MED31_SCHPO
ID MED31_SCHPO Reviewed; 139 AA.
AC Q9USH1;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 31;
DE AltName: Full=Cell separation protein sep10;
DE AltName: Full=Mediator complex subunit 31;
DE AltName: Full=Soh1 homolog;
GN Name=med31; Synonyms=sep10; ORFNames=SPCP31B10.03c;
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 [GENOMIC DNA].
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 [2]
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Mediator complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 31 family.
CC {ECO:0000305}.
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DR EMBL; AF284581; AAG02413.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB58369.1; -; Genomic_DNA.
DR PIR; T41693; T41693.
DR RefSeq; NP_587859.1; NM_001022852.2.
DR PDB; 5N9J; X-ray; 3.40 A; R=1-139.
DR PDB; 5U0P; EM; 4.40 A; 3=1-139.
DR PDB; 5U0S; EM; 7.80 A; 3=1-139.
DR PDBsum; 5N9J; -.
DR PDBsum; 5U0P; -.
DR PDBsum; 5U0S; -.
DR AlphaFoldDB; Q9USH1; -.
DR SMR; Q9USH1; -.
DR BioGRID; 276067; 6.
DR IntAct; Q9USH1; 2.
DR STRING; 4896.SPCP31B10.03c.1; -.
DR MaxQB; Q9USH1; -.
DR PaxDb; Q9USH1; -.
DR EnsemblFungi; SPCP31B10.03c.1; SPCP31B10.03c.1:pep; SPCP31B10.03c.
DR GeneID; 2539504; -.
DR KEGG; spo:SPCP31B10.03c; -.
DR PomBase; SPCP31B10.03c; med31.
DR VEuPathDB; FungiDB:SPCP31B10.03c; -.
DR eggNOG; KOG4086; Eukaryota.
DR HOGENOM; CLU_071681_3_1_1; -.
DR InParanoid; Q9USH1; -.
DR OMA; LSNPWYL; -.
DR PhylomeDB; Q9USH1; -.
DR PRO; PR:Q9USH1; -.
DR Proteomes; UP000002485; Chromosome III.
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; TAS:PomBase.
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 Gene3D; 1.10.10.1340; -; 1.
DR InterPro; IPR038089; Med31_sf.
DR InterPro; IPR008831; Mediator_Med31.
DR PANTHER; PTHR13186; PTHR13186; 1.
DR Pfam; PF05669; Med31; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..139
FT /note="Mediator of RNA polymerase II transcription subunit
FT 31"
FT /id="PRO_0000212533"
FT REGION 115..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 13..28
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 30..38
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 70..78
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 81..88
FT /evidence="ECO:0007829|PDB:5N9J"
FT HELIX 90..103
FT /evidence="ECO:0007829|PDB:5N9J"
SQ SEQUENCE 139 AA; 16896 MW; ACC93D4694A195F5 CRC64;
METKWLLSKV PDDKSRFEIE LEFVQMLSNP WYLNFLAQHK YFEDEAFLQY LEYMEYWREP
EYVKFIIYPT CLHMLTLLKN PQFRNDISRA DLSKQVNDEI YYEWLGKGLQ QYGSADDATL
SQPQQEEDEK KVDVKKENE
