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Mediator of RNA polymerase II transcription subunit 37a (Heat shock 70 kDa protein 11) (Heat shock protein 70-11) (AtHsp70-11) (Luminal-binding protein 1) (AtBP1) (BiP1)

 MD37A_ARATH             Reviewed;         669 AA.
Q9LKR3; Q41928; Q56Y82;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-APR-2018, entry version 149.
RecName: Full=Mediator of RNA polymerase II transcription subunit 37a;
AltName: Full=Heat shock 70 kDa protein 11;
AltName: Full=Heat shock protein 70-11;
Short=AtHsp70-11;
AltName: Full=Luminal-binding protein 1;
Short=AtBP1;
Short=BiP1;
Flags: Precursor;
Name=MED37A; Synonyms=BIP1, HSP70-11, MED37_5;
OrderedLocusNames=At5g28540; ORFNames=T26D3.10, T26D3_50;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Columbia;
Koizumi N., Sano H.;
"Isolation of two genes encoding luminal binding protein from
Arabidopsis thaliana.";
(er) Plant Gene Register PGR97-028(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 537-669.
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 620-669.
STRAIN=cv. Columbia; TISSUE=Green siliques;
PubMed=8281187; DOI=10.1046/j.1365-313X.1993.04061051.x;
Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M.,
Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P.,
Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R.,
Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y.,
de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M.,
Bardet C., Tremousaygue D., Lescure B.;
"An inventory of 1152 expressed sequence tags obtained by partial
sequencing of cDNAs from Arabidopsis thaliana.";
Plant J. 4:1051-1061(1993).
[7]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11599561; DOI=10.1379/1466-1268(2001)006<0201:GAOTHS>2.0.CO;2;
Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A.,
Delseny M.;
"Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana.";
Cell Stress Chaperones 6:201-208(2001).
[8]
DNAK GENE SUBFAMILY, INDUCTION, AND DEVELOPMENTAL STAGE.
PubMed=11402207; DOI=10.1104/pp.126.2.789;
Sung D.Y., Vierling E., Guy C.L.;
"Comprehensive expression profile analysis of the Arabidopsis Hsp70
gene family.";
Plant Physiol. 126:789-800(2001).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND NOMENCLATURE.
PubMed=17560376; DOI=10.1016/j.molcel.2007.05.007;
Baeckstroem S., Elfving N., Nilsson R., Wingsle G., Bjoerklund S.;
"Purification of a plant mediator from Arabidopsis thaliana identifies
PFT1 as the Med25 subunit.";
Mol. Cell 26:717-729(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=cv. Landsberg erecta;
PubMed=17272265; DOI=10.1074/mcp.M600408-MCP200;
Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.;
"Multidimensional protein identification technology (MudPIT) analysis
of ubiquitinated proteins in plants.";
Mol. Cell. Proteomics 6:601-610(2007).
[11]
INTERACTION WITH ERDJ3B.
PubMed=19763086; DOI=10.1038/emboj.2009.262;
Nekrasov V., Li J., Batoux M., Roux M., Chu Z.H., Lacombe S.,
Rougon A., Bittel P., Kiss-Papp M., Chinchilla D., van Esse H.P.,
Jorda L., Schwessinger B., Nicaise V., Thomma B.P., Molina A.,
Jones J.D., Zipfel C.;
"Control of the pattern-recognition receptor EFR by an ER protein
complex in plant immunity.";
EMBO J. 28:3428-3438(2009).
[12]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=20080634; DOI=10.1073/pnas.0905795107;
Maruyama D., Endo T., Nishikawa S.;
"BiP-mediated polar nuclei fusion is essential for the regulation of
endosperm nuclei proliferation in Arabidopsis thaliana.";
Proc. Natl. Acad. Sci. U.S.A. 107:1684-1689(2010).
[13]
INTERACTION WITH PDIL1-4.
