ID   MED29_CAEEL             Reviewed;         441 AA.
AC   Q9XUS2;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 29;
DE   AltName: Full=Mediator complex subunit 29;
GN   Name=mdt-29; ORFNames=K08E3.8;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, INTERACTION WITH SEL-7 AND SEL-8, AND DISRUPTION PHENOTYPE.
RX   PubMed=15020414; DOI=10.1534/genetics.166.1.151;
RA   Chen J., Li X., Greenwald I.;
RT   "sel-7, a positive regulator of lin-12 activity, encodes a novel nuclear
RT   protein in Caenorhabditis elegans.";
RL   Genetics 166:151-160(2004).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=19500563; DOI=10.1016/j.ydbio.2009.05.574;
RA   Xia D., Huang X., Zhang H.;
RT   "The temporally regulated transcription factor sel-7 controls developmental
RT   timing in C. elegans.";
RL   Dev. Biol. 332:246-257(2009).
CC   -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC       the regulated transcription of nearly all RNA polymerase II-dependent
CC       genes (By similarity). Mediator functions as a bridge to convey
CC       information from gene-specific regulatory proteins to the basal RNA
CC       polymerase II transcription machinery (By similarity). Mediator is
CC       recruited to promoters by direct interactions with regulatory proteins
CC       and serves as a scaffold for the assembly of a functional pre-
CC       initiation complex with RNA polymerase II and the general transcription
CC       factors (By similarity). Involved in development of gonad and seam
CC       cells (PubMed:19500563, PubMed:15020414). Plays a role in temporal
CC       regulation of seam cell division, probably acting as a part of the
CC       Mediator complex (PubMed:19500563). {ECO:0000250|UniProtKB:Q9NX70,
CC       ECO:0000269|PubMed:15020414, ECO:0000269|PubMed:19500563}.
CC   -!- SUBUNIT: Component of the Mediator complex (By similarity). May
CC       interact with sel-7 and sel-8 (PubMed:15020414).
CC       {ECO:0000250|UniProtKB:Q9NX70, ECO:0000269|PubMed:15020414}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown has no effect on seam
CC       cell division or differentiation, but in a sel-7 mutant background
CC       decreases number of seam cells (PubMed:19500563). Partially suppresses
CC       the hermaphrodite gonadal development defect in a lin-12 mutant
CC       background (PubMed:15020414). {ECO:0000269|PubMed:15020414,
CC       ECO:0000269|PubMed:19500563}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 29 family.
CC       {ECO:0000305}.
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DR   EMBL; BX284603; CAB04600.1; -; Genomic_DNA.
DR   PIR; T23461; T23461.
DR   RefSeq; NP_499847.1; NM_067446.4.
DR   AlphaFoldDB; Q9XUS2; -.
DR   BioGRID; 41982; 8.
DR   DIP; DIP-25904N; -.
DR   IntAct; Q9XUS2; 6.
DR   STRING; 6239.K08E3.8; -.
DR   EPD; Q9XUS2; -.
DR   PaxDb; Q9XUS2; -.
DR   PeptideAtlas; Q9XUS2; -.
DR   EnsemblMetazoa; K08E3.8.1; K08E3.8.1; WBGene00007025.
DR   EnsemblMetazoa; K08E3.8.2; K08E3.8.2; WBGene00007025.
DR   GeneID; 176817; -.
DR   KEGG; cel:CELE_K08E3.8; -.
DR   UCSC; K08E3.8; c. elegans.
DR   CTD; 176817; -.
DR   WormBase; K08E3.8; CE18874; WBGene00007025; mdt-29.
DR   eggNOG; ENOG502S549; Eukaryota.
DR   HOGENOM; CLU_597499_0_0_1; -.
DR   InParanoid; Q9XUS2; -.
DR   OMA; GEMANVN; -.
DR   OrthoDB; 1339572at2759; -.
DR   PRO; PR:Q9XUS2; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00007025; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; ISS:WormBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0046331; P:lateral inhibition; IGI:WormBase.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IGI:WormBase.
DR   GO; GO:0042659; P:regulation of cell fate specification; IGI:WormBase.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   InterPro; IPR021018; Mediator_Med29_met.
DR   Pfam; PF11568; Med29; 1.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..441
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   29"
FT                   /id="PRO_0000305706"
FT   REGION          1..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          416..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..158
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..441
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  48286 MW;  9EE26F4F97F9C540 CRC64;
     MSGQGPPPSM TPQQQHMLMQ QQQQQQMMRQ QQMQQQQMQQ QRQQQIQQQA QQPYQRARTP
     QMVPQGGSPG GAHLQMHPHL QPQGQMQPRS PLVGAQLQAP SSVPTAANPT TPQMMQQQMG
     MNQPMSLPPT HVSRPGSVAP PSSVPVNLQH TSGAPGLPGS QMEHQYPMHL QPQQQTLSRP
     GSQQSQHIQQ PGSIQRPGSV LAPGSIPPGG PASQTGPQSI QVFGPGSVQP PGSTQAPSSV
     QPASTFNPGS IQAPASQQPP ASVQPPPSAA SGSTVAGAQS SKEPLKPNEE QIRMVQDPVD
     LVRNLVQKDL RNSLVEMNKR GAELVRQKQE GEVNEDGKAQ YSRATNDFHA VCDEIDRTLT
     TVLETAKQLS KLDKVFFDRS SRDLDGEVMV NSVQNFVDNT EIVQRMFDDT IGSVTSSMES
     MRRRQKKWED QHKNDDVEMM E