DNAJ1_ARATH
ID DNAJ1_ARATH Reviewed; 408 AA.
AC Q38813; Q8GXI3; Q9FZ94;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Chaperone protein dnaJ 1, mitochondrial;
DE Short=AtDjB1;
DE Short=AtJ1;
DE Flags: Precursor;
GN Name=ATJ1; Synonyms=B1; OrderedLocusNames=At1g28210; ORFNames=F3H9.13;
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], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=8790294; DOI=10.1007/bf00042234;
RA Kroczynska B., Zhou R., Wood C., Miernyk J.A.;
RT "AtJ1, a mitochondrial homologue of the Escherichia coli DnaJ protein.";
RL Plant Mol. Biol. 31:619-629(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 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: Mitochondrion {ECO:0000269|PubMed:8790294}.
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=Q38813-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8790294}.
CC -!- SIMILARITY: Belongs to the DnaJ family. B/II subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB86798.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF98434.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U16246; AAB86798.1; ALT_FRAME; mRNA.
DR EMBL; AC021044; AAF98434.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30931.1; -; Genomic_DNA.
DR EMBL; AK118226; BAC42846.1; -; mRNA.
DR PIR; B86408; B86408.
DR PIR; S71190; S71190.
DR RefSeq; NP_174142.1; NM_102586.3.
DR RefSeq; NP_849719.1; NM_179388.2. [Q38813-1]
DR AlphaFoldDB; Q38813; -.
DR SMR; Q38813; -.
DR BioGRID; 24950; 1.
DR STRING; 3702.AT1G28210.2; -.
DR PaxDb; Q38813; -.
DR PRIDE; Q38813; -.
DR ProteomicsDB; 220711; -. [Q38813-1]
DR EnsemblPlants; AT1G28210.1; AT1G28210.1; AT1G28210. [Q38813-1]
DR GeneID; 839715; -.
DR Gramene; AT1G28210.1; AT1G28210.1; AT1G28210. [Q38813-1]
DR KEGG; ath:AT1G28210; -.
DR Araport; AT1G28210; -.
DR eggNOG; KOG0715; Eukaryota.
DR HOGENOM; CLU_017633_0_4_1; -.
DR InParanoid; Q38813; -.
DR OrthoDB; 894595at2759; -.
DR PhylomeDB; Q38813; -.
DR PRO; PR:Q38813; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38813; baseline and differential.
DR Genevisible; Q38813; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
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; 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 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 2: Evidence at transcript level;
KW Alternative splicing; Chaperone; Metal-binding; Mitochondrion;
KW Reference proteome; Repeat; Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..26
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 27..408
FT /note="Chaperone protein dnaJ 1, mitochondrial"
FT /id="PRO_0000007264"
FT DOMAIN 48..113
FT /note="J"
FT REPEAT 186..193
FT /note="CXXCXGXG motif"
FT REPEAT 203..210
FT /note="CXXCXGXG motif"
FT REPEAT 221..228
FT /note="CXXCXGXG motif"
FT REPEAT 235..242
FT /note="CXXCXGXG motif"
FT ZN_FING 173..247
FT /note="CR-type"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 206
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CONFLICT 122
FT /note="N -> S (in Ref. 4; BAC42846)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="S -> P (in Ref. 1; AAB86798)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="G -> A (in Ref. 1; AAB86798)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="G -> A (in Ref. 1; AAB86798)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 45678 MW; E0E1996683805DC8 CRC64;
MRRFNWVLRH VQARRTFDSA IGLRQGSQKP LFERYIHATG INNSSARNYY DVLGVSPKAT
REEIKKSFHE LAKKFHPDTN RNNPSAKRKF QEIREAYETL GNSERREEYD KLQYRNSDYV
NNDGGDSERF RRAYQSNFSD TFHKIFSEIF ENNQIKPDIR VELSLSLSEA AEGCTKRLSF
DAYVFCDSCD GLGHPSDAAM SICPTCRGVG RVTIPPFTAS CQTCKGTGHI IKEYCMSCRG
SGIVEGTKTA ELVIPGGVES EATITIVGAG NVSSRTSQPG NLYIKLKVAN DSTFTRDGSD
IYVDANISFT QAILGGKVVV PTLSGKIQLD IPKGTQPDQL LVLRGKGLPK QGFFVDHGDQ
YVRFRVNFPT EVNERQRAIL EEFAKEEINN ELSDSAEGSW LYQKLSTG
