HDAC5_CRIGR
ID HDAC5_CRIGR Reviewed; 1111 AA.
AC Q80ZH1;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Histone deacetylase 5;
DE Short=HD5;
DE EC=3.5.1.98;
GN Name=HDAC5;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Ovary;
RX PubMed=15525819; DOI=10.1093/glycob/cwi011;
RA Chen W., Tang J., Stanley P.;
RT "Suppressors of alpha(1,3)fucosylation identified by expression cloning in
RT the LEC11B gain-of-function CHO mutant.";
RL Glycobiology 15:259-269(2005).
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. Histone deacetylases act via the formation of
CC large multiprotein complexes. Involved in muscle maturation by
CC repressing transcription of myocyte enhancer MEF2C. During muscle
CC differentiation, it shuttles into the cytoplasm, allowing the
CC expression of myocyte enhancer factors (By similarity). Serves as a
CC corepressor of RARA and causes its deacetylation (By similarity). In
CC association with RARA, plays a role in the repression of microRNA-10a
CC and thereby in the inflammatory response (By similarity).
CC {ECO:0000250|UniProtKB:Q9UQL6}.
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 -!- SUBUNIT: Interacts with AHRR, BAHD1, BCOR, HDAC7, HDAC9, CTBP1, MEF2C,
CC NCOR2, NRIP1, PHB2 and a 14-3-3 chaperone protein. Interacts with BCL6,
CC DDIT3/CHOP, GRK5, KDM5B and MYOCD. Interacts with EP300 in the presence
CC of TFAP2C. Interacts with ANKRA2. Interacts with CUL7 (as part of the
CC 3M complex); negatively regulated by ANKRA2. Interacts with ZBTB7B; the
CC interaction allows the recruitment of HDAC4 on CD8 loci for
CC deacetylation and possible inhibition of CD8 genes expression (By
CC similarity). Interacts with RARA (By similarity).
CC {ECO:0000250|UniProtKB:Q9UQL6, ECO:0000250|UniProtKB:Q9Z2V6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Shuttles between the nucleus and the cytoplasm. In muscle cells,
CC it shuttles into the cytoplasm during myocyte differentiation. The
CC export to cytoplasm depends on the interaction with a 14-3-3 chaperone
CC protein and is due to its phosphorylation at Ser-250 and Ser-489 by
CC AMPK, CaMK1 and SIK1 (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The nuclear export sequence mediates the shuttling between the
CC nucleus and the cytoplasm.
CC -!- PTM: Phosphorylated by AMPK, CaMK1, SIK1 and PRKD1 at Ser-250 and Ser-
CC 489. The phosphorylation is required for the export to the cytoplasm
CC and inhibition. Phosphorylated by the PKC kinases PKN1 and PKN2,
CC impairing nuclear import (By similarity). Phosphorylated by GRK5,
CC leading to nuclear export of HDAC5 and allowing MEF2-mediated
CC transcription (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. Polyubiquitination however does not lead to its
CC degradation (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; AY145846; AAN46420.1; -; mRNA.
DR RefSeq; NP_001233710.1; NM_001246781.1.
DR RefSeq; XP_007643219.1; XM_007645029.2.
DR AlphaFoldDB; Q80ZH1; -.
DR SMR; Q80ZH1; -.
DR STRING; 10029.NP_001233710.1; -.
DR GeneID; 100689350; -.
DR KEGG; cge:100689350; -.
DR CTD; 10014; -.
DR eggNOG; KOG1343; Eukaryota.
DR OrthoDB; 1484694at2759; -.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004407; F:histone deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR GO; GO:0009889; P:regulation of biosynthetic process; IEA:UniProt.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IEA:InterPro.
DR GO; GO:0051239; P:regulation of multicellular organismal process; IEA:UniProt.
DR GO; GO:0010830; P:regulation of myotube differentiation; ISS:UniProtKB.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR Gene3D; 3.40.800.20; -; 1.
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; IPR030703; Histone_deacetylase_5.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR45364; PTHR45364; 1.
DR PANTHER; PTHR45364:SF2; PTHR45364:SF2; 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; SSF52768; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Chromatin regulator; Cytoplasm; Hydrolase; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc.
FT CHAIN 1..1111
FT /note="Histone deacetylase 5"
FT /id="PRO_0000357050"
FT REGION 40..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..495
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 645..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..1017
FT /note="Histone deacetylase"
FT REGION 1086..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1070..1109
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 240..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..606
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 822
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 693
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 770
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 250
FT /note="Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT MOD_RES 283
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT MOD_RES 489
FT /note="Phosphoserine; by AMPK, CaMK1, SIK1 and PKD/PRKD1"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT MOD_RES 524
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT MOD_RES 650
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UQL6"
SQ SEQUENCE 1111 AA; 120988 MW; 52559AE959E190E6 CRC64;
MNSPNESDGM PGREPSLEIL PRTPLHSIPV AVEVKPVLPG AMPSSMGGGG GGSPSPVELR
GALAGPMDPA LREQQLQQEL LVLKQQQQLQ KQLLFAEFQK QHDHLTRQHE VQLQKHLKQQ
QEMLAAKRQQ ELEQQRQREQ QRQEELEKQR LEQQLLILRN KEKSKESAIA STEVKLRLQE
FLLSKSKEPT PGSLNHSLPQ HPKCWGAHHA SLDQSSPPQS GPPGTPPSYK LPLLGPYDSR
DDFPLRKTAS EPNLKVRSRL KQKVAERRSS PLLRRKDGTV ISTFKKRAVE ITGTGPGVSS
VCNSAPGSGP SSPNSSHSAI AENGFTGSVP NIPTEMLPQH RALPLDSSPN QFSLYTSPSL
PNISLGLQAT VTVTNSHLTA SPKLSTQQEA ERQALQSLRQ GGTLTGKFMS TSSIPGCLLG
VTLEGDTSPH GHASLLQHVL LLEQARQQST LIAVPLHGQS PLVTGERVAT SMRTVGKLPR
HRPLSRTQSS PLPQSPQALQ QLVMQQQHQQ FLEKQKQQQM QLGKILTKTG ELPRQPTTHP
EETEEELTEQ QEALLGEGAL TMPREGSTES ESTQEDLEEE EDEEEEDEDC IQVKDEEGES
GPDEGPDLEE SSAGYKKLFT DAQQLQPLQV YQAPLSLATV PHQALGRTQS SPAAPGSMKS
PPDQPTKHLF TTGVVYDTFM LKHQCMCGNT HVHPEHAGRI QSIWSRLQET GLLSKCERIR
GRKATLDEIQ TVHSEYHTLL YGTSPLNRQK LDSKKLLGPI SQKMYAMLPC GGIGVDSDTV
WNEMHSSSAV RMAVGCLVEL AFKVAAGELK NGFAIIRPPG HHAEESTAMG FCFFNSVAIT
AKLLQQKLNV GKVLIVDWDI HHGNGTQQAF YDDPSVLYIS LHRYDNGNFF PGSGAPEEVG
GGPGMGYNVN VAWTGGVDPP IGDVEYLTAF RTVVMPIAHE FSPDVVLVSA GFDAVEGHLS
PLGGYSVTAR CFGHLTRQLM TLAGGRVVLA LEGGHDLTAI CDASEACVSA LLSVELQPLD
EAVLQQKPSI NAVATLEKVI EIQSKHWSCV QRFATGLGCS LQEAQAGETE EAETVSAMAL
LSVGAEQAQA VATQEHSPRP AEEPMEQEPT L