PubMed=21909944; DOI=10.1007/s10059-011-0150-3;
Cho E.J., Yuen C.Y., Kang B.H., Ondzighi C.A., Staehelin L.A.,
Christopher D.A.;
"Protein disulfide isomerase-2 of Arabidopsis mediates protein folding
and localizes to both the secretory pathway and nucleus, where it
interacts with maternal effect embryo arrest factor.";
Mol. Cells 32:459-475(2011).
[14]
IDENTIFICATION, SUBUNIT, AND NOMENCLATURE.
PubMed=22021418; DOI=10.1104/pp.111.188300;
Mathur S., Vyas S., Kapoor S., Tyagi A.K.;
"The Mediator complex in plants: structure, phylogeny, and expression
profiling of representative genes in a dicot (Arabidopsis) and a
monocot (rice) during reproduction and abiotic stress.";
Plant Physiol. 157:1609-1627(2011).
[15]
INTERACTION WITH BZIP28.
PubMed=23624714; DOI=10.1105/tpc.113.110684;
Srivastava R., Deng Y., Shah S., Rao A.G., Howell S.H.;
"BINDING PROTEIN is a master regulator of the endoplasmic reticulum
stress sensor/transducer bZIP28 in Arabidopsis.";
Plant Cell 25:1416-1429(2013).
-!- FUNCTION: Component of the Mediator complex, a coactivator
involved in the regulated transcription of nearly all RNA
polymerase II-dependent genes. Mediator functions as a bridge to
convey information from gene-specific regulatory proteins to the
basal RNA polymerase II transcription machinery. The Mediator
complex, having a compact conformation in its free form, is
recruited to promoters by direct interactions with regulatory
proteins and serves for the assembly of a functional pre-
initiation complex with RNA polymerase II and the general
transcription factors. {ECO:0000269|PubMed:20080634}.
-!- FUNCTION: Probably plays a role in facilitating the assembly of
multimeric protein complexes inside the ER. Involved in polar
nuclei fusion during female gametophyte development and is
essential for the regulation of endosperm nuclei proliferation.
{ECO:0000269|PubMed:20080634}.
-!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
preexistent proteins against aggregation and mediate the folding
of newly translated polypeptides in the cytosol as well as within
organelles. These chaperones participate in all these processes
through their ability to recognize nonnative conformations of
other proteins. They bind extended peptide segments with a net
hydrophobic character exposed by polypeptides during translation
and membrane translocation, or following stress-induced damage (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Component of the Mediator complex (PubMed:17560376,
PubMed:22021418). Interacts with PDIL1-4 and ERDJ3B
(PubMed:19763086, PubMed:21909944). Interacts with BZIP28 (via C-
terminus). MED37A/BIP1 and MED37B/BIP3 dissociates from BZIP28
under ER stress (PubMed:23624714). {ECO:0000269|PubMed:17560376,
ECO:0000269|PubMed:19763086, ECO:0000269|PubMed:21909944,
ECO:0000269|PubMed:22021418, ECO:0000269|PubMed:23624714}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000255|PROSITE-ProRule:PRU10138}. Nucleus {ECO:0000305}.
-!- DEVELOPMENTAL STAGE: Down-regulated during seed maturation. Up-
regulated during germination. {ECO:0000269|PubMed:11402207}.
-!- INDUCTION: By heat shock. {ECO:0000269|PubMed:11402207}.
-!- DISRUPTION PHENOTYPE: Bip1 and bip2 double mutation affects the
fusion of polar nuclei during female gametophyte development.
{ECO:0000269|PubMed:20080634}.
-!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33)
family. DnaK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D89341; BAA13947.1; -; Genomic_DNA.
EMBL; AF262043; AAF88019.1; -; Genomic_DNA.
EMBL; CP002688; AED93812.1; -; Genomic_DNA.
EMBL; BT000453; AAN17430.1; -; mRNA.
EMBL; BT001212; AAN65099.1; -; mRNA.
EMBL; AK221441; BAD94482.1; -; mRNA.
EMBL; Z17760; CAA79056.1; -; mRNA.
