H2AZL_XENLA
ID H2AZL_XENLA Reviewed; 128 AA.
AC P70094; O13272; O13273;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Histone H2A.Z-like;
DE Short=H2A.Zl;
DE AltName: Full=H2A.Z1;
DE AltName: Full=XH2AZ;
GN Name=h2a.zl1; Synonyms=h2a.zl2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Oocyte;
RX PubMed=8918796; DOI=10.1093/nar/24.20.3947;
RA Iouzalen N., Moreau J., Mechali M.;
RT "H2A.Zl, a new variant histone expressed during Xenopus early developement
RT exhibits several distinct features from the core histone H2A.";
RL Nucleic Acids Res. 24:3947-3952(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Aberger F., Grunz H., Richter K.;
RT "Histone H2A.z displays a neural-specific expression pattern in Xenopus.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg, and Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=15299007; DOI=10.1074/jbc.m408409200;
RA Ridgway P., Brown K.D., Rangasamy D., Svensson U., Tremethick D.J.;
RT "Unique residues on the H2A.Z containing nucleosome surface are important
RT for Xenopus laevis development.";
RL J. Biol. Chem. 279:43815-43820(2004).
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin,
CC limiting DNA accessibility to the cellular machineries which require
CC DNA as a template. Histones thereby play a central role in
CC transcription regulation, DNA repair, DNA replication and chromosomal
CC stability. DNA accessibility is regulated via a complex set of post-
CC translational modifications of histones, also called histone code, and
CC nucleosome remodeling. May be required at gastrulation for correct
CC mesoderm formation. {ECO:0000269|PubMed:15299007}.
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. The octamer wraps approximately 147 bp of
CC DNA. H2A or its variant H2A.Zl forms a heterodimer with H2B (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:8918796}.
CC -!- DEVELOPMENTAL STAGE: Expression is highest at the gastrula stage.
CC Expressed preferentially in tissues of mesoderm origin, such as the
CC notochord and some regions of the primitive ear.
CC {ECO:0000269|PubMed:15299007, ECO:0000269|PubMed:8918796}.
CC -!- PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic
CC transcriptional repression. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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DR EMBL; X98535; CAA67148.1; -; mRNA.
DR EMBL; X98536; CAA67149.1; -; mRNA.
DR EMBL; U77893; AAB36781.1; -; mRNA.
DR EMBL; BC044011; AAH44011.1; -; mRNA.
DR EMBL; BC091714; AAH91714.1; -; mRNA.
DR RefSeq; NP_001079528.1; NM_001086059.1.
DR RefSeq; NP_001081609.1; NM_001088140.1.
DR AlphaFoldDB; P70094; -.
DR SMR; P70094; -.
DR BioGRID; 97458; 2.
DR PRIDE; P70094; -.
DR DNASU; 379215; -.
DR DNASU; 397949; -.
DR GeneID; 379215; -.
DR GeneID; 397949; -.
DR KEGG; xla:379215; -.
DR KEGG; xla:397949; -.
DR CTD; 379215; -.
DR CTD; 397949; -.
DR Xenbase; XB-GENE-6256368; h2az1.L.
DR Xenbase; XB-GENE-17342536; h2az1.S.
DR OMA; FPMGRIH; -.
DR OrthoDB; 1504122at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 379215; Expressed in gastrula and 19 other tissues.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR CDD; cd00074; H2A; 1.
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 InterPro; IPR032454; Histone_H2A_C.
DR InterPro; IPR032458; Histone_H2A_CS.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; Developmental protein; DNA-binding;
KW Isopeptide bond; Nucleosome core; Nucleus; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..128
FT /note="Histone H2A.Z-like"
FT /id="PRO_0000239072"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 12
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 14
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 116
FT /note="N6-lactoyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 128 AA; 13486 MW; 18433898EB6E95AF CRC64;
MAGGKAGKDT GKAKATSITR SSRAGLQFPV GRIHRLLKNR TTSHGRVGGT AAVYTAAILE
YLTAEVLELA GNASKDLKVK RISPRHLQLA IRGDEELDAL IKATIAGGGV IPHIHKSLIG
KKGQQKTV
