H2AL1_MOUSE
ID H2AL1_MOUSE Reviewed; 105 AA.
AC Q5M8Q2;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Histone H2A-like 1 {ECO:0000305};
DE Short=H2A.L.1 {ECO:0000303|PubMed:17261847};
DE Short=H2AL1 {ECO:0000303|PubMed:17261847};
DE Short=Histone H2Alike 1 {ECO:0000303|PubMed:17261847};
GN Name=H2al1a {ECO:0000312|MGI:MGI:3714114};
GN and
GN Name=H2al1c {ECO:0000312|MGI:MGI:3711280};
GN and
GN Name=H2al1d {ECO:0000312|MGI:MGI:3710419};
GN and
GN Name=H2al1f {ECO:0000312|MGI:MGI:3649874};
GN and
GN Name=H2al1g {ECO:0000312|MGI:MGI:3710577};
GN and
GN Name=H2al1h {ECO:0000312|MGI:MGI:3711282};
GN and
GN Name=H2al1i {ECO:0000312|MGI:MGI:3710416};
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 [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 [2]
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 [3]
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 [4]
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 [5]
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).
CC -!- FUNCTION: Atypical histone H2A which can replace conventional H2A in
CC some nucleosomes and may play a role during spermatogenesis.
CC Nucleosomes wrap and compact DNA into chromatin, limiting DNA
CC accessibility to the cellular machineries which require DNA as a
CC template. Histones thereby play a central role in transcription
CC regulation, DNA repair, DNA replication and chromosomal stability. DNA
CC accessibility is regulated via a complex set of post-translational
CC modifications of histones, also called histone code, and nucleosome
CC remodeling. {ECO:0000305|PubMed:17261847}.
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. May be incorporated into a proportion of
CC nucleosomes, replacing one or more H2A molecules. Interacts with
CC H2BC1/TH2B; preferentially dimerizes with H2BC1/TH2B to form
CC nucleosomes (PubMed:17261847). {ECO:0000269|PubMed:17261847}.
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: Testis-specific. {ECO:0000269|PubMed:17261847}.
CC -!- DEVELOPMENTAL STAGE: Strongly enriched in step 12-16 spermatids and
CC accumulate during late spermiogenesis, in condensing spermatids
CC (PubMed:17261847). Remains present in mature spermatozoa isolated from
CC epididymis (PubMed:17261847). Rapidly disappears from the paternal
CC pericentric heterochromatin regions after sperm-egg fusion
CC (PubMed:18703863). {ECO:0000269|PubMed:17261847,
CC ECO:0000269|PubMed:18703863}.
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}.
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DR EMBL; BX294183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466584; EDL35683.1; -; Genomic_DNA.
DR EMBL; BC087913; AAH87913.1; -; mRNA.
DR CCDS; CCDS53003.1; -.
DR RefSeq; NP_001104507.1; NM_001111037.1.
DR RefSeq; NP_001229878.1; NM_001242949.1.
DR RefSeq; NP_001229879.1; NM_001242950.1.
DR RefSeq; NP_001229880.1; NM_001242951.1.
DR RefSeq; NP_001229881.1; NM_001242952.1.
DR RefSeq; NP_001229882.1; NM_001242953.1.
DR RefSeq; NP_001229883.1; NM_001242954.1.
DR AlphaFoldDB; Q5M8Q2; -.
DR SMR; Q5M8Q2; -.
DR STRING; 10090.ENSMUSP00000125841; -.
DR PaxDb; Q5M8Q2; -.
DR PRIDE; Q5M8Q2; -.
DR ProteomicsDB; 271379; -.
DR DNASU; 100042922; -.
DR Ensembl; ENSMUST00000164729; ENSMUSP00000125841; ENSMUSG00000095445.
DR Ensembl; ENSMUST00000177926; ENSMUSP00000136794; ENSMUSG00000099443.
DR Ensembl; ENSMUST00000178595; ENSMUSP00000137030; ENSMUSG00000094904.
DR Ensembl; ENSMUST00000178806; ENSMUSP00000135929; ENSMUSG00000096097.
