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Q9LKR3 (MD37A_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mediator of RNA polymerase II transcription subunit 37a
Alternative name(s):
Heat shock 70 kDa protein 11
Heat shock protein 70-11
Short name=AtHsp70-11
Luminal-binding protein 1
Short name=AtBP1
Short name=BiP1
Gene names
Name:MED37A
Synonyms:BIP1, HSP70-11, MED37_5
Ordered Locus Names:At5g28540
ORF Names:T26D3.10, T26D3_50
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length669 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 preinitiation complex with RNA polymerase II and the general transcription factors. Ref.11

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. Ref.11

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. Ref.11

Subunit structure

Component of the Mediator complex. Interacts with PDIL1-4. Ref.9 Ref.12 Ref.13

Subcellular location

Endoplasmic reticulum lumen By similarity. Nucleus Probable.

Developmental stage

Down-regulated during seed maturation. Up-regulated during germination. Ref.8

Induction

By heat shock. Ref.8

Post-translational modification

Ubiquitinated.

Disruption phenotype

Bip1 and bip2 double mutation affects the fusion of polar nuclei during female gametophyte development. Ref.11

Sequence similarities

Belongs to the heat shock protein 70 (TC 1.A.33) family. DnaK subfamily. [View classification]

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentEndoplasmic reticulum
Nucleus
   DomainSignal
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype PubMed 19060110. Source: TAIR

polar nucleus fusion

Inferred from genetic interaction Ref.11. Source: TAIR

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 22430844. Source: TAIR

cell wall

Inferred from direct assay PubMed 16287169. Source: TAIR

chloroplast

Inferred from direct assay PubMed 15028209PubMed 18431481. Source: TAIR

cytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

endoplasmic reticulum

Inferred from direct assay PubMed 22923678. Source: TAIR

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

mediator complex

Inferred from direct assay Ref.9. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 17317660. Source: TAIR

plasmodesma

Inferred from direct assay PubMed 21533090. Source: TAIR

vacuolar membrane

Inferred from direct assay PubMed 17151019. Source: TAIR

vacuole

Inferred from direct assay PubMed 15539469. Source: TAIR

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 669642Mediator of RNA polymerase II transcription subunit 37a
PRO_0000013588

Regions

Motif666 – 6694Prevents secretion from ER Potential

Experimental info

Sequence conflict215 – 2162YG → NV in BAA13947. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9LKR3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 20F38DA029F3F3F2

FASTA66973,629
        10         20         30         40         50         60 
MARSFGANST VVLAIIFFGC LFALSSAIEE ATKLGSVIGI DLGTTYSCVG VYKNGHVEII 

        70         80         90        100        110        120 
ANDQGNRITP SWVGFTDSER LIGEAAKNQA AVNPERTVFD VKRLIGRKFE DKEVQKDRKL 

       130        140        150        160        170        180 
VPYQIVNKDG KPYIQVKIKD GETKVFSPEE ISAMILTKMK ETAEAYLGKK IKDAVVTVPA 

       190        200        210        220        230        240 
YFNDAQRQAT KDAGVIAGLN VARIINEPTA AAIAYGLDKK GGEKNILVFD LGGGTFDVSV 

       250        260        270        280        290        300 
LTIDNGVFEV LSTNGDTHLG GEDFDHRVME YFIKLIKKKH QKDISKDNKA LGKLRRECER 

       310        320        330        340        350        360 
AKRALSSQHQ VRVEIESLFD GVDFSEPLTR ARFEELNNDL FRKTMGPVKK AMDDAGLQKS 

       370        380        390        400        410        420 
QIDEIVLVGG STRIPKVQQL LKDFFEGKEP NKGVNPDEAV AYGAAVQGGI LSGEGGDETK 

       430        440        450        460        470        480 
DILLLDVAPL TLGIETVGGV MTKLIPRNTV IPTKKSQVFT TYQDQQTTVS IQVFEGERSL 

       490        500        510        520        530        540 
TKDCRLLGKF DLNGIPPAPR GTPQIEVTFE VDANGILNVK AEDKASGKSE KITITNEKGR 

       550        560        570        580        590        600 
LSQEEIDRMV KEAEEFAEED KKVKEKIDAR NALETYVYNM KNQVNDKDKL ADKLEGDEKE 

