H18_BOVIN
ID H18_BOVIN Reviewed; 343 AA.
AC Q3HNG7;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Histone H1.8 {ECO:0000305};
DE AltName: Full=Histone H1oo;
DE AltName: Full=Oocyte-specific histone H1;
DE AltName: Full=Oocyte-specific linker histone H1;
GN Name=H1-8 {ECO:0000250|UniProtKB:Q8IZA3};
GN Synonyms=H1FOO {ECO:0000303|PubMed:16470586}, H1OO;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16470586; DOI=10.1002/mrd.20448;
RA McGraw S., Vigneault C., Tremblay K., Sirard M.-A.;
RT "Characterization of linker histone H1FOO during bovine in vitro embryo
RT development.";
RL Mol. Reprod. Dev. 73:692-699(2006).
CC -!- FUNCTION: May play a key role in the control of gene expression during
CC oogenesis and early embryogenesis, presumably through the perturbation
CC of chromatin structure. Essential for meiotic maturation of germinal
CC vesicle-stage oocytes. The somatic type linker histone H1c is rapidly
CC replaced by H1oo in a donor nucleus transplanted into an oocyte. The
CC greater mobility of H1oo as compared to H1c may contribute to this
CC rapid replacement and increased instability of the embryonic chromatin
CC structure. The rapid replacement of H1c with H1oo may play an important
CC role in nuclear remodeling (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16470586}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16470586}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:16470586}.
CC Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837,
CC ECO:0000269|PubMed:16470586}. Note=In the 1-, 2- and 4-cell embryo, it
CC is uniformly spread within the cytoplasm, while it is concentrated onto
CC the chromatin in the nucleus. In the 8- to 16-cell embryo, its presence
CC diminishes in the cytoplasm, although it is still strongly expressed in
CC the nucleus.
CC -!- TISSUE SPECIFICITY: Oocyte (at protein level).
CC {ECO:0000269|PubMed:16470586}.
CC -!- DEVELOPMENTAL STAGE: Found in the germinal vesicle (GV) oocyte and
CC diminishes constantly throughout embryonic development. The levels
CC compared to the initial amount found in the GV oocyte decreases to 41%,
CC 28% and 7% in the 2, 4, and 8-cell embryos. In the 16-cell embryo and
CC blastocyst, respectively, levels are 200 and 2000 times lower than in
CC the GV oocyte. {ECO:0000269|PubMed:16470586}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; DQ206443; ABA46814.1; -; mRNA.
DR RefSeq; NP_001030449.1; NM_001035372.1.
DR AlphaFoldDB; Q3HNG7; -.
DR SMR; Q3HNG7; -.
DR STRING; 9913.ENSBTAP00000002369; -.
DR PaxDb; Q3HNG7; -.
DR PRIDE; Q3HNG7; -.
DR GeneID; 527400; -.
DR KEGG; bta:527400; -.
DR CTD; 132243; -.
DR eggNOG; KOG4012; Eukaryota.
DR InParanoid; Q3HNG7; -.
DR OrthoDB; 1342218at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; ISS:CAFA.
DR GO; GO:0030527; F:structural constituent of chromatin; IDA:GO_Central.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
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:0040029; P:regulation of gene expression, epigenetic; ISS:CAFA.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 1.
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 SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW Chromosome; Cytoplasm; DNA-binding; Meiosis; Nucleus; Reference proteome.
FT CHAIN 1..343
FT /note="Histone H1.8"
FT /id="PRO_0000343411"
FT DOMAIN 52..130
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 161..176
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 343 AA; 35436 MW; AA101C7AA0B36CC5 CRC64;
MAPGSIASSD TSSSTSSSST SSASSASAEG SSRPLGSEKP GLARGAVRAP RRHPPVLRMV
LEALQAGERR RGTSVAAIKV YILQKYPTVD ALRLNHLLKQ ALATGLHRGL LIRPVNSKAK
GATGSFKLVP KDKRKIPPRK TAPRMPGQAE GKDPKKPSES KKDPANTVEV KKGSRKPREE
RAAPSKPGAA KKAPKKGTQT KDPEPRLGEA KKSSRRPDKA AQAPPSAGGP GGKSKVKERG
SRQADTKAHR KTQPGSQSSK STVTKGENGA PLAKKKMGGK VPKEAAGEGP KAKAPVPPKG
AGSKKEPGPL AGKAEASKGP RKPGIPTKSS VSKAASKKAE AEG
