DNJ63_ARATH
ID DNJ63_ARATH Reviewed; 572 AA.
AC Q9SR96;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=DnaJ protein ERDJ3A;
DE AltName: Full=Chaperone protein dnaJ 63;
DE Short=AtDjA63;
DE Short=AtJ63;
DE AltName: Full=Endoplasmic reticulum dnaJ domain-containing protein 3A;
DE Short=AtERdj3A;
DE AltName: Full=Protein SCJ1 homolog ERDJ3A;
DE AltName: Full=Protein THERMOSENSITIVE MALE STERILE 1;
DE Flags: Precursor;
GN Name=ERDJ3A; Synonyms=A63, TMS1; OrderedLocusNames=At3g08970;
GN ORFNames=T16O11.7;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11599562; DOI=10.1379/1466-1268(2001)006<0209:tjdpoa>2.0.co;2;
RA Miernyk J.A.;
RT "The J-domain proteins of Arabidopsis thaliana: an unexpectedly large and
RT diverse family of chaperones.";
RL Cell Stress Chaperones 6:209-218(2001).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY TUNICAMYCIN, LACK OF
RP GLYCOSYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=18718935; DOI=10.1093/pcp/pcn119;
RA Yamamoto M., Maruyama D., Endo T., Nishikawa S.;
RT "Arabidopsis thaliana has a set of J proteins in the endoplasmic reticulum
RT that are conserved from yeast to animals and plants.";
RL Plant Cell Physiol. 49:1547-1562(2008).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY HEAT SHOCK, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18980646; DOI=10.1111/j.1365-313x.2008.03732.x;
RA Yang K.Z., Xia C., Liu X.L., Dou X.Y., Wang W., Chen L.Q., Zhang X.Q.,
RA Xie L.F., He L., Ma X., Ye D.;
RT "A mutation in thermosensitive male sterile 1, encoding a heat shock
RT protein with DnaJ and PDI domains, leads to thermosensitive gametophytic
RT male sterility in Arabidopsis.";
RL Plant J. 57:870-882(2009).
RN [7]
RP INTERACTION WITH BIP1 AND BIP3, AND INDUCTION.
RX PubMed=26186593; DOI=10.1371/journal.pone.0132500;
RA Ma Z.X., Leng Y.J., Chen G.X., Zhou P.M., Ye D., Chen L.Q.;
RT "The THERMOSENSITIVE MALE STERILE 1 interacts with the BiPs via DnaJ domain
RT and stimulates their ATPase enzyme activities in Arabidopsis.";
RL PLoS ONE 10:E0132500-E0132500(2015).
CC -!- FUNCTION: Regulates protein folding in the endoplasmic reticulum (ER)
CC lumen. Functions probably as a co-molecular chaperone that is required
CC for normal growth of pollen tubes under high-temperature stress.
CC {ECO:0000269|PubMed:18980646}.
CC -!- SUBUNIT: Interacts with BIP1 and BIP3 (PubMed:26186593). The
CC interaction with BIP1 and BIP3 activates the ATPase enzyme activities
CC of BIP1 and BIP3 (PubMed:26186593). {ECO:0000269|PubMed:26186593}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000305|PubMed:18718935}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers, mature
CC pollen grains and growing pollen tubes. {ECO:0000269|PubMed:18718935,
CC ECO:0000269|PubMed:18980646}.
CC -!- INDUCTION: Induced by tunicamycin and heat shock (PubMed:18718935,
CC PubMed:18980646). Induced by DTT and azetidine-2-carboxylate
CC (PubMed:26186593). {ECO:0000269|PubMed:18718935,
CC ECO:0000269|PubMed:18980646, ECO:0000269|PubMed:26186593}.
CC -!- PTM: Not N-glycosylated.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (permissive temperature of 22 degrees Celsius), but mutant
CC plants show gametophytic male sterility due to defect in pollen tube
CC growth at temperature of 30 degrees Celsius.
CC {ECO:0000269|PubMed:18718935, ECO:0000269|PubMed:18980646}.
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DR EMBL; AC010871; AAF07843.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74703.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM65503.1; -; Genomic_DNA.
DR EMBL; BT003887; AAO41936.1; -; mRNA.
DR EMBL; BT005001; AAO50534.1; -; mRNA.
DR RefSeq; NP_001319504.1; NM_001337788.1.
DR RefSeq; NP_187509.1; NM_111731.4.
DR AlphaFoldDB; Q9SR96; -.
DR SMR; Q9SR96; -.
DR BioGRID; 5383; 4.
DR IntAct; Q9SR96; 3.
DR MINT; Q9SR96; -.
DR STRING; 3702.AT3G08970.1; -.
DR PaxDb; Q9SR96; -.
DR PRIDE; Q9SR96; -.
DR ProteomicsDB; 222608; -.
DR EnsemblPlants; AT3G08970.1; AT3G08970.1; AT3G08970.
DR EnsemblPlants; AT3G08970.2; AT3G08970.2; AT3G08970.
DR GeneID; 820049; -.
DR Gramene; AT3G08970.1; AT3G08970.1; AT3G08970.
DR Gramene; AT3G08970.2; AT3G08970.2; AT3G08970.
DR KEGG; ath:AT3G08970; -.
DR Araport; AT3G08970; -.
DR TAIR; locus:2097643; AT3G08970.
DR eggNOG; KOG0714; Eukaryota.
DR HOGENOM; CLU_035865_0_0_1; -.
DR InParanoid; Q9SR96; -.
DR OMA; INCETDA; -.
DR OrthoDB; 628964at2759; -.
DR PhylomeDB; Q9SR96; -.
DR PRO; PR:Q9SR96; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR96; baseline and differential.
DR Genevisible; Q9SR96; AT.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0016491; F:oxidoreductase activity; IDA:TAIR.
DR GO; GO:0034605; P:cellular response to heat; TAS:TAIR.
DR GO; GO:0009860; P:pollen tube growth; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IMP:TAIR.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Endoplasmic reticulum; Glycoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..572
FT /note="DnaJ protein ERDJ3A"
FT /id="PRO_0000430368"
FT DOMAIN 27..91
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 419..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 394..423
FT /evidence="ECO:0000255"
FT COMPBIAS 422..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 431
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ 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
