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DnaJ protein ERDJ3A (Chaperone protein dnaJ 63) (AtDjA63) (AtJ63) (Endoplasmic reticulum dnaJ domain-containing protein 3A) (AtERdj3A) (Protein SCJ1 homolog ERDJ3A) (THERMOSENSITIVE MALE STERILE 1, TMS1)

 DNJ63_ARATH             Reviewed;         572 AA.
Q9SR96;
01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
25-OCT-2017, entry version 131.
RecName: Full=DnaJ protein ERDJ3A;
AltName: Full=Chaperone protein dnaJ 63;
Short=AtDjA63;
Short=AtJ63;
AltName: Full=Endoplasmic reticulum dnaJ domain-containing protein 3A;
Short=AtERdj3A;
AltName: Full=Protein SCJ1 homolog ERDJ3A;
AltName: Full=THERMOSENSITIVE MALE STERILE 1, TMS1;
Flags: Precursor;
Name=ERDJ3A; Synonyms=A63; OrderedLocusNames=At3g08970;
ORFNames=T16O11.7;
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 [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).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[3]
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).
[4]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11599562; DOI=10.1379/1466-1268(2001)006<0209:TJDPOA>2.0.CO;2;
Miernyk J.A.;
"The J-domain proteins of Arabidopsis thaliana: an unexpectedly large
and diverse family of chaperones.";
Cell Stress Chaperones 6:209-218(2001).
[5]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY TUNICAMYCIN,
LACK OF GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
PubMed=18718935; DOI=10.1093/pcp/pcn119;
Yamamoto M., Maruyama D., Endo T., Nishikawa S.;
"Arabidopsis thaliana has a set of J proteins in the endoplasmic
reticulum that are conserved from yeast to animals and plants.";
Plant Cell Physiol. 49:1547-1562(2008).
[6]
FUNCTION, TISSUE SPECIFICITY, INDUCTION BY HEAT SHOCK, AND DISRUPTION
PHENOTYPE.
PubMed=18980646; DOI=10.1111/j.1365-313X.2008.03732.x;
Yang K.Z., Xia C., Liu X.L., Dou X.Y., Wang W., Chen L.Q., Zhang X.Q.,
Xie L.F., He L., Ma X., Ye D.;
"A mutation in thermosensitive male sterile 1, encoding a heat shock
protein with DnaJ and PDI domains, leads to thermosensitive
gametophytic male sterility in Arabidopsis.";
Plant J. 57:870-882(2009).
-!- FUNCTION: Regulates protein folding in the endoplasmic reticulum
(ER) lumen. Functions probably as a co-molecular chaperone that is
required for normal growth of pollen tubes under high-temperature
stress. {ECO:0000269|PubMed:18980646}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
{ECO:0000305|PubMed:18718935}.
-!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers,
mature pollen grains and growing pollen tubes.
{ECO:0000269|PubMed:18718935, ECO:0000269|PubMed:18980646}.
-!- INDUCTION: By tunicamycin and heat shock.
{ECO:0000269|PubMed:18718935, ECO:0000269|PubMed:18980646}.
-!- PTM: Not N-glycosylated.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions (permissive temperature of 22 degrees Celsius), but
mutant plants show gametophytic male sterility due to defect in
pollen tube growth at temperature of 30 degrees Celsius.
{ECO:0000269|PubMed:18718935, ECO:0000269|PubMed:18980646}.
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EMBL; AC010871; AAF07843.1; -; Genomic_DNA.
EMBL; CP002686; AEE74703.1; -; Genomic_DNA.
EMBL; CP002686; ANM65503.1; -; Genomic_DNA.
EMBL; BT003887; AAO41936.1; -; mRNA.
EMBL; BT005001; AAO50534.1; -; mRNA.
RefSeq; NP_001319504.1; NM_001337788.1.
RefSeq; NP_187509.1; NM_111731.4.
UniGene; At.40191; -.
ProteinModelPortal; Q9SR96; -.
SMR; Q9SR96; -.
BioGrid; 5383; 2.
IntAct; Q9SR96; 3.
MINT; MINT-7950490; -.
STRING; 3702.AT3G08970.1; -.
PaxDb; Q9SR96; -.
EnsemblPlants; AT3G08970.1; AT3G08970.1; AT3G08970.
EnsemblPlants; AT3G08970.2; AT3G08970.2; AT3G08970.
GeneID; 820049; -.
Gramene; AT3G08970.1; AT3G08970.1; AT3G08970.
Gramene; AT3G08970.2; AT3G08970.2; AT3G08970.
KEGG; ath:AT3G08970; -.
Araport; AT3G08970; -.
TAIR; locus:2097643; AT3G08970.
eggNOG; ENOG410IQB3; Eukaryota.
eggNOG; COG2214; LUCA.
HOGENOM; HOG000030834; -.
InParanoid; Q9SR96; -.
OMA; WRAISGM; -.
OrthoDB; EOG09360ARK; -.
PhylomeDB; Q9SR96; -.
PRO; PR:Q9SR96; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q9SR96; baseline and differential.
Genevisible; Q9SR96; AT.
GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0005773; C:vacuole; IEA:EnsemblPlants.
GO; GO:0016491; F:oxidoreductase activity; IDA:TAIR.
GO; GO:0034605; P:cellular response to heat; TAS:TAIR.
GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
GO; GO:0009408; P:response to heat; IMP:TAIR.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
InterPro; IPR036869; DnaJ_dom_sf.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR018253; DnaJ_domain_CS.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00226; DnaJ; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS00636; DNAJ_1; 1.
PROSITE; PS50076; DNAJ_2; 1.
1: Evidence at protein level;
Chaperone; Coiled coil; Complete proteome; Endoplasmic reticulum;
Glycoprotein; Reference proteome; Signal.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 572 DnaJ protein ERDJ3A.
/FTId=PRO_0000430368.
DOMAIN 27 91 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
COILED 394 423 {ECO:0000255}.
COMPBIAS 91 177 Gly-rich.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
SEQUENCE 572 AA; 62570 MW; 7A0E85475BA838E1 CRC64;
MVRTRLAISV VLVSTLLLLN VKAKSVDPYK VLGVSKDAKQ REIQKAFHKQ SLKYHPDKNK
DKGAQEKFAE INNAYEILSD EEKRKNYDLY GDEKGQPGFD SGFPGGNGGY SYSSSGGGFN
FGGPGGWQNM GGGGGSKSFS FSFGGPSESS FGFGMDDIFS MFSGGSSKGK EQFGGFGSSS
NAESKSKSST VAAIKTINSQ VYKKDVVDQG MTWLLLSYLP SQRGSQYHES IIEEVAESLQ
GALKVGRLNC ETESSLCKQL GIVPRRAPRM FVYSYTSSGK ATLAEYTEEL VAKKVKSFCQ
EHLPRFSKKI DLNTFDVSAV SSQKTPKVLL LSTKKDTPVI WRVLSGLYNG RFVFYNTEVH
DTSDPKIQKL GVDKFPAIVG WLSNGEKQVL KTGITVKNLK SAVQELGKLL EGLEKKNKKV
SSKSQAGQAP NESSEKIPLL SRPNFDSICG ENTPVCIIGA FRSSNGKEKL QSIMSKVSQK
SLSRRQASTT GSQDTVSYSL LDATKQSAFL SSLDKSEFKT SSDKLLIAYK PRRGKFATFK
GDMTIEEVEK FVAAVLNGDI QFTKTRQKPQ IK


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