DNAJ2_ARATH
ID DNAJ2_ARATH Reviewed; 419 AA.
AC P42825; Q43293; Q9C582;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Chaperone protein dnaJ 2;
DE Short=AtDjA2;
DE Flags: Precursor;
GN Name=ATJ2; Synonyms=A2, ATJ; OrderedLocusNames=At5g22060;
GN ORFNames=T6G21.11, T6G21_170;
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;
RX PubMed=7610169; DOI=10.1104/pp.108.2.821;
RA Zhou R., Kroczynska B., Hayman G.T., Miernyk J.A.;
RT "ATJ2, an Arabidopsis homolog of Escherichia coli dnaJ.";
RL Plant Physiol. 108:821-822(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 81-192.
RC STRAIN=cv. Columbia;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [6]
RP ISOPRENYLATION AT CYS-416.
RX PubMed=10873538; DOI=10.1006/prep.2000.1254;
RA Zhou R., Kroczynska B., Miernyk J.A.;
RT "Expression of the Arabidopsis thaliana AtJ2 cochaperone protein in Pichia
RT pastoris.";
RL Protein Expr. Purif. 19:253-258(2000).
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).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in both etiolated and light-grown
CC tissues. {ECO:0000269|PubMed:7610169}.
CC -!- PTM: Farnesylated. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DnaJ family. A/I subfamily. {ECO:0000305}.
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DR EMBL; L36113; AAB86799.1; -; mRNA.
DR EMBL; AL589883; CAC34499.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92977.1; -; Genomic_DNA.
DR EMBL; AK118386; BAC42997.1; -; mRNA.
DR EMBL; F20032; CAA23386.1; -; mRNA.
DR RefSeq; NP_568412.1; NM_122127.3.
DR AlphaFoldDB; P42825; -.
DR SMR; P42825; -.
DR BioGRID; 17542; 5.
DR IntAct; P42825; 1.
DR STRING; 3702.AT5G22060.1; -.
DR SwissPalm; P42825; -.
DR PaxDb; P42825; -.
DR PRIDE; P42825; -.
DR ProteomicsDB; 222001; -.
DR EnsemblPlants; AT5G22060.1; AT5G22060.1; AT5G22060.
DR GeneID; 832267; -.
DR Gramene; AT5G22060.1; AT5G22060.1; AT5G22060.
DR KEGG; ath:AT5G22060; -.
DR Araport; AT5G22060; -.
DR TAIR; locus:505006628; AT5G22060.
DR eggNOG; KOG0712; Eukaryota.
DR HOGENOM; CLU_017633_10_0_1; -.
DR InParanoid; P42825; -.
DR OMA; GMSAFNG; -.
DR OrthoDB; 1012379at2759; -.
DR PhylomeDB; P42825; -.
DR PRO; PR:P42825; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P42825; baseline and differential.
DR Genevisible; P42825; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; 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:0006457; P:protein folding; ISS:TAIR.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009408; P:response to heat; IEA:InterPro.
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 Chaperone; Lipoprotein; Membrane; Metal-binding; Methylation; Prenylation;
KW Reference proteome; Repeat; Zinc; Zinc-finger.
FT CHAIN 1..416
FT /note="Chaperone protein dnaJ 2"
FT /id="PRO_0000071078"
FT PROPEP 417..419
FT /note="Removed in mature form"
FT /evidence="ECO:0000305"
FT /id="PRO_0000396764"
FT DOMAIN 14..75
FT /note="J"
FT REPEAT 149..156
FT /note="CXXCXGXG motif"
FT REPEAT 165..172
FT /note="CXXCXGXG motif"
FT REPEAT 192..199
FT /note="CXXCXGXG motif"
FT REPEAT 208..215
FT /note="CXXCXGXG motif"
FT ZN_FING 136..220
FT /note="CR-type"
FT REGION 378..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT MOD_RES 416
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000305"
FT LIPID 416
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000305|PubMed:10873538"
FT CONFLICT 87
FT /note="G -> D (in Ref. 5; CAA23386)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="M -> L (in Ref. 1; AAB86799)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="C -> S (in Ref. 1; AAB86799)"
FT /evidence="ECO:0000305"
FT CONFLICT 328
FT /note="R -> S (in Ref. 1; AAB86799)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="D -> V (in Ref. 1; AAB86799)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="Q -> H (in Ref. 1; AAB86799)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46438 MW; A6CD4BEE2F55435E CRC64;
MFGRGPSRKS DNTKFYEILG VPKTAAPEDL KKAYKKAAIK NHPDKGGDPE KFKELAQAYE
VLSDPEKREI YDQYGEDALK EGMGGGGGGH DPFDIFSSFF GSGGHPFGSH SRGRRQRRGE
DVVHPLKVSL EDVYLGTTKK LSLSRKALCS KCNGKGSKSG ASMKCGGCQG SGMKISIRQF
GPGMMQQVQH ACNDCKGTGE TINDRDRCPQ CKGEKVVSEK KVLEVNVEKG MQHNQKITFS
GQADEAPDTV TGDIVFVIQQ KEHPKFKRKG EDLFVEHTIS LTEALCGFQF VLTHLDKRQL
LIKSKPGEVV KPDSYKAISD EGMPIYQRPF MKGKLYIHFT VEFPESLSPD QTKAIEAVLP
KPTKAAISDM EIDDCEETTL HDVNIEDEMK RKAQAQREAY DDDEEDHPGG AQRVQCAQQ
