ID   S30LB_XENLA             Reviewed;         181 AA.
AC   Q2TAD4;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Histone deacetylase complex subunit SAP30L-B;
DE   AltName: Full=Sin3 corepressor complex subunit SAP30L-B;
DE   AltName: Full=Sin3-associated protein p30-like B;
GN   Name=sap30l-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Functions as transcription repressor, probably via its
CC       interaction with histone deacetylase complexes. Involved in the
CC       functional recruitment of the class 1 Sin3-histone deacetylase complex
CC       (HDAC) to the nucleolus. Binds DNA, apparently without sequence-
CC       specificity, and bends bound double-stranded DNA. Binds phosphoinositol
CC       phosphates (phosphoinositol 3-phosphate, phosphoinositol 4-phosphate
CC       and phosphoinositol 5-phosphate) via the same basic sequence motif that
CC       mediates DNA binding and nuclear import.
CC       {ECO:0000250|UniProtKB:Q9HAJ7}.
CC   -!- SUBUNIT: Interacts with components of the histone deacetylase complex
CC       sin3a, hdac1 and hdac2. Binds histones and nucleosomes.
CC       {ECO:0000250|UniProtKB:Q9HAJ7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q9HAJ7}.
CC   -!- DOMAIN: The zinc-finger domain mediates direct interaction with DNA and
CC       phosphoinositol phosphates (phosphoinositol 3-phosphate,
CC       phosphoinositol 4-phosphate and phosphoinositol 5-phosphate). In vitro
CC       oxydation causes reversible disulfide bond formation between Cys
CC       residues in the zinc-finger domain and reversible loss of zinc ion
CC       binding. {ECO:0000250|UniProtKB:Q9HAJ7}.
CC   -!- SIMILARITY: Belongs to the SAP30 family. {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; BC110979; AAI10980.1; -; mRNA.
DR   RefSeq; NP_001089954.1; NM_001096485.1.
DR   AlphaFoldDB; Q2TAD4; -.
DR   SMR; Q2TAD4; -.
DR   DNASU; 735024; -.
DR   GeneID; 735024; -.
DR   KEGG; xla:735024; -.
DR   CTD; 735024; -.
DR   Xenbase; XB-GENE-960207; sap30l.L.
DR   OMA; QCARTKR; -.
DR   OrthoDB; 1520155at2759; -.
DR   Proteomes; UP000186698; Chromosome 3L.
DR   Bgee; 735024; Expressed in internal ear and 19 other tissues.
DR   GO; GO:0000118; C:histone deacetylase complex; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0044378; F:non-sequence-specific DNA binding, bending; ISS:UniProtKB.
DR   GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR   GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   Gene3D; 6.10.160.20; -; 1.
DR   InterPro; IPR024145; His_deAcase_SAP30/SAP30L.
DR   InterPro; IPR038291; SAP30_C_sf.
DR   InterPro; IPR025718; SAP30_Sin3-bd.
DR   InterPro; IPR025717; SAP30_zn-finger.
DR   PANTHER; PTHR13286; PTHR13286; 1.
DR   Pfam; PF13867; SAP30_Sin3_bdg; 1.
DR   Pfam; PF13866; zf-SAP30; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; DNA-binding; Lipid-binding; Metal-binding; Nucleus;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..181
FT                   /note="Histone deacetylase complex subunit SAP30L-B"
FT                   /id="PRO_0000309504"
FT   ZN_FING         26..74
FT                   /note="Atypical"
FT   REGION          82..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..87
FT                   /note="Important for DNA and phosphoinositide binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HAJ7"
FT   MOTIF           83..88
FT                   /note="Nuclear localization signal (NLS)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HAJ7"
FT   COMPBIAS        84..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        26..27
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        35..71
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   181 AA;  20848 MW;  BB82AA9639D36FB2 CRC64;
     MNGFSTEEDS RDGPPAQAAP FFGQTCCLID GGERCPRPAG NASFSKRVQK SISQKKLKLD
     IDKSVRHLYI CDFHKNYIQS VRNKRKRKTS DDGGDSPEHE TDVPEVDLFQ LQVNTLRRYK
     RYYKLQTRPG LNKAQLAETV SRHFRNIPVN EKETLAYFIY MVKSNRSRLD QKSESSKQLD
     A