H2AY_CHICK
ID H2AY_CHICK Reviewed; 372 AA.
AC O93327; O93326;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Core histone macro-H2A.1;
DE Short=Histone macroH2A1;
DE Short=mH2A1;
DE AltName: Full=H2A.y;
DE AltName: Full=H2A/y;
GN Name=MACROH2A1 {ECO:0000250|UniProtKB:O75367};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Brain;
RX PubMed=9611225; DOI=10.1093/nar/26.12.2837;
RA Pehrson J.R., Fuji R.N.;
RT "Evolutionary conservation of histone macroH2A subtypes and domains.";
RL Nucleic Acids Res. 26:2837-2842(1998).
RN [2]
RP FUNCTION, AND ADP-RIBOSYLATION.
RX PubMed=15718235; DOI=10.1074/jbc.m500170200;
RA Abbott D.W., Chadwick B.P., Thambirajah A.A., Ausio J.;
RT "Beyond the Xi: macroH2A chromatin distribution and post-translational
RT modification in an avian system.";
RL J. Biol. Chem. 280:16437-16445(2005).
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. The presence of macro-H2A enhances the
CC interaction of the histone octamer with the nucleosomal DNA and may
CC repress the ability of the nucleosome to be remodelled.
CC {ECO:0000269|PubMed:15718235}.
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.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=O93327-1; Sequence=Displayed;
CC Name=1;
CC IsoId=O93327-2; Sequence=VSP_017598, VSP_017599;
CC -!- TISSUE SPECIFICITY: Present in liver (at protein level).
CC {ECO:0000269|PubMed:9611225}.
CC -!- DEVELOPMENTAL STAGE: Present in immature erythrocytes (at protein
CC level). {ECO:0000269|PubMed:9611225}.
CC -!- PTM: Monoubiquitinated at either Lys-116 or Lys-117. {ECO:0000250}.
CC -!- PTM: ADP-ribosylated. {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; AF058445; AAC28846.1; -; mRNA.
DR EMBL; AF058446; AAC28847.1; -; mRNA.
DR RefSeq; NP_990338.1; NM_205007.1. [O93327-1]
DR AlphaFoldDB; O93327; -.
DR SMR; O93327; -.
DR STRING; 9031.ENSGALP00000010267; -.
DR PaxDb; O93327; -.
DR PRIDE; O93327; -.
DR Ensembl; ENSGALT00000068097; ENSGALP00000049554; ENSGALG00000040141. [O93327-1]
DR Ensembl; ENSGALT00000081254; ENSGALP00000048704; ENSGALG00000040141. [O93327-2]
DR GeneID; 395858; -.
DR KEGG; gga:395858; -.
DR CTD; 395858; -.
DR VEuPathDB; HostDB:geneid_395858; -.
DR eggNOG; KOG1756; Eukaryota.
DR eggNOG; KOG2633; Eukaryota.
DR GeneTree; ENSGT00940000159541; -.
DR HOGENOM; CLU_062828_0_0_1; -.
DR InParanoid; O93327; -.
DR OMA; GHNFPAK; -.
DR OrthoDB; 1504122at2759; -.
DR PhylomeDB; O93327; -.
DR TreeFam; TF332276; -.
DR PRO; PR:O93327; -.
DR Proteomes; UP000000539; Chromosome 13.
DR Bgee; ENSGALG00000040141; Expressed in brain and 13 other tissues.
DR ExpressionAtlas; O93327; baseline and differential.
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 GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR CDD; cd00074; H2A; 1.
DR CDD; cd02904; Macro_H2A-like; 1.
DR Gene3D; 1.10.20.10; -; 1.
DR Gene3D; 3.40.220.10; -; 1.
DR InterPro; IPR021171; Core_histone_macro-H2A.
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; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR035796; Macro_H2A.
DR PANTHER; PTHR23430; PTHR23430; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR Pfam; PF01661; Macro; 1.
DR PIRSF; PIRSF037942; Core_histone_macro-H2A; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00506; A1pp; 1.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Alternative splicing; Chromatin regulator; Chromosome;
KW DNA-binding; Isopeptide bond; Nucleosome core; Nucleus; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..372
FT /note="Core histone macro-H2A.1"
FT /id="PRO_0000227905"
FT DOMAIN 15..90
FT /note="Histone H2A"
FT DOMAIN 184..370
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT REGION 128..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..160
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT MOD_RES 9
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0C0S5"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 198..217
FT /note="NLIHSEISNLAGFEVEAIIN -> QVVQADIATIDSDAVVH (in
FT isoform 1)"
FT /evidence="ECO:0000303|PubMed:9611225"
FT /id="VSP_017598"
FT VAR_SEQ 221..229
FT /note="ADIDLKDDL -> SDFYTGGEV (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:9611225"
FT /id="VSP_017599"
SQ SEQUENCE 372 AA; 39656 MW; 8F5940ECD57C6E95 CRC64;
MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI
LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS
KGKLEAIITP PPAKKAKSPS QKKTVSKKTG GKKGARKSKK KQGEVSKSAS ADSTTEGTPA
DGFTVLSTKS LFLGQKLNLI HSEISNLAGF EVEAIINPTN ADIDLKDDLG STLEKKGGKE
FVEAVIELRK KNGPLDIAGA VVSAGHGLPA KFVIHCNSPG WGSDKCEELL EKTVKNCLAL
ADEKKLKSIA FPSIGSGRNG FPKQTAAQLI LKAISSYFVS TMSSSIKTVY FVLFDSESIG
IYVQEMAKLD AN
