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Database: UniProt
Entry: A0A3P8Y6G7_ESOLU
LinkDB: A0A3P8Y6G7_ESOLU
Original site: A0A3P8Y6G7_ESOLU 
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
//
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