ID   HDA1A_XENLA             Reviewed;         480 AA.
AC   Q91695; Q66IY9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 60.
DE   RecName: Full=Probable histone deacetylase 1-A;
DE            Short=HD1;
DE            EC=3.5.1.98;
DE   AltName: Full=Maternally-expressed histone deacetylase;
DE   AltName: Full=HDM;
DE   AltName: Full=AB21;
GN   Name=hdac1-A;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae;
OC   Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Oocyte;
RX   MEDLINE=98036059; PubMed=9370292; DOI=10.1016/S0378-1119(97)00325-9;
RA   Ladomery M.R., Lyons S., Sommerville J.;
RT   "Xenopus HDm, a maternally expressed histone deacetylase, belongs to
RT   an ancient family of acetyl-metabolizing enzymes.";
RL   Gene 198:275-280(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Oocyte;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH RBBP4.
RX   MEDLINE=99310815; PubMed=10381399;
RA   Ryan J., Llinas A.J., White D.A., Turner B.M., Sommerville J.;
RT   "Maternal histone deacetylase is accumulated in the nuclei of Xenopus
RT   oocytes as protein complexes with potential enzyme activity.";
RL   J. Cell Sci. 112:2441-2452(1999).
CC   -!- FUNCTION: Histone deacetylase that is only required during early
CC       steps of development. Responsible for the deacetylation of lysine
CC       residues on the N-terminal part of the core histones (H2A, H2B, H3
CC       and H4). Histone deacetylation gives a tag for epigenetic
CC       repression and plays an important role in transcriptional
CC       regulation, cell cycle progression and developmental events.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of an N(6)-acetyl-lysine residue of
CC       a histone to yield a deacetylated histone.
CC   -!- SUBUNIT: Part of a large multiprotein complex that also contains
CC       RBBP4.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- TISSUE SPECIFICITY: Oocyte.
CC   -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC       Accumulates in previtellogenic oocytes and is maintained at
CC       constant level throughout oogenesis and into early embryogenesis.
CC       Declines through gastrula to neurula. Not detectable between
CC       neurula and tailbud, nor in adult tissues other than ovary.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. Type 1
CC       subfamily.
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DR   EMBL; X78454; CAA55211.1; -; mRNA.
DR   EMBL; BC081136; AAH81136.1; -; mRNA.
DR   PIR; S60381; S60381.
DR   RefSeq; NP_001081491.1; -.
DR   UniGene; Xl.47990; -.
DR   HSSP; O67135; 1C3P.
DR   GeneID; 397868; -.
DR   KEGG; xla:397868; -.
DR   HOVERGEN; Q91695; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:InterPro.
DR   GO; GO:0016575; P:histone deacetylation; IEA:InterPro.
DR   GO; GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR003084; His_deacetylse_1.
DR   Gene3D; G3DSA:3.40.800.20; His_deacetylse; 1.
DR   PANTHER; PTHR10625; His_deacetylse; 1.
DR   PANTHER; PTHR10625:SF28; His_deacetylse_1; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
PE   1: Evidence at protein level;
KW   Chromatin regulator; Developmental protein; Hydrolase; Nucleus;
KW   Repressor; Transcription; Transcription regulation.
FT   CHAIN         1    480       Probable histone deacetylase 1-A.
FT                                /FTId=PRO_0000114691.
FT   REGION       10    321       Histone deacetylase.
FT   COMPBIAS    299    302       Poly-Gly.
FT   ACT_SITE    141    141       By similarity.
SQ   SEQUENCE   480 AA;  54748 MW;  7B831822235DADB5 CRC64;
     MALTLGTKKK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIFRPHKAS
     AEDMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSAGGSVAS
     AVKLNKQQTD ISVNWSGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV VYIDIDIHHG
     DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYALRD GIDDESYEAI
     FKPVMSKVME MFQPSAVVLQ CGADSLSGDR LGCFNLTIKG HAKCVEFIKT FNLPLLMLGG
     GGYTIRNVAR CWTYETAVAL DSEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE
     KIKQRLFENL RMLPHAPGVQ MQAVAEDSIH DDSGEEDEDD PDKRISIRSS DKRIACDEEF
     SDSEDEGEGG RKNVANFKKV KRVKTEEEKE GEDKKDVKEE EKAKDEKTDS KRVKEETKSV
//