H1T_MACMU
ID H1T_MACMU Reviewed; 208 AA.
AC P40286;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Histone H1t;
DE AltName: Full=Testicular H1 histone;
GN Name=H1-6 {ECO:0000250|UniProtKB:P22492}; Synonyms=H1FT, H1T;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8175896; DOI=10.1002/jcb.240540210;
RA Koppel D.A., Wolfe S.A., Fogelfeld L., Grimes S.R.;
RT "Primate testicular histone H1t genes are highly conserved and the human
RT H1t gene is located on chromosome 6.";
RL J. Cell. Biochem. 54:219-230(1994).
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 -!- PTM: Phosphorylated in early spermatids.
CC {ECO:0000250|UniProtKB:P06349}.
CC -!- PTM: Citrullination at Arg-58 (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; M97756; AAA19937.1; -; Unassigned_DNA.
DR PIR; I70195; I70195.
DR RefSeq; NP_001074230.1; NM_001080761.1.
DR AlphaFoldDB; P40286; -.
DR SMR; P40286; -.
DR STRING; 9544.ENSMMUP00000031274; -.
DR Ensembl; ENSMMUT00000083249; ENSMMUP00000079159; ENSMMUG00000051980.
DR GeneID; 696375; -.
DR KEGG; mcc:696375; -.
DR CTD; 3010; -.
DR VEuPathDB; HostDB:ENSMMUG00000051980; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000163525; -.
DR HOGENOM; CLU_052897_7_0_1; -.
DR InParanoid; P40286; -.
DR OMA; QHHKANI; -.
DR OrthoDB; 1565299at2759; -.
DR TreeFam; TF313664; -.
DR Proteomes; UP000006718; Chromosome 4.
DR Bgee; ENSMMUG00000051980; Expressed in spermatocyte and 2 other tissues.
DR ExpressionAtlas; P40286; baseline.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
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:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW Citrullination; Developmental protein; Differentiation; DNA-binding;
KW Phosphoprotein; Reference proteome; Spermatogenesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..208
FT /note="Histone H1t"
FT /id="PRO_0000195911"
FT DOMAIN 40..113
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..129
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..176
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..208
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 56
FT /note="Important for nucleosome binding properties"
FT /evidence="ECO:0000250|UniProtKB:P06349"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07133"
FT MOD_RES 58
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07133"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q07133"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07133"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07133"
SQ SEQUENCE 208 AA; 22093 MW; 0E390D62056E3995 CRC64;
MSETVPAASA GAVPAVMEKP LTKKRGKKPA GLTSASRKAP NLSVSKLITE ALSVSQERVG
MSLAALKKAL AAAGYDVEKN NSRIKLSLKS LVNKGILVQT RGTGASGSFK LSKKVLPKST
RRKANKSASA KTKKLVLSRD SKSPKTAKTN KRAKKPRATA PKKAVRSGRK AKGAKGKQQQ
KSPVKARATK PKLTQHHKAN IRKATSRK
