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SAP18_BOVIN
ID   SAP18_BOVIN             Reviewed;         153 AA.
AC   Q3T022;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) 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; BC102603; AAI02604.1; -; mRNA.
DR   RefSeq; NP_001030544.2; NM_001035467.2.
DR   AlphaFoldDB; Q3T022; -.
DR   BMRB; Q3T022; -.
DR   SMR; Q3T022; -.
DR   STRING; 9913.ENSBTAP00000024791; -.
DR   PaxDb; Q3T022; -.
DR   PRIDE; Q3T022; -.
DR   GeneID; 615692; -.
DR   KEGG; bta:615692; -.
DR   CTD; 10284; -.
DR   eggNOG; KOG3391; Eukaryota.
DR   HOGENOM; CLU_108681_0_1_1; -.
DR   InParanoid; Q3T022; -.
DR   OrthoDB; 1622057at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0061574; C:ASAP complex; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
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:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
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_0000245462"
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;  17579 MW;  73FE63FFF3D05772 CRC64;
     MAVESRVTQE EIKKEPEKPI DREKTCPLLL RVFTTNNGRH HRMDEFSRGN VPSSELQIYT
     WMDATLKELT SLVKEVYPEA RKKGTHFNFA IVFTDLKRPG YRVKEIGSTM SGRKGTDDSM
     TLQSQKFQIG DYLDIAITPP NRAPPTSGRM RPY
 
 
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