ID MED7_YEAST Reviewed; 222 AA. AC Q08278; D6W1T4; DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 29-SEP-2021, entry version 169. DE RecName: Full=Mediator of RNA polymerase II transcription subunit 7; DE AltName: Full=Mediator complex subunit 7; GN Name=MED7; OrderedLocusNames=YOL135C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX PubMed=8896270; RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1053::aid-yea993>3.0.co;2-s; RA Aldea M., Piedrafita L., Casas C., Casamayor A., Khalid H., Balcells L., RA Arino J., Herrero E.; RT "Sequence analysis of a 12 801 bp fragment of the left arm of yeast RT chromosome XV containing a putative 6-phosphofructo-2-kinase gene, a gene RT for a possible glycophospholipid-anchored surface protein and six other RT open reading frames."; RL Yeast 12:1053-1058(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169874; RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."; RL Nature 387:98-102(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF MEDIATOR COMPLEX. RX PubMed=9420330; DOI=10.1101/gad.12.1.45; RA Myers L.C., Gustafsson C.M., Bushnell D.A., Lui M., Erdjument-Bromage H., RA Tempst P., Kornberg R.D.; RT "The Med proteins of yeast and their function through the RNA polymerase II RT carboxy-terminal domain."; RL Genes Dev. 12:45-54(1998). RN [6] RP INTERACTION WITH MED1; MED4 AND SRB7, FUNCTION OF THE MEDIATOR COMPLEX, AND RP INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II. RX PubMed=11555651; DOI=10.1074/jbc.m105961200; RA Kang J.S., Kim S.H., Hwang M.S., Han S.J., Lee Y.C., Kim Y.-J.; RT "The structural and functional organization of the yeast mediator RT complex."; RL J. Biol. Chem. 276:42003-42010(2001). RN [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [8] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [9] RP ASSOCIATION WITH PROMOTER REGIONS. RX PubMed=14623974; DOI=10.1073/pnas.2036346100; RA Kuras L., Borggrefe T., Kornberg R.D.; RT "Association of the Mediator complex with enhancers of active genes."; RL Proc. Natl. Acad. Sci. U.S.A. 100:13887-13891(2003). RN [10] RP NOMENCLATURE. RX PubMed=15175151; DOI=10.1016/j.molcel.2004.05.011; RA Bourbon H.-M., Aguilera A., Ansari A.Z., Asturias F.J., Berk A.J., RA Bjoerklund S., Blackwell T.K., Borggrefe T., Carey M., Carlson M., RA Conaway J.W., Conaway R.C., Emmons S.W., Fondell J.D., Freedman L.P., RA Fukasawa T., Gustafsson C.M., Han M., He X., Herman P.K., Hinnebusch A.G., RA Holmberg S., Holstege F.C.P., Jaehning J.A., Kim Y.-J., Kuras L., Leutz A., RA Lis J.T., Meisterernest M., Naeaer A.M., Nasmyth K., Parvin J.D., RA Ptashne M., Reinberg D., Ronne H., Sadowski I., Sakurai H., Sipiczki M., RA Sternberg P.W., Stillman D.J., Strich R., Struhl K., Svejstrup J.Q., RA Tuck S., Winston F., Roeder R.G., Kornberg R.D.; RT "A unified nomenclature for protein subunits of mediator complexes linking RT transcriptional regulators to RNA polymerase II."; RL Mol. Cell 14:553-557(2004). RN [11] RP STRUCTURE OF THE MEDIATOR COMPLEX. RX PubMed=15477388; DOI=10.1093/nar/gkh878; RA Guglielmi B., van Berkum N.L., Klapholz B., Bijma T., Boube M., RA Boschiero C., Bourbon H.