H2AV_TETTS
ID H2AV_TETTS Reviewed; 146 AA.
AC P08992;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Histone H2A.Z;
DE AltName: Full=hv1;
GN Name=HTA3; Synonyms=HV1; ORFNames=TTHERM_00143660;
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2111857; DOI=10.1007/bf02101116;
RA van Daal A., White E.M., Elgin S.C.R., Gorovsky M.A.;
RT "Conservation of intron position indicates separation of major and variant
RT H2As is an early event in the evolution of eukaryotes.";
RL J. Mol. Evol. 30:449-455(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210;
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
RN [3]
RP PROTEIN SEQUENCE OF 2-62 AND 79-107, ACETYLATION AT LYS-5; LYS-8; LYS-11;
RP LYS-14; LYS-17 AND LYS-22, AND PHOSPHORYLATION.
RX PubMed=3944120; DOI=10.1016/s0021-9258(17)36034-9;
RA Allis C.D., Richman R., Gorovsky M.A., Ziegler Y.S., Touchstone B.,
RA Bradley W.A., Cook R.G.;
RT "hv1 is an evolutionarily conserved H2A variant that is preferentially
RT associated with active genes.";
RL J. Biol. Chem. 261:1941-1948(1986).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 9-146.
RC STRAIN=CU428;
RX PubMed=3340523; DOI=10.1093/nar/16.1.179;
RA White E.M., Shapiro D.L., Allis C.D., Gorovsky M.A.;
RT "Sequence and properties of the message encoding Tetrahymena hv1, a highly
RT evolutionarily conserved histone H2A variant that is associated with active
RT genes.";
RL Nucleic Acids Res. 16:179-198(1988).
RN [5]
RP ACETYLATION.
RC STRAIN=B;
RX PubMed=7061439; DOI=10.1016/s0021-9258(18)34965-2;
RA Vavra K.J., Allis C.D., Gorovsky M.A.;
RT "Regulation of histone acetylation in Tetrahymena macro- and micronuclei.";
RL J. Biol. Chem. 257:2591-2598(1982).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=B2086, and CU428;
RX PubMed=8276246; DOI=10.1101/gad.7.12b.2641;
RA Stargell L.A., Bowen J., Dadd C.A., Dedon P.C., Davis M., Cook R.G.,
RA Allis C.D., Gorovsky M.A.;
RT "Temporal and spatial association of histone H2A variant hv1 with
RT transcriptionally competent chromatin during nuclear development in
RT Tetrahymena thermophila.";
RL Genes Dev. 7:2641-2651(1993).
RN [7]
RP FUNCTION.
RC STRAIN=B2086, and CU428;
RX PubMed=8754831; DOI=10.1128/mcb.16.8.4305;
RA Liu X., Li B., Gorovsky M.A.;
RT "Essential and nonessential histone H2A variants in Tetrahymena
RT thermophila.";
RL Mol. Cell. Biol. 16:4305-4311(1996).
RN [8]
RP ACETYLATION AT LYS-5; LYS-8; LYS-11; LYS-14; LYS-17 AND LYS-22.
RC STRAIN=B2086, CU427, and CU428;
RX PubMed=11430834; DOI=10.1016/s1097-2765(01)00269-6;
RA Ren Q., Gorovsky M.A.;
RT "Histone H2A.Z acetylation modulates an essential charge patch.";
RL Mol. Cell 7:1329-1335(2001).
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes, preferentially in transcriptionally active
CC chromatin. 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. Essential for vegetative growth.
CC {ECO:0000269|PubMed:8754831}.
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 HTA3 forms a heterodimer with H2B.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8276246}. Chromosome
CC {ECO:0000269|PubMed:8276246}. Note=Localizes to the large,
CC transcriptionally active, somatic macronucleus (MAC) at all stages of
CC the cell cycle. Usually absent from the small, transcriptionally inert,
CC germ line micronucleus (MIC), it is shortly found in the MIC during an
CC early stage of conjugation.
CC -!- PTM: Phosphorylated on the C-terminal half.
CC {ECO:0000269|PubMed:3944120}.
CC -!- PTM: Acetylation occurs almost exclusively in the MAC.
CC {ECO:0000269|PubMed:11430834, ECO:0000269|PubMed:3944120,
CC ECO:0000269|PubMed:7061439}.
CC -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC -!- CAUTION: To ensure consistency between histone entries, we follow the
CC 'Brno' nomenclature for histone modifications, with positions referring
CC to those used in the literature for the 'closest' model organism. Due
CC to slight variations in histone sequences between organisms and to the
CC presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC actual positions of modified amino acids in the sequence generally
CC differ. In this entry the following conventions are used: H2A.ZK4ac =
CC acetylated Lys-5; H2A.ZK7ac = acetylated Lys-8; H2A.ZK10ac = acetylated
CC Lys-11; H2A.ZK13ac = acetylated Lys-14; H2A.ZK16ac = acetylated Lys-17;
CC H2A.ZK21ac = acetylated Lys-22. {ECO:0000305}.
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DR EMBL; X15548; CAA33554.1; -; Genomic_DNA.
DR EMBL; GG662793; EAR90860.2; -; Genomic_DNA.
DR EMBL; X06725; CAA29903.1; -; mRNA.
DR PIR; S08210; S08210.
DR RefSeq; XP_001011105.2; XM_001011105.3.
DR AlphaFoldDB; P08992; -.
DR SMR; P08992; -.
DR STRING; 5911.EAR90860; -.
DR iPTMnet; P08992; -.
DR PRIDE; P08992; -.
DR EnsemblProtists; EAR90860; EAR90860; TTHERM_00143660.
DR GeneID; 7827530; -.
DR KEGG; tet:TTHERM_00143660; -.
DR eggNOG; KOG1757; Eukaryota.
DR HOGENOM; CLU_062828_2_1_1; -.
DR InParanoid; P08992; -.
DR OMA; FPCGRIK; -.
DR OrthoDB; 1504122at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW Acetylation; Chromosome; Direct protein sequencing; DNA-binding;
KW Nucleosome core; Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3944120"
FT CHAIN 2..146
FT /note="Histone H2A.Z"
FT /id="PRO_0000055311"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:11430834,
FT ECO:0000269|PubMed:3944120"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:11430834,
FT ECO:0000269|PubMed:3944120"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:11430834,
FT ECO:0000269|PubMed:3944120"
FT MOD_RES 14
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:11430834,
FT ECO:0000269|PubMed:3944120"
FT MOD_RES 17
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:11430834,
FT ECO:0000269|PubMed:3944120"
FT MOD_RES 22
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:11430834,
FT ECO:0000269|PubMed:3944120"
SQ SEQUENCE 146 AA; 15315 MW; 5143E5DC0C60B517 CRC64;
MAGGKGGKGG KGGKGGKVGG AKNKKTPQSR SYKAGLQFPV GRIHRFLKGR VSAKNRVGAT
AAVYAAAILE YLTAEVLELA GNASKDFKVR RITPRHLLLA IRGDEELDIL IKATIAGGGV
IPHIHKALLG KHSTKNRSSA KTAEPR
