DJC27_ORYSJ
ID DJC27_ORYSJ Reviewed; 582 AA.
AC Q10MW6; A0A0P0VWC9; Q10MW5;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=DnaJ protein ERDJ3A {ECO:0000305};
DE AltName: Full=Chaperone protein dnaJ C27 {ECO:0000305};
DE Short=OsDjC27 {ECO:0000303|PubMed:23160806};
DE AltName: Full=Endoplasmic reticulum dnaJ domain-containing protein 3A {ECO:0000305};
DE Short=OsERdj3A {ECO:0000303|PubMed:24153418};
DE Flags: Precursor;
GN Name=ERDJ3A {ECO:0000303|PubMed:24153418}; Synonyms=DJC27 {ECO:0000305};
GN OrderedLocusNames=Os03g0293000 {ECO:0000312|EMBL:BAS83685.1},
GN LOC_Os03g18200 {ECO:0000312|EMBL:ABF95409.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16109971; DOI=10.1101/gr.3869505;
RG The rice chromosome 3 sequencing consortium;
RA Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-582.
RC STRAIN=cv. Nipponbare;
RX PubMed=12869764; DOI=10.1126/science.1081288;
RG The rice full-length cDNA consortium;
RT "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT japonica rice.";
RL Science 301:376-379(2003).
RN [6]
RP GENE FAMILY, NOMENCLATURE, AND INDUCTION BY HEAT SHOCK.
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, INTERACTION WITH BIP5, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=24153418; DOI=10.1093/jxb/ert312;
RA Ohta M., Wakasa Y., Takahashi H., Hayashi S., Kudo K., Takaiwa F.;
RT "Analysis of rice ER-resident J-proteins reveals diversity and functional
RT differentiation of the ER-resident Hsp70 system in plants.";
RL J. Exp. Bot. 64:5429-5441(2013).
CC -!- FUNCTION: May play a role in protein folding in the endoplasmic
CC reticulum. {ECO:0000305|PubMed:24153418}.
CC -!- SUBUNIT: Interacts with BIP5. {ECO:0000269|PubMed:24153418}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:24153418}. Vacuole. Note=Localizes to the vacuole
CC under ER stress. {ECO:0000269|PubMed:24153418}.
CC -!- INDUCTION: By dithiothreitol- and tunicamycin-induced endoplasmic
CC reticulum (ER) stress response (PubMed:24153418). Induced by heat shock
CC (PubMed:23160806). {ECO:0000269|PubMed:23160806,
CC ECO:0000269|PubMed:24153418}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABF95408.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=ABF95409.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF11722.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAS83685.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DP000009; ABF95408.1; ALT_SEQ; Genomic_DNA.
DR EMBL; DP000009; ABF95409.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008209; BAF11722.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014959; BAS83685.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AK063376; BAG88671.1; -; mRNA.
DR RefSeq; XP_015632727.1; XM_015777241.1.
DR AlphaFoldDB; Q10MW6; -.
DR SMR; Q10MW6; -.
DR STRING; 4530.OS03T0293000-01; -.
DR PRIDE; Q10MW6; -.
DR GeneID; 4332515; -.
DR KEGG; osa:4332515; -.
DR eggNOG; KOG0714; Eukaryota.
DR HOGENOM; CLU_035865_0_0_1; -.
DR OrthoDB; 628964at2759; -.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005773; C:vacuole; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
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 CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Endoplasmic reticulum; Glycoprotein;
KW Reference proteome; Signal; Vacuole.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..582
FT /note="DnaJ protein ERDJ3A"
FT /id="PRO_5004179725"
FT DOMAIN 29..93
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 178..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 407..437
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 582 AA; 63545 MW; FEF770CB81F83B77 CRC64;
MGIPVRSLLV ASIVLSSIAL HVAAAKNLDP YKVLGVDKSA SQRDIQKAFH KLSLKYHPDK
NKSKGAQEKF AEINNAYDIL SDEEKRKNYD LYGDEKGNPG FGGGNFGNRE GYTYFTGGGA
KTSHFSSGDG WQTMGGQGNT KTFSFSFGGG NPGAGGGNPF NFDFGDVFSN IFSGGSMGGS
QHTGSAGKAR RGTKSSGHDS SSVNIQEVTM QIFNKETADQ GITWLLLFYT PNTKGQFVLE
SVVEDVARSL DGALRAGKVN CDHEKALCKK AGVSIGKSAR LFIYSYTTTE KGSLHEYSGD
YDSKSLKTFC QEHLPRFSKR VDINQFSFPS NIIPNLPQVL LLSAKKDTPA MWRAVSGMFR
SRLIFYDAEV QDVSHPLLKS LGVKNIPALI GRSVNGEEQL LKDGISVKDL RSGIKELKNL
LENFEKKNKK LASNQAKKPA HTDQPKENKI PLLTASNFEE ICGEKTSVCI LGIFKSSKAK
ENLEAVLSEI SQKTLIRGQN YNSGNAVAYA LLDGNKQSAF LSTFDKSAFK SSDKLLLAYK
PRRGRYAVYD NEVTMEEAER FVVSVLNGDV QLSAAGRKPV LR