RefSeq; NP_198206.1; NM_122737.4.
UniGene; At.23381; -.
UniGene; At.49118; -.
UniGene; At.49188; -.
UniGene; At.64764; -.
ProteinModelPortal; Q9LKR3; -.
SMR; Q9LKR3; -.
BioGrid; 18223; 17.
IntAct; Q9LKR3; 4.
MINT; Q9LKR3; -.
STRING; 3702.AT5G28540.1; -.
iPTMnet; Q9LKR3; -.
SWISS-2DPAGE; Q9LKR3; -.
PaxDb; Q9LKR3; -.
PRIDE; Q9LKR3; -.
EnsemblPlants; AT5G28540.1; AT5G28540.1; AT5G28540.
GeneID; 832950; -.
Gramene; AT5G28540.1; AT5G28540.1; AT5G28540.
KEGG; ath:AT5G28540; -.
Araport; AT5G28540; -.
TAIR; locus:2182783; AT5G28540.
eggNOG; KOG0100; Eukaryota.
eggNOG; COG0443; LUCA.
HOGENOM; HOG000228135; -.
InParanoid; Q9LKR3; -.
KO; K09490; -.
OMA; EWNDPSV; -.
OrthoDB; EOG093604JO; -.
PhylomeDB; Q9LKR3; -.
Reactome; R-ATH-3371453; Regulation of HSF1-mediated heat shock response.
PRO; PR:Q9LKR3; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9LKR3; baseline and differential.
Genevisible; Q9LKR3; AT.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0009507; C:chloroplast; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0016592; C:mediator complex; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005773; C:vacuole; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:TAIR.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00014; ER_TARGET; 1.
PROSITE; PS00297; HSP70_1; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
ATP-binding; Chaperone; Complete proteome; Endoplasmic reticulum;
Nucleotide-binding; Nucleus; Reference proteome; Signal;
Transcription; Transcription regulation.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 669 Mediator of RNA polymerase II
transcription subunit 37a.
/FTId=PRO_0000013588.
MOTIF 666 669 Prevents secretion from ER.
{ECO:0000255|PROSITE-ProRule:PRU10138}.
CONFLICT 215 216 YG -> NV (in Ref. 2; BAA13947).
{ECO:0000305}.
SEQUENCE 669 AA; 73629 MW; 20F38DA029F3F3F2 CRC64;
MARSFGANST VVLAIIFFGC LFALSSAIEE ATKLGSVIGI DLGTTYSCVG VYKNGHVEII
ANDQGNRITP SWVGFTDSER LIGEAAKNQA AVNPERTVFD VKRLIGRKFE DKEVQKDRKL
VPYQIVNKDG KPYIQVKIKD GETKVFSPEE ISAMILTKMK ETAEAYLGKK IKDAVVTVPA
YFNDAQRQAT KDAGVIAGLN VARIINEPTA AAIAYGLDKK GGEKNILVFD LGGGTFDVSV
LTIDNGVFEV LSTNGDTHLG GEDFDHRVME YFIKLIKKKH QKDISKDNKA LGKLRRECER
AKRALSSQHQ VRVEIESLFD GVDFSEPLTR ARFEELNNDL FRKTMGPVKK AMDDAGLQKS
QIDEIVLVGG STRIPKVQQL LKDFFEGKEP NKGVNPDEAV AYGAAVQGGI LSGEGGDETK
DILLLDVAPL TLGIETVGGV MTKLIPRNTV IPTKKSQVFT TYQDQQTTVS IQVFEGERSL
TKDCRLLGKF DLNGIPPAPR GTPQIEVTFE VDANGILNVK AEDKASGKSE KITITNEKGR
LSQEEIDRMV KEAEEFAEED KKVKEKIDAR NALETYVYNM KNQVNDKDKL ADKLEGDEKE
KIEAATKEAL EWLDENQNSE KEEYDEKLKE VEAVCNPIIT AVYQRSGGAP GGAGGESSTE
EEDESHDEL


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