ID A0A3P8Y6G7_ESOLU Unreviewed; 1162 AA.
AC A0A3P8Y6G7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 26.
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};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000012287.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000012287.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000012287.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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)-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|PIRNR:PIRNR037911};
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 AlphaFoldDB; A0A3P8Y6G7; -.
DR STRING; 8010.ENSELUP00000012229; -.
DR Ensembl; ENSELUT00000020550.2; ENSELUP00000012287.2; ENSELUG00000012563.2.
DR GeneTree; ENSGT00940000157440; -.
DR InParanoid; A0A3P8Y6G7; -.
DR OMA; XAVASTE; -.
DR Proteomes; UP000265140; LG16.
DR Bgee; ENSELUG00000012563; Expressed in pharyngeal gill and 15 other cell types or tissues.
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; IPR017320; Histone_deAcase_II_euk.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364:SF7; HISTONE DEACETYLASE 4; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037911-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000265140};
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 100..187
FT /note="Histone deacetylase glutamine rich N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12203"
FT DOMAIN 683..994
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 240..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 125..191
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 240..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..557
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 805
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 675
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 677
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 683
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 753
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 978
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 1162 AA; 128775 MW; 4305A09D14B68B26 CRC64;
MLLVCSDGSQ EKCAWRQGLL SRLAQLLEHD DCNVDGLPRK EQPLELLKPS GLNYIQSVDV
SAALPMQVPP SGLPMELRLD QPFGLALRPD DPGQRGQVPG QREQQLQQEL LALKHKQQVQ
RQVLIAEFQR QHEQLSRQHE AQLQEHVKHQ QDLLALKHQQ ELLEHQRKME RHRHEQEMEK
QQREQKLLLL KNKERGQESA VASTEVKMRL QEFVLNKKKA LAQRSLNHCM STDPRYWYGK
TQHSSLDQSS PPQTGMSTYN HTILGMYDPK DDFPLRKTAS EPNLKLRSRL KQKVTERRSS
PLLRRKEGPI TTAKKRSLDM AESACNSAPG SGPSSPNNSS SNITNENGVV GATSSSSVEG
SVVHRLAGRE GPLSQLSLYT SPSLPNITLG LPASGPASVT SGQQDGDRLS MHERLQKGIP
ITTPFIPGAH LPSYLTNGGS AHNPLLQHMA LLEQSQNQLG LGGMALQSPS IHKLRGQHRP
LGRTQSAPLP QNAQALQQLV VQQQHQQFLE KHKQQFQQQQ LHINKMMAKP SEPGPGPGRQ
HESHPEETEE ELREHQALCP QDGGLLRGVT IKQEPPEPQE EERDHRERMV DQELLFRQQA
VLLEQQRIHQ LRNYQASMEA AGLSITFPVH RPLSRAQSSP ASSCFPPIVV QQETPTKPRF
TTGLVYDTLM QKHQCMCGNT NTHPEHAGRI QSIWSRLQET GLRTKCECIR GRKATLEELQ
TVHSEAHVLL YGTNPLRQKL DSSVTPMFVR LPCGGVGVDS DTIWNEVHSS SAARLAVGSV
LELVFKVTSG ELKNGFAVVR PPGHHAEEST PMGFCYFNSV AIAAKLLQQR LNVSKILIVD
WDVHHGNGTQ QAFYSDPNVL YLSLHRYDDG NFFPGSGAPD EVGAGAGLGF NVNMAFTGGL
DPPMGDAEYL AAFRTVVMPI ANQFAPDVVL VSSGFDAVEG HASPLGGYRL TAKCFGYLTR
QLMGLAGGRL VLALEGGHDL TAICDASEAC VSALLGIELD PIPGEVMQQR PNSNAVRSLE
KVLEAHGEYW PCLQRGASTL GYSLSEACRC ETEEAETVTA MASLSVANKQ RRCVPFCVCD
PEWSHDILPN TCRISVLSLM PVIPSSGARR SQWRRRRQCN WLTRAPSPFR DPSDLQFSPQ
PTTNLCFNWT PSLCNAHTPS GS
//