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Histone H2A-Bbd type 1 (H2A Barr body-deficient) (H2A.Bbd) (Histone H2A-like 2) (H2A.L.2) (H2AL2) (Histone H2Alike 2) (Testis-specific expressed gene 1 protein) (TSEG-1)

 H2AB1_MOUSE             Reviewed;         111 AA.
Q9CQ70; Q9D9Q5;
03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-APR-2018, entry version 137.
RecName: Full=Histone H2A-Bbd type 1 {ECO:0000305};
AltName: Full=H2A Barr body-deficient {ECO:0000250|UniProtKB:P0C5Y9};
Short=H2A.Bbd {ECO:0000250|UniProtKB:P0C5Y9};
AltName: Full=Histone H2A-like 2 {ECO:0000303|PubMed:17261847};
Short=H2A.L.2 {ECO:0000303|PubMed:28366643};
Short=H2AL2 {ECO:0000303|PubMed:17261847};
Short=Histone H2Alike 2 {ECO:0000303|PubMed:17261847};
AltName: Full=Testis-specific expressed gene 1 protein {ECO:0000303|PubMed:20188161};
Short=TSEG-1 {ECO:0000303|PubMed:20188161};
Name=H2afb1 {ECO:0000312|MGI:MGI:1915481};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
AND POSSIBLE FUNCTION.
STRAIN=BALB/cJ; TISSUE=Testis;
PubMed=20188161; DOI=10.1016/j.ygeno.2010.02.005;
Gu C., Tong Q., Zheng L., Liang Z., Pu J., Mei H., Hu T., Du Z.,
Tian F., Zeng F.;
"TSEG-1, a novel member of histone H2A variants, participates in
spermatogenesis via promoting apoptosis of spermatogenic cells.";
Genomics 95:278-289(2010).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
TISSUE SPECIFICITY.
PubMed=20008104; DOI=10.1093/nar/gkp1129;
Ishibashi T., Li A., Eirin-Lopez J.M., Zhao M., Missiaen K.,
Abbott D.W., Meistrich M., Hendzel M.J., Ausio J.;
"H2A.Bbd: an X-chromosome-encoded histone involved in mammalian
spermiogenesis.";
Nucleic Acids Res. 38:1780-1789(2010).
[7]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=17261847; DOI=10.1083/jcb.200604141;
Govin J., Escoffier E., Rousseaux S., Kuhn L., Ferro M., Thevenon J.,
Catena R., Davidson I., Garin J., Khochbin S., Caron C.;
"Pericentric heterochromatin reprogramming by new histone variants
during mouse spermiogenesis.";
J. Cell Biol. 176:283-294(2007).
[8]
DEVELOPMENTAL STAGE.
PubMed=18703863;
Wu F., Caron C., De Robertis C., Khochbin S., Rousseaux S.;
"Testis-specific histone variants H2AL1/2 rapidly disappear from
paternal heterochromatin after fertilization.";
J. Reprod. Dev. 54:413-417(2008).
[9]
FUNCTION, AND SUBUNIT.
PubMed=19506029; DOI=10.1093/nar/gkp473;
Syed S.H., Boulard M., Shukla M.S., Gautier T., Travers A., Bednar J.,
Faivre-Moskalenko C., Dimitrov S., Angelov D.;
"The incorporation of the novel histone variant H2AL2 confers unusual
structural and functional properties of the nucleosome.";
Nucleic Acids Res. 37:4684-4695(2009).
[10]
FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH HIST1H2BA, AND
DISRUPTION PHENOTYPE.
PubMed=28366643; DOI=10.1016/j.molcel.2017.02.025;
Barral S., Morozumi Y., Tanaka H., Montellier E., Govin J.,
de Dieuleveult M., Charbonnier G., Coute Y., Puthier D., Buchou T.,
Boussouar F., Urahama T., Fenaille F., Curtet S., Hery P.,
Fernandez-Nunez N., Shiota H., Gerard M., Rousseaux S., Kurumizaka H.,
Khochbin S.;
"Histone variant H2A.L.2 guides transition protein-dependent protamine
assembly in male germ cells.";
Mol. Cell 66:89-101(2017).
-!- FUNCTION: Atypical histone H2A which replaces conventional H2A
during late spermatogenesis and is involved in the replacement of
histones to protamine in male germ cells (PubMed:28366643). Core
component of nucleosome: nucleosomes wrap and compact DNA into
chromatin, limiting DNA accessibility to the cellular machineries
which require DNA as a template (PubMed:19506029). Nucleosomes
containing H2AFB1 only wrap 130 bp of DNA, compared to 147 bp for
classical nucleosomes (PubMed:19506029). In condensing spermatids,
the heterodimer between H2AFB1 and HIST1H2BA/TH2B is loaded onto
the nucleosomes and promotes loading of transition proteins (TNP1
and TNP2) onto the nucleosomes (PubMed:28366643). Inclusion of the
H2AFB1-HIST1H2BA/TH2B dimer into chromatin opens the nucleosomes,
releasing the nucleosomal DNA ends and allowing the invasion of
nucleosomes by transition proteins (TNP1 and TNP2)
(PubMed:28366643). Then, transition proteins drive the recruitment
and processing of protamines, which are responsible for histone
eviction (PubMed:28366643). {ECO:0000269|PubMed:19506029,
ECO:0000269|PubMed:28366643}.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers (PubMed:19506029).
Incorporated into nucleosomes during late spermatogenesis
(PubMed:19506029). Interacts with HIST1H2BA/TH2B; preferentially
dimerizes with HIST1H2BA/TH2B to form nucleosomes
(PubMed:17261847, PubMed:28366643). {ECO:0000269|PubMed:17261847,
ECO:0000269|PubMed:19506029, ECO:0000269|PubMed:28366643}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17261847}.
