MED7_YEAST
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 03-AUG-2022, entry version 172.
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}.
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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 AlphaFoldDB; Q08278; -.
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; PQHFDRR; -.
DR BioCyc; YEAST:G3O-33529-MON; -.
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:0005634; C:nucleus; IDA:ComplexPortal.
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:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:ComplexPortal.
DR Gene3D; 6.10.140.200; -; 1.
DR InterPro; IPR037212; Med7/Med21-like.
DR InterPro; IPR009244; Mediatior_Med7.
DR InterPro; IPR044888; Mediatior_Med7_sf.
DR PANTHER; PTHR21428; PTHR21428; 1.
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
