DJA8_ORYSJ
ID DJA8_ORYSJ Reviewed; 447 AA.
AC P0DO03; Q5W730;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=Chaperone protein dnaJ A8, chloroplastic {ECO:0000305};
DE Short=OsDjA8 {ECO:0000303|PubMed:23160806};
DE Flags: Precursor;
GN Name=DJA8 {ECO:0000303|PubMed:23160806};
GN OrderedLocusNames=Os05g0334400 {ECO:0000312|EMBL:BAS93446.1},
GN LOC_Os05g26926 {ECO:0000305};
GN ORFNames=OJ1005_D04.18 {ECO:0000312|EMBL:AAV43842.1},
GN OSJNBa0049D13.4 {ECO:0000312|EMBL:AAW57781.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PCNA, AND INDUCTION.
RX PubMed=15806324; DOI=10.1007/s10265-005-0197-3;
RA Yamamoto T., Mori Y., Ishibashi T., Uchiyama Y., Ueda T., Ando T.,
RA Hashimoto J., Kimura S., Sakaguchi K.;
RT "Interaction between proliferating cell nuclear antigen (PCNA) and a DnaJ
RT induced by DNA damage.";
RL J. Plant Res. 118:91-97(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16261349; DOI=10.1007/s00438-005-0039-y;
RA Cheng C.-H., Chung M.C., Liu S.-M., Chen S.-K., Kao F.Y., Lin S.-J.,
RA Hsiao S.-H., Tseng I.C., Hsing Y.-I.C., Wu H.-P., Chen C.-S., Shaw J.-F.,
RA Wu J., Matsumoto T., Sasaki T., Chen H.-C., Chow T.-Y.;
RT "A fine physical map of the rice chromosome 5.";
RL Mol. Genet. Genomics 274:337-345(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23160806; DOI=10.1007/s12192-012-0384-9;
RA Sarkar N.K., Thapar U., Kundnani P., Panwar P., Grover A.;
RT "Functional relevance of J-protein family of rice (Oryza sativa).";
RL Cell Stress Chaperones 18:321-331(2013).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26210810; DOI=10.1016/j.gene.2015.07.067;
RA Zhu X., Liang S., Yin J., Yuan C., Wang J., Li W., He M., Wang J., Chen W.,
RA Ma B., Wang Y., Qin P., Li S., Chen X.;
RT "The DnaJ OsDjA7/8 is essential for chloroplast development in rice (Oryza
RT sativa).";
RL Gene 574:11-19(2015).
CC -!- FUNCTION: Plays pivotal roles in chloroplast development. Is essential
CC for the regulation of chloroplast development and differentiation.
CC {ECO:0000269|PubMed:26210810}.
CC -!- SUBUNIT: Interacts with PCNA. {ECO:0000269|PubMed:15806324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:26210810}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and panicles.
CC {ECO:0000269|PubMed:26210810}.
CC -!- INDUCTION: Induced by UV and hydrogen peroxide. Down-regulated during
CC sucrose starvation. Transiently down-regulated by heat shock.
CC {ECO:0000269|PubMed:15806324}.
CC -!- MISCELLANEOUS: Plants silencing DJA7 exhibit albino lethal phenotypes,
CC display abnormal cellular structures, organelles and chloroplasts, and
CC strong reduction of the expression of CAB1R, CAB2R, PsaA and PsbA
CC genes, tightly associated with chloroplast development.
CC {ECO:0000269|PubMed:26210810}.
CC -!- SIMILARITY: Belongs to the DnaJ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB70509.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB055405; BAB70509.1; ALT_FRAME; mRNA.
DR EMBL; AC117264; AAV43842.1; -; Genomic_DNA.
DR EMBL; AC144739; AAW57781.1; -; Genomic_DNA.
DR EMBL; AP008211; BAF17144.1; -; Genomic_DNA.
DR EMBL; AP014961; BAS93446.1; -; Genomic_DNA.
DR RefSeq; XP_015639177.1; XM_015783691.1.