Chromosome {ECO:0000269|PubMed:17261847}. Note=Specifically
localizes to the pericentric regions in condensing spermatids
(PubMed:17261847). {ECO:0000269|PubMed:17261847}.
-!- TISSUE SPECIFICITY: Highly expressed in adult testis, mainly in
spermatocytes (PubMed:20008104, PubMed:20188161, PubMed:17261847).
{ECO:0000269|PubMed:17261847, ECO:0000269|PubMed:20008104,
ECO:0000269|PubMed:20188161}.
-!- DEVELOPMENTAL STAGE: Expressed since postnatal day (P) 21, peaks
at P30, and gradually decreases in the testis of aging mouse
(PubMed:20008104, PubMed:20188161). Coexpressed with transition
proteins during late spermiogenesis (PubMed:28366643). Strongly
enriched in step 12-16 spermatids and accumulate during late
spermiogenesis, in condensing spermatids (PubMed:17261847).
Remains present in mature spermatozoa isolated from epididymis
(PubMed:17261847). Rapidly disappears from the paternal
pericentric heterochromatin regions after sperm-egg fusion
(PubMed:18703863). {ECO:0000269|PubMed:17261847,
ECO:0000269|PubMed:18703863, ECO:0000269|PubMed:20008104,
ECO:0000269|PubMed:20188161, ECO:0000269|PubMed:28366643}.
-!- DISRUPTION PHENOTYPE: Male mice are completely sterile due to
defects in spermatogenesis. Chromatin in mature spermatozoa shows
defects in density, due to impaired histone replacement by
protamines. A significant proportion of Prm2 remains unprocessed.
{ECO:0000269|PubMed:28366643}.
-!- MISCELLANEOUS: In contrast to other H2A histones, it does not
contain the conserved residues that are the target of post-
translational modifications. {ECO:0000305}.
-!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
-!- CAUTION: Although related to variant histone H2AFB1 in human (AC
P0C5Y9), it is unclear whether human and mouse H2AFB1 proteins are
involved in similar processes. In mouse, variant histone H2AFB1 is
specifically required to direct the transformation of dissociating
nucleosomes to protamine in male germ cells during spermatogenesis
(PubMed:28366643). It is however unclear whether human protein,
which participates to mRNA processing and is associated with
active transcription, is also involved in nucleosomes to protamine
replacement. {ECO:0000269|PubMed:28366643}.
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EMBL; EU079024; ABU52995.1; -; mRNA.
EMBL; AK006586; BAB24661.1; -; mRNA.
EMBL; AK015538; BAB29887.1; -; mRNA.
EMBL; AK018839; BAB31458.1; -; mRNA.
EMBL; AK018922; BAB31484.1; -; mRNA.
EMBL; AK018951; BAB31492.1; -; mRNA.
EMBL; AK018962; BAB31496.1; -; mRNA.
EMBL; AK160415; BAE35779.1; -; mRNA.
EMBL; AL928589; CAM21795.1; -; Genomic_DNA.
EMBL; CH466542; EDL08091.1; -; Genomic_DNA.
EMBL; BC061062; AAH61062.1; -; mRNA.
CCDS; CCDS38050.1; -.
RefSeq; NP_080903.1; NM_026627.2.
UniGene; Mm.23887; -.
ProteinModelPortal; Q9CQ70; -.
STRING; 10090.ENSMUSP00000100618; -.
PhosphoSitePlus; Q9CQ70; -.
PaxDb; Q9CQ70; -.
PRIDE; Q9CQ70; -.
Ensembl; ENSMUST00000105001; ENSMUSP00000100618; ENSMUSG00000062651.
GeneID; 68231; -.
KEGG; mmu:68231; -.
UCSC; uc008ili.1; mouse.
CTD; 474382; -.
MGI; MGI:1915481; H2afb1.
eggNOG; KOG1756; Eukaryota.
eggNOG; COG5262; LUCA.
GeneTree; ENSGT00910000144462; -.
HOGENOM; HOG000234652; -.
HOVERGEN; HBG009342; -.
InParanoid; Q9CQ70; -.
KO; K11251; -.
OMA; REGQFAN; -.
OrthoDB; EOG091G14WU; -.
PhylomeDB; Q9CQ70; -.
TreeFam; TF300137; -.
PRO; PR:Q9CQ70; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000062651; -.
Genevisible; Q9CQ70; MM.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0000788; C:nuclear nucleosome; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006342; P:chromatin silencing; IBA:GO_Central.
GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IDA:UniProtKB.
Gene3D; 1.10.20.10; -; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR002119; Histone_H2A.
InterPro; IPR007125; Histone_H2A/H2B/H3.
Pfam; PF00125; Histone; 1.
PRINTS; PR00620; HISTONEH2A.
SMART; SM00414; H2A; 1.
SUPFAM; SSF47113; SSF47113; 1.
1: Evidence at protein level;
Chromosome; Complete proteome; Differentiation; DNA-binding;
Nucleosome core; Nucleus; Reference proteome; Spermatogenesis.
CHAIN 1 111 Histone H2A-Bbd type 1.
/FTId=PRO_0000419684.
CONFLICT 89 89 E -> G (in Ref. 2; BAB24661).
{ECO:0000305}.
SEQUENCE 111 AA; 12843 MW; BCE5ADE3DA416069 CRC64;
MARKRQRRRR RKVTRSQRAE LQFPVSRVDR FLREGNYSRR LSSSAPVFLA GVLEYLTSNI
LELAGEVAHT TGRKRIAPEH VCRVVQNNEQ LHQLFKQGGT SVFEPPEPDD N


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