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Database: UniProt
Entry: Q13217
LinkDB: Q13217
Original site: Q13217 
ID   DNJC3_HUMAN             Reviewed;         504 AA.
AC   Q13217; Q86WT9; Q8N4N2;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   26-NOV-2014, entry version 133.
DE   RecName: Full=DnaJ homolog subfamily C member 3;
DE   AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 6;
DE            Short=ER-resident protein ERdj6;
DE            Short=ERdj6;
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, PRKRI;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=8666242; DOI=10.1016/0378-1119(95)00883-7;
RA   Korth M.J., Lyons C.N., Wambach M., Katze M.G.;
RT   "Cloning, expression, and cellular localization of the oncogenic 58-
RT   kDa inhibitor of the RNA-activated human and mouse protein kinase.";
RL   Gene 170:181-188(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NIEHS SNPs program;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
RA   Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
RA   Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
RA   Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
RA   Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
RA   Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
RA   Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
RA   Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
RA   Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
RA   Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
RA   Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
RA   Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
RA   King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
RA   Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
RA   Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
RA   Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
RA   Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
RA   Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
RA   Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Leukocyte;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH EIF2AK2.
RX   PubMed=8576172; DOI=10.1074/jbc.271.3.1702;
RA   Polyak S.J., Tang N., Wambach M., Barber G.N., Katze M.G.;
RT   "The P58 cellular inhibitor complexes with the interferon-induced,
RT   double-stranded RNA-dependent protein kinase, PKR, to regulate its
RT   autophosphorylation and activity.";
RL   J. Biol. Chem. 271:1702-1707(1996).
RN   [6]
RP   FUNCTION, INTERACTION WITH PRKRIR, AND INDUCTION.
RX   PubMed=9447982;
RA   Gale M.J. Jr., Blakely C.M., Hopkins D.A., Melville M.W., Wambach M.,
RA   Romano P.R., Katze M.G.;
RT   "Regulation of interferon-induced protein kinase PKR: modulation of
RT   P58IPK inhibitory function by a novel protein, P52rIPK.";
RL   Mol. Cell. Biol. 18:859-871(1998).
RN   [7]
RP   FUNCTION, INTERACTION WITH DNAJB1 AND HSPA8, AND INDUCTION.
RX   PubMed=9920933; DOI=10.1074/jbc.274.6.3797;
RA   Melville M.W., Tan S.-L., Wambach M., Song J., Morimoto R.I.,
RA   Katze M.G.;
RT   "The cellular inhibitor of the PKR protein kinase, P58(IPK), is an
RT   influenza virus-activated co-chaperone that modulates heat shock
RT   protein 70 activity.";
RL   J. Biol. Chem. 274:3797-3803(1999).
RN   [8]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=12601012; DOI=10.1074/jbc.M212074200;
RA   van Huizen R., Martindale J.L., Gorospe M., Holbrook N.J.;
RT   "P58IPK, a novel endoplasmic reticulum stress-inducible protein and
RT   potential negative regulator of eIF2alpha signaling.";
RL   J. Biol. Chem. 278:15558-15564(2003).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 35-461, AND DISULFIDE BONDS.
RX   PubMed=21799829; DOI=10.1371/journal.pone.0022337;
RA   Svard M., Biterova E.I., Bourhis J.M., Guy J.E.;
RT   "The crystal structure of the human co-chaperone P58(IPK).";
RL   PLoS ONE 6:E22337-E22337(2011).
CC   -!- FUNCTION: Involved in the unfolded protein response (UPR) during
CC       ER stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase
CC       activity. May inhibit both the autophosphorylation of EIF2AK2/PKR
CC       and the ability of EIF2AK2 to catalyze phosphorylation of the
CC       EIF2A. May inhibit EIF2AK3/PERK activity.
CC       {ECO:0000269|PubMed:12601012, ECO:0000269|PubMed:8576172,
CC       ECO:0000269|PubMed:9447982, ECO:0000269|PubMed:9920933}.
