SDS3_PONAB
ID SDS3_PONAB Reviewed; 328 AA.
AC Q5RBB8;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Sin3 histone deacetylase corepressor complex component SDS3;
DE AltName: Full=Suppressor of defective silencing 3 protein homolog;
GN Name=SUDS3; Synonyms=SDS3;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Regulatory protein which represses transcription and augments
CC histone deacetylase activity of HDAC1. May have a potential role in
CC tumor suppressor pathways through regulation of apoptosis. May function
CC in the assembly and/or enzymatic activity of the mSin3A corepressor
CC complex or in mediating interactions between the complex and other
CC regulatory complexes (By similarity). {ECO:0000250|UniProtKB:Q9H7L9}.
CC -!- SUBUNIT: Interacts with HCFC1. Homodimer. Component of the SIN3 histone
CC deacetylase (HDAC) corepressor complex. Interacts with SIN3A.
CC Interaction with SIN3B enhances the interaction between SIN3B and HDAC1
CC to form a complex. Component of a mSin3A corepressor complex that
CC contains SIN3A, SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2.
CC Interacts with USP17L2; the interaction is direct (By similarity).
CC Interacts with FOXK2 (By similarity). {ECO:0000250|UniProtKB:Q9H7L9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H7L9}.
CC -!- DOMAIN: The C-terminus is involved in transcriptional repression by
CC HDAC-independent mechanisms. {ECO:0000250|UniProtKB:Q9H7L9}.
CC -!- PTM: Polyubiquitinated. 'Lys-63'-polyubiquitinated SUDS3 positively
CC regulates histone deacetylation. Regulated through deubiquitination by
CC USP17L2/USP17 that cleaves 'Lys-63'-linked ubiquitin chains (By
CC similarity). {ECO:0000250|UniProtKB:Q9H7L9}.
CC -!- SIMILARITY: Belongs to the SDS3 family. {ECO:0000305}.
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DR EMBL; CR858733; CAH90942.1; -; mRNA.
DR RefSeq; NP_001125541.1; NM_001132069.1.
DR AlphaFoldDB; Q5RBB8; -.
DR SMR; Q5RBB8; -.
DR STRING; 9601.ENSPPYP00000005714; -.
DR GeneID; 100172453; -.
DR KEGG; pon:100172453; -.
DR CTD; 64426; -.
DR eggNOG; KOG4466; Eukaryota.
DR InParanoid; Q5RBB8; -.
DR OrthoDB; 1456563at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProt.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016575; P:histone deacetylation; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR InterPro; IPR013907; Sds3.
DR PANTHER; PTHR21964; PTHR21964; 1.
DR Pfam; PF08598; Sds3; 1.
DR SMART; SM01401; Sds3; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Chromatin regulator; Coiled coil; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT CHAIN 2..328
FT /note="Sin3 histone deacetylase corepressor complex
FT component SDS3"
FT /id="PRO_0000290582"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..170
FT /note="Mediates interaction with USP17L2"
FT /evidence="ECO:0000250"
FT REGION 188..226
FT /note="Sin3 interaction domain (SID)"
FT REGION 226..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 66..171
FT /evidence="ECO:0000255"
FT COMPBIAS 35..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 49
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 53
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 234
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT CROSSLNK 69
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
FT CROSSLNK 201
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H7L9"
SQ SEQUENCE 328 AA; 38150 MW; B4A6AEA519017A2A CRC64;
MSAAGLLAPA PAQAGAPPAP EYYPEEDEEL ESAEEDERSC RGRESDEDTE DASETDLAKH
DEEDYVEMKE QMYQDKLASL KRQLQQLQEG TLQEYQKRMK KLDQQYKERI RNAELFLQLE
TEQVERNYIK EKKAAVKEFE DKKVELKENL IAELEEKKKM IENEKLTMEL TGDSMEVKPI
MTRKLRRRPN DPVPIPDKRR KPAPAQLNYL LTDEQIMEDL RTLNKLKSPK RPASPSSPEH
LPATPAESPA QRFEARIEDG KLYYDKRWYH KSQAIYLESK DNQKLSCVIS SVGANEIWVR
KTSDSTKMRI YLGQLQRGLF VIRRRSAA