       610        620        630        640        650        660 
KIEAATKEAL EWLDENQNSE KEEYDEKLKE VEAVCNPIIT AVYQRSGGAP GGAGGESSTE 


EEDESHDEL 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of two genes encoding luminal binding protein from Arabidopsis thaliana."
Koizumi N., Sano H.
Plant Gene Register PGR97-028
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. Columbia.
[2]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
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. expand/collapse author list , 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.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
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. expand/collapse author list , 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.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: cv. Columbia.
[5]"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
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. expand/collapse author list , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 537-669.
Strain: cv. Columbia.
[6]"An inventory of 1152 expressed sequence tags obtained by partial sequencing of cDNAs from Arabidopsis thaliana."
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. expand/collapse author list , Grellet F., Delseny M., Parmentier Y., de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., Bardet C., Tremousaygue D., Lescure B.
Plant J. 4:1051-1061(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 620-669.
Strain: cv. Columbia.
Tissue: Green siliques.
[7]"Genomic analysis of the Hsp70 superfamily in Arabidopsis thaliana."
Lin B.L., Wang J.S., Liu H.C., Chen R.W., Meyer Y., Barakat A., Delseny M.
Cell Stress Chaperones 6:201-208(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[8]"Comprehensive expression profile analysis of the Arabidopsis Hsp70 gene family."
Sung D.Y., Vierling E., Guy C.L.
Plant Physiol. 126:789-800(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: DNAK GENE SUBFAMILY, INDUCTION, DEVELOPMENTAL STAGE.
[9]"Purification of a plant mediator from Arabidopsis thaliana identifies PFT1 as the Med25 subunit."
Baeckstroem S., Elfving N., Nilsson R., Wingsle G., Bjoerklund S.
Mol. Cell 26:717-729(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, NOMENCLATURE.
[10]"Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis."
Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M., Vierstra R.D.
Plant J. 59:344-358(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS].
[11]"BiP-mediated polar nuclei fusion is essential for the regulation of endosperm nuclei proliferation in Arabidopsis thaliana."
Maruyama D., Endo T., Nishikawa S.
Proc. Natl. Acad. Sci. U.S.A. 107:1684-1689(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[12]"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."
Cho E.J., Yuen C.Y., Kang B.H., Ondzighi C.A., Staehelin L.A., Christopher D.A.
Mol. Cells 32:459-475(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDIL1-4.
[13]"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."
Mathur S., Vyas S., Kapoor S., Tyagi A.K.
Plant Physiol. 157:1609-1627(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION, SUBUNIT, NOMENCLATURE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89341 Genomic DNA. Translation: BAA13947.1.
AF262043 Genomic DNA. Translation: AAF88019.1.
CP002688 Genomic DNA. Translation: AED93812.1.
BT000453 mRNA. Translation: AAN17430.1.
BT001212 mRNA. Translation: AAN65099.1.
AK221441 mRNA. Translation: BAD94482.1.
Z17760 mRNA. Translation: CAA79056.1.
RefSeqNP_198206.1. NM_122737.3.
UniGeneAt.23381.
At.49118.
At.49188.
At.64764.

3D structure databases

ProteinModelPortalQ9LKR3.
SMRQ9LKR3. Positions 34-652.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid18223. 10 interactions.
IntActQ9LKR3. 4 interactions.
MINTMINT-7950246.

2D gel databases

SWISS-2DPAGEQ9LKR3.

Proteomic databases

PaxDbQ9LKR3.
PRIDEQ9LKR3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G28540.1; AT5G28540.1; AT5G28540.
GeneID832950.
KEGGath:AT5G28540.

Organism-specific databases

TAIRAT5G28540.

Phylogenomic databases

eggNOGCOG0443.
InParanoidQ9LKR3.
KOK09490.
OMACWIALLF.
PhylomeDBQ9LKR3.

Enzyme and pathway databases

BioCycARA:GQT-238-MONOMER.

Gene expression databases

GenevestigatorQ9LKR3.

Family and domain databases

Gene3D1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMD37A_ARATH
AccessionPrimary (citable) accession number: Q9LKR3
Secondary accession number(s): Q41928, Q56Y82
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names