ID A0A7M4FTE3_CROPO Unreviewed; 871 AA.
AC A0A7M4FTE3;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 22.
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:ENSCPRP00005006134.1};
OS Crocodylus porosus (Saltwater crocodile) (Estuarine crocodile).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Longirostres; Crocodylidae;
OC Crocodylus.
OX NCBI_TaxID=8502 {ECO:0000313|Ensembl:ENSCPRP00005006134.1, ECO:0000313|Proteomes:UP000594220};
RN [1] {ECO:0000313|Ensembl:ENSCPRP00005006134.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [2] {ECO:0000313|Ensembl:ENSCPRP00005006134.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) 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=N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] +
CC acetate; 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; A0A7M4FTE3; -.
DR Ensembl; ENSCPRT00005007196.1; ENSCPRP00005006134.1; ENSCPRG00005004147.1.
DR GeneTree; ENSGT00940000159065; -.
DR Proteomes; UP000594220; Unplaced.
DR GO; GO:0000118; C:histone deacetylase complex; IEA:TreeGrafter.
DR GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:TreeGrafter.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd10008; HDAC7; 1.
DR FunFam; 3.40.800.20:FF:000002; Histone deacetylase; 1.
DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR InterPro; IPR046949; HDAC4/5/7/9.
DR InterPro; IPR000286; HDACs.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR PANTHER; PTHR10625:SF42; HISTONE DEACETYLASE 7; 1.
DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 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|ARBA:ARBA00022853,
KW ECO:0000256|PIRNR:PIRNR037911};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037911-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000594220};
KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|PIRNR:PIRNR037911};
KW Transcription {ECO:0000256|ARBA:ARBA00023163,
KW ECO:0000256|PIRNR:PIRNR037911};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015,
KW ECO:0000256|PIRNR:PIRNR037911};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037911-2}.
FT DOMAIN 474..792
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 104..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..198
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 603
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 474
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 551
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT SITE 776
FT /note="Contributes to catalysis"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-3"
SQ SEQUENCE 871 AA; 94898 MW; 78D001DDF3D34390 CRC64;
MDLRIGQRFV KPGSDTALLA LKQTQQLQHQ FFLASLHQQQ CYSQAAGPAL LSSDWSPHHE
AEVGQQEQEL RQLLNKDKSK RSAVASTVVK QKLAEVILKK QQAALERTSN PNPSAMPYST
IDTPEHFPLR KTASEPNLKV RYKPKKSLDR RKNPLTRKES APPSLKRRPP EAIGEGLPWL
QPTALLPPSP KPLTPPLSPQ GEADRHMLSS LTHGRVPVLN GPVLAGTHPP MFIPASLEQH
EPGGTLSPRV IILEPSVTHT PLVAVPGLGP VPFSFAPSLI SAERLPLSGH HKPLGRTRSE
PLPQNPKAIQ QQLAYQQHHA QFLERLKQQT ALGKPLSALA CPLQRMTKSS EKPRLRQIPS
SEDMEAEVGY PEGGGGRSDQ ARGRLESARP GASVKEPERT QKPMQPQEEL VLQQVPWVKL
CPAPRPECLA EIWGTGGQGE PPGPCRLTPL SAAGLVYDSV MLKHQCSCGD NSNHPEHAGR
IQSIWSRLQE RGLRSQCECL RGRKATLEEL QSVHNERHVF LYGTNPLNRL KLDNGKLAGI
LSQRMFVMLP CGGVGVDSDT IWNELHSSNA ARWAAGSVTE LAFKVAMREL KNGFAVVRPP
GHHADPSTAM GFCFFNSVAI AARQLQQKGK LSKILIVDWD VHHGNGTQQV FYRDPDILYI
SIHRHDDGNF FPGSGAADEV GSGLGEGFNV NVAWTGGLDP PMGDPEYLAA FRTVVIPIAH
EFSPDVVLVS AGFDAADGHP PPLGGYKVSA KCFGYMTKQL MSLAGGAVVL ALEGGHDLTA
ICDASEACVS ALLGNEPDPL PEESLRQKPN PNAVRSLETV IQVQSKYWST VQRFASKVGC
SFLEAQHHEA EEVETVTALA SLSVAVMAEK R
//
