H18_MOUSE
ID H18_MOUSE Reviewed; 304 AA.
AC Q8VIK3;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
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=H1f8 {ECO:0000312|MGI:MGI:2176207},
GN H1foo {ECO:0000303|PubMed:15371275}, H1oo {ECO:0000312|MGI:MGI:2176207};
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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Ovary;
RX PubMed=11171391; DOI=10.1242/dev.128.5.655;
RA Tanaka M., Hennebold J.D., Macfarlane J., Adashi E.Y.;
RT "A mammalian oocyte-specific linker histone gene H1oo: homology with the
RT genes for the oocyte-specific cleavage stage histone (cs-H1) of sea urchin
RT and the B4/H1M histone of the frog.";
RL Development 128:655-664(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15371275; DOI=10.1095/biolreprod.104.032474;
RA Tanaka M., Kihara M., Hennebold J.D., Eppig J.J., Viveiros M.M.,
RA Emery B.R., Carrell D.T., Kirkman N.J., Meczekalski B., Zhou J.,
RA Bondy C.A., Becker M., Schultz R.M., Misteli T., De La Fuente R.,
RA King G.J., Adashi E.Y.;
RT "H1FOO is coupled to the initiation of oocytic growth.";
RL Biol. Reprod. 72:135-142(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14729479; DOI=10.1016/j.ydbio.2003.10.004;
RA Teranishi T., Tanaka M., Kimoto S., Ono Y., Miyakoshi K., Kono T.,
RA Yoshimura Y.;
RT "Rapid replacement of somatic linker histones with the oocyte-specific
RT linker histone H1foo in nuclear transfer.";
RL Dev. Biol. 266:76-86(2004).
RN [7]
RP FUNCTION.
RX PubMed=17519519; DOI=10.1262/jrd.19008;
RA Furuya M., Tanaka M., Teranishi T., Matsumoto K., Hosoi Y., Saeki K.,
RA Ishimoto H., Minegishi K., Iritani A., Yoshimura Y.;
RT "H1foo is indispensable for meiotic maturation of the mouse oocyte.";
RL J. Reprod. Dev. 53:895-902(2007).
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. {ECO:0000269|PubMed:11171391,
CC ECO:0000269|PubMed:14729479, ECO:0000269|PubMed:15371275,
CC ECO:0000269|PubMed:17519519}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. Chromosome.
CC Note=In the germinal vesicle oocyte, localizes to the condensed
CC chromosomes. In the 1-cell embryo found in condensed maternal metaphase
CC chromatin but not in the sperm head. Following second polar body
CC extrusion, detected in the swollen sperm head as well as in the second
CC polar body. Reduced expression in the nucleus in 2-cell embryo is seen
CC as compared to 1-cell embryo.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Alpha;
CC IsoId=Q8VIK3-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta;
CC IsoId=Q8VIK3-2; Sequence=VSP_034593;
CC -!- TISSUE SPECIFICITY: Oocyte-specific. {ECO:0000269|PubMed:11171391,
CC ECO:0000269|PubMed:15371275}.
CC -!- DEVELOPMENTAL STAGE: Expressed as early as the germinal vesicle (GV)
CC stage oocyte, and persists into the metaphase II stage oocyte, the
CC oocytic polar bodies, and the 2-cell embryo, and disappears at the
CC 4- to 8-cell embryonic stage. {ECO:0000269|PubMed:11171391}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; AY007195; AAG01890.1; -; mRNA.
DR EMBL; AK135944; BAE22736.1; -; mRNA.
DR EMBL; AK162137; BAE36747.1; -; mRNA.
DR EMBL; CH466523; EDK99547.1; -; Genomic_DNA.
DR EMBL; BC137916; AAI37917.1; -; mRNA.
DR CCDS; CCDS20447.1; -. [Q8VIK3-1]
DR CCDS; CCDS85133.1; -. [Q8VIK3-2]
DR RefSeq; NP_001333631.1; NM_001346702.1. [Q8VIK3-2]
DR RefSeq; NP_612184.1; NM_138311.3. [Q8VIK3-1]
DR AlphaFoldDB; Q8VIK3; -.
DR SMR; Q8VIK3; -.
DR STRING; 10090.ENSMUSP00000036951; -.
DR iPTMnet; Q8VIK3; -.
DR PhosphoSitePlus; Q8VIK3; -.
DR PaxDb; Q8VIK3; -.
DR PRIDE; Q8VIK3; -.
DR ProteomicsDB; 269643; -. [Q8VIK3-1]
DR ProteomicsDB; 269644; -. [Q8VIK3-2]
DR Antibodypedia; 33282; 183 antibodies from 26 providers.
DR DNASU; 171506; -.
DR Ensembl; ENSMUST00000037831; ENSMUSP00000036951; ENSMUSG00000042279. [Q8VIK3-1]
DR Ensembl; ENSMUST00000161969; ENSMUSP00000123797; ENSMUSG00000042279. [Q8VIK3-2]
DR GeneID; 171506; -.
DR KEGG; mmu:171506; -.
DR UCSC; uc009djl.1; mouse. [Q8VIK3-1]
DR UCSC; uc009djm.1; mouse. [Q8VIK3-2]
DR CTD; 171506; -.
DR MGI; MGI:2176207; H1f8.
DR VEuPathDB; HostDB:ENSMUSG00000042279; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00940000160900; -.
DR HOGENOM; CLU_070976_1_0_1; -.
DR InParanoid; Q8VIK3; -.
DR OMA; MADMAHT; -.
DR OrthoDB; 1342218at2759; -.
DR PhylomeDB; Q8VIK3; -.
DR TreeFam; TF333386; -.
DR BioGRID-ORCS; 171506; 3 hits in 72 CRISPR screens.
DR ChiTaRS; H1foo; mouse.
DR PRO; PR:Q8VIK3; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q8VIK3; protein.
DR Bgee; ENSMUSG00000042279; Expressed in animal zygote and 32 other tissues.
DR ExpressionAtlas; Q8VIK3; baseline and differential.
DR Genevisible; Q8VIK3; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0001674; C:female germ cell nucleus; IDA:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IDA:UniProtKB.
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; ISA:MGI.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:GO_Central.
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 2: Evidence at transcript level;
KW Alternative splicing; Chromosome; Cytoplasm; DNA-binding; Meiosis; Nucleus;
KW Reference proteome.
FT CHAIN 1..304
FT /note="Histone H1.8"
FT /id="PRO_0000343413"
FT DOMAIN 45..123
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 110..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 154..170
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 244..304
FT /note="QNSVASLAKRKMADMAHTVTVVQGAETVQETKVPTPSQDIGHKVQPIPRVRK
FT AKTPENTQA -> GPE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15371275"
FT /id="VSP_034593"
SQ SEQUENCE 304 AA; 32223 MW; 716400ADF8CA8FE4 CRC64;
MAPGSVSSVS SSSFPSRDTS PSGSCGLPGA DKPGPSCRRI QAGQRNPTML HMVLEALKAR
EARQGTSVVA IKVYIQHKYP TVDTTRFKYL LKQALETGVR RGLLTRPAHS KAKGATGSFK
LVPKPKTKKA CAPKAGRGAA GAKETGSKKS GLLKKDQVGK ATMEKGQKRR AYPCKAATLE
MAPKKAKAKP KEVRKAPLKQ DKAAGAPLTA NGGQKVKRSG SRQEANAHGK TKGEKSKPLA
SKVQNSVASL AKRKMADMAH TVTVVQGAET VQETKVPTPS QDIGHKVQPI PRVRKAKTPE
NTQA
