MED17_DROME
ID MED17_DROME Reviewed; 642 AA.
AC Q9VEC1;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 17;
DE AltName: Full=Mediator complex subunit 17;
DE AltName: Full=dMED17;
DE AltName: Full=dTRAP80;
GN Name=MED17; Synonyms=Trap80; ORFNames=CG7957;
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, AND DEVELOPMENTAL STAGE.
RX PubMed=11090137; DOI=10.1101/gad.17900;
RA Boube M., Faucher C., Joulia L., Cribbs D.L., Bourbon H.-M.;
RT "Drosophila homologs of transcriptional mediator complex subunits are
RT required for adult cell and segment identity specification.";
RL Genes Dev. 14:2906-2917(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Southworth J.W., Kennison J.A.;
RT "Transcriptional coactivators in Drosophila.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP INTERACTION WITH HSF, AND SUBCELLULAR LOCATION.
RX PubMed=11511356; DOI=10.1016/s1097-2765(01)00296-9;
RA Park J.M., Werner J., Kim J.M., Lis J.T., Kim Y.-J.;
RT "Mediator, not holoenzyme, is directly recruited to the heat shock promoter
RT by HSF upon heat shock.";
RL Mol. Cell 8:9-19(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION OF THE MEDIATOR COMPLEX,
RP IDENTIFICATION IN A COMPLEX WITH CDK8; MED4; MED6; MED14; MED18; MED20;
RP MED21 AND MED31, AND DEVELOPMENTAL STAGE.
RX PubMed=11259581; DOI=10.1128/mcb.21.7.2312-2323.2001;
RA Park J.M., Gim B.S., Kim J.M., Yoon J.H., Kim H.-S., Kang J.-G., Kim Y.-J.;
RT "Drosophila Mediator complex is broadly utilized by diverse gene-specific
RT transcription factors at different types of core promoters.";
RL Mol. Cell. Biol. 21:2312-2323(2001).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP COMPLEX, AND FUNCTION OF THE MEDIATOR COMPLEX.
RX PubMed=12021283; DOI=10.1074/jbc.m204144200;
RA Gu J.-Y., Park J.M., Song E.J., Mizuguchi G., Yoon J.H., Kim-Ha J.,
RA Lee K.-J., Kim Y.-J.;
RT "Novel Mediator proteins of the small Mediator complex in Drosophila SL2
RT cells.";
RL J. Biol. Chem. 277:27154-27161(2002).
RN [9]
RP FUNCTION.
RX PubMed=16751183; DOI=10.1101/gad.1418806;
RA Marr M.T. II, Isogai Y., Wright K.J., Tjian R.;
RT "Coactivator cross-talk specifies transcriptional output.";
RL Genes Dev. 20:1458-1469(2006).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors. Required for activated
CC transcription of the MtnA, MtnB and MtnD genes. Negatively regulates
CC sex comb development. {ECO:0000269|PubMed:11090137,
CC ECO:0000269|PubMed:11259581, ECO:0000269|PubMed:12021283,
CC ECO:0000269|PubMed:16751183}.
CC -!- SUBUNIT: Component of the Mediator complex, which includes at least
CC CDK8, MED4, MED6, MED11, MED14, MED17, MED18, MED20, MED21, MED22,
CC MED27, MED28, MED30 and MED31. Interacts with Hsf.
CC {ECO:0000269|PubMed:11259581, ECO:0000269|PubMed:11511356,
CC ECO:0000269|PubMed:12021283}.
CC -!- INTERACTION:
CC Q9VEC1; P91641: MED20; NbExp=6; IntAct=EBI-135284, EBI-175591;
CC Q9VEC1; Q8MSX2: MED6; NbExp=6; IntAct=EBI-135284, EBI-194467;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11511356}. Chromosome
CC {ECO:0000269|PubMed:11511356}. Note=Colocalizes with RNA polymerase II
CC on pachytene chromosomes.
CC -!- DEVELOPMENTAL STAGE: Maternally encoded. Expression decreases during
CC larval stages then rises during mid-pupal metamorphosis.
CC {ECO:0000269|PubMed:11090137, ECO:0000269|PubMed:11259581}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 17 family.
CC {ECO:0000305}.
