H1T_MOUSE
ID H1T_MOUSE Reviewed; 208 AA.
AC Q07133; Q0VEA3; Q8CGP8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Histone H1t;
DE AltName: Full=Testicular H1 histone;
GN Name=H1-6 {ECO:0000250|UniProtKB:P22492};
GN Synonyms=H1f6 {ECO:0000312|MGI:MGI:1888530}, H1ft, H1t,
GN Hist1h1t {ECO:0000312|MGI:MGI:1888530};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=BALB/cJ; TISSUE=Leukocyte;
RX PubMed=8241275; DOI=10.1016/0167-4781(93)90162-7;
RA Drabent B., Bode C., Doenecke D.;
RT "Structure and expression of the mouse testicular H1 histone gene (H1t).";
RL Biochim. Biophys. Acta 1216:311-313(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CD-1; TISSUE=Testis;
RA van Wert J., Wright J., Wolfe S.A., Grimes S.R.;
RL Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12408966; DOI=10.1006/geno.2002.6850;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION AT SER-9; SER-141; THR-156 AND SER-178.
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 PROTEIN SEQUENCE OF 2-24, AND PHOSPHORYLATION AT SER-141; THR-156; SER-163
RP AND SER-178.
RX PubMed=18698803; DOI=10.1021/pr8003908;
RA Rose K.L., Li A., Zalenskaya I., Zhang Y., Unni E., Hodgson K.C., Yu Y.,
RA Shabanowitz J., Meistrich M.L., Hunt D.F., Ausio J.;
RT "C-terminal phosphorylation of murine testis-specific histone H1t in
RT elongating spermatids.";
RL J. Proteome Res. 7:4070-4078(2008).
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. {ECO:0000269|PubMed:8241275}.
CC -!- DEVELOPMENTAL STAGE: This histone is a testis-specific H1 variant that
CC appears during meiosis in spermatogenesis.
CC {ECO:0000269|PubMed:8241275}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L28753; AAB38417.1; -; Genomic_DNA.
DR EMBL; X72805; CAA51325.1; -; Genomic_DNA.
DR EMBL; U06232; AAA18359.1; -; Unassigned_DNA.
DR EMBL; AY158908; AAO06219.1; -; Genomic_DNA.
DR EMBL; BC119305; AAI19306.1; -; mRNA.
DR EMBL; BC119307; AAI19308.1; -; mRNA.
DR PIR; S43434; S43434.
DR RefSeq; NP_034507.2; NM_010377.3.
DR AlphaFoldDB; Q07133; -.
DR SMR; Q07133; -.
DR BioGRID; 223727; 4.
DR STRING; 10090.ENSMUSP00000037304; -.
DR iPTMnet; Q07133; -.
DR PhosphoSitePlus; Q07133; -.
DR jPOST; Q07133; -.
DR MaxQB; Q07133; -.
DR PaxDb; Q07133; -.
DR PRIDE; Q07133; -.
DR ProteomicsDB; 270907; -.
DR DNASU; 107970; -.
DR GeneID; 107970; -.
DR KEGG; mmu:107970; -.
DR CTD; 107970; -.
DR MGI; MGI:1888530; H1f6.
DR eggNOG; KOG4012; Eukaryota.
DR InParanoid; Q07133; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; Q07133; -.
DR BioGRID-ORCS; 107970; 3 hits in 71 CRISPR screens.
DR PRO; PR:Q07133; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q07133; protein.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IMP:CAFA.
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; IGI:MGI.
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; IGI:MGI.
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; IGI:MGI.
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:18698803"
FT CHAIN 2..208
FT /note="Histone H1t"
FT /id="PRO_0000195919"
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 95..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 SITE 54
FT /note="Important for nucleosome binding properties"
FT /evidence="ECO:0000250|UniProtKB:P06349"
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:18698803,
FT ECO:0000269|PubMed:19043117"
FT MOD_RES 156
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18698803,
FT ECO:0000269|PubMed:19043117"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18698803"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18698803,
FT ECO:0000269|PubMed:19043117"
FT CONFLICT 18
FT /note="E -> EE (in Ref. 3; AAO06219)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="G -> R (in Ref. 2; AAB38417/AAA18359)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 21540 MW; 25E35B84008B22C5 CRC64;
MSETAPAASS TLVPAPVEKP SSKRRGKKPG LAPARKPRGF SVSKLIPEAL STSQERAGMS
LAALKKALAA AGYDVEKNNS RIKLALKRLV NKGVLVQTKG TGASGSFKLS KKAASGNDKG
KGKKSASAKA KKMGLPRASR SPKSSKTKAV KKPKATPTKA SGSGRKTKGA KGVQQRKSPA
KARAANPNSG KAKMVMQKTD LRKAAGRK
