ID   DNJ13_ARATH             Reviewed;         538 AA.
AC   Q39079; Q9SL89;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 2.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Chaperone protein dnaJ 13;
DE            Short=AtDjB13;
DE            Short=AtJ13;
GN   Name=ATJ13; Synonyms=B13, D3; OrderedLocusNames=At2g35720;
GN   ORFNames=T20F21.9;
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], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=cv. Columbia; TISSUE=Leaf;
RX   PubMed=7479844; DOI=10.1073/pnas.92.23.10580;
RA   Kushnir S., Babiychuk E., Kampfenkel K., Belles-Boix E., Van Montagu M.,
RA   Inze D.;
RT   "Characterization of Arabidopsis thaliana cDNAs that render yeasts tolerant
RT   toward the thiol-oxidizing drug diamide.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:10580-10584(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(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   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   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC   -!- FUNCTION: Plays a continuous role in plant development probably in the
CC       structural organization of compartments (By similarity). Seems to be
CC       involved in resistance to oxidative stresses mediated by thiol-
CC       oxidizing agents such as diamide. {ECO:0000250,
CC       ECO:0000269|PubMed:7479844}.
CC   -!- INTERACTION:
CC       Q39079; Q9FE22: HFR1; NbExp=3; IntAct=EBI-2461966, EBI-626001;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Constitutively expressed in roots, stems, leaves
CC       and flowers. {ECO:0000269|PubMed:7479844}.
CC   -!- INDUCTION: Not induced by methyl viologen (paraquat), menadione,
CC       diamide, t-BuOOH, dithiothreitol (DTT) and H(2)O(2).
CC       {ECO:0000269|PubMed:7479844}.
CC   -!- SIMILARITY: Belongs to the DnaJ family. B/II subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD15443.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; Z49238; CAA89204.1; -; mRNA.
DR   EMBL; AC006068; AAD15443.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP002685; AEC09150.1; -; Genomic_DNA.
DR   PIR; B84772; B84772.
DR   PIR; S58287; S58287.
DR   RefSeq; NP_181115.2; NM_129128.4.
DR   AlphaFoldDB; Q39079; -.
DR   SMR; Q39079; -.
DR   IntAct; Q39079; 1.
DR   STRING; 3702.AT2G35720.1; -.
DR   iPTMnet; Q39079; -.
DR   PaxDb; Q39079; -.
DR   PRIDE; Q39079; -.
DR   ProteomicsDB; 222079; -.
DR   EnsemblPlants; AT2G35720.1; AT2G35720.1; AT2G35720.
DR   GeneID; 818142; -.
DR   Gramene; AT2G35720.1; AT2G35720.1; AT2G35720.
DR   KEGG; ath:AT2G35720; -.
DR   Araport; AT2G35720; -.
DR   TAIR; locus:2058704; AT2G35720.
DR   eggNOG; KOG0718; Eukaryota.
DR   HOGENOM; CLU_019611_0_1_1; -.
DR   InParanoid; Q39079; -.
DR   OMA; SMSTQID; -.
DR   OrthoDB; 532187at2759; -.
DR   PhylomeDB; Q39079; -.
DR   PRO; PR:Q39079; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q39079; baseline and differential.
DR   Genevisible; Q39079; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:TAIR.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0055122; P:response to very low light intensity stimulus; IMP:TAIR.
DR   GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; -; 1.
DR   InterPro; IPR042162; AtJ13.
DR   InterPro; IPR024586; DnaJ-like_C11_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR44914; PTHR44914; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF11875; DUF3395; 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   Acetylation; Chaperone; Coiled coil; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..538
FT                   /note="Chaperone protein dnaJ 13"
FT                   /id="PRO_0000071082"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          15..83
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   COILED          96..124
FT                   /evidence="ECO:0000255"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CONFLICT        459
FT                   /note="E -> EE (in Ref. 1; CAA89204)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   538 AA;  59232 MW;  7DFCB509E216AC76 CRC64;
     MMGQEAAPTG PPNRELYALL NLSPEASDEE IRKAYRQWAQ VYHPDKIQSP QMKEVATENF
     QRICEAYEIL SDETKRLIYD LYGMEGLNSG LELGPRLSKA DEIKEELERI KRRNEEAKKM
     AHFQPTGSIL FNLSVPHFLV GDGIMRGMVM ASQVQSQLSK DDAIAIGGNL AANEKSGGGV
     ATAILRRQIS PVSSIEFVAS TGLQSLIGVQ TTRQLTIHST ATINISKSLS DGSINLTNTW
     TRQLSETSSG NIELALGMRS AITVGWKKRD ENVSAAGDFK IESGGLGASA RYTRKLSSKS
     HGRIVGRIGS NALEIELGGG RQISEFSTVR MMYTVGLKGI FWKVELHRGS QKLIVPILLS
     AHLAPVFATG AFIVPTSLYF LLKKFVVKPY LLKREKQKAL ENMEKTWGQV GEARARAEKA
     QQLLQTVATR KKNRQVETDG LIVTKALYGD PKAIERRNEG VEGLDSGVID VTVPMNFLVS
     DSGQLKLHEG VKKSGIMGFC DPCPGQPKQL YIAYTYHSQP FEVIVGDYEE LSIPQEGQ