ID F7FJQ1_ORNAN Unreviewed; 488 AA.
AC F7FJQ1;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 3.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Histone deacetylase 2 {ECO:0000256|PIRNR:PIRNR037913};
DE Short=HD2 {ECO:0000256|PIRNR:PIRNR037913};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037913};
GN Name=HDAC2 {ECO:0000313|Ensembl:ENSOANP00000005760.3};
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258 {ECO:0000313|Ensembl:ENSOANP00000005760.3, ECO:0000313|Proteomes:UP000002279};
RN [1] {ECO:0000313|Ensembl:ENSOANP00000005760.3, ECO:0000313|Proteomes:UP000002279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000005760.3,
RC ECO:0000313|Proteomes:UP000002279};
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2] {ECO:0000313|Ensembl:ENSOANP00000005760.3}
RP IDENTIFICATION.
RC STRAIN=Glennie {ECO:0000313|Ensembl:ENSOANP00000005760.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Histone deacetylase that catalyzes the deacetylation of
CC lysine residues on the N-terminal part of the core histones (H2A, H2B,
CC H3 and H4). Histone deacetylation gives a tag for epigenetic repression
CC and plays an important role in transcriptional regulation, cell cycle
CC progression and developmental events. Histone deacetylases act via the
CC formation of large multiprotein complexes.
CC {ECO:0000256|PIRNR:PIRNR037913}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(2E)-butenoyl-L-lysyl-[protein] = (2E)-2-butenoate
CC + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:35899, ChEBI:CHEBI:137954;
CC Evidence={ECO:0000256|ARBA:ARBA00029357};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC Evidence={ECO:0000256|ARBA:ARBA00029357};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[histone] = acetate + L-lysyl-
CC [histone]; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; EC=3.5.1.98;
CC Evidence={ECO:0000256|ARBA:ARBA00029372};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC Evidence={ECO:0000256|ARBA:ARBA00029372};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] = acetate + L-lysyl-
CC [protein]; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:61930; Evidence={ECO:0000256|ARBA:ARBA00029349};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC Evidence={ECO:0000256|ARBA:ARBA00029349};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR037913}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD Type 1
CC subfamily. {ECO:0000256|PIRNR:PIRNR037913}.
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DR AlphaFoldDB; F7FJQ1; -.
DR STRING; 9258.ENSOANP00000005760; -.
DR Ensembl; ENSOANT00000005762.3; ENSOANP00000005760.3; ENSOANG00000003631.3.
DR eggNOG; KOG1342; Eukaryota.
DR GeneTree; ENSGT00940000155725; -.
DR HOGENOM; CLU_007727_7_4_1; -.
DR InParanoid; F7FJQ1; -.
DR OMA; EHRWDKH; -.
DR OrthoDB; 1327607at2759; -.
DR TreeFam; TF106171; -.
DR Proteomes; UP000002279; Chromosome 2.
DR Bgee; ENSOANG00000003631; Expressed in fibroblast and 8 other cell types or tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0035098; C:ESC/E(Z) complex; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016581; C:NuRD complex; IBA:GO_Central.
DR GO; GO:0070822; C:Sin3-type complex; IEA:Ensembl.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0160009; F:histone decrotonylase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051059; F:NF-kappaB binding; IEA:Ensembl.
DR GO; GO:0160010; F:protein de-2-hydroxyisobutyrylase activity; IEA:Ensembl.
DR GO; GO:0031507; P:heterochromatin formation; IEA:Ensembl.
DR GO; GO:0010944; P:negative regulation of transcription by competitive promoter binding; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0045862; P:positive regulation of proteolysis; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd10011; HDAC2; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR003084; His_deacetylse_1.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF2; HISTONE DEACETYLASE 2; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR PRINTS; PR01270; HDASUPER.
DR PRINTS; PR01271; HISDACETLASE.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW ECO:0000256|PIRNR:PIRNR037913}; Hydrolase {ECO:0000256|PIRNR:PIRNR037913};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037913-3};
KW Nucleus {ECO:0000256|PIRNR:PIRNR037913};
KW Reference proteome {ECO:0000313|Proteomes:UP000002279};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Transcription {ECO:0000256|PIRNR:PIRNR037913};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037913}.
FT DOMAIN 29..318
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 389..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-1"
FT BINDING 100
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
FT BINDING 177
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 179
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 265
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-3"
FT BINDING 304
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR037913-2"
SQ SEQUENCE 488 AA; 55277 MW; 67550C16FDBA56BF CRC64;
MAYSQGGGKK KVCYYYDGDI GNYYYGQGHP MKPHRIRMTH NLLLNYGLYR KMEIYRPHKA
TAEEMTKYHS DEYIKFLRSI RPDNMSEYSK QMQRFNVGED CPVFDGLFEF CQLSTGGSVA
GAVKLNRQQT DMAVNWAGGL HHAKKSEASG FCYVNDIVLA ILELLKYHQR VLYIDIDIHH
GDGVEEAFYT TDRVMTVSFH KYGEYFPGTG DLRDIGAGKG KYYAVNFPMR DGIDDESYGQ
IFKPIISKVM EMYQPSAVVL QCGADSLSGD RLGCFNLTVK GHAKCVEVVK TFNLPLLMLG
GGGYTIRNVA RCWTYETAVA LDCEIPNELP YNDYFEYFGP DFKLHISPSN MTNQNTPEYM
EKIKQRLFEN LRMLPHAPGV QMQAIPEDAV HEDSGDEDGE DPDKRISIRA SDKRIACDEE
FSDSEDEGEG GRRNVADHKK GAKKARIEED KKETEDKKAD VKEEDKSKDS SGEKTDTKGA
KSEQLSNP
//
