DNJC3_RAT
ID DNJC3_RAT Reviewed; 504 AA.
AC Q9R0T3; Q6P7A0;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DnaJ homolog subfamily C member 3;
DE AltName: Full=Interferon-induced, double-stranded RNA-activated protein kinase inhibitor;
DE AltName: Full=Protein kinase inhibitor of 58 kDa;
DE Short=Protein kinase inhibitor p58;
DE Flags: Precursor;
GN Name=Dnajc3; Synonyms=P58ipk;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pancreas;
RA Inada A., Yamada Y., Seino Y.;
RT "Rat protein kinase inhibitor p58 complete cDNA.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-434.
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in the unfolded protein response (UPR) during ER
CC stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity.
CC May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability
CC of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit
CC EIF2AK3/PERK activity (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with EIF2AK2 and EIF2AK3. Forms a trimeric complex
CC with DNAJB1 and HSPA8. Interacts with THAP12 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC -!- DOMAIN: The J domain mediates interaction with HSPA8.
CC -!- DOMAIN: Binding to misfolded proteins is mediated by a hydrophobic
CC patch forming a large groove within the first two TPR repeats.
CC {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61764.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AB017702; BAA86882.3; -; mRNA.
DR EMBL; BC061764; AAH61764.1; ALT_SEQ; mRNA.
DR RefSeq; NP_071568.1; NM_022232.1.
DR AlphaFoldDB; Q9R0T3; -.
DR SMR; Q9R0T3; -.
DR IntAct; Q9R0T3; 6.
DR STRING; 10116.ENSRNOP00000014182; -.
DR iPTMnet; Q9R0T3; -.
DR PhosphoSitePlus; Q9R0T3; -.
DR jPOST; Q9R0T3; -.
DR PaxDb; Q9R0T3; -.
DR PRIDE; Q9R0T3; -.
DR Ensembl; ENSRNOT00000014182; ENSRNOP00000014182; ENSRNOG00000010352.
DR GeneID; 63880; -.
DR KEGG; rno:63880; -.
DR UCSC; RGD:708518; rat.
DR CTD; 5611; -.
DR RGD; 708518; Dnajc3.
DR eggNOG; KOG0624; Eukaryota.
DR GeneTree; ENSGT00940000159806; -.
DR HOGENOM; CLU_015935_0_0_1; -.
DR InParanoid; Q9R0T3; -.
DR OMA; PFAHFQH; -.
DR OrthoDB; 1106865at2759; -.
DR PhylomeDB; Q9R0T3; -.
DR TreeFam; TF105162; -.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR PRO; PR:Q9R0T3; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000010352; Expressed in pancreas and 19 other tissues.
DR ExpressionAtlas; Q9R0T3; baseline and differential.
DR Genevisible; Q9R0T3; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISO:RGD.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0051787; F:misfolded protein binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0070417; P:cellular response to cold; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1903912; P:negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation; ISS:UniProtKB.
DR GO; GO:0036494; P:positive regulation of translation initiation in response to endoplasmic reticulum stress; ISS:UniProtKB.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:RGD.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; ISO:RGD.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF13181; TPR_8; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS50005; TPR; 8.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Phosphoprotein; Reference proteome;
KW Repeat; Signal; TPR repeat; Unfolded protein response.
FT SIGNAL 1..31
FT /evidence="ECO:0000255"
FT CHAIN 32..504
FT /note="DnaJ homolog subfamily C member 3"
FT /id="PRO_0000071047"
FT REPEAT 37..70
FT /note="TPR 1"
FT REPEAT 72..104
FT /note="TPR 2"
FT REPEAT 105..138
FT /note="TPR 3"
FT REPEAT 154..187
FT /note="TPR 4"
FT REPEAT 188..221
FT /note="TPR 5"
FT REPEAT 222..255
FT /note="TPR 6"
FT REPEAT 268..301
FT /note="TPR 7"
FT REPEAT 306..339
FT /note="TPR 8"
FT REPEAT 340..373
FT /note="TPR 9"
FT DOMAIN 394..462
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 375..393
FT /note="Flexible linker"
FT /evidence="ECO:0000250"
FT REGION 451..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13217"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT DISULFID 248..258
FT /evidence="ECO:0000250"
FT DISULFID 313..329
FT /evidence="ECO:0000250"
FT CONFLICT 312
FT /note="I -> V (in Ref. 1; BAA86882)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="A -> T (in Ref. 1; BAA86882)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 57561 MW; 1268B6A7771163DD CRC64;
MVAPGSVRSR LGAVFPFLLV LVDLQYEGAE CGVNADVEKH LELGKKLLAA GQLADALSQF
HAAVDGDPDN YIAYYRRATV FLAMGKSKAA LPDLTRVIEL KMDFTAARLQ RGHLLLKQGR
LAEAEDDFKK VLKSNPSENE EKEAQSQLVK ADEMQRLRAQ ALDAFDSADY TAAITFLDEI
LEVCVWDAEL RELRAECFIK EGEPRKAISD LKAASKLKND NTEAFYKISI LYYQLGDHEL
SLSEVRECLK LDQDHKRCFA HYKQVKKLNK LIGSAEELIR DGRYTDATSK YESVMKAEPS
VAEYTVRSKE RICHCFSKDE KPVEAIKICS EVLQLEPDNV NALKDRAEAY LIEEMYDEAI
QDYEAAQEQN ENDQQIREGL EKAQRLLKQS QKRDYYKILG VKRNAKKQEI IKAYRKLALQ
WHPDNFQSEE EKKKAEKKFI DIAAAKEVLS DPEMRRKFDD GEDPLDAETQ QGGGSNPFHR
SWDSWQGFNP FSSGGPFRFK FHFN