-M., Holstege F.C.P., Werner M.; RT "A high resolution protein interaction map of the yeast Mediator complex."; RL Nucleic Acids Res. 32:5379-5391(2004). RN [12] RP CHARACTERIZATION OF THE MEDIATOR COMPLEX. RX PubMed=16002404; DOI=10.1074/jbc.c500150200; RA Takagi Y., Chadick J.Z., Davis J.A., Asturias F.J.; RT "Preponderance of free mediator in the yeast Saccharomyces cerevisiae."; RL J. Biol. Chem. 280:31200-31207(2005). RN [13] RP FUNCTION OF THE MEDIATOR COMPLEX. RX PubMed=16076843; DOI=10.1074/jbc.m506067200; RA Nair D., Kim Y., Myers L.C.; RT "Mediator and TFIIH govern carboxyl-terminal domain-dependent transcription RT in yeast extracts."; RL J. Biol. Chem. 280:33739-33748(2005). RN [14] RP FUNCTION OF THE MEDIATOR COMPLEX. RX PubMed=16263706; DOI=10.1074/jbc.m508253200; RA Takagi Y., Kornberg R.D.; RT "Mediator as a general transcription factor."; RL J. Biol. Chem. 281:80-89(2006). RN [15] RP SUBCELLULAR LOCATION. RX PubMed=16630888; DOI=10.1016/j.molcel.2006.03.023; RA Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G., RA van de Peppel J., Werner M., Holstege F.C.P.; RT "Genome-wide location of the coactivator mediator: binding without RT activation and transient Cdk8 interaction on DNA."; RL Mol. Cell 22:179-192(2006). RN [16] RP CHARACTERIZATION OF THE MEDIATOR COMPLEX, AND INTERACTION OF THE MEDIATOR RP COMPLEX WITH RNA POLYMERASE II. RX PubMed=17192271; DOI=10.1074/jbc.m609484200; RA Baidoobonso S.M., Guidi B.W., Myers L.C.; RT "Med19(Rox3) regulates intermodule interactions in the Saccharomyces RT cerevisiae mediator complex."; RL J. Biol. Chem. 282:5551-5559(2007). RN [17] RP ELECTRON MICROSCOPY OF MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE II. RX PubMed=12191485; DOI=10.1016/s1097-2765(02)00598-1; RA Davis J.A., Takagi Y., Kornberg R.D., Asturias F.J.; RT "Structure of the yeast RNA polymerase II holoenzyme: mediator conformation RT and polymerase interaction."; RL Mol. Cell 10:409-415(2002). RN [18] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 102-205 IN COMPLEX WITH SRB7. RX PubMed=15710619; DOI=10.1074/jbc.m413466200; RA Baumli S., Hoeppner S., Cramer P.; RT "A conserved mediator hinge revealed in the structure of the MED7-MED21 RT (Med7-Srb7) heterodimer."; RL J. Biol. Chem. 280:18171-18178(2005). 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. The Mediator complex, having a compact CC conformation in its free form, is recruited to promoters by direct CC interactions with regulatory proteins and serves for the assembly of a CC functional preinitiation complex with RNA polymerase II and the general CC transcription factors. The Mediator complex unfolds to an extended CC conformation and partially surrounds RNA polymerase II, specifically CC interacting with the unphosphorylated form of the C-terminal domain CC (CTD) of RNA polymerase II. The Mediator complex dissociates from the CC RNA polymerase II holoenzyme and stays at the promoter when CC transcriptional elongation begins. {ECO:0000269|PubMed:11555651, CC ECO:0000269|PubMed:16076843, ECO:0000269|PubMed:16263706}. CC -!- SUBUNIT: Component of the Mediator complex, which is composed of at CC least 21 subunits that form three structurally distinct submodules. The CC Mediator head module contains MED6, MED8, MED11, SRB4/MED17, CC SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the middle module CC contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, NUT2/MED10, SRB7/MED21 CC and SOH1/MED31, and the tail module contains MED2, PGD1/MED3, CC RGR1/MED14, GAL11/MED15 and SIN4/MED16. The head and the middle modules CC interact directly with RNA polymerase II, whereas the elongated tail CC module interacts with gene-specific regulatory proteins. MED7 interacts CC directly with MED1, MED4 and SRB7/MED21. {ECO:0000269|PubMed:11555651, CC ECO:0000269|PubMed:15710619, ECO:0000269|PubMed:17192271}. CC -!