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Q39043 (MD37F_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mediator of RNA polymerase II transcription subunit 37f
Alternative name(s):
Heat shock 70 kDa protein 12
Heat shock protein 70-12
Short name=AtHsp70-12
Luminal-binding protein 2
Short name=AtBP2
Short name=BiP2
Gene names
Name:MED37F
Synonyms:BIP, BIP2, HSP70-11, MED37_6
Ordered Locus Names:At5g42020
ORF Names:MJC20.12
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length668 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.12

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.12

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.12

Subunit structure

Component of the Mediator complex. Interacts with BAG7. Ref.9 Ref.13 Ref.14

Subcellular location

Endoplasmic reticulum lumen By similarity. Nucleus Probable.

Developmental stage

Down-regulated during seed maturation. Up-regulated during germination. Ref.7

Induction

By heat shock, by sugar. Up-regulated by light, DTT and tunicamycin treatment. Ref.1 Ref.7 Ref.8 Ref.10

Post-translational modification

Ubiquitinated.

Disruption phenotype

Bip1 and bip2 double mutation affects the fusion of polar nuclei during female gametophyte development. Ref.12

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
   Coding sequence diversityAlternative splicing
   DomainSignal
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMUbl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpolar nucleus fusion

Inferred from genetic interaction Ref.12. Source: TAIR

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

response to cadmium ion

Inferred from expression pattern PubMed 16502469. Source: TAIR

response to endoplasmic reticulum stress

Inferred from expression pattern PubMed 18574595. Source: TAIR

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell wall

Inferred from direct assay PubMed 16287169. Source: TAIR

endoplasmic reticulum

Inferred from direct assay PubMed 16618929PubMed 22923678. Source: TAIR

endoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

mediator complex

Inferred from direct assay Ref.9. Source: UniProtKB

membrane

Inferred from direct assay PubMed 17432890. Source: TAIR

nucleolus

Inferred from direct assay PubMed 15496452. Source: TAIR

nucleus

Inferred from direct assay PubMed 14617066. Source: TAIR

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...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q39043-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 668645Mediator of RNA polymerase II transcription subunit 37f
PRO_0000013589

Regions

Motif665 – 6684Prevents secretion from ER Potential

Experimental info

Sequence conflict1631A → T in BAA13948. Ref.2
Sequence conflict4851R → S in BAA12348. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 584DB253E91E68CA

FASTA66873,561
        10         20         30         40         50         60 
MARSFGANST VVLAIIFFGC LFAFSTAKEE 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 GEDFDHRIME YFIKLIKKKH QKDISKDNKA LGKLRRECER 

       310        320        330        340        350        360 
AKRALSSQHQ VRVEIESLFD GVDLSEPLTR 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 DLTGVPPAPR GTPQIEVTFE VDANGILNVK AEDKASGKSE KITITNEKGR 

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

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


EDESHDEL 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and responses to stress of a gene that encodes a luminal binding protein in Arabidopsis thaliana."
Koizumi N.
Plant Cell Physiol. 37:862-865(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Strain: cv. Landsberg erecta.
[2]"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.
[3]"Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones."
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S.
DNA Res. 6:183-195(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[4]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[5]"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.
[6]"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.
[7]"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.
[8]"Induction of BiP by sugar independent of a cis-element for the unfolded protein response in Arabidopsis thaliana."
Tajima H., Koizumi N.
Biochem. Biophys. Res. Commun. 346:926-930(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY SUGAR.
[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]"Light enhances the unfolded protein response as measured by BiP2 gene expression and the secretory GFP-2SC marker in Arabidopsis."
Lu D.P., Christopher D.A.
Physiol. Plantarum 134:360-368(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY LIGHT; DTT AND TUNICAMYCIN.
[11]"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].
[12]"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.
[13]"AtBAG7, an Arabidopsis Bcl-2-associated athanogene, resides in the endoplasmic reticulum and is involved in the unfolded protein response."
Williams B., Kabbage M., Britt R., Dickman M.B.
Proc. Natl. Acad. Sci. U.S.A. 107:6088-6093(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAG7.
[14]"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
D84414 mRNA. Translation: BAA12348.1.
D89342 Genomic DNA. Translation: BAA13948.1.
AB017067 Genomic DNA. Translation: BAB08435.1.
CP002688 Genomic DNA. Translation: AED94755.1.
BT002392 mRNA. Translation: AAO00752.1.
BT008406 mRNA. Translation: AAP37765.1.
PIRS71171.
RefSeqNP_851119.1. NM_180788.2. [Q39043-1]
UniGeneAt.23381.
At.33073.
At.49118.
At.49188.

3D structure databases

ProteinModelPortalQ39043.
SMRQ39043. Positions 34-652.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid19457. 7 interactions.
IntActQ39043. 3 interactions.
MINTMINT-7950442.

2D gel databases

SWISS-2DPAGEQ39043.

Proteomic databases

PaxDbQ39043.
PRIDEQ39043.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G42020.1; AT5G42020.1; AT5G42020. [Q39043-1]
GeneID834207.
KEGGath:AT5G42020.

Organism-specific databases

TAIRAT5G42020.

Phylogenomic databases

eggNOGCOG0443.
HOGENOMHOG000228135.
InParanoidQ39043.
KOK09490.
OMADKRAVQK.
PhylomeDBQ39043.

Enzyme and pathway databases

BioCycARA:GQT-1925-MONOMER.
ARA:GQT-1926-MONOMER.

Gene expression databases

GenevestigatorQ39043.

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 nameMD37F_ARATH
AccessionPrimary (citable) accession number: Q39043
Secondary accession number(s): Q39042
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 117 of the entry and version 2 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