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Probable mediator of RNA polymerase II transcription subunit 37c (Heat shock 70 kDa protein 4) (Heat shock cognate 70 kDa protein 4) (Heat shock cognate protein 70-4) (AtHsc70-4) (Heat shock protein 70-4) (AtHsp70-4)

 MD37C_ARATH             Reviewed;         650 AA.
Q9LHA8; Q9ZS55;
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 127.
RecName: Full=Probable mediator of RNA polymerase II transcription subunit 37c;
AltName: Full=Heat shock 70 kDa protein 4;
AltName: Full=Heat shock cognate 70 kDa protein 4;
AltName: Full=Heat shock cognate protein 70-4;
Short=AtHsc70-4;
AltName: Full=Heat shock protein 70-4;
Short=AtHsp70-4;
Name=MED37C; Synonyms=HSC70-4, HSP70, HSP70-4, MED37_2;
OrderedLocusNames=At3g12580; ORFNames=T16H11.7, T2E22.11;
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 [MRNA].
STRAIN=cv. Columbia; TISSUE=Silique;
Hinderhofer K., Praendl R., Schoeffl F.;
"Seed-maturation-induced subset of heat shock protein mRNAs and heat-
shock-element-binding protein complexes are dependent on ABI3 in
Arabidopsis thaliana.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10907853; DOI=10.1093/dnares/7.3.217;
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 3. II.
Sequence features of the 4,251,695 bp regions covered by 90 P1, TAC
and BAC clones.";
DNA Res. 7:217-221(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[4]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
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).
[7]
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).
[8]
INTERACTION WITH HSFA1A/HSF1.
PubMed=11807141; DOI=10.1093/jexbot/53.367.371;
Kim B.H., Schoeffl F.;
"Interaction between Arabidopsis heat shock transcription factor 1 and
70 kDa heat shock proteins.";
J. Exp. Bot. 53:371-375(2002).
[9]
INDUCTION.
PubMed=15805473; DOI=10.1104/pp.104.058958;
Aparicio F., Thomas C.L., Lederer C., Niu Y., Wang D., Maule A.J.;
"Virus induction of heat shock protein 70 reflects a general response
to protein accumulation in the plant cytosol.";
Plant Physiol. 138:529-536(2005).
[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]
INDUCTION BY PATHOGEN.
PubMed=18065690; DOI=10.1105/tpc.107.051896;
Noel L.D., Cagna G., Stuttmann J., Wirthmueller L., Betsuyaku S.,
Witte C.P., Bhat R., Pochon N., Colby T., Parker J.E.;
"Interaction between SGT1 and cytosolic/nuclear HSC70 chaperones
regulates Arabidopsis immune responses.";
Plant Cell 19:4061-4076(2007).
[12]
INDUCTION.
PubMed=19704521; DOI=10.4161/psb.3.10.6021;
Scarpeci T.E., Zanor M.I., Valle E.M.;
"Investigating the role of plant heat shock proteins during oxidative
stress.";
Plant Signal. Behav. 3:856-857(2008).
[13]
FUNCTION, INTERACTION WITH CHIP, AND DISRUPTION PHENOTYPE.
PubMed=20028838; DOI=10.1105/tpc.109.071548;
Lee S., Lee D.W., Lee Y., Mayer U., Stierhof Y.D., Lee S., Jurgens G.,
Hwang I.;
"Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP,
mediate plastid-destined precursor degradation through the ubiquitin-
26S proteasome system in Arabidopsis.";
Plant Cell 21:3984-4001(2009).
[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).
-!- 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 (By similarity). {ECO:0000250}.
-!- FUNCTION: ATP-dependent molecular chaperone that assists folding
of unfolded or misfolded proteins under stress conditions.
Mediates plastid precursor degradation to prevent cytosolic
precursor accumulation, together with the E3 ubiquitin-protein
ligase CHIP. Recognizes specific sequence motifs in transit
peptides and thereby led to precursor degradation through the
ubiquitin-proteasome system. Plays a critical role in
embryogenesis. {ECO:0000269|PubMed:20028838}.
-!- 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 (Probable). Interacts
with CHIP. Interacts with HSFA1A/HSF1.
{ECO:0000269|PubMed:11807141, ECO:0000269|PubMed:20028838,
ECO:0000269|PubMed:22021418, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus
{ECO:0000305}.
-!- DEVELOPMENTAL STAGE: Up-regulated during seed maturation.
{ECO:0000269|PubMed:11402207}.
-!- INDUCTION: By heat shock, cold, high light treatment and oxidative
stress. Up-regulated by virus infection and by pathogen attack
(P.syringae). {ECO:0000269|PubMed:11402207,
ECO:0000269|PubMed:15805473, ECO:0000269|PubMed:18065690,
ECO:0000269|PubMed:19704521}.
-!- DISRUPTION PHENOTYPE: Abnormal embryogenesis. Defective seedlings
with high levels of reactive oxygen species and monoubiquitinated
LHCB4 precursors. {ECO:0000269|PubMed:20028838}.
-!- SIMILARITY: Belongs to the heat shock protein 70 (TC 1.A.33)
family. DnaK subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ002551; CAA05547.1; -; mRNA.
EMBL; AP002055; BAB02269.1; -; Genomic_DNA.
EMBL; AC069474; AAG51030.1; -; Genomic_DNA.
EMBL; CP002686; AEE75218.1; -; Genomic_DNA.
