ID HDA22_DICDI Reviewed; 1704 AA. AC Q54VQ7; DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot. DT 24-MAY-2005, sequence version 1. DT 27-MAR-2024, entry version 106. DE RecName: Full=Type-2 histone deacetylase 2; DE Short=DdHdaC; DE EC=3.5.1.98; GN Name=hdaC; ORFNames=DDB_G0280195; OS Dictyostelium discoideum (Social amoeba). OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales; OC Dictyosteliaceae; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AX4; RX PubMed=15875012; DOI=10.1038/nature03481; RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G., RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.; RT "The genome of the social amoeba Dictyostelium discoideum."; RL Nature 435:43-57(2005). RN [2] RP DEVELOPMENTAL STAGE. RX PubMed=19576222; DOI=10.1016/j.jmb.2009.06.067; RA Sawarkar R., Visweswariah S.S., Nellen W., Nanjundiah V.; RT "Histone deacetylases regulate multicellular development in the social RT amoeba Dictyostelium discoideum."; RL J. Mol. Biol. 391:833-848(2009). 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 plays an important role in transcriptional regulation, CC cell cycle progression and developmental events. Histone deacetylases CC act via the formation of large multiprotein complexes (By similarity). CC {ECO:0000250}. 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. CC -!- DEVELOPMENTAL STAGE: Expressed after cells enter the multicellular CC phase upon starvation. {ECO:0000269|PubMed:19576222}. CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAFI02000035; EAL67324.1; -; Genomic_DNA. DR RefSeq; XP_641298.1; XM_636206.1. DR AlphaFoldDB; Q54VQ7; -. DR SMR; Q54VQ7; -. DR STRING; 44689.Q54VQ7; -. DR PaxDb; 44689-DDB0237658; -. DR EnsemblProtists; EAL67324; EAL67324; DDB_G0280195. DR GeneID; 8622431; -. DR KEGG; ddi:DDB_G0280195; -. DR dictyBase; DDB_G0280195; hdaC. DR eggNOG; KOG1343; Eukaryota. DR HOGENOM; CLU_240787_0_0_1; -. DR InParanoid; Q54VQ7; -. DR OMA; NSEFETH; -. DR Reactome; R-DDI-3371511; HSF1 activation. DR Reactome; R-DDI-5617833; Cilium Assembly. DR PRO; PR:Q54VQ7; -. DR Proteomes; UP000002195; Chromosome 3. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central. DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd11599; HDAC_classII_2; 1. DR Gene3D; 3.40.800.20; Histone deacetylase domain; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. 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 InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1. DR PANTHER; PTHR10625:SF26; TYPE-2 HISTONE DEACETYLASE 2; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PRINTS; PR01270; HDASUPER. DR SUPFAM; SSF52768; Arginase/deacetylase; 1. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. PE 2: Evidence at transcript level; KW Chromatin regulator; Cytoplasm; Hydrolase; Metal-binding; Nucleus; KW Reference proteome; Repressor; Transcription; Transcription regulation. FT CHAIN 1..1704 FT /note="Type-2 histone deacetylase 2" FT /id="PRO_0000331372" FT REGION 1..303 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 315..383 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 540..634 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1485..1704 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..78 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 79..114 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 117..153 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 161..182 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 183..199 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 216..293 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 315..355 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 540..598 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 599..622 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1485..1643 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1650..1704 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 1165 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 1227 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 1256 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250" FT BINDING 1258 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250" FT BINDING 1350 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000250" SQ SEQUENCE 1704 AA; 190816 MW; 84E83B42FB36896E CRC64; MSTNNIIEGD EDTKTTITNE SNTDNNNNNN DDNKNNTENT TSPTNNNNTN DNDNNSDNNN NKNNNNNNSQ VTEEQQVTLE DSGSEDDINF EEHELSDSAE EDEDEMEDDD EDADGRQNQN PNSAGGKRRG RPSKVQQSTN THLSQTTPES PTIFTPDGKV PKRISTSTNN TPNTQSALKT NKRPRLTSDE EKDLMLSEES DGGVGEDDDS IMSTNDKPQD ENQSNQNQNN NNNNNNNTTT TTTTTNNSNN NNQNLNQNNN NNNNNNNINN NNNNNNSNND NNNNNNRPAR GRPKTNGSRS EERKRIQLQQ YIQATQGSST TTSDPNNQNN QINQINQNNQ NNQNNQNNQN NSLGEEEFGE EFEEEEEDMG QPKKKTKYKT SKKSVPNHLD IRPCWFVGCV KADRSLKILR PCLIPTCKTH AIKSEVRISE ALRRGDFVND ESSGVKDKVC GICGDKKDLH HCGNNGCAFG FCNDCVEIAA MKHNNHPNGN KWICWVCQFV RTKAKEKERT RWVKEQLNPG LTSISRKFRR GPELDMAQAQ FLQQQQQQQT SPNEKRSSQF NSNNSNNNNN NNSNNNNNNS GFDPSGSPNN QQNQKRLRKK INASSDIYET RKYTKKRNDE DSAPPSPTSI IGNSVMVGSS GAAGGGIIKN TTVVVEQQGY SATPPSPNTL MVQQQQQLQQ THQQARLSQQ QAQLQQLKAL QQQHQHQQQN NGNFNNLIES VLSPNREPLN PIDNFVDQTF TAVKFFSTLS QNPPDEIKER IDNFVDLMMR IKTVRWASDY GLVWRMIEEL SNLIKRNLLS SQSVVEMYSE LKSLEEGALE NMTTNARNVP LERAITMVFE NHETAGLIGK ECCSTRNALI YSIEVALRAI ADYQHDLEDN LMEESLRSNK VSTEIEQIEH QIKANLDEIH KFKYQEVELL DSLSKVRGAI AAHESIRDTL QKKSSELKVD MLLIKNGISD KEKETKSQQA TLENEIYALK LLITMVESIY WIHDYFYESR VGECEKLINN KLSQLQNKLE TQIPHPPNAL DNAIPNTTTT VMGEDGQPVI VPTTVDIKNK FKTIAIYHKI CMQHKVPNFH LEKPDRIQVA VSCINEFASN PLVDIFDNPP EVDMRYVMAV HDANYIKKLE TSLPPENSEF ETHLESDKSG AMVTVASHKD FEGDDDNIYD TFVSHRSIKA ALRASGSVCA AVDSVSRSGY TRAFCAIRPP GHHAGRYGRT SDAPSQGYCL INNVAIGAKY ASLTAGYSRI AVVDFDVHHG NGTQEILSGD DNFLFISIHV CDEKRYFYPG TGQDVGDIDE VSGQFDGNIL NIGLKRNTGS AVFLQQWMNK IIPRLEAYKP QLIFLSAGFD GHKDDPTNGL KLNEEDYFVI TKMIKTVAFK YCKGRIISVL EGGYGIEKTN SLQRCVNSHL KALIEDTDEE IHLANISYGH FSETQETAIP KFNINNFISN PNKRGKKNNL NTINFINNNM NNINNNITNS LSNKQLERQK QLQQQQQQAQ QAQQQQSPQQ SQTIENTSIT TTTTTTSTTT TLSTSDSESN NNINNNNNDY NNNNNNNSNN NNNNSNNNQP TNFNSSTSSP ILSGNNNNNN NNNNNNNNNN INNNNNNNSN NNNNMNTSNP TNQQSSVIIS DDMDDVQTNS NPPNPQYPLS PNSVNRGNNP SNISMSGAQR SAPLIISPKP SNSPNSPSTS NNNGTPQNIN NSDN //