ID A0A1L8EPF2_XENLA Unreviewed; 1066 AA.
AC A0A1L8EPF2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Histone deacetylase {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111, ECO:0000256|PIRNR:PIRNR037911};
GN Name=hdac4.S {ECO:0000313|RefSeq:XP_018094400.1,
GN ECO:0000313|Xenbase:XB-GENE-6486313};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018094400.1};
RN [1] {ECO:0000313|RefSeq:XP_018094400.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018094400.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018094400.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Responsible for the deacetylation of lysine residues on the
CC N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone
CC deacetylation gives a tag for epigenetic repression and plays an
CC important role in transcriptional regulation, cell cycle progression
CC and developmental events. {ECO:0000256|PIRNR:PIRNR037911}.
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:PIRNR037911}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000256|ARBA:ARBA00007738,
CC ECO:0000256|PIRNR:PIRNR037911}.
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DR RefSeq; XP_018094400.1; XM_018238911.2.
DR AlphaFoldDB; A0A1L8EPF2; -.
DR STRING; 8355.A0A1L8EPF2; -.
DR PaxDb; 8355-A0A1L8EPF2; -.
DR GeneID; 108703026; -.
DR KEGG; xla:108703026; -.
DR AGR; Xenbase:XB-GENE-6486313; -.
DR CTD; 108703026; -.
DR Xenbase; XB-GENE-6486313; hdac4.S.
DR OMA; XAVASTE; -.
DR OrthoDB; 124800at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 108703026; Expressed in blastula and 19 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd10162; ClassIIa_HDAC4_Gln-rich-N; 1.
DR Gene3D; 6.10.250.1550; -; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR046949; HDAC4/5/7/9.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR024643; Hist_deacetylase_Gln_rich_N.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF11; HISTONE DEACETYLASE; 1.
DR PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR Pfam; PF12203; HDAC4_Gln; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Repressor {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription {ECO:0000256|PIRNR:PIRNR037911};
KW Transcription regulation {ECO:0000256|PIRNR:PIRNR037911};
KW Zinc {ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 63..152
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 663..975
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 134..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..569
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 786
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 655
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 657
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 663
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 734
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 959
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1066 AA; 117853 MW; 32D70888215D7293 CRC64;
MSSHTHSDGI SGLDQPVDLL TQTRAKHMPS PVDVSAALPL QVAPSALPMD LRLDPQYTIS
AQEPSGREQQ LQQELLSLKQ KQQIQRQLLI AEFQRQHEQL SRQHEAQLHE HIKQQQELLA
MKHQQELLEH QRKLEQHRQE QQMEKQQRDQ KLLQLKNKEK GKESAVASTE VKMKLQEFVL
NKKKALAHRS LNHCMSSDPR LWKTQHSSLD QSPPPQGLVS ASYHQAVLGM YDSKDDFPLR
KTASEPNLKL RSRLKQKVAE RRSSPLLRRK DGPGITTLKK RPLDVSDSAC NSAPGSGPSS
PNNSSSNISS ENGIAGPLGL QTEASLAHRL VNRENSITQL PLYTSPSLPN ITLGLPASGS
TNGGSGQENE CLSLPALQQR LSLFPAAHLT SYLGPEATNS HNQLLQHMVL LEQPGAQSSL
ISGLGTLPLH SQSLVSPDRV SPTMHKLRQH RPLGRTQSAP LPQNSHALQH LVIQQQHQQF
LEKHKQQFQQ QQLHLNKMIP KVNEASRQHE SHPEETEEEL REHQALHEEP YTERLAEQKE
LSPGNVVHVK QEKEESDDEE NTLDLERSKM QSDPDLLFRQ QTLLLEQQRI HQLRNYQASL
EAAGLVVPFS GHRPLSRAQS SPASASFPMS VQEAPSKTRF TTGLVYDTLM LKHQCICGNT
NSHPEHAGRI QSIWSRLQET GLRSMCECIR GRKATLEELQ TVHSEAHTIL YGTNPLNRQK
LEGSLASLFV RLTCGGVGVD SDTIWNEVHS SGAARLAVGC VVELASKVVS GELKNGFAVV
RPPGHHAEES TPMGFCYFNS VAIAAKVLQQ RLNVAKTLIV DWDVHHGNGT QQAFYSDPNV
LYISLHRYDD GNFFPGSGAP DEVGTGAGVG FNVNMAFTGG LDPPMGDAEY LAAFRTVVMP
IAAKFSPDVV LVSAGFDAVE GHPSPLGGYT VSAKCFGYLT KQLMEISGGR IVLALEGGHD
LTAICDASEA CVSALLGNKL EPLPESVLQQ RPNINAVKSM ENVIQIQSEY WPCLHISSST
VSYSLIEAQK CENEEAETVT AMASLSVDVR QERRTEDEPM DEEPPL
//
