ID A0A1S3F4E2_DIPOR Unreviewed; 371 AA.
AC A0A1S3F4E2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Core histone macro-H2A {ECO:0000256|PIRNR:PIRNR037942};
GN Name=LOC105985507 {ECO:0000313|RefSeq:XP_012871528.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012871528.1};
RN [1] {ECO:0000313|RefSeq:XP_012871528.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012871528.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes. {ECO:0000256|PIRNR:PIRNR037942}.
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. {ECO:0000256|PIRNR:PIRNR037942}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037942}.
CC Chromosome {ECO:0000256|PIRNR:PIRNR037942}.
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DR RefSeq; XP_012871528.1; XM_013016074.1.
DR AlphaFoldDB; A0A1S3F4E2; -.
DR GeneID; 105985507; -.
DR OrthoDB; 235643at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031490; F:chromatin DNA binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR CDD; cd00074; H2A; 1.
DR CDD; cd02904; Macro_H2A-like; 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; 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:SF20; CORE HISTONE MACRO-H2A.1; 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 PIRSF; PIRSF037942; Core_histone_macro-H2A; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00506; A1pp; 1.
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 ECO:0000256|PIRNR:PIRNR037942}; Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037942};
KW Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW ECO:0000256|PIRNR:PIRNR037942}; Nucleus {ECO:0000256|PIRNR:PIRNR037942};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT DOMAIN 183..369
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT REGION 128..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037942-1"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000256|PIRSR:PIRSR037942-1"
SQ SEQUENCE 371 AA; 39535 MW; A0B8E9FC0CE928BC CRC64;
MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI
LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS
KGKLEAIITP PPAKKAKSPS QKKPVSKKAG GKKGARKSKK QGEVSKAASA DSTTEGTPTD
GFTVLSTKSL FLGQKLNLIH SEISNLAGFE VEAIINPTNA DIDLKDDLGN TLEKKGGKEF
VEAVLELRKK NGPLEVAGAA MSAGHGLPAK FVIHCNSPVW GADKCEELLE KTVKNCLALA
DDKKLKSIAF PSIGSGRNGF PKQTAAQLIL KAISSYFVAT MSSSIKTVYF VLFDSESIGI
YVQEMAKLDA N
//
