HDA1_CANAL
ID HDA1_CANAL Reviewed; 833 AA.
AC Q5A960; A0A1D8PS43;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Histone deacetylase HDA1;
DE EC=3.5.1.98;
GN Name=HDA1; OrderedLocusNames=CAALFM_CR02050CA;
GN ORFNames=CaO19.10137, CaO19.2606;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=11404352; DOI=10.1093/genetics/158.2.919;
RA Klar A.J., Srikantha T., Soll D.R.;
RT "A histone deacetylation inhibitor and mutant promote colony-type switching
RT of the human pathogen Candida albicans.";
RL Genetics 158:919-924(2001).
RN [5]
RP FUNCTION.
RX PubMed=11443097; DOI=10.1128/jb.183.15.4614-4625.2001;
RA Srikantha T., Tsai L., Daniels K., Klar A.J., Soll D.R.;
RT "The histone deacetylase genes HDA1 and RPD3 play distinct roles in
RT regulation of high-frequency phenotypic switching in Candida albicans.";
RL J. Bacteriol. 183:4614-4625(2001).
RN [6]
RP FUNCTION.
RX PubMed=12798685; DOI=10.1016/s0022-2836(03)00505-9;
RA Tebarth B., Doedt T., Krishnamurthy S., Weide M., Monterola F.,
RA Dominguez A., Ernst J.F.;
RT "Adaptation of the Efg1p morphogenetic pathway in Candida albicans by
RT negative autoregulation and PKA-dependent repression of the EFG1 gene.";
RL J. Mol. Biol. 329:949-962(2003).
RN [7]
RP FUNCTION.
RX PubMed=20730094; DOI=10.1371/journal.pone.0012171;
RA Zacchi L.F., Schulz W.L., Davis D.A.;
RT "HOS2 and HDA1 encode histone deacetylases with opposing roles in Candida
RT albicans morphogenesis.";
RL PLoS ONE 5:E12171-E12171(2010).
RN [8]
RP FUNCTION.
RX PubMed=21811397; DOI=10.1371/journal.pbio.1001105;
RA Lu Y., Su C., Wang A., Liu H.;
RT "Hyphal development in Candida albicans requires two temporally linked
RT changes in promoter chromatin for initiation and maintenance.";
RL PLoS Biol. 9:E1001105-E1001105(2011).
RN [9]
RP FUNCTION.
RX PubMed=23041319; DOI=10.1016/j.celrep.2012.08.035;
RA Robbins N., Leach M.D., Cowen L.E.;
RT "Lysine deacetylases Hda1 and Rpd3 regulate Hsp90 function thereby
RT governing fungal drug resistance.";
RL Cell Rep. 2:878-888(2012).
RN [10]
RP FUNCTION, INTERACTION WITH BRG1, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=22536157; DOI=10.1371/journal.ppat.1002663;
RA Lu Y., Su C., Liu H.;
RT "A GATA transcription factor recruits Hda1 in response to reduced Tor1
RT signaling to establish a hyphal chromatin state in Candida albicans.";
RL PLoS Pathog. 8:E1002663-E1002663(2012).
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. Histone deacetylases act via the formation of
CC large multiprotein complexes. Deacetylates the YNG2 subunit of NuA4
CC histone acetyltransferase (HAT) module, leading to the reduction of
CC YNG2 and NuA4 HAT at the promoters of hypha-specific genes. Plays a key
CC role in the regulation of filamentous growth and virulence. Involved in
CC the switch between two heritable states, the white and opaque states.
CC These two cell types differ in many characteristics, including cell
CC structure, mating competence, and virulence. Each state is heritable
CC for many generations, and switching between states occurs
CC stochastically at low frequency. {ECO:0000269|PubMed:11404352,
CC ECO:0000269|PubMed:11443097, ECO:0000269|PubMed:12798685,
CC ECO:0000269|PubMed:20730094, ECO:0000269|PubMed:21811397,
CC ECO:0000269|PubMed:22536157, ECO:0000269|PubMed:23041319}.
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 -!- SUBUNIT: Interacts with BRG1. {ECO:0000269|PubMed:22536157}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22536157}.
CC Note=Recruited to promoters of hypha-specific genes by BRG1 in a
CC rapamycin-dependent manner.
CC -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC subfamily. {ECO:0000305}.
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DR EMBL; CP017630; AOW30956.1; -; Genomic_DNA.
DR RefSeq; XP_718271.1; XM_713178.1.
DR AlphaFoldDB; Q5A960; -.
DR SMR; Q5A960; -.
DR STRING; 237561.Q5A960; -.
DR ESTHER; canal-hda1; Arb2_domain.
DR PRIDE; Q5A960; -.
DR GeneID; 3640154; -.
DR KEGG; cal:CAALFM_CR02050CA; -.
DR CGD; CAL0000201463; HDA1.
DR VEuPathDB; FungiDB:CR_02050C_A; -.
