H2AB1_MOUSE
ID H2AB1_MOUSE Reviewed; 111 AA.
AC Q9CQ70; Q9D9Q5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Histone H2A-Bbd type 1 {ECO:0000305};
DE AltName: Full=H2A Barr body-deficient {ECO:0000250|UniProtKB:P0C5Y9};
DE Short=H2A.Bbd {ECO:0000250|UniProtKB:P0C5Y9};
DE AltName: Full=Histone H2A-like 2 {ECO:0000303|PubMed:17261847};
DE Short=H2A.L.2 {ECO:0000303|PubMed:28366643};
DE Short=H2AL2 {ECO:0000303|PubMed:17261847};
DE Short=Histone H2Alike 2 {ECO:0000303|PubMed:17261847};
DE AltName: Full=Testis-specific expressed gene 1 protein {ECO:0000303|PubMed:20188161};
DE Short=TSEG-1 {ECO:0000303|PubMed:20188161};
GN Name=H2ab1;
GN Synonyms=H2afb1 {ECO:0000312|MGI:MGI:1915481},
GN H2al2a {ECO:0000312|MGI:MGI:1915481};
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], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP POSSIBLE FUNCTION.
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=20188161; DOI=10.1016/j.ygeno.2010.02.005;
RA Gu C., Tong Q., Zheng L., Liang Z., Pu J., Mei H., Hu T., Du Z., Tian F.,
RA Zeng F.;
RT "TSEG-1, a novel member of histone H2A variants, participates in
RT spermatogenesis via promoting apoptosis of spermatogenic cells.";
RL Genomics 95:278-289(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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].
RC TISSUE=Testis;
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 TISSUE SPECIFICITY.
RX PubMed=20008104; DOI=10.1093/nar/gkp1129;
RA Ishibashi T., Li A., Eirin-Lopez J.M., Zhao M., Missiaen K., Abbott D.W.,
RA Meistrich M., Hendzel M.J., Ausio J.;
RT "H2A.Bbd: an X-chromosome-encoded histone involved in mammalian
RT spermiogenesis.";
RL Nucleic Acids Res. 38:1780-1789(2010).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=17261847; DOI=10.1083/jcb.200604141;
RA Govin J., Escoffier E., Rousseaux S., Kuhn L., Ferro M., Thevenon J.,
RA Catena R., Davidson I., Garin J., Khochbin S., Caron C.;
RT "Pericentric heterochromatin reprogramming by new histone variants during
RT mouse spermiogenesis.";
RL J. Cell Biol. 176:283-294(2007).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=18703863; DOI=10.1262/jrd.20067;
RA Wu F., Caron C., De Robertis C., Khochbin S., Rousseaux S.;
RT "Testis-specific histone variants H2AL1/2 rapidly disappear from paternal
RT heterochromatin after fertilization.";
RL J. Reprod. Dev. 54:413-417(2008).
RN [9]
RP FUNCTION, AND SUBUNIT.
RX PubMed=19506029; DOI=10.1093/nar/gkp473;
RA Syed S.H., Boulard M., Shukla M.S., Gautier T., Travers A., Bednar J.,
RA Faivre-Moskalenko C., Dimitrov S., Angelov D.;
RT "The incorporation of the novel histone variant H2AL2 confers unusual
RT structural and functional properties of the nucleosome.";
RL Nucleic Acids Res. 37:4684-4695(2009).
RN [10]
RP FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH H2BC1, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28366643; DOI=10.1016/j.molcel.2017.02.025;
RA Barral S., Morozumi Y., Tanaka H., Montellier E., Govin J.,
RA de Dieuleveult M., Charbonnier G., Coute Y., Puthier D., Buchou T.,
RA Boussouar F., Urahama T., Fenaille F., Curtet S., Hery P.,
RA Fernandez-Nunez N., Shiota H., Gerard M., Rousseaux S., Kurumizaka H.,
RA Khochbin S.;
RT "Histone variant H2A.L.2 guides transition protein-dependent protamine
RT assembly in male germ cells.";
RL Mol. Cell 66:89-101(2017).
CC -!- FUNCTION: Atypical histone H2A which replaces conventional H2A during
CC late spermatogenesis and is involved in the replacement of histones to
CC protamine in male germ cells (PubMed:28366643). Core component of
CC nucleosome: nucleosomes wrap and compact DNA into chromatin, limiting
CC DNA accessibility to the cellular machineries which require DNA as a
CC template (PubMed:19506029). Nucleosomes containing H2AB1 only wrap 130
CC bp of DNA, compared to 147 bp for classical nucleosomes
CC (PubMed:19506029). In condensing spermatids, the heterodimer between
CC H2AB1 and H2BC1/TH2B is loaded onto the nucleosomes and promotes
CC loading of transition proteins (TNP1 and TNP2) onto the nucleosomes
CC (PubMed:28366643). Inclusion of the H2AB1-H2BC1/TH2B dimer into
CC chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and
CC allowing the invasion of nucleosomes by transition proteins (TNP1 and
CC TNP2) (PubMed:28366643). Then, transition proteins drive the
CC recruitment and processing of protamines, which are responsible for
CC histone eviction (PubMed:28366643). {ECO:0000269|PubMed:19506029,
CC ECO:0000269|PubMed:28366643}.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers (PubMed:19506029). Incorporated into
CC nucleosomes during late spermatogenesis (PubMed:19506029). Interacts
CC with H2BC1/TH2B; preferentially dimerizes with H2BC1/TH2B to form
CC nucleosomes (PubMed:17261847, PubMed:28366643).
