ID   SP130_CHICK             Reviewed;        1057 AA.
AC   Q5F3U0;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Histone deacetylase complex subunit SAP130;
DE   AltName: Full=130 kDa Sin3-associated polypeptide;
DE   AltName: Full=Sin3-associated polypeptide p130;
GN   Name=SAP130; ORFNames=RCJMB04_7d5;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Acts as a transcriptional repressor. May function in the
CC       assembly and/or enzymatic activity of the mSin3A corepressor complex or
CC       in mediating interactions between the complex and other regulatory
CC       complexes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Component of a mSin3A corepressor complex that contains SIN3A,
CC       SAP130, SUDS3/SAP45, ARID4B/SAP180, HDAC1 and HDAC2. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The N-terminus may interact with a transcriptional coactivator.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The C-terminus may interact with HDAC-dependent and HDAC-
CC       independent corepressors. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SAP130 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; AJ851560; CAH65194.1; -; mRNA.
DR   RefSeq; NP_001026472.1; NM_001031301.1.
DR   AlphaFoldDB; Q5F3U0; -.
DR   SMR; Q5F3U0; -.
DR   STRING; 9031.ENSGALP00000003216; -.
DR   PaxDb; Q5F3U0; -.
DR   PRIDE; Q5F3U0; -.
DR   GeneID; 424756; -.
DR   KEGG; gga:424756; -.
DR   CTD; 79595; -.
DR   VEuPathDB; HostDB:geneid_424756; -.
DR   eggNOG; ENOG502QQ6P; Eukaryota.
DR   InParanoid; Q5F3U0; -.
DR   OrthoDB; 242848at2759; -.
DR   PhylomeDB; Q5F3U0; -.
DR   PRO; PR:Q5F3U0; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0070822; C:Sin3-type complex; IBA:GO_Central.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR024137; His_deAcase_cplx_SAP130.
DR   InterPro; IPR031963; SAP130_C.
DR   PANTHER; PTHR13497; PTHR13497; 1.
DR   Pfam; PF16014; SAP130_C; 1.
PE   2: Evidence at transcript level;
KW   Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1057
FT                   /note="Histone deacetylase complex subunit SAP130"
FT                   /id="PRO_0000283738"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          556..594
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          827..880
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..594
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..644
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        863..880
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1057 AA;  110852 MW;  4573869EEAF51987 CRC64;
     MSSQQFPRSG APPPGLGANP PTGPASGTAG LIAPAATTSD ESVRDPEVAP RDQHLGPGGP
     APPREEKQEP VVVRPYPQVQ MLAPHHPVPP GAPVTVAAPP AHLAPAVPLS FSDGLMKPPL
     KPTMPSRPIA PAPPSTLSAP TKVPGQVTVT MESSIPQAPT IPVATISGQQ GHPSNLHHIM
     ATNVQMSIIR SSAPGPPLHI GASHLPRGAA AAAVMSSSKV TTVLRPASQL PNAATAQPAV
     QHIIHQPIQS RPPVTTSSTI PPAVVATVSA TRAQSPVITT TAAHATESTL SRPTLSIQQH
     PPSAAISIQR PAQPRDAATR ITLPSHPAIG AQKQQLHTMA QKTIFSTGTP VAAATVAPIL
     ATNTIASATT AGSVSHTQAP TSTIVTMTMP SHSSHATAVT TSNIPVAKVV PQQITHTSPR
     IQSDYTAERS NLIPLSSHRA SPNPVAMETR NDNRQSVPVQ FQYFLPTYPP SAYPLTAHTY
     TPITSSVSTI RQYPVSAQAP NSAITAQTGV GVASTVHLNP MQLMTVDASH ARHIQGIQPA
     PISAQGIQPA PIGAQGIQPA PIGTQGLHPA APIGTQGLQP APISAQQPQA DTKTSVVLAD
     GATIVANPIS NTFNTASAAT TVVQTHSQSA SAPAQGSSPR PSILRKKPTT DGLAVRKSLI
     PPQPPEVAST RVENTMRSTS GSPRPAGAKP KPEIHVSMAT PVTVSMEAVS NQGSEQPTIA
     VPPSSQQPPS AIPTIIAAAS PTSQPAAALS TIPGAVPAAP PTSTTIVAAP APPATMSGAL
     SAVLGPVVPE IKIKEEAEPM DIMRPVSAVP PLTTSTVSPS LALLANNLSM PPSDLPPGAS
     PRKKPRKQQH VISTEEGDMM ETNSTDDEKS TAKSLLVKAE KRKSPPKEYI DEEGVRYVPV
     RPRPPITLLR HYRNPWKAAY HHFQRYSDVR VKEEKKAMLQ EIANQKGVSC RAQGWKVHLC
     AAQLLQLTNL EHDVYERLTA LQEGLIPKKK AATDDDLHRI NELIQGNMQR CKLVMDQINE
     ARDSMLKVLD HKDRVLKLLN KNGTVKKVSK LKRKEKV