CC   -!- SUBUNIT: Interacts with EIF2AK3 (By similarity) and EIF2AK2. Forms
CC       a trimeric complex with DNAJB1 and HSPA8. Interacts with
CC       PRKRIR/P52RIPK. {ECO:0000269|PubMed:8576172,
CC       ECO:0000269|PubMed:9447982, ECO:0000269|PubMed:9920933}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Widely expressed with high level in the
CC       pancreas and testis. Also expressed in cell lines with different
CC       levels. {ECO:0000269|PubMed:8666242}.
CC   -!- INDUCTION: Up-regulated during an endoplasmic reticulum stress via
CC       ATF6. Activated in response to infection by influenza virus
CC       through the dissociation of DNAJB1. Down-regulated by DNAJB1 and
CC       PRKRIR/P52RIPK. {ECO:0000269|PubMed:12601012,
CC       ECO:0000269|PubMed:9447982, ECO:0000269|PubMed:9920933}.
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   -!- SIMILARITY: Contains 1 J domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00286}.
CC   -!- SIMILARITY: Contains 9 TPR repeats. {ECO:0000255|PROSITE-
CC       ProRule:PRU00339}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/dnajc3/";
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DR   EMBL; U28424; AAC50502.1; -; mRNA.
DR   EMBL; AY795482; AAV40838.1; -; Genomic_DNA.
DR   EMBL; AL138955; CAH70090.1; -; Genomic_DNA.
DR   EMBL; BC047936; AAH47936.2; -; mRNA.
DR   CCDS; CCDS9479.1; -.
DR   PIR; JC4775; JC4775.
DR   RefSeq; NP_006251.1; NM_006260.4.
DR   UniGene; Hs.59214; -.
DR   PDB; 2Y4T; X-ray; 3.00 A; A/B/C=35-461.
DR   PDB; 2Y4U; X-ray; 3.20 A; A=35-461.
DR   PDBsum; 2Y4T; -.
DR   PDBsum; 2Y4U; -.
DR   ProteinModelPortal; Q13217; -.
DR   SMR; Q13217; 35-455.
DR   BioGrid; 111597; 9.
DR   IntAct; Q13217; 1.
DR   MINT; MINT-1531270; -.
DR   STRING; 9606.ENSP00000365991; -.
DR   PhosphoSite; Q13217; -.
DR   DMDM; 73620807; -.
DR   MaxQB; Q13217; -.
DR   PaxDb; Q13217; -.
DR   PeptideAtlas; Q13217; -.
DR   PRIDE; Q13217; -.
DR   Ensembl; ENST00000602402; ENSP00000473631; ENSG00000102580.
DR   GeneID; 5611; -.
DR   KEGG; hsa:5611; -.
DR   UCSC; uc001vmq.3; human.
DR   CTD; 5611; -.
DR   GeneCards; GC13P096329; -.
DR   HGNC; HGNC:9439; DNAJC3.
DR   HPA; HPA039336; -.
DR   HPA; HPA041326; -.
DR   MIM; 601184; gene.
DR   neXtProt; NX_Q13217; -.
DR   PharmGKB; PA27420; -.
DR   eggNOG; COG0484; -.
DR   GeneTree; ENSGT00720000108760; -.
DR   HOGENOM; HOG000193351; -.
DR   HOVERGEN; HBG053820; -.
DR   InParanoid; Q13217; -.
DR   KO; K09523; -.
DR   OMA; QNENDQQ; -.
DR   OrthoDB; EOG70KGPH; -.
DR   PhylomeDB; Q13217; -.
DR   TreeFam; TF105162; -.
DR   Reactome; REACT_18273; XBP1(S) activates chaperone genes.
DR   Reactome; REACT_9491; Viral mRNA Translation.
DR   ChiTaRS; DNAJC3; human.
DR   GeneWiki; DNAJC3; -.
DR   GenomeRNAi; 5611; -.
DR   NextBio; 21810; -.
DR   PRO; PR:Q13217; -.
DR   Bgee; Q13217; -.
DR   CleanEx; HS_DNAJC3; -.
DR   ExpressionAtlas; Q13217; baseline and differential.
DR   Genevestigator; Q13217; -.
