ID   SRB8_PICST              Reviewed;        1654 AA.
AC   A3GF47;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 2.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 12;
DE   AltName: Full=Mediator complex subunit 12;
GN   Name=SRB8; Synonyms=MED12; ORFNames=PICST_86078;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(2007).
CC   -!- FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a
CC       regulatory module of the Mediator complex which is itself involved in
CC       regulation of basal and activated RNA polymerase II-dependent
CC       transcription. The SRB8-11 complex may be involved in the
CC       transcriptional repression of a subset of genes regulated by Mediator.
CC       It may inhibit the association of the Mediator complex with RNA
CC       polymerase II to form the holoenzyme complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the SRB8-11 complex, which itself associates with
CC       the Mediator complex. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 12 family.
CC       {ECO:0000305}.
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DR   EMBL; AAVQ01000001; EAZ63285.2; -; Genomic_DNA.
DR   RefSeq; XP_001387308.2; XM_001387271.1.
DR   AlphaFoldDB; A3GF47; -.
DR   STRING; 4924.XP_001387308.2; -.
DR   PRIDE; A3GF47; -.
DR   EnsemblFungi; EAZ63285; EAZ63285; PICST_86078.
DR   GeneID; 4850896; -.
DR   KEGG; pic:PICST_86078; -.
DR   eggNOG; KOG4522; Eukaryota.
DR   HOGENOM; CLU_003142_0_0_1; -.
DR   InParanoid; A3GF47; -.
DR   OMA; EKFEIHW; -.
DR   OrthoDB; 285540at2759; -.
DR   Proteomes; UP000002258; Chromosome 1.
DR   GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR   GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   InterPro; IPR019035; Mediator_Med12.
DR   Pfam; PF09497; Med12; 1.
DR   SMART; SM01281; Med12; 1.
PE   3: Inferred from homology;
KW   Activator; Nucleus; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1654
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   12"
FT                   /id="PRO_0000312977"
FT   REGION          52..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1481..1530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..70
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1481..1499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1515..1530
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1654 AA;  189211 MW;  10550E6CBCF9B173 CRC64;
     MSKARSRNSL LSSSNRAQFG NSTQDELLKL KFSMEKPDIG LYPLNDLDNG VDLNGDNSRS
     QHTAGSGVLS GNEVTYPDYK PWKDHTALPN DKKEQEHQKL NNAAYLNKGY FETPVVANEY
     YSARNLIQAT VFSSTENCNE VLKELSQHLA NAYKTRNEII NKIKYESNNF KIPPRVTLTA
     SKKESWLKDL ANPDLALSKI AEKIPHGIRN KILIDAVCNK SVPINRALWF TKCVLFGELV
     ALRRKHQSRM SLNSPIPQSL DINTPEKFEI HWLQEWTQQV ADYIYKFSKE SSNFNTIERK
     QYYMNKMTYL LTYIQALYVE FLLDKSFFLA LIIKFLKEGL PLDPLHVSEL LSSTRSETDD
     LIQESWIEDL DLNYGQRLFA LTLIKIFWND ILKFDYICKE LSETLLLNYL FISKINAYSF
     KQSHVQNHKA SIPEPLRQKI LDMIGDTITY LFKFNTNVFI IPNYWMLING VLFTILLNKN
     VTKTEGELDE ISKQFDLIKY RNESLILNMR NVQPSITDRA TPNSAGRRGS SIWNQSFVSA
     AESTATKIDI FDNEATFINR SSDDILKIIS QLDSLKLNDE LANFLKPVTS SSALTSTAIK
     GCPKWRTNLK VVLYWCITRH RNSRESSEDI LIICNFLKRK VLQTLGPTRS SSQLKAEFES
     EILDIIYNIA DTNSSKVVNY DLYVLINELY QLKVLTIASY LRKLIASGIF YVAPDAEDNI
     LNDNSNSLVK THLSILQNLP VINNRQCDSI LKKWTSTGFN FKEKFEMGQE ILKRELIDRI
     VNNTFDDQFE SHIVYVKDLN VGLKFLLVNW VTNELKSAIT ESPKLIHINP LIISNLFNFY
     SICDNLTVFF KVLVKFILKN EGGMIIFYLE SLYLIARLII KHFKLVKFIA GNSYGSNSTA
     YELFKLIIQN YKDCKTREFD YFKFDQVWNF IDTAVESNYS SDKNTDSRSS GKRSGIFNKE
     QFDSPMKINT SENVIAKMED RYTSADFRND LDLLLESTFQ PMDSNEVSEV VATLKLEFEE
     NEMKSHRNVV PKVLDLLKSN LTEESEGLAA KLLINSQYLI KSDDVNAFDK LVQDYILELV
     KSDMEILLVA KFLKKLIVHE IIRINDLFAF FEPIAEDPAF RVKLKALMFD LVIGLSDEER
     EYLSNSQILQ LEIMRQWYRE RSTSSFLVLI LKGIKTIEGS IFDCPLMEKY GSSIFRILNA
     LIVANTKLLS DELISKISTE DSIRLLSTLN NENFTPINSL QDLERIASEV DEFNLPIFQL
     LLRVLTIKEL SPLQENEIQE RLKVLLESFL ENLSFGFTPM NSYFGELFIY LPWEYVVSIL
     GMLEDKFLCS TTFNFDQWDN DKSVLSLTNS VGNTNLLPVF NDYFKKFSSS SSNVVESSSS
     FFQALSKFLS KLLLIVNSDN CLEDTFEDTS SAISIFLRIL IIHKLTLTRL IVTQDGEQFQ
     FIKNLILLIN SKFIAEGNEK LRILLYDLLL LMKSSVTEEV SKQTENELSE GTSPGFGMTA
     QSPPPVEDAS KITEPLSSAR PSSEAASFQT NPISTYDQVS SLFNLPEPTE TNPFKDYITE
     DRVECALTLS EDELQSGGDI HGFNESNLVL ISSSNDSTFS GAFALITNPH QRPKGQPFKL
     RSFEILEGTS TTSLNDGCIN LQLFDSYTTK ENPP