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H2AZL_XENTR
ID   H2AZL_XENTR             Reviewed;         128 AA.
AC   Q6DER6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Histone H2A.Z-like;
DE            Short=H2A.Zl;
GN   Name=h2a.zl; ORFNames=TGas044m04.1, TGas104o01.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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   -!- 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; CR761793; CAJ81557.1; -; mRNA.
DR   EMBL; CR761734; CAJ83823.1; -; mRNA.
DR   EMBL; BC077029; AAH77029.1; -; mRNA.
DR   RefSeq; NP_001005097.1; NM_001005097.2.
DR   AlphaFoldDB; Q6DER6; -.
DR   SMR; Q6DER6; -.
DR   DNASU; 448675; -.
DR   Ensembl; ENSXETT00000095443; ENSXETP00000083916; ENSXETG00000037946.
DR   GeneID; 448675; -.
DR   KEGG; xtr:448675; -.
DR   CTD; 3015; -.
DR   Xenbase; XB-GENE-485054; h2az1.
DR   InParanoid; Q6DER6; -.
DR   OrthoDB; 1504122at2759; -.
DR   Reactome; R-XTR-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR   Reactome; R-XTR-110331; Cleavage of the damaged purine.
DR   Reactome; R-XTR-171306; Packaging Of Telomere Ends.
DR   Reactome; R-XTR-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-XTR-212300; PRC2 methylates histones and DNA.
DR   Reactome; R-XTR-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-XTR-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-XTR-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR   Reactome; R-XTR-3214858; RMTs methylate histone arginines.
DR   Reactome; R-XTR-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-XTR-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-XTR-5578749; Transcriptional regulation by small RNAs.
DR   Reactome; R-XTR-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
DR   Reactome; R-XTR-68616; Assembly of the ORC complex at the origin of replication.
DR   Reactome; R-XTR-73728; RNA Polymerase I Promoter Opening.
DR   Reactome; R-XTR-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR   Reactome; R-XTR-9018519; Estrogen-dependent gene expression.
DR   Reactome; R-XTR-9670095; Inhibition of DNA recombination at telomere.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000037946; Expressed in ovary and 17 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; 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   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_0000239073"
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
 
 
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