DR eggNOG; KOG1343; Eukaryota.
DR HOGENOM; CLU_007727_4_0_1; -.
DR InParanoid; Q5A960; -.
DR OrthoDB; 1484694at2759; -.
DR PRO; PR:Q5A960; -.
DR Proteomes; UP000000559; Chromosome R.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IEA:EnsemblFungi.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070823; C:HDA1 complex; IEA:EnsemblFungi.
DR GO; GO:1990342; C:heterochromatin island; IEA:EnsemblFungi.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0031934; C:mating-type region heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0005730; C:nucleolus; IEA:EnsemblFungi.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0033553; C:rDNA heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0070824; C:SHREC complex; IEA:EnsemblFungi.
DR GO; GO:0110129; C:SHREC2 complex; IEA:EnsemblFungi.
DR GO; GO:0003682; F:chromatin binding; IEA:EnsemblFungi.
DR GO; GO:0004407; F:histone deacetylase activity; IBA:GO_Central.
DR GO; GO:0031078; F:histone deacetylase activity (H3-K14 specific); IEA:EnsemblFungi.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0071469; P:cellular response to alkaline pH; IMP:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036177; P:filamentous growth of a population of unicellular organisms in response to pH; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:EnsemblFungi.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010621; P:negative regulation of transcription by transcription factor localization; IEA:EnsemblFungi.
DR GO; GO:0036166; P:phenotypic switching; IMP:CGD.
DR GO; GO:1900445; P:positive regulation of filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:1900743; P:positive regulation of filamentous growth of a population of unicellular organisms in response to pH; IMP:CGD.
DR GO; GO:1900436; P:positive regulation of filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0090053; P:positive regulation of pericentric heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:EnsemblFungi.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IEA:EnsemblFungi.
DR GO; GO:1900239; P:regulation of phenotypic switching; IMP:CGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CGD.
DR GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IEA:EnsemblFungi.
DR Gene3D; 3.40.800.20; -; 1.
DR InterPro; IPR019154; Arb2_domain.
DR InterPro; IPR000286; His_deacetylse.
DR InterPro; IPR023801; His_deacetylse_dom.
DR InterPro; IPR037138; His_deacetylse_dom_sf.
DR InterPro; IPR017321; Hist_deAcase_II_yeast.
DR InterPro; IPR023696; Ureohydrolase_dom_sf.
DR Pfam; PF09757; Arb2; 2.
DR Pfam; PF00850; Hist_deacetyl; 1.
DR PIRSF; PIRSF037919; HDAC_II_yeast; 1.
DR PRINTS; PR01270; HDASUPER.
DR SUPFAM; SSF52768; SSF52768; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; Hydrolase; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Virulence.
FT CHAIN 1..833
FT /note="Histone deacetylase HDA1"
FT /id="PRO_0000422800"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 5..52
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 760..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 833 AA; 92913 MW; AB2ACF03720A926F CRC64;
MSTGQEEHLD SKLENQISEE ENQSQNQNFP TAIEDSIQAS IEKLDEVDDE INPIEVKDEF
PTTIGTTYDI LHPREPFPKR IKLEETETEP DSNGIADNDQ TMVVVPPKKP QLFYTPLKTG
LVYDVRMRYH AKVFTSYSEY IDPHPEDPRR IYRIYKKLVE AGIVLDPSLA GINEIGPFML
KIPIREATSE EILQVHSEDH LKFIQSTEDM SRDQLLKETE TGDSIYVNND SYLSAKLSCG
GTIEACKAVI EGRVKNSLAI VRPPGHHAEP NTPAGFCLFS NVAVAAKNML KNYPESVRRI
VIVDWDIHHG NGTQKAFYND PRVLYISLHR FENGKFYPGT KYGDLNQVGE GPGEGFTINI
PWRSSGMHDG DYVYAFNKII QPVISEFDPD LIIVSSGFDA ADGDVIGACH VTPAGYGYMT
HTLKGIARGK LAVILEGGYN LDSISKSALA VAKVLVGEPP ENTITLRPQA EAIEVVDEVI
KIQSKYFKSL RNGIPNGIFE DVYDLADVEK SNYKLVNIAD PIRSHQVEKL FNEKEFINIP
IISSPSNGEK PPFTTDLPDQ LEDLIVASPD IYNCTTIILT IHDPPEIWAN INPTNGVIET
NSTMVLEHPL VQIMDKIQKE KDPENQEKFG YLDINIPSFQ LPIPGTTSES STYNPIIFAQ
EVLLYIWDNY IAYFQQLKNL VMVGFGDSYQ SIVNLYGKRP SNEIKDLIKG TVAFLNRTTL
KPLIPVMDES MVDWYYQNSI IFTSNFNTCW TGGSGAGNGN GNGNGNNGNS SNGGGNKSAD
SNGHDDFSKR PRKKFGRVIK AKTDGLCDVI QEKFDEGVDF ILDSIEDYSS SED
