SAP18_PONAB
ID SAP18_PONAB Reviewed; 153 AA.
AC Q5RDT5;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Histone deacetylase complex subunit SAP18;
DE AltName: Full=18 kDa Sin3-associated polypeptide;
DE AltName: Full=Sin3-associated polypeptide p18;
GN Name=SAP18;
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: Component of the SIN3-repressing complex. Enhances the
CC ability of SIN3-HDAC1-mediated transcriptional repression. When
CC tethered to the promoter, it can direct the formation of a repressive
CC complex to core histone proteins. Auxiliary component of the splicing-
CC dependent multiprotein exon junction complex (EJC) deposited at splice
CC junction on mRNAs. The EJC is a dynamic structure consisting of core
CC proteins and several peripheral nuclear and cytoplasmic associated
CC factors that join the complex only transiently either during EJC
CC assembly or during subsequent mRNA metabolism. Component of the ASAP
CC and PSAP complexes which bind RNA in a sequence-independent manner and
CC are proposed to be recruited to the EJC prior to or during the splicing
CC process and to regulate specific excision of introns in specific
CC transcription subsets. The ASAP complex can inhibit mRNA processing
CC during in vitro splicing reactions. The ASAP complex promotes apoptosis
CC and is disassembled after induction of apoptosis. Involved in the
CC splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic
CC genes); specifically inhibits the formation of proapoptotic isoforms
CC such as Bcl-X(S); the activity is different from the established EJC
CC assembly and function (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Found in a mRNA splicing-dependent exon junction complex
CC (EJC). Component of the heterotrimeric ASAP (apoptosis- and splicing-
CC associated protein) and PSAP complexes consisting of RNPS1, SAP18 and
CC either ACIN1 or PNN, respectively; the ASAP and PSAP complexes probably
CC are formed mutually exclusive. For the ASAP complex, the association of
CC SAP18 seems to require a preformed RNPS1:ACIN1 complex. Forms a complex
CC with SIN3A and HDAC1. Interacts with SUFU (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O00422}. Cytoplasm
CC {ECO:0000250|UniProtKB:O00422}. Nucleus speckle
CC {ECO:0000250|UniProtKB:O00422}. Note=Shuttles between the nucleus and
CC the cytoplasm (By similarity). Colocalizes with ACIN1 and SRSF2 in
CC nuclear speckles (By similarity). {ECO:0000250|UniProtKB:O00422}.
CC -!- SIMILARITY: Belongs to the SAP18 family. {ECO:0000305}.
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DR EMBL; CR857814; CAH90072.1; -; mRNA.
DR RefSeq; NP_001129009.1; NM_001135537.1.
DR AlphaFoldDB; Q5RDT5; -.
DR BMRB; Q5RDT5; -.
DR SMR; Q5RDT5; -.
DR STRING; 9601.ENSPPYP00000005921; -.
DR Ensembl; ENSPPYT00000006154; ENSPPYP00000005921; ENSPPYG00000005198.
DR GeneID; 100190849; -.
DR KEGG; pon:100190849; -.
DR CTD; 10284; -.
DR eggNOG; KOG3391; Eukaryota.
DR GeneTree; ENSGT00390000003152; -.
DR HOGENOM; CLU_108681_0_1_1; -.
DR InParanoid; Q5RDT5; -.
DR OMA; VYPNFRN; -.
DR OrthoDB; 1622057at2759; -.
DR TreeFam; TF313032; -.
DR Proteomes; UP000001595; Chromosome 13.
DR GO; GO:0061574; C:ASAP complex; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0035145; C:exon-exon junction complex; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.550; -; 1.
DR InterPro; IPR017250; Hist_deAcase_cplx_SAP18.
DR InterPro; IPR010516; SAP18.
DR InterPro; IPR042534; SAP18_sf.
DR PANTHER; PTHR13082; PTHR13082; 1.
DR Pfam; PF06487; SAP18; 1.
DR PIRSF; PIRSF037637; HDAC_SAP18; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Isopeptide bond; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00422"
FT CHAIN 2..153
FT /note="Histone deacetylase complex subunit SAP18"
FT /id="PRO_0000290197"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..153
FT /note="Involved in splicing regulation activity"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O00422"
FT CROSSLNK 13
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O00422"
SQ SEQUENCE 153 AA; 17561 MW; C7E479FFE9CA5774 CRC64;
MAVESRVTQE EIKKEPEKPI DREKTCPLLL RVFTTNNGRH HRMDEFSRGN VPSSELQIYT
WMDATLKELT SLVKEVYPEA RKKGTHFNFA IVFTDVKRPG YRVKEIGSTM SGRKGTDDSM
TLQSQKFQIG DYLDIAITPP NRAPPPSGRM RPY
