H2AZ_CRYNJ
ID H2AZ_CRYNJ Reviewed; 138 AA.
AC P0CO00; Q55LU3; Q5K8Y2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Histone H2A.Z;
GN Name=HTZ1; OrderedLocusNames=CNL04080;
OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS MYA-565) (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=214684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEC21 / ATCC MYA-565;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
CC -!- FUNCTION: Variant histone H2A which can replace H2A in some
CC nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting
CC DNA 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. This variant is enriched at promoters, it may keep them in
CC a repressed state until the appropriate activation signal is received.
CC Near telomeres, it may counteract gene silencing caused by the spread
CC of heterochromatin proteins. Required for the RNA polymerase II and
CC SPT15/TBP recruitment to the target genes. Involved in chromosome
CC stability (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.Z forms a heterodimer with H2B. H2A.Z
CC associates with the VPS72/SWC2 subunit of the SWR1 chromatin remodeling
CC complex. Interacts also with RBP1/DNA-directed RNA polymerase II
CC largest subunit (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Acetylated once deposited into chromatin. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017352; AAW46445.1; -; Genomic_DNA.
DR RefSeq; XP_567962.1; XM_567962.1.
DR AlphaFoldDB; P0CO00; -.
DR SMR; P0CO00; -.
DR STRING; 5207.AAW46445; -.
DR PaxDb; P0CO00; -.
DR EnsemblFungi; AAW46445; AAW46445; CNL04080.
DR GeneID; 3254928; -.
DR KEGG; cne:CNL04080; -.
DR VEuPathDB; FungiDB:CNL04080; -.
DR eggNOG; KOG1757; Eukaryota.
DR HOGENOM; CLU_062828_2_1_1; -.
DR InParanoid; P0CO00; -.
DR OMA; FPCGRIK; -.
DR OrthoDB; 1504122at2759; -.
DR Proteomes; UP000002149; Chromosome 12.
DR GO; GO:0000791; C:euchromatin; IEA:EnsemblFungi.
DR GO; GO:0031011; C:Ino80 complex; IEA:EnsemblFungi.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0000812; C:Swr1 complex; IEA:EnsemblFungi.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:EnsemblFungi.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:EnsemblFungi.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:EnsemblFungi.
DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IEA:EnsemblFungi.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IEA:EnsemblFungi.
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 3: Inferred from homology;
KW Acetylation; Activator; Chromatin regulator; Chromosome; DNA-binding;
KW Nucleosome core; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..138
FT /note="Histone H2A.Z"
FT /id="PRO_0000055331"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 138 AA; 14714 MW; E692242A5B1BE140 CRC64;
MSSKVGGGKG GKSKTSSEAK VLTTRSSKAG LQFPVGRIHR FLRNKNANNV RIGAKAAVYV
ASIMEYLTAE VLELAGNAAK DLRVKRITPR HLQLAIRGDE ELDLLIRATI AGGGVLPHIH
KSLVAKNAPL KKPKALDA