DR Ensembl; ENSMUST00000179004; ENSMUSP00000136695; ENSMUSG00000095655.
DR Ensembl; ENSMUST00000179859; ENSMUSP00000137575; ENSMUSG00000095662.
DR Ensembl; ENSMUST00000188439; ENSMUSP00000140925; ENSMUSG00000100626.
DR GeneID; 100042922; -.
DR GeneID; 100042929; -.
DR GeneID; 100042931; -.
DR GeneID; 100042939; -.
DR GeneID; 100042943; -.
DR GeneID; 100042944; -.
DR GeneID; 100042946; -.
DR KEGG; mmu:100042922; -.
DR KEGG; mmu:100042929; -.
DR KEGG; mmu:100042931; -.
DR KEGG; mmu:100042939; -.
DR KEGG; mmu:100042943; -.
DR KEGG; mmu:100042944; -.
DR KEGG; mmu:100042946; -.
DR UCSC; uc029xib.1; mouse.
DR CTD; 100042922; -.
DR CTD; 100042929; -.
DR CTD; 100042931; -.
DR CTD; 100042939; -.
DR CTD; 100042943; -.
DR CTD; 100042944; -.
DR CTD; 100042946; -.
DR MGI; MGI:3714114; H2al1a.
DR MGI; MGI:3711280; H2al1c.
DR MGI; MGI:3710419; H2al1d.
DR MGI; MGI:3649874; H2al1f.
DR MGI; MGI:3710577; H2al1g.
DR MGI; MGI:3711282; H2al1h.
DR MGI; MGI:3710416; H2al1i.
DR VEuPathDB; HostDB:ENSMUSG00000094904; -.
DR VEuPathDB; HostDB:ENSMUSG00000095445; -.
DR VEuPathDB; HostDB:ENSMUSG00000095655; -.
DR VEuPathDB; HostDB:ENSMUSG00000095662; -.
DR VEuPathDB; HostDB:ENSMUSG00000096097; -.
DR VEuPathDB; HostDB:ENSMUSG00000099443; -.
DR VEuPathDB; HostDB:ENSMUSG00000100626; -.
DR eggNOG; KOG1756; Eukaryota.
DR GeneTree; ENSGT00940000162492; -.
DR HOGENOM; CLU_062828_3_2_1; -.
DR InParanoid; Q5M8Q2; -.
DR OrthoDB; 1561614at2759; -.
DR PhylomeDB; Q5M8Q2; -.
DR TreeFam; TF300137; -.
DR BioGRID-ORCS; 100042922; 0 hits in 1 CRISPR screen.
DR BioGRID-ORCS; 100042929; 0 hits in 3 CRISPR screens.
DR BioGRID-ORCS; 100042931; 0 hits in 3 CRISPR screens.
DR BioGRID-ORCS; 100042939; 0 hits in 18 CRISPR screens.
DR BioGRID-ORCS; 100042943; 0 hits in 3 CRISPR screens.
DR BioGRID-ORCS; 100042944; 0 hits in 1 CRISPR screen.
DR BioGRID-ORCS; 100042946; 0 hits in 4 CRISPR screens.
DR ChiTaRS; H2al1g; mouse.
DR PRO; PR:Q5M8Q2; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q5M8Q2; protein.
DR Bgee; ENSMUSG00000094904; Expressed in spermatid and 6 other tissues.
DR GO; GO:0044815; C:DNA packaging complex; IDA:MGI.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IDA:MGI.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Chromosome; Differentiation; DNA-binding; Nucleosome core; Nucleus;
KW Reference proteome; Spermatogenesis.
FT CHAIN 1..105
FT /note="Histone H2A-like 1"
FT /id="PRO_0000440627"
SQ SEQUENCE 105 AA; 12122 MW; 306B0E56FC34A8B8 CRC64;
MAKKMQRRRR QKRTRSQRGE LPFSLVDRFL REEFHSSRLS SSALSFLTSV LEYLTSNILE
LAGEVAQTTG RKRIAPEDVR LVVQNNEQLR QLFKPGGTSV NEDDN
