ID   H1T_PIG                 Reviewed;         211 AA.
AC   P06348;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Histone H1t;
GN   Name=H1-6 {ECO:0000250|UniProtKB:P22492}; Synonyms=H1FT;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND ACETYLATION
RP   AT ALA-1.
RX   PubMed=6389534; DOI=10.1016/s0021-9258(18)89801-5;
RA   Cole K.D., York R.G., Kistler W.S.;
RT   "The amino acid sequence of boar H1t, a testis-specific H1 histone
RT   variant.";
RL   J. Biol. Chem. 259:13695-13702(1984).
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:6389534}.
CC   -!- DEVELOPMENTAL STAGE: This histone is a testis-specific H1 variant that
CC       appears during meiosis in spermatogenesis.
CC       {ECO:0000269|PubMed:6389534}.
CC   -!- PTM: Phosphorylated in early spermatids.
CC       {ECO:0000250|UniProtKB:P06349}.
CC   -!- PTM: Citrullination at Arg-57 (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   PIR; A02581; HSPG1T.
DR   AlphaFoldDB; P06348; -.
DR   SMR; P06348; -.
DR   iPTMnet; P06348; -.
DR   PeptideAtlas; P06348; -.
DR   PRIDE; P06348; -.
DR   InParanoid; P06348; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
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   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   Acetylation; Chromosome; Citrullination; Developmental protein;
KW   Differentiation; Direct protein sequencing; DNA-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Spermatogenesis.
FT   CHAIN           1..211
FT                   /note="Histone H1t"
FT                   /id="PRO_0000195920"
FT   DOMAIN          39..112
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          101..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..146
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..179
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            55
FT                   /note="Important for nucleosome binding properties"
FT                   /evidence="ECO:0000250|UniProtKB:P06349"
FT   MOD_RES         1
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:6389534"
FT   MOD_RES         57
FT                   /note="Citrulline"
FT                   /evidence="ECO:0000250|UniProtKB:P43275"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07133"
FT   MOD_RES         158
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07133"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07133"
FT   MOD_RES         181
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q07133"
SQ   SEQUENCE   211 AA;  22059 MW;  EACA47C51A8F5364 CRC64;
     AETAPAAPAD SVPASVEKPP AKKRGKKPVG LTGTSRKAPS ASVSKLITEA LSVSQERAGM
     SLAALKKALA AAGYDVEKNN SRIKLGLKSL VGKGILVQTR GTGASGSFKL SKKAAPEPRK
     GKVKKPAAAK TKKLVLSRDS KSPKSAKANK RAKKSRTTAA QKAARSGRKT KEAKVKQQRK
     SPAKARAAKP KAGNPKLTQQ KTNPRKATNR K