ID K7DID2_PANTR Unreviewed; 991 AA.
AC K7DID2; A0A2J8LQJ3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 59.
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|EMBL:JAA41494.1,
GN ECO:0000313|Ensembl:ENSPTRP00000080898.1, 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|EMBL:JAA41494.1};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000080898.1, 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|EMBL:JAA41494.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Skeletal muscle {ECO:0000313|EMBL:JAA41494.1}, Skin
RC {ECO:0000313|EMBL:JAA29183.1}, and Smooth vascular
RC {ECO:0000313|EMBL:JAA16832.1};
RA Maudhoo M.D., Meehan D.T., Norgren R.B.Jr.;
RT "De novo assembly of the reference chimpanzee transcriptome from NextGen
RT mRNA sequences.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPTRP00000080898.1}
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 EMBL; GABF01005313; JAA16832.1; -; mRNA.
DR EMBL; GABD01003917; JAA29183.1; -; mRNA.
DR EMBL; GABE01003245; JAA41494.1; -; mRNA.
DR RefSeq; XP_016779040.1; XM_016923551.1.
DR PaxDb; 9598-ENSPTRP00000008320; -.
DR Ensembl; ENSPTRT00000108000.1; ENSPTRP00000080898.1; ENSPTRG00000004868.6.
DR GeneID; 466968; -.
DR KEGG; ptr:466968; -.
DR CTD; 51564; -.
DR VGNC; VGNC:5414; HDAC7.
DR GeneTree; ENSGT00940000159065; -.
DR OMA; WPLSWTR; -.
DR OrthoDB; 124800at2759; -.
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 2: Evidence at transcript level;
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 580..898
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 709
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 580
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 SITE 882
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 991 AA; 106686 MW; 1E7B2FA5B72094C5 CRC64;
MHSPGADGTQ VSPGAHYCSP TGAGCPRPCA DTPGPQPQPM DLRVGQRPPV EPPPEPTLLA
LQRPQRLHHH LFLAGLQQQR SVDPMRLSMD TPMPELQVGP QEQELRQLLH KDKSKRSAVA
SSVVKQKLAE VILKKQQAAL ERTVHPNSPG IPYRTLEPLE TEGATRSMLS SFLPPVPSLP
SDPPEHFPLR KTVSEPNLKL RYKPKKSLER RKNPLLRKES APPSLRRRPA ETLGDSSPSS
SSTPASGCSS PNDSEHGPNP ILGSEALLGQ RLRLQETSVA PFALPTVSLL PAITLGLPAP
ARADGDRRTH PTLGPRGPIL GSPHTPLFLP HGLEPEAGGT LPSRLQPILL LDPSGSHAPL
LTVPGLGPLP FHFAQSLMTT ERLSGSGLHW PLSRTRSEPL PPSATAPPPP GPMQPRLEQL
KTHVQVIKRS AKPSEKPRLR QIPSAEDLET DGGGPGQVVD DGLEHRELGH GQPEARGPAS
LQQHPQVLLW EQQRLAGRLP RGSTGDTVLL PLAQGGHRPL SRAQSSPAAP ASLSAPEPAS
QARVLSSSET PARTLPFTTG LIYDSVMLKH QCSCGDNSRH PEHAGRIQSI WSRLQERGLR
SQCECLRGRK ASLEELQSVH SERHVLLYGT NPLSRLKLDN GKLAGLLAQR MFVMLPCGGV
GVDTDTIWNE LHSSNAARWA AGSVTDLAFK VASRELKNGF AVVRPPGHHA DHSTAMGFCF
FNSVAIACRQ LQQQSKASKI LIVDWDVHHG NGTQQTFYQD PSVLYISLHR HDDGNFFPGS
GAVDEVGAGS GEGFNVNVAW AGGLDPPMGD PEYLAAFRIV VMPIAREFSP DLVLVSAGFD
AAEGHPAPLG GYHVSAKCFG YMTQQLMNLA GGAVVLALEG GHDLTAICDA SEACVAALLG
NRVDPLSEEG WKQKPNLNAI RSLEAVIRVH SKYWGCMQRL ASCPDSWVPR VPGADKEEVE
AVTALASLSV GILAEDRPSE QLVEEEEPMN L
//
