MD33B_ARATH
ID MD33B_ARATH Reviewed; 1275 AA.
AC F4IN69; Q39169; Q9ZU78;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 33B;
DE AltName: Full=Protein REDUCED EPIDERMAL FLUORESCENCE 4;
DE Short=AtREF4;
GN Name=MED33B; Synonyms=MED24B, MED5_1, MED5B, REF4;
GN OrderedLocusNames=At2g48110; ORFNames=F11L15.1, T9J23.26;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-944.
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 927-1275.
RC STRAIN=cv. Columbia;
RX PubMed=8709959; DOI=10.1007/bf02173642;
RA Grevelding C., Suter-Crazzolara C., Menges A., von Kempner E.,
RA Masterson R., Schell J., Reiss B.;
RT "Characterisation of a new allele of pale cress and its role in greening in
RT Arabidopsis thaliana.";
RL Mol. Gen. Genet. 251:532-541(1996).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP COMPLEX, AND NOMENCLATURE.
RX PubMed=17560376; DOI=10.1016/j.molcel.2007.05.007;
RA Baeckstroem S., Elfving N., Nilsson R., Wingsle G., Bjoerklund S.;
RT "Purification of a plant mediator from Arabidopsis thaliana identifies PFT1
RT as the Med25 subunit.";
RL Mol. Cell 26:717-729(2007).
RN [5]
RP FUNCTION, MUTAGENESIS OF GLY-357; ASP-601 AND PRO-873, DISRUPTION
RP PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=18430946; DOI=10.1534/genetics.107.083881;
RA Stout J., Romero-Severson E., Ruegger M.O., Chapple C.;
RT "Semidominant mutations in reduced epidermal fluorescence 4 reduce
RT phenylpropanoid content in Arabidopsis.";
RL Genetics 178:2237-2251(2008).
RN [6]
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 [7]
RP FUNCTION, AND MUTAGENESIS OF ARG-361.
RX PubMed=22167189; DOI=10.1074/jbc.m111.312298;
RA Bonawitz N.D., Soltau W.L., Blatchley M.R., Powers B.L., Hurlock A.K.,
RA Seals L.A., Weng J.K., Stout J., Chapple C.;
RT "REF4 and RFR1, subunits of the transcriptional coregulatory complex
RT mediator, are required for phenylpropanoid homeostasis in Arabidopsis.";
RL J. Biol. Chem. 287:5434-5445(2012).
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. Involved in the repression of phenylpropanoid
CC biosynthesis. May compete with MED33B for common binding partners or
CC for occupancy in Mediator. {ECO:0000269|PubMed:18430946,
CC ECO:0000269|PubMed:22167189}.
CC -!- SUBUNIT: Component of the Mediator complex.
CC {ECO:0000269|PubMed:17560376}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:18430946}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:18430946}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 33 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD13716.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CP002685; AEC10938.1; -; Genomic_DNA.
DR EMBL; AC006072; AAD13716.3; ALT_SEQ; Genomic_DNA.
DR EMBL; X96481; CAA65335.1; -; mRNA.
DR PIR; E84923; E84923.
DR RefSeq; NP_566125.4; NM_130378.5.
DR AlphaFoldDB; F4IN69; -.
DR STRING; 3702.AT2G48110.1; -.
DR iPTMnet; F4IN69; -.
DR PaxDb; F4IN69; -.
DR PRIDE; F4IN69; -.
DR ProteomicsDB; 250834; -.
DR EnsemblPlants; AT2G48110.1; AT2G48110.1; AT2G48110.
DR GeneID; 819423; -.
DR Gramene; AT2G48110.1; AT2G48110.1; AT2G48110.
DR KEGG; ath:AT2G48110; -.
DR Araport; AT2G48110; -.
DR TAIR; locus:2039356; AT2G48110.
DR eggNOG; ENOG502QRBB; Eukaryota.
DR HOGENOM; CLU_003077_0_0_1; -.
DR InParanoid; F4IN69; -.
DR OMA; WATWQAY; -.
DR OrthoDB; 87466at2759; -.
DR PRO; PR:F4IN69; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; F4IN69; baseline and differential.
DR Genevisible; F4IN69; AT.
DR GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; TAS:TAIR.
DR GO; GO:0009698; P:phenylpropanoid metabolic process; IMP:TAIR.
DR GO; GO:2000762; P:regulation of phenylpropanoid metabolic process; IGI:TAIR.
