ID F6R4S6_CIOIN Unreviewed; 992 AA.
AC F6R4S6;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Histone deacetylase {ECO:0000256|PIRNR:PIRNR037911};
DE EC=3.5.1.98 {ECO:0000256|PIRNR:PIRNR037911};
OS Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis).
OC Eukaryota; Metazoa; Chordata; Tunicata; Ascidiacea; Phlebobranchia;
OC Cionidae; Ciona.
OX NCBI_TaxID=7719 {ECO:0000313|Ensembl:ENSCINP00000016829.3, ECO:0000313|Proteomes:UP000008144};
RN [1] {ECO:0000313|Proteomes:UP000008144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12481130; DOI=10.1126/science.1080049;
RA Dehal P., Satou Y., Campbell R.K., Chapman J., Degnan B., De Tomaso A.,
RA Davidson B., Di Gregorio A., Gelpke M., Goodstein D.M., Harafuji N.,
RA Hastings K.E., Ho I., Hotta K., Huang W., Kawashima T., Lemaire P.,
RA Martinez D., Meinertzhagen I.A., Necula S., Nonaka M., Putnam N., Rash S.,
RA Saiga H., Satake M., Terry A., Yamada L., Wang H.G., Awazu S., Azumi K.,
RA Boore J., Branno M., Chin-Bow S., DeSantis R., Doyle S., Francino P.,
RA Keys D.N., Haga S., Hayashi H., Hino K., Imai K.S., Inaba K., Kano S.,
RA Kobayashi K., Kobayashi M., Lee B.I., Makabe K.W., Manohar C., Matassi G.,
RA Medina M., Mochizuki Y., Mount S., Morishita T., Miura S., Nakayama A.,
RA Nishizaka S., Nomoto H., Ohta F., Oishi K., Rigoutsos I., Sano M.,
RA Sasaki A., Sasakura Y., Shoguchi E., Shin-i T., Spagnuolo A., Stainier D.,
RA Suzuki M.M., Tassy O., Takatori N., Tokuoka M., Yagi K., Yoshizaki F.,
RA Wada S., Zhang C., Hyatt P.D., Larimer F., Detter C., Doggett N.,
RA Glavina T., Hawkins T., Richardson P., Lucas S., Kohara Y., Levine M.,
RA Satoh N., Rokhsar D.S.;
RT "The draft genome of Ciona intestinalis: insights into chordate and
RT vertebrate origins.";
RL Science 298:2157-2167(2002).
RN [2] {ECO:0000313|Ensembl:ENSCINP00000016829.3}
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|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; EAAA01000513; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; F6R4S6; -.
DR Ensembl; ENSCINT00000016829.3; ENSCINP00000016829.3; ENSCING00000008243.3.
DR GeneTree; ENSGT00940000169192; -.
DR HOGENOM; CLU_006530_0_1_1; -.
DR Proteomes; UP000008144; Chromosome 10.
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 CDD; cd11681; HDAC_classIIa; 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:SF15; HISTONE DEACETYLASE; 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|PIRNR:PIRNR037911};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR037911};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037911-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000008144};
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 621..955
FT /note="Histone deacetylase"
FT /evidence="ECO:0000259|Pfam:PF00850"
FT REGION 229..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..582
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 764
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-1"
FT BINDING 615
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 617
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 621
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
FT BINDING 708
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037911-2"
SQ SEQUENCE 992 AA; 111169 MW; CCAEBFB1492EB62B CRC64;
MGERQYQEKL KRMRHQHEIE NQLLMAQFNY QTSNLQHQHQ LQQHLNITNE IRISVCSKHV
ISKQRERVAE QMAALDQRSE LINSVRNKEK NREKTGAVAS NAVKQHLQKF VKCRQKFKDS
HPSMERLLHI SPGGNYLACF TYVVTHRSPL QWTPSLEGKN GGHEVPAHYS SLLHTQYDFP
LRKTASEPNL KLKSRLKQKL LEDRVERSSP LMPRRGDIKA DLANRIKKKI NIENVNEQRN
SHNSAPNSGP SSPPNSSNDI KQSTPHMQTE FYNQQTDYYE ESNSSGNHDL YSSPSLPNIS
IGLTNKKSTD RSMLVVSEEL SKRGTRGSSL SDPMIQSDKP LFQSHDRTVA AIINKTFLVY
VFMHQHFTAK LHEIDLTQAV QANLLPPHKT VLHGTYHLCT QASTPPGPIR HSQTTRQHKA
LSRTQSAPTA ASQLQLHILQ LKRRQKMLQQ QQKKGLMHGV AEVDSHSYSI LPTHLETEDG
EQWVKRNQYS HAQSTPNQPF IPSNKIASTQ AQLVASKPEI PDSMLPMFIN KHSGSSFYNK
PTQEEGGIAG TRHLPPQSTI PIHSQPSSLS DQNKPRLLRT QSSPATSFIK KLPHFKKYRY
TTGIAYSPVM LKHGCACRDD HTEHAGRLRA IWERLTKSKL VNDPSCGGTS GKSSCELLEA
RKATTDELQL VHTQEHTLRY GTTSLARKEL GEKLLCQELT SKFIVLPCGG VGVDNGIDID
TVWNELDTIN AARMAVGCTV DITLEVAQNR LKNGFALVRP PGHHAQKDLA MAFCYFNSVA
VAARKLQHEC PDTVRRVLIV DWDVHHCNGT QNIFFDDPSV LVISIHRYDS GNFFPGTGAI
NECGRGGGLG YNVNIGFSGG LDPPMEDADY LAVFRTIVLP IARQFDPHFV LVSCGFSAAN
GHPSTLGGYK LTPNCYGLLT RLLSEVAGGK IVLVLEGGFE LEPLCDCTEA CVRTLLGNHE
YSNLSMESME RRPSKNAIDT IKNVITIQEK HW
//