EMBL; AY054183; AAL06844.1; -; mRNA.
EMBL; AY054190; AAL06851.1; -; mRNA.
EMBL; AY059885; AAL24367.1; -; mRNA.
PIR; JA0171; JA0171.
RefSeq; NP_187864.1; NM_112093.3.
UniGene; At.47608; -.
ProteinModelPortal; Q9LHA8; -.
SMR; Q9LHA8; -.
BioGrid; 5772; 22.
IntAct; Q9LHA8; 8.
MINT; MINT-2584399; -.
STRING; 3702.AT3G12580.1; -.
iPTMnet; Q9LHA8; -.
PaxDb; Q9LHA8; -.
PRIDE; Q9LHA8; -.
EnsemblPlants; AT3G12580.1; AT3G12580.1; AT3G12580.
GeneID; 820438; -.
Gramene; AT3G12580.1; AT3G12580.1; AT3G12580.
KEGG; ath:AT3G12580; -.
Araport; AT3G12580; -.
TAIR; locus:2101222; AT3G12580.
eggNOG; KOG0101; Eukaryota.
eggNOG; COG0443; LUCA.
HOGENOM; HOG000228135; -.
InParanoid; Q9LHA8; -.
KO; K03283; -.
OMA; EAYLGCK; -.
OrthoDB; EOG093604KP; -.
PhylomeDB; Q9LHA8; -.
Reactome; R-ATH-3371453; Regulation of HSF1-mediated heat shock response.
Reactome; R-ATH-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-ATH-3371568; Attenuation phase.
Reactome; R-ATH-3371571; HSF1-dependent transactivation.
Reactome; R-ATH-6798695; Neutrophil degranulation.
Reactome; R-ATH-72163; mRNA Splicing - Major Pathway.
Reactome; R-ATH-8876725; Protein methylation.
PRO; PR:Q9LHA8; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9LHA8; baseline and differential.
Genevisible; Q9LHA8; AT.
GO; GO:0048046; C:apoplast; IDA:TAIR.
GO; GO:0005618; C:cell wall; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
GO; GO:0005739; C:mitochondrion; IDA:TAIR.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:TAIR.
GO; GO:0005774; C:vacuolar membrane; IDA:TAIR.
GO; GO:0005524; F:ATP binding; IDA:TAIR.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IMP:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0009617; P:response to bacterium; IEP:TAIR.
GO; GO:0046686; P:response to cadmium ion; IEP:TAIR.
GO; GO:0009408; P:response to heat; IEP:UniProtKB.
GO; GO:0009644; P:response to high light intensity; IEP:TAIR.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
GO; GO:0009266; P:response to temperature stimulus; IEP:TAIR.
GO; GO:0009615; P:response to virus; IEP:TAIR.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100920; SSF100920; 1.
SUPFAM; SSF100934; SSF100934; 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; Cytoplasm;
Nucleotide-binding; Nucleus; Reference proteome; Stress response;
Transcription; Transcription regulation; Ubl conjugation pathway.
CHAIN 1 650 Probable mediator of RNA polymerase II
transcription subunit 37c.
/FTId=PRO_0000397045.
CONFLICT 126 126 M -> I (in Ref. 1; CAA05547).
{ECO:0000305}.
CONFLICT 149 149 T -> I (in Ref. 1; CAA05547).
{ECO:0000305}.
CONFLICT 161 161 A -> G (in Ref. 1; CAA05547).
{ECO:0000305}.
CONFLICT 342 342 L -> V (in Ref. 1; CAA05547).
{ECO:0000305}.
CONFLICT 356 356 L -> V (in Ref. 1; CAA05547).
{ECO:0000305}.
SEQUENCE 650 AA; 71101 MW; 33381E896461C5B9 CRC64;
MAGKGEGPAI GIDLGTTYSC VGVWQHDRVE IIANDQGNRT TPSYVAFTDS ERLIGDAAKN
QVAMNPTNTV FDAKRLIGRR YSDPSVQADK SHWPFKVVSG PGEKPMIVVN HKGEEKQFSA
EEISSMVLIK MREIAEAFLG SPVKNAVVTV PAYFNDSQRQ ATKDAGVISG LNVMRIINEP
TAAAIAYGLD KKASSVGEKN VLIFDLGGGT FDVSLLTIEE GIFEVKATAG DTHLGGEDFD
NRMVNHFVQE FKRKNKKDIT GNPRALRRLR TACERAKRTL SSTAQTTIEI DSLFEGIDFY
TTITRARFEE LNMDLFRKCM EPVEKCLRDA KMDKSSVHDV VLVGGSTRIP KVQQLLQDFF
NGKELCKSIN PDEAVAYGAA VQAAILSGEG NEKVQDLLLL DVTPLSLGLE TAGGVMTVLI
PRNTTIPTKK EQIFSTYSDN QPGVLIQVYE GERARTKDNN LLGKFELSGI PPAPRGVPQI
TVCFDIDANG ILNVSAEDKT TGQKNKITIT NDKGRLSKEE IEKMVQEAEK YKAEDEEHKK
KVDAKNALEN YAYNMRNTIK DEKIASKLDA ADKKKIEDAI DQAIEWLDGN QLAEADEFED
KMKELESLCN PIIARMYQGA GPDMGGAGGM DDDTPAGGSG GAGPKIEEVD


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