ID MED7_YEAST STANDARD; PRT; 222 AA. AC Q08278; DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 25-JUL-2006, entry version 45. DE RNA polymerase II mediator complex subunit 7 (RNA polymerase II DE transcriptional regulation mediator 7). GN Name=MED7; OrderedLocusNames=YOL135C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 96604 / S288c / FY1679; RX MEDLINE=97051593; 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 96604 / S288c / FY1679; RX MEDLINE=97313270; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RA Marsischky G., Rolfs A., Richardson A., Kane M., Baqui M., Taycher E., RA Hu Y., Vannberg F., Weger J., Kramer J., Moreira D., Kelley F., RA Zuo D., Raphael J., Hogle C., Jepson D., Williamson J., Camargo A., RA Gonzaga L., Vasconcelos A.T., Simpson A., Kolodner R., Harlow E., RA LaBaer J.; RT "Creation of the YFLEX clone resource: cloning of Saccharomyces RT cerevisiae ORFs in the Gateway recombinational cloning system."; RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY, AND COMPONENT OF MEDIATOR RP COMPLEX. RX PubMed=9420330; 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 [5] RP INTERACTION WITH MED1; MED4 AND SRB7. 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 [6] RP ELECTRON MICROSCOPY OF MEDIATOR COMPLEX IN COMPLEX WITH RNA POLYMERASE RP II. RX MEDLINE=22179692; 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 [7] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923954; 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 MEDLINE=22923965; 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 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., Jaehning J.A., Kim Y.-J., RA Kuras L., Leutz A., Lis J.T., Meisterernest M., Naar A.M., Nasmyth K., RA Parvin J.D., Ptashne M., Reinberg D., Ronne H., Sadowski I., RA Sakurai H., Sipiczki M., Sternberg P.W., Stillman D.J., Strich R., RA Struhl K., Svejstrup J.Q., Tuck S., Winston F., Roeder R.G., RA 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 [10] 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 regulated gene transcription of nearly all RNA CC polymerase II-dependent genes. The mediator functions as a bridge CC to convey information from gene-specific regulatory proteins to CC the 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 -!- SUBUNIT: The RNA polymerase II mediator complex is composed of at CC 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. CC -!- INTERACTION: CC P43592:FAR7; NbExp=1; IntAct=EBI-10674, EBI-22932; CC P38633:SOH1; NbExp=1; IntAct=EBI-10674, EBI-17658; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- MISCELLANEOUS: Present with 7598 molecules/cell. CC -!- SIMILARITY: Belongs to the mediator complex subunit 7 family. 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 PIR; S66832; S66832. DR PDB; 1YKE; X-ray; A/C=102-205. DR PDB; 1YKH; X-ray; A=102-205. DR IntAct; Q08278; -. DR GermOnline; 143557; -. DR Ensembl; YOL135C; Saccharomyces cerevisiae. DR GenomeReviews; Y13140_GR; YOL135C. DR SGD; S000005495; MED7. DR BioCyc; SCER-S28-01:SCER-S28-01-005418-MONOMER; -. DR LinkHub; Q08278; -. DR GO; GO:0000119; C:mediator complex; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0016455; F:RNA polymerase II transcription mediator ac...; IDA. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA. DR InterPro; IPR009244; MED7. DR Pfam; PF05983; MED7; 1. KW 3D-structure; Activator; Complete proteome; Nuclear protein; KW Transcription; Transcription regulation. FT CHAIN 1 222 RNA polymerase II mediator complex FT subunit 7. FT /FTId=PRO_0000096393. FT HELIX 112 133 FT TURN 134 134 FT STRAND 135 137 FT HELIX 141 164 FT TURN 165 165 FT HELIX 166 203 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 //