MED17_SCHPO
ID MED17_SCHPO Reviewed; 545 AA.
AC P87306;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 17;
DE AltName: Full=Mediator complex subunit 17;
DE AltName: Full=Suppressor of RNA polymerase B 4 homolog;
GN Name=med17; Synonyms=srb4; ORFNames=SPBC31F10.04c;
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 IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10625684; DOI=10.1074/jbc.275.2.1351;
RA Spaehr H., Beve J., Larsson T., Bergstroem J., Karlsson K.-A.,
RA Gustafsson C.M.;
RT "Purification and characterization of RNA polymerase II holoenzyme from
RT Schizosaccharomyces pombe.";
RL J. Biol. Chem. 275:1351-1356(2000).
RN [3]
RP FUNCTION.
RX PubMed=16630887; DOI=10.1016/j.molcel.2006.03.032;
RA Zhu X., Wiren M., Sinha I., Rasmussen N.N., Linder T., Holmberg S.,
RA Ekwall K., Gustafsson C.M.;
RT "Genome-wide occupancy profile of mediator and the Srb8-11 module reveals
RT interactions with coding regions.";
RL Mol. Cell 22:169-178(2006).
RN [4]
RP INTERACTION WITH MED18; 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:16630887}.
CC -!- SUBUNIT: Component of the Mediator complex. Interacts with med18, prk1
CC and rbp1. {ECO:0000269|PubMed:10625684, ECO:0000269|PubMed:17043218}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 17 family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAB10081.1; -; Genomic_DNA.
DR PIR; T40207; T40207.
DR RefSeq; NP_596566.1; NM_001022487.2.
DR PDB; 4H63; X-ray; 3.40 A; Q=78-545.
DR PDB; 5N9J; X-ray; 3.40 A; W=1-545.
DR PDB; 5U0P; EM; 4.40 A; Q=1-545.
DR PDB; 5U0S; EM; 7.80 A; Q=1-545.
DR PDBsum; 4H63; -.
DR PDBsum; 5N9J; -.
DR PDBsum; 5U0P; -.
DR PDBsum; 5U0S; -.
DR AlphaFoldDB; P87306; -.
DR SMR; P87306; -.
DR BioGRID; 276825; 5.
DR DIP; DIP-38758N; -.
DR IntAct; P87306; 8.
DR STRING; 4896.SPBC31F10.04c.1; -.
DR MaxQB; P87306; -.
DR PaxDb; P87306; -.
DR EnsemblFungi; SPBC31F10.04c.1; SPBC31F10.04c.1:pep; SPBC31F10.04c.
DR GeneID; 2540294; -.
DR KEGG; spo:SPBC31F10.04c; -.
DR PomBase; SPBC31F10.04c; -.
DR VEuPathDB; FungiDB:SPBC31F10.04c; -.
DR eggNOG; ENOG502QS9H; Eukaryota.
DR HOGENOM; CLU_499822_0_0_1; -.
DR InParanoid; P87306; -.
DR OMA; EAQICEN; -.
DR PRO; PR:P87306; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0070847; C:core mediator complex; IBA:GO_Central.
DR GO; GO:0016592; C:mediator complex; IDA: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 InterPro; IPR019313; Mediator_Med17.
DR PANTHER; PTHR13114; PTHR13114; 1.
DR Pfam; PF10156; Med17; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..545
FT /note="Mediator of RNA polymerase II transcription subunit
FT 17"
FT /id="PRO_0000096365"
FT REGION 148..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 101..130
FT /evidence="ECO:0007829|PDB:4H63"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 168..213
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4H63"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 242..246
FT /evidence="ECO:0007829|PDB:4H63"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 293..320
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:4H63"
FT TURN 338..340
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 342..348
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 374..407
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 425..447
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 451..457
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 459..461
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 466..472
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 479..486
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 487..490
FT /evidence="ECO:0007829|PDB:5N9J"
FT STRAND 493..497
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 509..512
FT /evidence="ECO:0007829|PDB:4H63"
FT STRAND 517..522
FT /evidence="ECO:0007829|PDB:4H63"
FT HELIX 523..534
FT /evidence="ECO:0007829|PDB:4H63"
FT TURN 535..537
FT /evidence="ECO:0007829|PDB:5N9J"
SQ SEQUENCE 545 AA; 62480 MW; 5BC16074D9D0A05B CRC64;
MAEEANKDAD ISSLSLSLDP EIIGGQNNFL ENNLQQIFQK IIQERGPFRD LKEEDLQKEL
QKESIKDESS AKSSETENVL EFATLDSKRN VNDTEVESMD SQAYKKELIE QIMIAQTECS
LALDMTSLLL SKFKENSIET ISPFLKSTVP PSSLQFSRSQ PPESKESDAT LAKCWKEKSL
TSSCKFLFEA KERLTSVVET EHEYYTELVK VKEASWPLFN SQGSNHLSVQ YSCLGGISLG
LGLIRMKPES KSFEVQSSLL YSQAALKISI LNKDRDEIGS STWSWPSQNC NSVLLKDIYK
LQEILFEMDI WNSLLQEAQS CGNQGVNFTG DEILVPISDD HVVRITLETS SKNTESGFTE
DKKSNEDTST NFVTIKQEKE LLKCLCDTLN AIAHILFLKH CRKSDRRSQQ PELYMAIDAN
APLILRPLIF YYNLNQESLE FQRWLKQRDI SFKFMPNYPW EKAKDFLELE NSLSINRLSI
SWRIMVSNFE PAIFIQHTPT LHGTDKSVWR CKDQYSSNQF SSLKNVCQYI EHHINSLSRR
SKKTE
