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Database: UniProt
Entry: A0A1S3F680_DIPOR
LinkDB: A0A1S3F680_DIPOR
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ID   A0A1S3F680_DIPOR        Unreviewed;       369 AA.
AC   A0A1S3F680;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Core histone macro-H2A {ECO:0000256|PIRNR:PIRNR037942};
GN   Name=LOC105985507 {ECO:0000313|RefSeq:XP_012871529.1};
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_012871529.1};
RN   [1] {ECO:0000313|RefSeq:XP_012871529.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012871529.1};
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_012871529.1; XM_013016075.1.
DR   AlphaFoldDB; A0A1S3F680; -.
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          184..367
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
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   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   369 AA;  39243 MW;  741AFE4CCBC8F378 CRC64;
     MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI
     LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS
     KGKLEAIITP PPAKKAKSPS QKKPVSKKAG GKKGARKSKK KQGEVSKAAS ADSTTEGTPT
     DGFTVLSTKS LFLGQKLQVV QADIASIDSD AVVHPTNNDF YIGGEVGNTL EKKGGKEFVE
     AVLELRKKNG PLEVAGAAMS AGHGLPAKFV IHCNSPVWGA DKCEELLEKT VKNCLALADD
     KKLKSIAFPS IGSGRNGFPK QTAAQLILKA ISSYFVATMS SSIKTVYFVL FDSESIGIYV
     QEMAKLDAN
//
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