MD26C_ARATH
ID MD26C_ARATH Reviewed; 353 AA.
AC F4KFC7; Q93Z47; Q9FIC1;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Probable mediator of RNA polymerase II transcription subunit 26c;
GN Name=MED26C; Synonyms=MED26_3; OrderedLocusNames=At5g09850;
GN ORFNames=MYH9.6;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=22021418; DOI=10.1104/pp.111.188300;
RA Mathur S., Vyas S., Kapoor S., Tyagi A.K.;
RT "The Mediator complex in plants: structure, phylogeny, and expression
RT profiling of representative genes in a dicot (Arabidopsis) and a monocot
RT (rice) during reproduction and abiotic stress.";
RL Plant Physiol. 157:1609-1627(2011).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-84, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(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. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. The Mediator complex, having a compact
CC conformation in its free form, is recruited to promoters by direct
CC interactions with regulatory proteins and serves for the assembly of a
CC functional preinitiation complex with RNA polymerase II and the general
CC transcription factors (By similarity). May play a role in transcription
CC elongation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the Mediator complex. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 26 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL25557.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB09406.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB016893; BAB09406.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED91455.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69897.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69898.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM69899.1; -; Genomic_DNA.
DR EMBL; AY058141; AAL25557.1; ALT_FRAME; mRNA.
DR EMBL; AY093710; AAM10334.1; -; mRNA.
DR RefSeq; NP_001331542.1; NM_001343073.1.
DR RefSeq; NP_001331543.1; NM_001343074.1.
DR RefSeq; NP_001331544.1; NM_001343071.1.
DR RefSeq; NP_568218.1; NM_121022.3.
DR AlphaFoldDB; F4KFC7; -.
DR SMR; F4KFC7; -.
DR STRING; 3702.AT5G09850.1; -.
DR iPTMnet; F4KFC7; -.
DR PaxDb; F4KFC7; -.
DR PRIDE; F4KFC7; -.
DR ProteomicsDB; 250831; -.
DR EnsemblPlants; AT5G09850.1; AT5G09850.1; AT5G09850.
DR EnsemblPlants; AT5G09850.2; AT5G09850.2; AT5G09850.
DR EnsemblPlants; AT5G09850.4; AT5G09850.4; AT5G09850.
DR EnsemblPlants; AT5G09850.5; AT5G09850.5; AT5G09850.
DR GeneID; 830845; -.
DR Gramene; AT5G09850.1; AT5G09850.1; AT5G09850.
DR Gramene; AT5G09850.2; AT5G09850.2; AT5G09850.
DR Gramene; AT5G09850.4; AT5G09850.4; AT5G09850.
DR Gramene; AT5G09850.5; AT5G09850.5; AT5G09850.
DR KEGG; ath:AT5G09850; -.
DR Araport; AT5G09850; -.
DR TAIR; locus:2178173; AT5G09850.
DR eggNOG; ENOG502QTFQ; Eukaryota.
DR HOGENOM; CLU_071165_0_0_1; -.
DR InParanoid; F4KFC7; -.
DR OMA; TMREQKD; -.
DR OrthoDB; 1161867at2759; -.
DR PRO; PR:F4KFC7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4KFC7; baseline and differential.
DR Genevisible; F4KFC7; AT.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR044790; MD26C-like.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR PANTHER; PTHR47210; PTHR47210; 1.
DR Pfam; PF08711; Med26; 1.
DR SMART; SM00509; TFS2N; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Elongation factor; Nucleus; Phosphoprotein;
KW Protein biosynthesis; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..353
FT /note="Probable mediator of RNA polymerase II transcription
FT subunit 26c"
FT /id="PRO_0000418355"
FT DOMAIN 125..199
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT REGION 225..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 298..327
FT /evidence="ECO:0000255"
FT COMPBIAS 225..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..283
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19376835"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157,
FT ECO:0007744|PubMed:19245862"
SQ SEQUENCE 353 AA; 40058 MW; 75E3F07E68A9FDDE CRC64;
MDLDDFRSVM DNAGVDVWTF IDTAILVASL DYGQELKRRR DNIVERLYAT SMANKCRNCD
FGGGGNVTEA AIGRVNNGRV HEETEEEDEE GVTAAAEEEV REKSVNVEDD DDFDPFAGLF
DDEQKSIVEI KEKLEDPDLS EESLVELLQN LEDMDITFQA LQETDIGRHV NRVRKHPSNN
VRRLAKQLVK KWKETVDEWV KFNQPGDLEP PSLIADEDSP VQKALHNGSR QQVPDFGYSP
VPQNGYSSSS KNSNITEPER KPRPVAPQPR RESPSPAKPS RPSPSQQTIP RDKEHKEVDF
DTARKRLQQN YRQAENAKKQ RTIQVMDIHD IPKPKKGGFF PRKGGSSQGG RHW
