SAP18_DROME
ID SAP18_DROME Reviewed; 150 AA.
AC Q9VEX9; Q1LYZ7; Q8SZF6; Q9N9Z3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Histone deacetylase complex subunit SAP18;
DE AltName: Full=18 kDa Sin3-associated polypeptide;
DE AltName: Full=Bicoid-interacting protein 1;
DE AltName: Full=dSAP18;
GN Name=Bin1; Synonyms=SAP18; ORFNames=CG6046;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH BCD, AND DEVELOPMENTAL STAGE.
RX PubMed=11455422; DOI=10.1007/s004270100135;
RA Zhu W., Foehr M., Jaynes J.B., Hanes S.D.;
RT "Drosophila SAP18, a member of the Sin3/Rpd3 histone deacetylase complex,
RT interacts with Bicoid and inhibits its activity.";
RL Dev. Genes Evol. 211:109-117(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-150, FUNCTION, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH TRL.
RX PubMed=11256608; DOI=10.1093/embo-reports/kvd046;
RA Espinas M.L., Canudas S., Fanti L., Pimpinelli S., Casanova J., Azorin F.;
RT "The GAGA factor of Drosophila interacts with SAP18, a Sin3-associated
RT polypeptide.";
RL EMBO Rep. 1:253-259(2000).
CC -!- FUNCTION: Involved in the tethering of the SIN3 complex to core histone
CC proteins. Interacts with bicoid (bcd) to repress transcription of
CC bicoid target genes in the anterior tip of the embryo; a process known
CC as retraction. Interacts with Trl and binds to Polycomb response
CC elements at the bithorax complex. May contribute to the regulation of
CC other homeotic gene expressions. {ECO:0000269|PubMed:11256608,
CC ECO:0000269|PubMed:11455422}.
CC -!- SUBUNIT: Forms a complex with SIN3 and histone deacetylase (By
CC similarity). Interacts with the N-terminal residues of TRL. Interacts
CC with BCD; in vitro and yeast cells. {ECO:0000250,
CC ECO:0000269|PubMed:11256608, ECO:0000269|PubMed:11455422}.
CC -!- INTERACTION:
CC Q9VEX9; P09081: bcd; NbExp=2; IntAct=EBI-129424, EBI-196628;
CC Q9VEX9; P42124: E(z); NbExp=7; IntAct=EBI-129424, EBI-112315;
CC Q9VEX9; Q08605-2: Trl; NbExp=4; IntAct=EBI-129424, EBI-665803;
CC Q9VEX9; P60953: CDC42; Xeno; NbExp=2; IntAct=EBI-129424, EBI-81752;
CC Q9VEX9; P07274: PFY1; Xeno; NbExp=3; IntAct=EBI-129424, EBI-13892;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11256608,
CC ECO:0000269|PubMed:11455422}. Cytoplasm {ECO:0000250|UniProtKB:O00422}.
CC Note=Shuttles between the nucleus and the cytoplasm.
CC {ECO:0000250|UniProtKB:O00422}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:11455422}.
CC -!- SIMILARITY: Belongs to the SAP18 family. {ECO:0000305}.
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DR EMBL; AF297546; AAG34996.1; -; mRNA.
DR EMBL; AE014297; AAF55284.1; -; Genomic_DNA.
DR EMBL; AY070913; AAL48535.1; -; mRNA.
DR EMBL; BT025229; ABF17920.1; -; mRNA.
DR EMBL; AJ278500; CAB95728.1; -; mRNA.
DR RefSeq; NP_001303440.1; NM_001316511.1.
DR RefSeq; NP_001303441.1; NM_001316512.1.
DR RefSeq; NP_524377.1; NM_079653.3.
DR AlphaFoldDB; Q9VEX9; -.
DR SMR; Q9VEX9; -.
DR BioGRID; 67016; 27.
DR DIP; DIP-19160N; -.
DR IntAct; Q9VEX9; 15.
DR MINT; Q9VEX9; -.
DR STRING; 7227.FBpp0082731; -.
DR PaxDb; Q9VEX9; -.
DR PRIDE; Q9VEX9; -.
DR DNASU; 41965; -.
DR EnsemblMetazoa; FBtr0083279; FBpp0082731; FBgn0024491.
DR EnsemblMetazoa; FBtr0347200; FBpp0312505; FBgn0024491.
DR EnsemblMetazoa; FBtr0347201; FBpp0312506; FBgn0024491.
DR GeneID; 41965; -.
DR KEGG; dme:Dmel_CG6046; -.
DR CTD; 274; -.
DR FlyBase; FBgn0024491; Bin1.
DR VEuPathDB; VectorBase:FBgn0024491; -.
DR eggNOG; KOG3391; Eukaryota.
DR GeneTree; ENSGT00390000003152; -.
DR HOGENOM; CLU_108681_0_1_1; -.
DR InParanoid; Q9VEX9; -.
DR OMA; VYPNFRN; -.
DR OrthoDB; 1622057at2759; -.
DR PhylomeDB; Q9VEX9; -.
DR Reactome; R-DME-3214815; HDACs deacetylate histones.
DR SignaLink; Q9VEX9; -.
DR BioGRID-ORCS; 41965; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 41965; -.
DR PRO; PR:Q9VEX9; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0024491; Expressed in eye disc (Drosophila) and 53 other tissues.
DR ExpressionAtlas; Q9VEX9; baseline and differential.
DR Genevisible; Q9VEX9; DM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; HDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0071011; C:precatalytic spliceosome; HDA:FlyBase.
DR GO; GO:0003714; F:transcription corepressor activity; IGI:FlyBase.
DR GO; GO:0008134; F:transcription factor binding; IPI:FlyBase.
DR GO; GO:0031507; P:heterochromatin assembly; IGI:FlyBase.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:FlyBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:FlyBase.
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 1: Evidence at protein level;
KW Cytoplasm; Developmental protein; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..150
FT /note="Histone deacetylase complex subunit SAP18"
FT /id="PRO_0000220978"
FT CONFLICT 57
FT /note="T -> A (in Ref. 4; AAL48535)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 150 AA; 17288 MW; 94947F206D8FA0AD CRC64;
MANVESMIVE EKTQVKQIDR EKTCPMLLRV FCSTGRHHSV SEYMFGNVPT NELQIYTWQD
ATLHELTSLV RDVNPDTRKK GTYFDFAVVY PNFRSNHFQM REIGVTCTGQ KGIDDNKTLA
QAKFSIGDFL DISITPPNRL PPTARRQRPY