DR InterPro; IPR039638; MED33A/B.
DR PANTHER; PTHR33739; PTHR33739; 2.
PE 1: Evidence at protein level;
KW Nucleus; Phenylpropanoid metabolism; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..1275
FT /note="Mediator of RNA polymerase II transcription subunit
FT 33B"
FT /id="PRO_0000418345"
FT REGION 772..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 357
FT /note="G->S: In ref4-3; Semidominant dwarfing and decreased
FT accumulation of phenylpropanoids. Reduced phenotype; when
FT associated with H-361. No effect; when associated with L-
FT 873."
FT /evidence="ECO:0000269|PubMed:18430946"
FT MUTAGEN 361
FT /note="R->H: Partial reversion back to wild-type phenotype;
FT when associated with S-357."
FT /evidence="ECO:0000269|PubMed:22167189"
FT MUTAGEN 601
FT /note="D->N: In ref4-1; Semidominant dwarfing and decreased
FT accumulation of phenylpropanoids."
FT /evidence="ECO:0000269|PubMed:18430946"
FT MUTAGEN 873
FT /note="P->L: Reversion back to wild-type phenotype; when
FT associated with S-357."
FT /evidence="ECO:0000269|PubMed:18430946"
SQ SEQUENCE 1275 AA; 139564 MW; 43A4EDFA0CEAFE68 CRC64;
MAPSEFQPSL WESVTSLIRS AQEKNVDPLH WALQLRLTLA SAGISLPSPD LAQFLVTHIF
WENHSPLSWK LLEKAISVNI VPPLLVLALL SPRVIPNRKL HPAAYRLYME LLKRHAFSFM
PLIRAPGYHK TMNSIDDILH LSETFGVQDQ EPGSILLAFV FSIVWELLDA SLDEEGLLEL
TSNKRSKWPS SPHDMDLDGL ENSVKRNENH DALEKANTEM AIELIQEFLQ NKVTSRILHL
ASQNMESKTI PRGEFHAIVS SGSKLALTSD SALWLPIDLF FEDIMDGTQA AAASAVENLT
GLVKALQAAN STSWHDAFLA LWLAALRLVQ RENLCLRYCF FMHMLEILSE ERDPIEGPVP
RTDTFLCVLL SVTPLAVANI IEEEESQWID QTSSSPSNQW KEKKGKCRQG LINSLQQLGD
YESLLTPPRS VQSVANQAAA KAIMFISGIT NSNGSYENTS MSESASGCCK VRFSLFTLKM
FVVMGVYLLC NISCWSLVMK GSPLTPSLTN SLITTPASSL AEIEKMYEVA TTGSEDEKIA
VASILCGASL FRGWSIQEHV IIFIVTLLSP PAPADLSGSY SHLINSAPFL NVLLVGISPI
DCVHIFSLHG VVPLLAGALM PICEAFGSGV PNITWTLPTG ELISSHAVFS TAFTLLLRLW
RFDHPPLDYV LGDVPPVGPQ PSPEYLLLVR NCRLECFGKS PKDRMARRRF SKVIDISVDP
IFMDSFPRLK QWYRQHQECM ASILSELKTG SPVHHIVDSL LSMMFKKANK GGSQSLTPSS
GSSSLSTSGG DDSSDQLKLP AWDILEAAPF VLDAALTACA HGSLSPRELA TGLKILADFL
PATLGTMVSY FSSEVTRGLW KPVSMNGTDW PSPAANLASV EQQIEKILAA TGVDVPRLPA
DGISAATLPL PLAALVSLTI TYKLDKATER FLVLVGPALD SLAAACPWPC MPIVTSLWTQ
KVKRWSDFLI FSASRTVFHH NRDAVIQLLR SCFTCTLGLT PTSQLCSYGG VGALLGHGFG
SRYSGGISTA APGILYIKVH RSIRDVMFLT EEILSLLMFS VKSIATRELP AGQAEKLKKT
KDGSRYGIGQ VSLSLAMRRV KLAASLGASL VWISGGLNLV QALIKETLPS WFISVHGEED
ELGGMVPMLR GYALAYFAIL SSAFAWGVDS SYPASKRRPR VLWLHLEFMV SALEGKISLG
CDWATWQAYV TGFVSLMVQC TPAWVLEVDV EVIKRLSKSL RQWNEQDLAL ALLCAGGLGT
MGAATELIVE TCHQH
