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MED21_ARATH
ID   MED21_ARATH             Reviewed;         139 AA.
AC   C0LU16; Q84WP9; Q9M0Z8; Q9ZS95;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Mediator of RNA polymerase II transcription subunit 21;
DE   AltName: Full=Mediator complex subunit 21;
DE   AltName: Full=RNAPII complex component SRB7;
GN   Name=MED21; Synonyms=MED21_1, SRB7; OrderedLocusNames=At4g04780;
GN   ORFNames=T4B21.7;
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 [MRNA], INTERACTION WITH HUB1, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=19286969; DOI=10.1105/tpc.108.062364;
RA   Dhawan R., Luo H., Foerster A.M., Abuqamar S., Du H.N., Briggs S.D.,
RA   Mittelsten Scheid O., Mengiste T.;
RT   "HISTONE MONOUBIQUITINATION1 interacts with a subunit of the mediator
RT   complex and regulates defense against necrotrophic fungal pathogens in
RT   Arabidopsis.";
RL   Plant Cell 21:1000-1019(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
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   [4]
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, 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   [6]
RP   IDENTIFICATION, SUBUNIT, 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).
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. Required for embryo development
CC       and defense against necrotrophic fungal pathogens.
CC   -!- SUBUNIT: Component of the Mediator complex. Interacts with HUB1.
CC       {ECO:0000269|PubMed:17560376, ECO:0000269|PubMed:19286969,
CC       ECO:0000269|PubMed:22021418}.
CC   -!- INTERACTION:
CC       C0LU16; Q94AI7: TPL; NbExp=6; IntAct=EBI-21254755, EBI-2119299;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethal. {ECO:0000269|PubMed:19286969}.
CC   -!- SIMILARITY: Belongs to the Mediator complex subunit 21 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD03443.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAO22731.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC       Sequence=CAB80843.1; Type=Erroneous gene model prediction; Note=The predicted gene At4g04780 has been split into 2 genes: At4g04775 and At4g04780.; Evidence={ECO:0000305};
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DR   EMBL; FJ769239; ACN81041.1; -; mRNA.
DR   EMBL; AF118223; AAD03443.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161501; CAB80843.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE82425.1; -; Genomic_DNA.
DR   EMBL; BT002915; AAO22731.1; ALT_INIT; mRNA.
DR   PIR; B85060; B85060.
DR   RefSeq; NP_192387.2; NM_116716.5.
DR   AlphaFoldDB; C0LU16; -.
DR   SMR; C0LU16; -.
DR   BioGRID; 11126; 1.
DR   IntAct; C0LU16; 4.
DR   STRING; 3702.AT4G04780.1; -.
DR   PaxDb; C0LU16; -.
DR   PRIDE; C0LU16; -.
DR   ProteomicsDB; 238252; -.
DR   EnsemblPlants; AT4G04780.1; AT4G04780.1; AT4G04780.
DR   GeneID; 825815; -.
DR   Gramene; AT4G04780.1; AT4G04780.1; AT4G04780.
DR   KEGG; ath:AT4G04780; -.
DR   Araport; AT4G04780; -.
DR   TAIR; locus:2138957; AT4G04780.
DR   eggNOG; KOG1510; Eukaryota.
DR   HOGENOM; CLU_113074_0_0_1; -.
DR   InParanoid; C0LU16; -.
DR   OMA; TDNCINF; -.
DR   OrthoDB; 1527634at2759; -.
DR   PRO; PR:C0LU16; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; C0LU16; baseline and differential.
DR   GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
DR   GO; GO:0043078; C:polar nucleus; IMP:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0050832; P:defense response to fungus; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:TAIR.
DR   InterPro; IPR037212; Med7/Med21-like.
DR   InterPro; IPR021384; Mediator_Med21.
DR   PANTHER; PTHR13381; PTHR13381; 1.
DR   Pfam; PF11221; Med21; 1.
DR   SUPFAM; SSF140718; SSF140718; 1.
PE   1: Evidence at protein level;
KW   Activator; Coiled coil; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..139
FT                   /note="Mediator of RNA polymerase II transcription subunit
FT                   21"
FT                   /id="PRO_0000397046"
FT   REGION          28..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          92..132
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        39..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   139 AA;  15041 MW;  3CC962AB85A8EFA3 CRC64;
     MDIISQLQEQ VNTIAAITFN AFGTLQRDAP PVQLSPNYPE PPATTTVTDD ATPFPEQPKQ
     LSAGLVKAAK QFDALVAALP LSEGGEGAQL KRIAELQVEN DLVGQELQKQ LEAAEKELKQ
     VQELFGQAAD NCLNMKKPE
 
 
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