SAP30_DROME
ID SAP30_DROME Reviewed; 173 AA.
AC Q9VXB3;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Histone deacetylase complex subunit SAP30 homolog;
DE AltName: Full=SIN3-associated polypeptide 30;
GN Name=Sap30; ORFNames=CG4756;
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=12077326; DOI=10.1128/mcb.22.14.4965-4976.2002;
RA Pile L.A., Schlag E.M., Wassarman D.A.;
RT "The SIN3/RPD3 deacetylase complex is essential for G(2) phase cell cycle
RT progression and regulation of SMRTER corepressor levels.";
RL Mol. Cell. Biol. 22:4965-4976(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84; SER-88; THR-91 AND
RP THR-93, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Component of the class 1 Sin3A-histone deacetylase
CC (HDAC1/Rpd3) complex (HDAC). Appears to be a non-essential subunit of
CC this complex which is not required for cell cycle regulation of
CC progression through the G2 phase of the cell cycle.
CC {ECO:0000269|PubMed:12077326}.
CC -!- SUBUNIT: Component of the class 1 Sin3A-histone deacetylase
CC (HDAC1/Rpd3) complex (HDAC). Not essential for stability of the
CC complex, recruitment of the complex to some promoters, or the
CC deacetylase activity of the complex. {ECO:0000269|PubMed:12077326}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Does not cause cell morphology changes, cell
CC growth defects, cell cycle phenotypes, or loss of Smr/SMRTER protein
CC from the Sin3A-histone deacetylase (HDAC1/Rpd3) complex.
CC {ECO:0000269|PubMed:12077326}.
CC -!- SIMILARITY: Belongs to the SAP30 family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48664.1; -; Genomic_DNA.
DR EMBL; AY071452; AAL49074.1; -; mRNA.
DR RefSeq; NP_001285352.1; NM_001298423.1.
DR RefSeq; NP_573162.1; NM_132934.4.
DR AlphaFoldDB; Q9VXB3; -.
DR SMR; Q9VXB3; -.
DR BioGRID; 58997; 6.
DR IntAct; Q9VXB3; 2.
DR STRING; 7227.FBpp0074105; -.
DR iPTMnet; Q9VXB3; -.
DR PaxDb; Q9VXB3; -.
DR DNASU; 32664; -.
DR EnsemblMetazoa; FBtr0074331; FBpp0074105; FBgn0030788.
DR EnsemblMetazoa; FBtr0344089; FBpp0310514; FBgn0030788.
DR GeneID; 32664; -.
DR KEGG; dme:Dmel_CG4756; -.
DR UCSC; CG4756-RA; d. melanogaster.
DR CTD; 8819; -.
DR FlyBase; FBgn0030788; Sap30.
DR VEuPathDB; VectorBase:FBgn0030788; -.
DR eggNOG; ENOG502QWFH; Eukaryota.
DR HOGENOM; CLU_097961_1_0_1; -.
DR InParanoid; Q9VXB3; -.
DR OMA; QCARTKR; -.
DR OrthoDB; 1520155at2759; -.
DR PhylomeDB; Q9VXB3; -.
DR Reactome; R-DME-3214815; HDACs deacetylate histones.
DR BioGRID-ORCS; 32664; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Sap30; fly.
DR GenomeRNAi; 32664; -.
DR PRO; PR:Q9VXB3; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030788; Expressed in cleaving embryo and 22 other tissues.
DR ExpressionAtlas; Q9VXB3; baseline and differential.
DR Genevisible; Q9VXB3; DM.
DR GO; GO:0000118; C:histone deacetylase complex; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 6.10.160.20; -; 1.
DR InterPro; IPR024145; His_deAcase_SAP30/SAP30L.
DR InterPro; IPR038291; SAP30_C_sf.
DR InterPro; IPR025718; SAP30_Sin3-bd.
DR InterPro; IPR025717; SAP30_zn-finger.
DR PANTHER; PTHR13286; PTHR13286; 1.
DR Pfam; PF13867; SAP30_Sin3_bdg; 1.
DR Pfam; PF13866; zf-SAP30; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..173
FT /note="Histone deacetylase complex subunit SAP30 homolog"
FT /id="PRO_0000309508"
FT ZN_FING 20..68
FT /note="Atypical"
FT REGION 73..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 173 AA; 20192 MW; 260C27D5D8249514 CRC64;
MNNGFSTGEE DSRGHTDQTC CLIDDMERCR NQAGYASYSK RIQKTVAQKR LKLSSDPAAQ
HIYICDHHKE RIQSVRTKRR RKDSEDDSNE TDTDLHEFPD LYQLGVSTLR RYKRHFKVQT
RQGMKRAQLA DTIMKHFKTI PIKEKEIITF FVYMVKMGSN KLDQKNGLGN DTT
