ID A0A2U4BEV9_TURTR Unreviewed; 342 AA.
AC A0A2U4BEV9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Core histone macro-H2A.2 isoform X2 {ECO:0000313|RefSeq:XP_019791716.1};
GN Name=LOC101315936 {ECO:0000313|RefSeq:XP_019791716.1};
OS Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Delphinidae; Tursiops.
OX NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019791716.1};
RN [1] {ECO:0000313|RefSeq:XP_019791716.1}
RP IDENTIFICATION.
RC TISSUE=Spleen {ECO:0000313|RefSeq:XP_019791716.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_019791716.1; XM_019936157.2.
DR AlphaFoldDB; A0A2U4BEV9; -.
DR SMR; A0A2U4BEV9; -.
DR GeneID; 101315936; -.
DR OrthoDB; 235643at2759; -.
DR Proteomes; UP000245320; Chromosome 16.
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 GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd00074; H2A; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 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; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR PANTHER; PTHR23430:SF37; CORE HISTONE MACRO-H2A.2; 1.
DR PANTHER; PTHR23430; HISTONE H2A; 1.
DR Pfam; PF00125; Histone; 1.
DR Pfam; PF16211; Histone_H2A_C; 1.
DR Pfam; PF01661; Macro; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF52949; Macro domain-like; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleosome core {ECO:0000256|ARBA:ARBA00023269};
KW Reference proteome {ECO:0000313|Proteomes:UP000245320};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 184..340
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT REGION 115..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..157
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 342 AA; 36834 MW; 7C0FACD93DAE030D CRC64;
MSGRSGKKKM SKLSRSARAG VIFPVGRLMR YLKKGTFKYR ISVGAPVYMA AVIEYLAAEI
LELAGNAARD NKKARIAPRH ILLAVANDEE LNQLLKGVTI ASGGVLPRIH PELLAKKRGT
KGKSETILSP PPEKRGRKAT SGKKGGKKSK AAKPRTSKKS KPKDSDKEGT SNSTSEDGPG
DGFTILSSKS LVLGQKLSLT QSDISHIGSM RVEGIVHPTT AEIDLKEDIA AVSQSSGLAA
KFVIHCHIPQ WGSDKCEEQL EETIKNCLSA AEDKKLKSVA FPPFPSGRNC FPKQTAAQVT
LKAISAHFDD SSASSLKNVY FLLFDSESIG IYVQEMAKLD AK
//
