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 15-MAR-2017, entry version 139. 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; OC Saccharomycetes; 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>3.3.CO;2-J; RA Aldea M., Piedrafita L., Casas C., Casamayor A., Khalid H., RA Balcells L., 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 RT gene for a possible glycophospholipid-anchored surface protein and six RT other 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., RA Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., RA Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., RA Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H., RA Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., RA Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., RA 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., RA Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., RA Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., RA Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., RA Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., RA Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., RA Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., RA Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., RA 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., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT 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., RA Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., RA Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., RA Kolodner R.D., LaBaer J.; RT "Approaching a complete repository of sequence-verified protein- RT encoding clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF MEDIATOR RP COMPLEX. RX PubMed=9420330; DOI=10.1101/gad.12.1.45; RA Myers L.C., Gustafsson C.M., Bushnell D.A., Lui M., RA Erdjument-Bromage H., Tempst P., Kornberg R.D.; RT "The Med proteins of yeast and their function through the RNA RT polymerase II carboxy-terminal domain."; RL Genes Dev. 12:45-54(1998). RN [6] RP INTERACTION WITH MED1; MED4 AND SRB7, FUNCTION OF THE MEDIATOR RP COMPLEX, AND INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE RP 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., RA Dephoure N., 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., RA Hinnebusch A.G., Holmberg S., Holstege F.C.P., Jaehning J.A., RA Kim Y.-J., Kuras L., Leutz A., Lis J.T., Meisterernest M., RA Naeaer A.M., Nasmyth K., Parvin J.D., Ptashne M., Reinberg D., RA Ronne H., Sadowski I., Sakurai H., Sipiczki M., Sternberg P.W., RA Stillman D.J., Strich R., Struhl K., Svejstrup J.Q., Tuck S., RA Winston F., Roeder R.G., Kornberg R.D.; RT "A unified nomenclature for protein subunits of mediator complexes RT linking 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 RT 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 RT 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 RT transcription 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 RP MEDIATOR 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 RP 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 RT conformation 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- RT MED21 (Med7-Srb7) heterodimer."; RL J. Biol. Chem. 280:18171-18178(2005). CC -!- FUNCTION: Component of the Mediator complex, a coactivator CC involved in the regulated transcription of nearly all RNA CC polymerase II-dependent genes. Mediator functions as a bridge to CC convey information from gene-specific regulatory proteins to the CC basal RNA polymerase II transcription machinery. The Mediator CC complex, having a compact conformation in its free form, is CC recruited to promoters by direct interactions with regulatory CC proteins and serves for the assembly of a functional preinitiation CC complex with RNA polymerase II and the general transcription CC factors. The Mediator complex unfolds to an extended conformation CC and partially surrounds RNA polymerase II, specifically CC interacting with the unphosphorylated form of the C-terminal CC domain (CTD) of RNA polymerase II. The Mediator complex CC dissociates from the RNA polymerase II holoenzyme and stays at the CC promoter when transcriptional elongation begins. CC {ECO:0000269|PubMed:11555651, ECO:0000269|PubMed:16076843, CC ECO:0000269|PubMed:16263706}. CC -!- SUBUNIT: Component of the Mediator complex, which is composed of CC at least 21 subunits that form three structurally distinct CC submodules. The Mediator head module contains MED6, MED8, MED11, CC SRB4/MED17, SRB5/MED18, ROX3/MED19, SRB2/MED20 and SRB6/MED22, the CC middle module contains MED1, MED4, NUT1/MED5, MED7, CSE2/MED9, CC NUT2/MED10, SRB7/MED21 and SOH1/MED31, and the tail module CC contains MED2, PGD1/MED3, RGR1/MED14, GAL11/MED15 and SIN4/MED16. CC The head and the middle modules interact directly with RNA CC polymerase II, whereas the elongated tail module interacts with CC gene-specific regulatory proteins. MED7 interacts directly with CC MED1, MED4 and SRB7/MED21. {ECO:0000269|PubMed:11555651, CC ECO:0000269|PubMed:15710619, ECO:0000269|PubMed:17192271}. CC -!- INTERACTION: CC P33308:CSE2; NbExp=3; IntAct=EBI-10674, EBI-5174; CC Q12321:MED1; NbExp=4; IntAct=EBI-10674, EBI-32854; CC Q12343:MED4; NbExp=5; IntAct=EBI-10674, EBI-31503; CC Q06213:NUT2; NbExp=6; IntAct=EBI-10674, EBI-12414; CC P47822:SRB7; NbExp=6; 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 CC medium. {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; 5SVA; EM; 15.30 A; U=1-222. DR PDBsum; 1YKE; -. DR PDBsum; 1YKH; -. DR PDBsum; 3FBI; -. DR PDBsum; 3FBN; -. DR PDBsum; 5SVA; -. DR ProteinModelPortal; Q08278; -. DR SMR; Q08278; -. DR BioGrid; 34241; 461. DR DIP; DIP-1435N; -. DR IntAct; Q08278; 47. DR MINT; MINT-390686; -. DR iPTMnet; Q08278; -. DR MaxQB; Q08278; -. DR PRIDE; Q08278; -. DR EnsemblFungi; YOL135C; YOL135C; YOL135C. DR GeneID; 853985; -. DR KEGG; sce:YOL135C; -. DR EuPathDB; FungiDB:YOL135C; -. DR SGD; S000005495; MED7. DR GeneTree; ENSGT00530000064187; -. DR HOGENOM; HOG000000771; -. DR InParanoid; Q08278; -. DR KO; K15148; -. DR OMA; DRAFELK; -. DR OrthoDB; EOG092C5KDU; -. DR BioCyc; YEAST:G3O-33529-MONOMER; -. DR EvolutionaryTrace; Q08278; -. DR PRO; PR:Q08278; -. DR Proteomes; UP000002311; Chromosome XV. DR GO; GO:0070847; C:core mediator complex; IDA:SGD. DR GO; GO:0016592; C:mediator complex; IBA:GO_Central. DR GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IEA:InterPro. DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:SGD. DR GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:SGD. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR009244; Mediatior_Med7. DR PANTHER; PTHR21428; PTHR21428; 1. DR Pfam; PF05983; Med7; 1. PE 1: Evidence at protein level; KW 3D-structure; Activator; Complete proteome; Nucleus; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1 222 Mediator of RNA polymerase II FT transcription subunit 7. FT /FTId=PRO_0000096393. FT HELIX 18 22 {ECO:0000244|PDB:3FBI}. FT HELIX 25 39 {ECO:0000244|PDB:3FBI}. FT HELIX 61 65 {ECO:0000244|PDB:3FBI}. FT HELIX 74 76 {ECO:0000244|PDB:3FBI}. FT HELIX 112 133 {ECO:0000244|PDB:1YKH}. FT STRAND 135 137 {ECO:0000244|PDB:1YKH}. FT HELIX 141 143 {ECO:0000244|PDB:1YKH}. FT HELIX 144 164 {ECO:0000244|PDB:1YKH}. FT HELIX 166 203 {ECO:0000244|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 //