MED18_SCHPO
ID MED18_SCHPO Reviewed; 207 AA.
AC O14198; Q96VF9;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 14-AUG-2001, sequence version 3.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 18;
DE AltName: Full=Cell separation protein sep11;
DE AltName: Full=Mediator complex subunit 18;
DE AltName: Full=RNA polymerase II mediator complex protein pmc6;
GN Name=med18; Synonyms=pmc6, sep11; ORFNames=SPAC5D6.05;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-172, AND FUNCTION.
RX PubMed=12471453; DOI=10.1007/s00438-002-0773-3;
RA Szilagyi Z., Grallert A., Nemeth N., Sipiczki M.;
RT "The Schizosaccharomyces pombe genes sep10 and sep11 encode putative
RT general transcriptional regulators involved in multiple cellular
RT processes.";
RL Mol. Genet. Genomics 268:553-562(2002).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RX PubMed=11572939; DOI=10.1073/pnas.211253898;
RA Spaehr H., Samuelsen C.O., Baraznenok V., Ernest I., Huylebroeck D.,
RA Remacle J.E., Samuelsson T., Kieselbach T., Holmberg S., Gustafsson C.M.;
RT "Analysis of Schizosaccharomyces pombe mediator reveals a set of essential
RT subunits conserved between yeast and metazoan cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11985-11990(2001).
RN [4]
RP INTERACTION WITH MED17; PRK1 AND RBP1.
RX PubMed=17043218; DOI=10.1073/pnas.0607483103;
RA Elmlund H., Baraznenok V., Lindahl M., Samuelsen C.O., Koeck P.J.B.,
RA Holmberg S., Hebert H., Gustafsson C.M.;
RT "The cyclin-dependent kinase 8 module sterically blocks Mediator
RT interactions with RNA polymerase II.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15788-15793(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. {ECO:0000269|PubMed:12471453}.
CC -!- SUBUNIT: Component of the Mediator complex. Interacts with med17, prk1
CC and rbp1. {ECO:0000269|PubMed:11572939, ECO:0000269|PubMed:17043218}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 18 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; CU329670; CAB10853.2; -; Genomic_DNA.
DR EMBL; AJ313525; CAC44901.1; -; mRNA.
DR PIR; T38961; T38961.
DR RefSeq; NP_593364.1; NM_001018796.2.
DR PDB; 3C0T; X-ray; 2.40 A; A=1-207.
DR PDB; 4H63; X-ray; 3.40 A; R=1-207.
DR PDB; 5N9J; X-ray; 3.40 A; X=1-207.
DR PDB; 5U0P; EM; 4.40 A; R=1-207.
DR PDB; 5U0S; EM; 7.80 A; R=1-207.
DR PDBsum; 3C0T; -.
DR PDBsum; 4H63; -.
DR PDBsum; 5N9J; -.
DR PDBsum; 5U0P; -.
DR PDBsum; 5U0S; -.
DR AlphaFoldDB; O14198; -.
DR SMR; O14198; -.
DR BioGRID; 278413; 11.
DR DIP; DIP-38760N; -.
DR IntAct; O14198; 4.
DR STRING; 4896.SPAC5D6.05.1; -.
DR MaxQB; O14198; -.
DR PaxDb; O14198; -.
DR EnsemblFungi; SPAC5D6.05.1; SPAC5D6.05.1:pep; SPAC5D6.05.
DR GeneID; 2541925; -.
DR KEGG; spo:SPAC5D6.05; -.
DR PomBase; SPAC5D6.05; med18.
DR VEuPathDB; FungiDB:SPAC5D6.05; -.
DR eggNOG; ENOG502S7EN; Eukaryota.
DR HOGENOM; CLU_1327068_0_0_1; -.
DR InParanoid; O14198; -.
DR OMA; SHEYIVQ; -.
DR EvolutionaryTrace; O14198; -.
DR PRO; PR:O14198; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0070847; C:core mediator complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0016592; C:mediator complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:PomBase.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IC:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR InterPro; IPR019095; Mediator_Med18.
DR PANTHER; PTHR13321; PTHR13321; 1.
DR Pfam; PF09637; Med18; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..207
FT /note="Mediator of RNA polymerase II transcription subunit
FT 18"
FT /id="PRO_0000096367"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:3C0T"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3C0T"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:3C0T"
FT STRAND 26..41
FT /evidence="ECO:0007829|PDB:3C0T"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:3C0T"
FT STRAND 55..61
FT /evidence="ECO:0007829|PDB:3C0T"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:3C0T"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:3C0T"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:3C0T"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 95..104
FT /evidence="ECO:0007829|PDB:3C0T"
FT HELIX 109..115
FT /evidence="ECO:0007829|PDB:3C0T"
FT STRAND 118..133
FT /evidence="ECO:0007829|PDB:3C0T"
FT STRAND 136..148
FT /evidence="ECO:0007829|PDB:3C0T"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:3C0T"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:3C0T"
FT HELIX 179..196
FT /evidence="ECO:0007829|PDB:3C0T"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:3C0T"
SQ SEQUENCE 207 AA; 24027 MW; A3A3B518E3D85A62 CRC64;
MQELYLLGVV PSRRFEAVVN SLSKTLDGPK TILEFWVVYR PKDVPPNLPR QPDSWLRLCS
NIESHDETDT EWSKNTQWSM YLEGNSEPKR EDKCGIRPVN RAKLTNGSVT EFVEKMGYEF
SHEYIIQGLE YFFFDTTVRI YQTLIPSQQR SIKPPFHPMN EEQPWILHVY THVADASNQV
AMAKAEANLT KVKTLLSAFC DLKNVRL
