ID H2Q5S6_PANTR Unreviewed; 974 AA.
AC H2Q5S6; A0A2J8LQI7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 66.
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=HDAC7 {ECO:0000313|Ensembl:ENSPTRP00000008320.6,
GN ECO:0000313|VGNC:VGNC:5414};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000008320.6, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000008320.6, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000008320.6}
RP IDENTIFICATION.
RG Ensembl;
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)-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 EMBL; AACZ04012877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016779041.1; XM_016923552.1.
DR AlphaFoldDB; H2Q5S6; -.
DR Ensembl; ENSPTRT00000009008.6; ENSPTRP00000008320.6; ENSPTRG00000004868.6.
DR GeneID; 466968; -.
DR CTD; 51564; -.
DR VGNC; VGNC:5414; HDAC7.
DR eggNOG; KOG1343; Eukaryota.
DR GeneTree; ENSGT00940000159065; -.
DR HOGENOM; CLU_006530_2_0_1; -.
DR OrthoDB; 124800at2759; -.
DR TreeFam; TF106174; -.
DR Proteomes; UP000002277; Chromosome 12.
DR Bgee; ENSPTRG00000004868; Expressed in thymus and 21 other cell types or tissues.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProt.
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 CDD; cd10008; HDAC7; 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; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF44; HISTONE DEACETYLASE 7; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037911; HDAC_II_euk; 2.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE 3: Inferred from homology;
KW Chromatin regulator {ECO:0000256|PIRNR:PIRNR037911};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
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 563..881
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..398
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 692
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 640
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 865
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 974 AA; 105057 MW; AC02D2BB1FA19EBA CRC64;
MHSPGAGCPR PCADTPGPQP QPMDLRVGQR PPVEPPPEPT LLALQRPQRL HHHLFLAGLQ
QQRSVDPMRL SMDTPMPELQ VGPQEQELRQ LLHKDKSKRS AVASSVVKQK LAEVILKKQQ
AALERTVHPN SPGIPYRTLE PLETEGATRS MLSSFLPPVP SLPSDPPEHF PLRKTVSEPN
LKLRYKPKKS LERRKNPLLR KESAPPSLRR RPAETLGDSS PSSSSTPASG CSSPNDSEHG
PNPILGSEAL LGQRLRLQET SVAPFALPTV SLLPAITLGL PAPARADGDR RTHPTLGPRG
PILGSPHTPL FLPHGLEPEA GGTLPSRLQP ILLLDPSGSH APLLTVPGLG PLPFHFAQSL
MTTERLSGSG LHWPLSRTRS EPLPPSATAP PPPGPMQPRL EQLKTHVQVI KRSAKPSEKP
RLRQIPSAED LETDGGGPGQ VVDDGLEHRE LGHGQPEARG PASLQQHPQV LLWEQQRLAG
RLPRGSTGDT VLLPLAQGGH RPLSRAQSSP AAPASLSAPE PASQARVLSS SETPARTLPF
TTGLIYDSVM LKHQCSCGDN SRHPEHAGRI QSIWSRLQER GLRSQCECLR GRKASLEELQ
SVHSERHVLL YGTNPLSRLK LDNGKLAGLL AQRMFVMLPC GGVGVDTDTI WNELHSSNAA
RWAAGSVTDL AFKVASRELK NGFAVVRPPG HHADHSTAMG FCFFNSVAIA CRQLQQQSKA
SKILIVDWDV HHGNGTQQTF YQDPSVLYIS LHRHDDGNFF PGSGAVDEVG AGSGEGFNVN
VAWAGGLDPP MGDPEYLAAF RIVVMPIARE FSPDLVLVSA GFDAAEGHPA PLGGYHVSAK
CFGYMTQQLM NLAGGAVVLA LEGGHDLTAI CDASEACVAA LLGNRVDPLS EEGWKQKPNL
NAIRSLEAVI RVHSKYWGCM QRLASCPDSW VPRVPGADKE EVEAVTALAS LSVGILAEDR
PSEQLVEEEE PMNL
//
