ID   H2AV2_DICDI             Reviewed;         286 AA.
AC   Q54HV9;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Histone H2A.v2;
GN   Name=H2Av2; ORFNames=DDB_G0289193;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other members of the histone H2A family, this
CC       protein is much longer and has a highly divergent N-terminus. It is
CC       therefore unclear whether it is a real histone. {ECO:0000305}.
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DR   EMBL; AAFI02000131; EAL62830.1; -; Genomic_DNA.
DR   RefSeq; XP_636330.1; XM_631238.1.
DR   AlphaFoldDB; Q54HV9; -.
DR   SMR; Q54HV9; -.
DR   STRING; 44689.DDB0220642; -.
DR   PaxDb; Q54HV9; -.
DR   EnsemblProtists; EAL62830; EAL62830; DDB_G0289193.
DR   GeneID; 8627003; -.
DR   KEGG; ddi:DDB_G0289193; -.
DR   dictyBase; DDB_G0289193; H2Av2.
DR   eggNOG; KOG1756; Eukaryota.
DR   HOGENOM; CLU_974633_0_0_1; -.
DR   InParanoid; Q54HV9; -.
DR   Reactome; R-DDI-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-DDI-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-DDI-3214815; HDACs deacetylate histones.
DR   Reactome; R-DDI-3214858; RMTs methylate histone arginines.
DR   Reactome; R-DDI-427359; SIRT1 negatively regulates rRNA expression.
DR   Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR   Reactome; R-DDI-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-DDI-68616; Assembly of the ORC complex at the origin of replication.
DR   Reactome; R-DDI-73772; RNA Polymerase I Promoter Escape.
DR   PRO; PR:Q54HV9; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
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   Gene3D; 1.10.20.10; -; 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   PANTHER; PTHR23430; PTHR23430; 1.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF16211; Histone_H2A_C; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..286
FT                   /note="Histone H2A.v2"
FT                   /id="PRO_0000389156"
FT   REGION          1..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..100
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        108..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   286 AA;  31051 MW;  91D7A4EF31A4FBE1 CRC64;
     MKSNGHPSNN SINEPIKQQE TKQNNKSSHK TPHKPPYLAR AKFQPKTSSF SNSSFQSSTP
     PKPQIALKSP SPSPSQPKTS SSSYSSLSSP SPSQPKTSSP SLPSSTPPKP RQIALKSPSS
     SSSSQPKTSS SSYSSLPSST PPKPQHIELK SPSTVKKSPI VKKTNSPKGS KFKKTIRSSR
     STRAGLTISV SRVEKLLRGR RYSKRVSPTS CVFLAAVLEY MVLELLELSL NELSLSKKSR
     RIKNRHINLS ILKDVELSAL LNDVIICSGG VLSSIHPSLL KLKKDQ