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DR EMBL; AF244916; AAF63336.1; -; mRNA.
DR EMBL; AF289995; AAG02460.1; -; mRNA.
DR EMBL; AE014297; AAF55506.1; -; Genomic_DNA.
DR EMBL; AY118662; AAM50031.1; -; mRNA.
DR RefSeq; NP_650686.1; NM_142429.3.
DR AlphaFoldDB; Q9VEC1; -.
DR SMR; Q9VEC1; -.
DR BioGRID; 67196; 56.
DR DIP; DIP-20967N; -.
DR IntAct; Q9VEC1; 15.
DR STRING; 7227.FBpp0082980; -.
DR PaxDb; Q9VEC1; -.
DR PRIDE; Q9VEC1; -.
DR DNASU; 42175; -.
DR EnsemblMetazoa; FBtr0083558; FBpp0082980; FBgn0038578.
DR GeneID; 42175; -.
DR KEGG; dme:Dmel_CG7957; -.
DR CTD; 9440; -.
DR FlyBase; FBgn0038578; MED17.
DR VEuPathDB; VectorBase:FBgn0038578; -.
DR eggNOG; KOG4512; Eukaryota.
DR GeneTree; ENSGT00390000011810; -.
DR HOGENOM; CLU_028003_1_0_1; -.
DR InParanoid; Q9VEC1; -.
DR OMA; CQIYQHQ; -.
DR OrthoDB; 976669at2759; -.
DR PhylomeDB; Q9VEC1; -.
DR SignaLink; Q9VEC1; -.
DR BioGRID-ORCS; 42175; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 42175; -.
DR PRO; PR:Q9VEC1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0038578; Expressed in eye disc (Drosophila) and 47 other tissues.
DR Genevisible; Q9VEC1; DM.
DR GO; GO:0070847; C:core mediator complex; IBA:GO_Central.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0005721; C:pericentric heterochromatin; IPI:FlyBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0003712; F:transcription coregulator activity; IMP:UniProtKB.
DR GO; GO:0009987; P:cellular process; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0060260; P:regulation of transcription initiation from RNA polymerase II promoter; ISS:FlyBase.
DR GO; GO:0045498; P:sex comb development; IGI:FlyBase.
DR InterPro; IPR019313; Mediator_Med17.
DR PANTHER; PTHR13114; PTHR13114; 1.
DR Pfam; PF10156; Med17; 1.
PE 1: Evidence at protein level;
KW Activator; Chromosome; Developmental protein; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..642
FT /note="Mediator of RNA polymerase II transcription subunit
FT 17"
FT /id="PRO_0000304706"
FT REGION 210..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 642 AA; 71557 MW; 9EBD4E084788AF58 CRC64;
MSNSVNISVE TTCENQIREI GYDGTELYQP PPTLSESLAK CAARIDFSKT SLDDLKKEEK
SAAAAADEDK DATQFQESLW PWDAVRNKLK DALTEICVLS DVISIAKDKR YLVLDPLLEE
ADDTKPIVQV YSRKKAISQA AQVLLSGAER LRNAHSEQRN RNVSDFHIEL LRLRQNWRLK
KVSNAIIGDL SYRTAGSKFG MSGTFEVTKA EETGDEDTAS SSNSSSSVSG NNGMQLKASS
ALRVIVPAEL QGVAYIKVIT QKDQEDLCTA QLNLMGHGPN ITAQVGVWQK TLEFAQNVLF
CKELFAQLAR EAIQLQAPIP HVVIGNQIRA TLLPNIQLII SLCHSTTFDS SQPAPINDHD
HVLEHSLHQL LREVHYKNSH HPFPHPASAP LGPTKKRMLA GPMAADRETL LDMTKSQTIL
EQIIAQAQHI FMRKRTQYVL DTLARDVKDP QIVSHWNAMN SPTMSCVKIN IVTHGYDAIG
RTSLVIHVKE RSLKCICRDG RVMRLSYEPQ ELRDLILCQI NSHQISCLIS LARCMSWTVL
SNSNHLGIGK VEPLGNASSC LLASPNSDRM IAVQIRCDPQ IDVKVYIARS PRQDFFPSPL
VPEKLWENLG GTFKEVRFDK IEGKSFLNKM EFLMASLTSN TA