DR RefSeq; XP_015639179.1; XM_015783693.1.
DR RefSeq; XP_015639180.1; XM_015783694.1.
DR RefSeq; XP_015639647.1; XM_015784161.1.
DR AlphaFoldDB; P0DO03; -.
DR SMR; P0DO03; -.
DR STRING; 39947.P0DO03; -.
DR EnsemblPlants; Os05t0333500-01; Os05t0333500-01; Os05g0333500.
DR EnsemblPlants; Os05t0333500-02; Os05t0333500-02; Os05g0333500.
DR EnsemblPlants; Os05t0334000-01; Os05t0334000-01; Os05g0334000.
DR EnsemblPlants; Os05t0334000-02; Os05t0334000-02; Os05g0334000.
DR EnsemblPlants; Os05t0334400-01; Os05t0334400-01; Os05g0334400.
DR GeneID; 107275576; -.
DR GeneID; 4338449; -.
DR GeneID; 4338452; -.
DR Gramene; Os05t0333500-01; Os05t0333500-01; Os05g0333500.
DR Gramene; Os05t0333500-02; Os05t0333500-02; Os05g0333500.
DR Gramene; Os05t0334000-01; Os05t0334000-01; Os05g0334000.
DR Gramene; Os05t0334000-02; Os05t0334000-02; Os05g0334000.
DR Gramene; Os05t0334400-01; Os05t0334400-01; Os05g0334400.
DR KEGG; osa:107275576; -.
DR KEGG; osa:4338449; -.
DR KEGG; osa:4338452; -.
DR OMA; DLHCTVT; -.
DR OrthoDB; 894595at2759; -.
DR Proteomes; UP000000763; Chromosome 5.
DR Proteomes; UP000059680; Chromosome 5.
DR ExpressionAtlas; P0DO03; baseline.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProt.
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; IEA:InterPro.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
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 TIGRFAMs; TIGR02349; DnaJ_bact; 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 Chloroplast; Metal-binding; Plastid; Reference proteome; Repeat;
KW Transit peptide; Zinc; Zinc-finger.
FT TRANSIT 1..86
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 87..447
FT /note="Chaperone protein dnaJ A8, chloroplastic"
FT /id="PRO_0000440259"
FT DOMAIN 90..154
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REPEAT 230..237
FT /note="CXXCXGXG motif 1"
FT /evidence="ECO:0000305"
FT REPEAT 247..254
FT /note="CXXCXGXG motif 2"
FT /evidence="ECO:0000305"
FT REPEAT 273..280
FT /note="CXXCXGXG motif 3"
FT /evidence="ECO:0000305"
FT REPEAT 286..293
FT /note="CXXCXGXG motif 4"
FT /evidence="ECO:0000305"
FT ZN_FING 217..298
FT /note="CR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00546"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q96EY1"
SQ SEQUENCE 447 AA; 48215 MW; 5DA6B89FF4764715 CRC64;
MALLQFGGTL APKLGEKPQL LPRSPALTRV IYADPRFLVS KSGSGGRLKH LVSPTASLQS
RTSSRLFNHA PSPRFRHRRS SRFIVRADAD FYSTLGVSRN ASKSEIKSAY RKLARSYHPD
VNKDPGAEQK FKDISNAYEV LSDDEKRSIY DKYGEAGLKG AGMGTGDYSN PFDLFESLFE
GFGGMGGMGG RAARNRPMQG DDEAYNLVLN FKEAVFGVEK EIEITRLEGC NTCDGTGAKP
GTKPTTCKTC GGQGQVVSST RTPLGIFQQV STCNTCGGTG EFSTPCNTCG GDGRVRKTKR
ISLKVPAGVD SGSRLRVRSE GNAGRRGGPP GDLYVFIDVL SDPVLKRDGT NILYTCKVSY
IDAILGTTVK VPTVDGMVDL KIPSGTQPGT TLVMSKKGVP LLGKSNARGD QLVRVQVEIP
KRLSSDERKL IEELANLNKA QTANSRR
