DNJ19_ARATH
ID DNJ19_ARATH Reviewed; 346 AA.
AC Q9LZK5;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DnaJ protein ERDJ3B;
DE AltName: Full=Chaperone protein dnaJ 19;
DE Short=AtDjB19;
DE Short=AtJ19;
DE AltName: Full=Endoplasmic reticulum dnaJ domain-containing protein 3B;
DE Short=AtERdj3B;
DE AltName: Full=Protein SCJ1 homolog ERDJ3B;
DE Flags: Precursor;
GN Name=ERDJ3B; Synonyms=B19; OrderedLocusNames=At3g62600; ORFNames=F26K9.30;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION BY TUNICAMYCIN,
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 [7]
RP FUNCTION, INTERACTION WITH SDF2 AND MED37A/BIP1, AND DISRUPTION PHENOTYPE.
RX PubMed=19763086; DOI=10.1038/emboj.2009.262;
RA Nekrasov V., Li J., Batoux M., Roux M., Chu Z.H., Lacombe S., Rougon A.,
RA Bittel P., Kiss-Papp M., Chinchilla D., van Esse H.P., Jorda L.,
RA Schwessinger B., Nicaise V., Thomma B.P., Molina A., Jones J.D., Zipfel C.;
RT "Control of the pattern-recognition receptor EFR by an ER protein complex
RT in plant immunity.";
RL EMBO J. 28:3428-3438(2009).
CC -!- FUNCTION: Regulates protein folding in the endoplasmic reticulum (ER)
CC lumen. Forms a complex in the ER with SDF2 and MED37A/BIP1 which is
CC required for the proper accumulation and function of the surface-
CC exposed leucine-rich repeat receptor kinases EFR involved in pathogen-
CC associated molecular pattern (PAMP) triggered immunity.
CC {ECO:0000269|PubMed:19763086}.
CC -!- SUBUNIT: Interacts with SDF2 and MED37A/BIP1.
CC {ECO:0000269|PubMed:19763086}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000305|PubMed:18718935}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, flower buds and flowers.
CC {ECO:0000269|PubMed:18718935}.
CC -!- INDUCTION: By tunicamycin. {ECO:0000269|PubMed:18718935}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18718935}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants are insensitive to seedling growth
CC inhibition in response to the pathogen-associated molecular pattern
CC (PAMP) elf18. The double mutant erdj3b and p58ipk is male gametophytic
CC lethal. {ECO:0000269|PubMed:18718935, ECO:0000269|PubMed:19763086}.
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DR EMBL; AL162651; CAB83110.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80368.1; -; Genomic_DNA.
DR EMBL; AY125534; AAM78044.1; -; mRNA.
DR EMBL; AY094429; AAM19802.1; -; mRNA.
DR EMBL; AY087640; AAM65179.1; -; mRNA.
DR PIR; T48049; T48049.
DR RefSeq; NP_191819.1; NM_116125.3.
DR AlphaFoldDB; Q9LZK5; -.
DR SMR; Q9LZK5; -.
DR BioGRID; 10748; 3.
DR IntAct; Q9LZK5; 4.
DR MINT; Q9LZK5; -.
DR STRING; 3702.AT3G62600.1; -.
DR iPTMnet; Q9LZK5; -.
DR PaxDb; Q9LZK5; -.
DR PRIDE; Q9LZK5; -.
DR ProteomicsDB; 222082; -.
DR EnsemblPlants; AT3G62600.1; AT3G62600.1; AT3G62600.
DR GeneID; 825434; -.
DR Gramene; AT3G62600.1; AT3G62600.1; AT3G62600.
DR KEGG; ath:AT3G62600; -.
DR Araport; AT3G62600; -.
DR TAIR; locus:2081725; AT3G62600.
DR eggNOG; KOG0713; Eukaryota.
DR HOGENOM; CLU_017633_0_0_1; -.
DR InParanoid; Q9LZK5; -.
DR OMA; DHCRGSG; -.
DR OrthoDB; 687505at2759; -.
DR PhylomeDB; Q9LZK5; -.
DR PRO; PR:Q9LZK5; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LZK5; baseline and differential.
DR Genevisible; Q9LZK5; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:TAIR.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0002221; P:pattern recognition receptor signaling pathway; IMP:TAIR.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR002939; DnaJ_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR044713; DNJA1/2-like.
DR InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43888; PTHR43888; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Endoplasmic reticulum; Glycoprotein; Reference proteome; Signal;
KW Stress response.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..346
FT /note="DnaJ protein ERDJ3B"
FT /id="PRO_0000430363"
FT DOMAIN 26..91
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 346 AA; 39200 MW; 9631C98ABD2AF0B8 CRC64;
MAIRWSELCI VLFALSYAIC VLAGKSYYDV LQVPKGASDE QIKRAYRKLA LKYHPDKNQG
NEEATRKFAE INNAYEVLSD EEKREIYNKY GEEGLKQFSA NGGRGGGGGG MNMQDIFSSF
FGGGSMEEEE KVVKGDDVIV ELEATLEDLY MGGSMKVWRE KNVIKPAPGK RKCNCRNEVY
HRQIGPGMFQ QMTEQVCDKC PNVKYEREGY FVTVDIEKGM KDGEEVSFYE DGEPILDGDP
GDLKFRIRTA PHARFRRDGN DLHMNVNITL VEALVGFEKS FKHLDDHEVD ISSKGITKPK
EVKKFKGEGM PLHYSTKKGN LFVTFEVLFP SSLTDDQKKK IKEVFA