CC {ECO:0000269|PubMed:17261847, ECO:0000269|PubMed:19506029,
CC ECO:0000269|PubMed:28366643}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17261847}. Chromosome
CC {ECO:0000269|PubMed:17261847}. Note=Specifically localizes to the
CC pericentric regions in condensing spermatids (PubMed:17261847).
CC {ECO:0000269|PubMed:17261847}.
CC -!- TISSUE SPECIFICITY: Highly expressed in adult testis, mainly in
CC spermatocytes (PubMed:20008104, PubMed:20188161, PubMed:17261847).
CC {ECO:0000269|PubMed:17261847, ECO:0000269|PubMed:20008104,
CC ECO:0000269|PubMed:20188161}.
CC -!- DEVELOPMENTAL STAGE: Expressed since postnatal day (P) 21, peaks at
CC P30, and gradually decreases in the testis of aging mouse
CC (PubMed:20008104, PubMed:20188161). Coexpressed with transition
CC proteins during late spermiogenesis (PubMed:28366643). Strongly
CC enriched in step 12-16 spermatids and accumulate during late
CC spermiogenesis, in condensing spermatids (PubMed:17261847). Remains
CC present in mature spermatozoa isolated from epididymis
CC (PubMed:17261847). Rapidly disappears from the paternal pericentric
CC heterochromatin regions after sperm-egg fusion (PubMed:18703863).
CC {ECO:0000269|PubMed:17261847, ECO:0000269|PubMed:18703863,
CC ECO:0000269|PubMed:20008104, ECO:0000269|PubMed:20188161,
CC ECO:0000269|PubMed:28366643}.
CC -!- DISRUPTION PHENOTYPE: Male mice are completely sterile due to defects
CC in spermatogenesis. Chromatin in mature spermatozoa shows defects in
CC density, due to impaired histone replacement by protamines. A
CC significant proportion of Prm2 remains unprocessed.
CC {ECO:0000269|PubMed:28366643}.
CC -!- MISCELLANEOUS: In contrast to other H2A histones, it does not contain
CC the conserved residues that are the target of post-translational
CC modifications. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC -!- CAUTION: Although related to variant histone H2AB1 in human (AC
CC P0C5Y9), it is unclear whether human and mouse H2AB1 proteins are
CC involved in similar processes. In mouse, variant histone H2AB1 is
CC specifically required to direct the transformation of dissociating
CC nucleosomes to protamine in male germ cells during spermatogenesis
CC (PubMed:28366643). It is however unclear whether human protein, which
CC participates in mRNA processing and is associated with active
CC transcription, is also involved in nucleosomes to protamine
CC replacement. {ECO:0000269|PubMed:28366643}.
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DR EMBL; EU079024; ABU52995.1; -; mRNA.
DR EMBL; AK006586; BAB24661.1; -; mRNA.
DR EMBL; AK015538; BAB29887.1; -; mRNA.
DR EMBL; AK018839; BAB31458.1; -; mRNA.
DR EMBL; AK018922; BAB31484.1; -; mRNA.
DR EMBL; AK018951; BAB31492.1; -; mRNA.
DR EMBL; AK018962; BAB31496.1; -; mRNA.
DR EMBL; AK160415; BAE35779.1; -; mRNA.
DR EMBL; AL928589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08091.1; -; Genomic_DNA.
DR EMBL; BC061062; AAH61062.1; -; mRNA.
DR CCDS; CCDS38050.1; -.
DR RefSeq; NP_080903.1; NM_026627.2.
DR AlphaFoldDB; Q9CQ70; -.
DR SMR; Q9CQ70; -.
DR STRING; 10090.ENSMUSP00000100618; -.
DR PhosphoSitePlus; Q9CQ70; -.
DR PaxDb; Q9CQ70; -.
DR PRIDE; Q9CQ70; -.
DR ProteomicsDB; 270912; -.
DR DNASU; 68231; -.
DR Ensembl; ENSMUST00000105001; ENSMUSP00000100618; ENSMUSG00000062651.
DR GeneID; 68231; -.
DR KEGG; mmu:68231; -.
DR UCSC; uc008ili.1; mouse.
DR CTD; 68231; -.
DR MGI; MGI:1915481; H2al2a.
DR VEuPathDB; HostDB:ENSMUSG00000062651; -.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT00940000162492; -.
DR HOGENOM; CLU_062828_3_2_1; -.
DR InParanoid; Q9CQ70; -.
DR OMA; REGQFAN; -.
DR OrthoDB; 1561614at2759; -.
DR PhylomeDB; Q9CQ70; -.
DR TreeFam; TF300137; -.
DR BioGRID-ORCS; 68231; 1 hit in 72 CRISPR screens.
DR ChiTaRS; H2al2a; mouse.
DR PRO; PR:Q9CQ70; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CQ70; protein.
DR Bgee; ENSMUSG00000062651; Expressed in testis and 9 other tissues.
DR Genevisible; Q9CQ70; MM.
DR GO; GO:0044815; C:DNA packaging complex; IDA:MGI.
DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0051276; P:chromosome organization; IDA:MGI.
DR GO; GO:0006334; P:nucleosome assembly; IDA:MGI.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IDA:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR002119; Histone_H2A.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Chromosome; Differentiation; DNA-binding; Nucleosome core; Nucleus;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..111
FT /note="Histone H2A-Bbd type 1"
FT /id="PRO_0000419684"
FT CONFLICT 89
FT /note="E -> G (in Ref. 2; BAB24661)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 111 AA; 12843 MW; BCE5ADE3DA416069 CRC64;
MARKRQRRRR RKVTRSQRAE LQFPVSRVDR FLREGNYSRR LSSSAPVFLA GVLEYLTSNI
LELAGEVAHT TGRKRIAPEH VCRVVQNNEQ LHQLFKQGGT SVFEPPEPDD N