DR   GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR   GO; GO:0031205; C:endoplasmic reticulum Sec complex; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR   GO; GO:0004860; F:protein kinase inhibitor activity; TAS:ProtInc.
DR   GO; GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:Reactome.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; TAS:GOC.
DR   GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:Ensembl.
DR   Gene3D; 1.10.287.110; -; 1.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR026901; DNAJC3.
DR   InterPro; IPR013026; TPR-contain_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR24078:SF165; PTHR24078:SF165; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00515; TPR_1; 2.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00028; TPR; 7.
DR   SUPFAM; SSF46565; SSF46565; 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   3D-structure; Antiviral defense; Chaperone; Complete proteome;
KW   Disulfide bond; Endoplasmic reticulum; Reference proteome; Repeat;
KW   Signal; TPR repeat; Unfolded protein response.
FT   SIGNAL        1     31       {ECO:0000255}.
FT   CHAIN        32    504       DnaJ homolog subfamily C member 3.
FT                                /FTId=PRO_0000071045.
FT   REPEAT       37     70       TPR 1.
FT   REPEAT       72    104       TPR 2.
FT   REPEAT      105    138       TPR 3.
FT   REPEAT      154    187       TPR 4.
FT   REPEAT      189    221       TPR 5.
FT   REPEAT      222    255       TPR 6.
FT   REPEAT      268    301       TPR 7.
FT   REPEAT      306    339       TPR 8.
FT   REPEAT      340    373       TPR 9.
FT   DOMAIN      394    462       J. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00286}.
FT   REGION      375    393       Flexible linker.
FT   DISULFID    248    258       {ECO:0000269|PubMed:21799829}.
FT   DISULFID    313    329       {ECO:0000269|PubMed:21799829}.
FT   HELIX        35     49       {ECO:0000244|PDB:2Y4T}.
FT   HELIX        53     66       {ECO:0000244|PDB:2Y4T}.
FT   HELIX        71     83       {ECO:0000244|PDB:2Y4T}.
FT   HELIX        87    100       {ECO:0000244|PDB:2Y4T}.
FT   TURN        101    103       {ECO:0000244|PDB:2Y4U}.
FT   HELIX       105    117       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       121    132       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       138    167       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       170    183       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       188    200       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       204    207       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       208    218       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       222    234       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       238    251       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       256    281       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       284    297       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       302    317       {ECO:0000244|PDB:2Y4T}.
FT   TURN        318    320       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       322    335       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       340    352       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       356    367       {ECO:0000244|PDB:2Y4T}.
FT   STRAND      370    372       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       374    391       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       396    398       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       409    420       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       423    425       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       429    448       {ECO:0000244|PDB:2Y4T}.
FT   HELIX       451    454       {ECO:0000244|PDB:2Y4T}.
SQ   SEQUENCE   504 AA;  57580 MW;  E720A1E7F618B912 CRC64;
     MVAPGSVTSR LGSVFPFLLV LVDLQYEGAE CGVNADVEKH LELGKKLLAA GQLADALSQF
     HAAVDGDPDN YIAYYRRATV FLAMGKSKAA LPDLTKVIQL KMDFTAARLQ RGHLLLKQGK
     LDEAEDDFKK VLKSNPSENE EKEAQSQLIK SDEMQRLRSQ ALNAFGSGDY TAAIAFLDKI
     LEVCVWDAEL RELRAECFIK EGEPRKAISD LKAASKLKND NTEAFYKIST LYYQLGDHEL
     SLSEVRECLK LDQDHKRCFA HYKQVKKLNK LIESAEELIR DGRYTDATSK YESVMKTEPS
     IAEYTVRSKE RICHCFSKDE KPVEAIRVCS EVLQMEPDNV NALKDRAEAY LIEEMYDEAI
     QDYETAQEHN ENDQQIREGL EKAQRLLKQS QKRDYYKILG VKRNAKKQEI IKAYRKLALQ
     WHPDNFQNEE EKKKAEKKFI DIAAAKEVLS DPEMRKKFDD GEDPLDAESQ QGGGGNPFHR
     SWNSWQGFNP FSSGGPFRFK FHFN
//
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