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Database: UniProt
Entry: A0A3P8RV84_AMPPE
LinkDB: A0A3P8RV84_AMPPE
Original site: A0A3P8RV84_AMPPE 
ID   A0A3P8RV84_AMPPE        Unreviewed;       370 AA.
AC   A0A3P8RV84;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Core histone macro-H2A {ECO:0000256|PIRNR:PIRNR037942};
OS   Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000004558.1, ECO:0000313|Proteomes:UP000265080};
RN   [1] {ECO:0000313|Ensembl:ENSAPEP00000004558.1, ECO:0000313|Proteomes:UP000265080}
RP   NUCLEOTIDE SEQUENCE.
RA   Lehmann R.;
RT   "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT   of the orange clownfish Amphiprion percula.";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSAPEP00000004558.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A3P8RV84; -.
DR   Ensembl; ENSAPET00000004682.1; ENSAPEP00000004558.1; ENSAPEG00000003265.1.
DR   GeneTree; ENSGT00940000158120; -.
DR   Proteomes; UP000265080; Chromosome 20.
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: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   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:UP000265080};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          182..368
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   REGION          117..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..141
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..156
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   370 AA;  40181 MW;  AB5EAA2C39A5C15F CRC64;
     MSARGGKKKA TKLSRSARAG VIFPVGRMMR YLRTGTHKYR IGMGAPVYMA AVIEYLAAEI
     LELAGNAARD NKKGRITPRH IKLAVANDEE LNQLLRGVTI SNGGVLPRIH PELLSKKRGS
     RVKVETQASV PDKQEGRSKS KKPVKPFKKV KGKRGRKPKR TDNDKESVPN STAEDGPGDG
     FTILSAKSLF LGQKLSLTES EIGKIGTIKV EGIINPTNAE MDLKDGVGNA LEKAGGREFL
     EGVKELRKAQ GPLEVASVAV SQANGMAARF IIHCNIPQWG SEKCEDQLEK TVKNCLSAAE
     EKKLKSVAFP SLPAGRNGFP KQTAAQLILK AISNHFVSST SSSLKNIYFV LFDSESIGIY
     LQEMAKLDTK
//
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