DNJ20_ARATH
ID DNJ20_ARATH Reviewed; 197 AA.
AC Q9SDN0; Q9SVN0;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Chaperone protein dnaJ 20, chloroplastic;
DE Short=AtDjC20;
DE Short=AtJ20;
DE Flags: Precursor;
GN Name=ATJ20; Synonyms=C20, J20; OrderedLocusNames=At4g13830;
GN ORFNames=F18A5.220;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RA Miernyk J.A., Coop N.E.;
RT "AtJ20, a plastid-localized type III J-domain protein from Arabidopsis
RT thaliana.";
RL (er) Plant Gene Register PGR00-027(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [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 INDUCTION.
RX PubMed=15347791; DOI=10.1104/pp.104.044594;
RA Kimbrough J.M., Salinas-Mondragon R., Boss W.F., Brown C.S., Sederoff H.W.;
RT "The fast and transient transcriptional network of gravity and mechanical
RT stimulation in the Arabidopsis root apex.";
RL Plant Physiol. 136:2790-2805(2004).
CC -!- FUNCTION: Plays a continuous role in plant development probably in the
CC structural organization of compartments. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9SDN0; Q38854: DXS; NbExp=4; IntAct=EBI-6897500, EBI-4476357;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SDN0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Light-grown seedlings. {ECO:0000269|Ref.1}.
CC -!- INDUCTION: Down-regulated by mechanical and gravity stimulations.
CC {ECO:0000269|PubMed:15347791}.
CC -!- SIMILARITY: Belongs to the DnaJ family. C/III subfamily. {ECO:0000305}.
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DR EMBL; AF214107; AAF24498.1; -; mRNA.
DR EMBL; AL035528; CAB36847.1; -; Genomic_DNA.
DR EMBL; AL161537; CAB78425.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE83331.1; -; Genomic_DNA.
DR EMBL; AF370236; AAK44051.1; -; mRNA.
DR EMBL; AY113929; AAM44977.1; -; mRNA.
DR PIR; T05252; T05252.
DR RefSeq; NP_193119.1; NM_117457.5. [Q9SDN0-1]
DR AlphaFoldDB; Q9SDN0; -.
DR SMR; Q9SDN0; -.
DR BioGRID; 12314; 1.
DR IntAct; Q9SDN0; 1.
DR STRING; 3702.AT4G13830.2; -.
DR PaxDb; Q9SDN0; -.
DR PRIDE; Q9SDN0; -.
DR ProteomicsDB; 222083; -. [Q9SDN0-1]
DR EnsemblPlants; AT4G13830.2; AT4G13830.2; AT4G13830. [Q9SDN0-1]
DR GeneID; 827017; -.
DR Gramene; AT4G13830.2; AT4G13830.2; AT4G13830. [Q9SDN0-1]
DR KEGG; ath:AT4G13830; -.
DR Araport; AT4G13830; -.
DR TAIR; locus:2119465; AT4G13830.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_9_0_1; -.
DR InParanoid; Q9SDN0; -.
DR OMA; QYDEGME; -.
DR OrthoDB; 1280195at2759; -.
DR PhylomeDB; Q9SDN0; -.
DR PRO; PR:Q9SDN0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SDN0; baseline and differential.
DR Genevisible; Q9SDN0; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IMP:TAIR.
DR GO; GO:1902395; P:regulation of 1-deoxy-D-xylulose-5-phosphate synthase activity; IMP:TAIR.
DR GO; GO:0010322; P:regulation of isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; 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 Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Chloroplast; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..197
FT /note="Chaperone protein dnaJ 20, chloroplastic"
FT /id="PRO_0000007267"
FT DOMAIN 66..133
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 169..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 146
FT /note="Q -> R (in Ref. 1; AAF24498)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 197 AA; 23361 MW; 0C1294A54FC76642 CRC64;
MKCYKSSSIL STNHHPFFYK QQPISSLQPT SIPTTISYPT RTRFSSTRIQ SRLTHDDPVK
QSEDLSFYDL LGVTESVTLP EIKQAYKQLA RKYHPDVSPP DRVEEYTDRF IRVQEAYETL
SDPRRRVLYD RDLSMGFSFS FSGRRQNRYD QEVVEEKSEW KAKWQTQLSG LRRRSNQKDN
NTMSWAARMR RQQQESS
