DNAJ3_ARATH
ID DNAJ3_ARATH Reviewed; 420 AA.
AC Q94AW8; O22663; Q42530;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Chaperone protein dnaJ 3;
DE Short=AtDjA3;
DE Short=AtJ3;
DE Flags: Precursor;
GN Name=ATJ3; Synonyms=A3, J3; OrderedLocusNames=At3g44110; ORFNames=F26G5.60;
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], INDUCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia;
RA Zhou R., Kroczyska B., Miernyk J.A.;
RT "AtJ3, an Arabidopsis thaliana J-protein homologous to Saccharomyces
RT cerevisiae YDJ1p.";
RL (er) Plant Gene Register PGR99-162(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RA Zhou R., Kroczynska B., Miernyk J.A.;
RT "The genomic sequence encoding the Arabidopsis thaliana molecular chaperone
RT AtJ3.";
RL (er) Plant Gene Register PGR00-003(2000).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
CC -!- FUNCTION: Plays a continuous role in plant development probably in the
CC structural organization of compartments. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per monomer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q94AW8; Q9SZU7: KAI2; NbExp=3; IntAct=EBI-1999282, EBI-25519488;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {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=Q94AW8-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Roots, shoots, flowers, siliques and cotyledons.
CC {ECO:0000269|Ref.1}.
CC -!- INDUCTION: A heat shock at 35 degrees Celsius for 5 hours resulted in a
CC 5-fold increase in levels. {ECO:0000269|Ref.1}.
CC -!- PTM: Farnesylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DnaJ family. A/I subfamily. {ECO:0000305}.
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DR EMBL; U22340; AAB49030.1; -; mRNA.
DR EMBL; AF032883; AAB86892.1; -; Genomic_DNA.
DR EMBL; AL353814; CAB88419.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77863.1; -; Genomic_DNA.
DR EMBL; AY035087; AAK59592.1; -; mRNA.
DR EMBL; AY045655; AAK74013.1; -; mRNA.
DR EMBL; AY113878; AAM44926.1; -; mRNA.
DR EMBL; AY088078; AAM65624.1; -; mRNA.
DR PIR; S71199; S71199.
DR PIR; T49127; T49127.
DR RefSeq; NP_189997.1; NM_114279.4. [Q94AW8-1]
DR AlphaFoldDB; Q94AW8; -.
DR SMR; Q94AW8; -.
DR BioGRID; 8851; 11.
DR IntAct; Q94AW8; 3.
DR STRING; 3702.AT3G44110.1; -.
DR iPTMnet; Q94AW8; -.
DR PaxDb; Q94AW8; -.
DR PRIDE; Q94AW8; -.
DR ProteomicsDB; 220710; -. [Q94AW8-1]
DR EnsemblPlants; AT3G44110.1; AT3G44110.1; AT3G44110. [Q94AW8-1]
DR GeneID; 823531; -.
DR Gramene; AT3G44110.1; AT3G44110.1; AT3G44110. [Q94AW8-1]
DR KEGG; ath:AT3G44110; -.
DR Araport; AT3G44110; -.
DR TAIR; locus:2081378; AT3G44110.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; Q94AW8; -.
DR OMA; GNDLHMV; -.
DR PhylomeDB; Q94AW8; -.
DR PRO; PR:Q94AW8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q94AW8; baseline and differential.
DR Genevisible; Q94AW8; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR GO; GO:0048573; P:photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0009911; P:positive regulation of flower development; IMP:TAIR.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0043462; P:regulation of ATP-dependent activity; IMP:TAIR.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd10719; DnaJ_zf; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR HAMAP; MF_01152; DnaJ; 1.
DR InterPro; IPR012724; DnaJ.
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; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR43888; PTHR43888; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF01556; DnaJ_C; 1.
DR Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF49493; SSF49493; 2.
DR SUPFAM; SSF57938; SSF57938; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51188; ZF_CR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Lipoprotein; Membrane; Metal-binding;
KW Methylation; Prenylation; Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..417
FT /note="Chaperone protein dnaJ 3"
FT /id="PRO_0000071079"
FT PROPEP 418..420
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396765"
FT DOMAIN 14..75
FT /note="J"
FT REPEAT 148..155
FT /note="CXXCXGXG motif"
FT REPEAT 164..171
FT /note="CXXCXGXG motif"
FT REPEAT 191..198
FT /note="CXXCXGXG motif"
FT REPEAT 207..214
FT /note="CXXCXGXG motif"
FT ZN_FING 135..219
FT /note="CR-type"
FT REGION 376..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..398
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 417
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 417
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 227
FT /note="E -> K (in Ref. 5; AAK74013)"
FT /evidence="ECO:0000305"
FT CONFLICT 264
FT /note="K -> Q (in Ref. 1; AAB49030)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 420 AA; 46444 MW; 3F213CF7B2E43E04 CRC64;
MFGRGPSKKS DNTKFYEILG VPKSASPEDL KKAYKKAAIK NHPDKGGDPE KFKELAQAYE
VLSDPEKREI YDQYGEDALK EGMGGGGGGH DPFDIFSSFF GGGPFGGNTS RQRRQRRGED
VVHPLKVSLE DVYLGTMKKL SLSRNALCSK CNGKGSKSGA SLKCGGCQGS GMKVSIRQLG
PGMIQQMQHA CNECKGTGET INDRDRCPQC KGDKVIPEKK VLEVNVEKGM QHSQKITFEG
QADEAPDTVT GDIVFVLQQK EHPKFKRKGE DLFVEHTLSL TEALCGFQFV LTHLDGRSLL
IKSNPGEVVK PDSYKAISDE GMPIYQRPFM KGKLYIHFTV EFPDSLSPDQ TKALEAVLPK
PSTAQLSDME IDECEETTLH DVNIEDEMRR KAQAQREAYD DDDEDDDHPG GAQRVQCAQQ
