosomes and compact polynucleosomes into a higher-order chromatin
CC configuration. {ECO:0000250|UniProtKB:P22492}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Testis-specific (PubMed:2423516, PubMed:1706721).
CC Expressed in pachytene spermatocytes during meiotic prophase I
CC (PubMed:1706721). {ECO:0000269|PubMed:1706721,
CC ECO:0000269|PubMed:2423516}.
CC -!- DEVELOPMENTAL STAGE: This histone is a testis-specific H1 variant that
CC appears during meiosis in spermatogenesis.
CC {ECO:0000269|PubMed:1706721}.
CC -!- DOMAIN: The Gln-54 residue in the globular domain forms a hydrogen bond
CC with the main chain carbonyl of Met-52 and is spatially oriented away
CC from the nucleosome dyad axis, leading to lower affinity towards Four-
CC way junction DNA and reconstituted 5S mononucleosomes.
CC {ECO:0000269|PubMed:17052712}.
CC -!- PTM: Phosphorylated in early spermatids. {ECO:0000269|PubMed:19043117}.
CC -!- PTM: Citrullination at Arg-56 (H1R54ci) by PADI4 takes place within the
CC DNA-binding site of H1 and results in its displacement from chromatin
CC and global chromatin decondensation, thereby promoting pluripotency and
CC stem cell maintenance. {ECO:0000250|UniProtKB:P43275}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; M13170; AAA41328.1; -; Genomic_DNA.
DR EMBL; M28409; AAA41305.1; -; Genomic_DNA.
DR PIR; A27779; HSRT1T.
DR RefSeq; NP_036711.1; NM_012579.1.
DR AlphaFoldDB; P06349; -.
DR SMR; P06349; -.
DR BioGRID; 246603; 2.
DR iPTMnet; P06349; -.
DR PhosphoSitePlus; P06349; -.
DR jPOST; P06349; -.
DR PRIDE; P06349; -.
DR Ensembl; ENSRNOT00000081345; ENSRNOP00000070024; ENSRNOG00000061863.
DR GeneID; 24438; -.
DR KEGG; rno:24438; -.
DR UCSC; RGD:2778; rat.
DR CTD; 107970; -.
DR RGD; 2778; H1f6.
DR GeneTree; ENSGT00940000163525; -.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P06349; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; P06349; -.
DR TreeFam; TF313664; -.
DR PRO; PR:P06349; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000061863; Expressed in testis and 11 other tissues.
DR Genevisible; P06349; RN.
DR GO; GO:0000794; C:condensed nuclear chromosome; ISO:RGD.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:RGD.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0007283; P:spermatogenesis; IEP:RGD.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005819; H1/H5.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW Chromosome; Citrullination; Developmental protein; Differentiation;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3947637"
FT CHAIN 2..208
FT /note="Histone H1t"
FT /id="PRO_0000195925"
FT DOMAIN 38..111
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..172
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 54
FT /note="Important for nucleosome binding properties"
FT /evidence="ECO:0000269|PubMed:17052712"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19043117"
FT MOD_RES 56
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19043117"
FT MOD_RES 156
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:19043117"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07133"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19043117"
FT MOD_RES 187
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:19043117"
FT MUTAGEN 54
FT /note="Q->K: Increased affinity for DNA."
FT /evidence="ECO:0000269|PubMed:17052712"
SQ SEQUENCE 208 AA; 21726 MW; FAB7DAA110D850CE CRC64;
MSETAPAASS TLVPAPVEKP ATKRRGKKPG MATARKPRGF SVSKLIPEAL SMSQERAGMS
LAALKKALAA AGYDVEKNNS RIKLALKRLV NKGVLVQTKG TGASGSFKLS KKAASGNDKG
KGKKSASAKA KKLGLSRASR SPKSSKTKVV KKPKATPTKG SGSRRKTKGA KGLQQRKSPA
KARATNSNSG KSKMVMQKTD LRKAAGRK