- INTERACTION: CC Q08278; Q12321: MED1; NbExp=3; IntAct=EBI-10674, EBI-32854; CC Q08278; Q12343: MED4; NbExp=4; IntAct=EBI-10674, EBI-31503; CC Q08278; Q06213: NUT2; NbExp=6; IntAct=EBI-10674, EBI-12414; CC Q08278; P47822: SRB7; NbExp=5; IntAct=EBI-10674, EBI-18046; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:16630888}. CC -!- MISCELLANEOUS: Present with 7598 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the Mediator complex subunit 7 family. CC {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; X95465; CAA64734.1; -; Genomic_DNA. DR EMBL; Z74877; CAA99156.1; -; Genomic_DNA. DR EMBL; AY692889; AAT92908.1; -; Genomic_DNA. DR EMBL; BK006948; DAA10650.1; -; Genomic_DNA. DR PIR; S66832; S66832. DR RefSeq; NP_014506.1; NM_001183389.1. DR PDB; 1YKE; X-ray; 3.30 A; A/C=102-205. DR PDB; 1YKH; X-ray; 3.00 A; A=102-205. DR PDB; 3FBI; X-ray; 2.80 A; A/C=2-83. DR PDB; 3FBN; X-ray; 3.01 A; A/C=2-83. DR PDB; 5OQM; EM; 5.80 A; i=1-222. DR PDB; 5SVA; EM; 15.30 A; U=1-222. DR PDBsum; 1YKE; -. DR PDBsum; 1YKH; -. DR PDBsum; 3FBI; -. DR PDBsum; 3FBN; -. DR PDBsum; 5OQM; -. DR PDBsum; 5SVA; -. DR SMR; Q08278; -. DR BioGRID; 34241; 503. DR ComplexPortal; CPX-3226; Core mediator complex. DR DIP; DIP-1435N; -. DR IntAct; Q08278; 46. DR MINT; Q08278; -. DR STRING; 4932.YOL135C; -. DR iPTMnet; Q08278; -. DR MaxQB; Q08278; -. DR PaxDb; Q08278; -. DR PRIDE; Q08278; -. DR EnsemblFungi; YOL135C_mRNA; YOL135C; YOL135C. DR GeneID; 853985; -. DR KEGG; sce:YOL135C; -. DR SGD; S000005495; MED7. DR VEuPathDB; FungiDB:YOL135C; -. DR eggNOG; KOG0570; Eukaryota. DR GeneTree; ENSGT00940000165241; -. DR HOGENOM; CLU_065214_0_1_1; -. DR InParanoid; Q08278; -. DR OMA; MQFDHKR; -. DR EvolutionaryTrace; Q08278; -. DR PRO; PR:Q08278; -. DR Proteomes; UP000002311; Chromosome XV. DR RNAct; Q08278; protein. DR GO; GO:0070847; C:core mediator complex; IDA:SGD. DR GO; GO:0016592; C:mediator complex; IBA:GO_Central. DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR InterPro; IPR037212; Med7/Med21-like. DR InterPro; IPR009244; Mediatior_Med7. DR Pfam; PF05983; Med7; 1. DR SUPFAM; SSF140718; SSF140718; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Nucleus; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..222 FT /note="Mediator of RNA polymerase II transcription subunit FT 7" FT /id="PRO_0000096393" FT REGION 34..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT HELIX 18..22 FT /evidence="ECO:0007829|PDB:3FBI" FT HELIX 25..39 FT /evidence="ECO:0007829|PDB:3FBI" FT HELIX 61..65 FT /evidence="ECO:0007829|PDB:3FBI" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:3FBI" FT HELIX 112..133 FT /evidence="ECO:0007829|PDB:1YKH" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:1YKH" FT HELIX 141..143 FT /evidence="ECO:0007829|PDB:1YKH" FT HELIX 144..164 FT /evidence="ECO:0007829|PDB:1YKH" FT HELIX 166..203 FT /evidence="ECO:0007829|PDB:1YKH" SQ SEQUENCE 222 AA; 25585 MW; A88301E4EF3223C9 CRC64; MSNDPGNEVS SLYPPPPPYV KFFTQSNLEK LPKYKEKKAA SAKQTAPNNS NGGSEEEITC ALDYLIPPPM PKNQQYRAFG SIWQVKDQLP DLESMGLTQL YKKSTENEST NYQYKIQELR KLLKSLLLNY LELIGVLSIN PDMYERKVEN IRTILVNIHH LLNEYRPHQS RESLIMLLEE QLEYKRGEIR EIEQVCKQVH DKLTSIQDTL RTGSQSPPSS SQ //