DJC11_HUMAN
ID DJC11_HUMAN Reviewed; 559 AA.
AC Q9NVH1; Q4VWF5; Q5VZN0; Q6PK20; Q6PK70; Q8NDM2; Q96CL7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=DnaJ homolog subfamily C member 11;
GN Name=DNAJC11;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Xu J., Xie Y., Mao Y.;
RT "Identification of a novel human DNAJ domain-containing protein.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-267.
RC TISSUE=Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP SER-290.
RC TISSUE=Brain, Lung, and Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 8-559 (ISOFORM 1).
RC TISSUE=Mammary cancer;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP SUBUNIT.
RX PubMed=17624330; DOI=10.1016/j.febslet.2007.06.052;
RA Xie J., Marusich M.F., Souda P., Whitelegge J., Capaldi R.A.;
RT "The mitochondrial inner membrane protein mitofilin exists as a complex
RT with SAM50, metaxins 1 and 2, coiled-coil-helix coiled-coil-helix domain-
RT containing protein 3 and 6 and DnaJC11.";
RL FEBS Lett. 581:3545-3549(2007).
RN [7]
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., Buerckstuemmer T.,
RA 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RX PubMed=25111180; DOI=10.1371/journal.pone.0104237;
RA Ioakeimidis F., Ott C., Kozjak-Pavlovic V., Violitzi F., Rinotas V.,
RA Makrinou E., Eliopoulos E., Fasseas C., Kollias G., Douni E.;
RT "A splicing mutation in the novel mitochondrial protein DNAJC11 causes
RT motor neuron pathology associated with cristae disorganization, and
RT lymphoid abnormalities in mice.";
RL PLoS ONE 9:E104237-E104237(2014).
RN [10]
RP INTERACTION WITH THE MICOS COMPLEX, INTERACTION WITH SAM COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=25997101; DOI=10.7554/elife.06265;
RA Guarani V., McNeill E.M., Paulo J.A., Huttlin E.L., Froehlich F.,
RA Gygi S.P., Van Vactor D., Harper J.W.;
RT "QIL1 is a novel mitochondrial protein required for MICOS complex stability
RT and cristae morphology.";
RL Elife 4:0-0(2015).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: [Isoform 1]: Required for mitochondrial inner membrane
CC organization. Seems to function through its association with the MICOS
CC complex and the mitochondrial outer membrane sorting assembly machinery
CC (SAM) complex. {ECO:0000269|PubMed:25111180, ECO:0000305}.
CC -!- SUBUNIT: Associates with the mitochondrial contact site and cristae
CC organizing system (MICOS) complex, composed of at least MICOS10/MIC10,
CC CHCHD3/MIC19, CHCHD6/MIC25, APOOL/MIC27, IMMT/MIC60, APOO/MIC23/MIC26
CC and QIL1/MIC13. This complex was also known under the names MINOS or
CC MitOS complex. The MICOS complex associates with mitochondrial outer
CC membrane proteins SAMM50, MTX1 and MTX2 (together described as
CC components of the mitochondrial outer membrane sorting assembly
CC machinery (SAM) complex) and DNAJC11, mitochondrial inner membrane
CC protein TMEM11 and with HSPA9 (PubMed:25997101). The MICOS and SAM
CC complexes together with DNAJC11 are part of a large protein complex
CC spanning both mitochondrial membranes termed the mitochondrial
CC intermembrane space bridging (MIB) complex.
CC {ECO:0000269|PubMed:17624330, ECO:0000269|PubMed:25997101,
CC ECO:0000305}.
CC -!- INTERACTION:
CC Q9NVH1; P42858: HTT; NbExp=3; IntAct=EBI-1055336, EBI-466029;
CC Q9NVH1; Q9BS40: LXN; NbExp=3; IntAct=EBI-1055336, EBI-1044504;
CC Q9NVH1; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-1055336, EBI-11339910;
CC Q9NVH1; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-1055336, EBI-2799833;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25997101}.
CC Note=Isoforms show differential submitochondrial localization. A 57 kDa
CC form (potentially isoform 3) shows either mitochondrial matrix or
CC innermembrane (IM) localization, possibly anchored to the IM facing the
CC matrix. A 35 kDa form behaved either as an inner membrane space (IMS)
CC or an IM protein exposed to the IMS. {ECO:0000269|PubMed:25111180}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:25111180}; Peripheral membrane protein
CC {ECO:0000269|PubMed:25111180}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.
CC {ECO:0000305|PubMed:25111180};
CC Name=1;
CC IsoId=Q9NVH1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVH1-2; Sequence=VSP_019933;
CC Name=3;
CC IsoId=Q9NVH1-3; Sequence=VSP_019932;
CC -!- SIMILARITY: Belongs to the DNAJC11 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH08772.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY336749; AAR02411.1; -; mRNA.
DR EMBL; AK001599; BAA91780.1; -; mRNA.
DR EMBL; AL031447; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL159177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006086; AAH06086.1; -; mRNA.
DR EMBL; BC008772; AAH08772.1; ALT_INIT; mRNA.
DR EMBL; BC014145; AAH14145.1; -; mRNA.
DR EMBL; AL833841; CAD38701.1; -; mRNA.
DR CCDS; CCDS87.1; -. [Q9NVH1-1]
DR RefSeq; NP_060668.2; NM_018198.3. [Q9NVH1-1]
DR AlphaFoldDB; Q9NVH1; -.
DR SMR; Q9NVH1; -.
DR BioGRID; 120854; 211.
DR CORUM; Q9NVH1; -.
DR IntAct; Q9NVH1; 71.
DR MINT; Q9NVH1; -.
DR STRING; 9606.ENSP00000366800; -.
DR GlyGen; Q9NVH1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVH1; -.
DR PhosphoSitePlus; Q9NVH1; -.
DR SwissPalm; Q9NVH1; -.
DR BioMuta; DNAJC11; -.
DR DMDM; 110808199; -.
DR EPD; Q9NVH1; -.
DR jPOST; Q9NVH1; -.
DR MassIVE; Q9NVH1; -.
DR MaxQB; Q9NVH1; -.
DR PaxDb; Q9NVH1; -.
DR PeptideAtlas; Q9NVH1; -.
DR PRIDE; Q9NVH1; -.
DR ProteomicsDB; 82796; -. [Q9NVH1-1]
DR ProteomicsDB; 82797; -. [Q9NVH1-2]
DR ProteomicsDB; 82798; -. [Q9NVH1-3]
DR Antibodypedia; 27462; 113 antibodies from 23 providers.
DR DNASU; 55735; -.
DR Ensembl; ENST00000294401.11; ENSP00000294401.7; ENSG00000007923.17. [Q9NVH1-3]
DR Ensembl; ENST00000377577.10; ENSP00000366800.5; ENSG00000007923.17. [Q9NVH1-1]
DR GeneID; 55735; -.
DR KEGG; hsa:55735; -.
DR MANE-Select; ENST00000377577.10; ENSP00000366800.5; NM_018198.4; NP_060668.2.
DR UCSC; uc001aof.3; human. [Q9NVH1-1]
DR CTD; 55735; -.
DR DisGeNET; 55735; -.
DR GeneCards; DNAJC11; -.
DR HGNC; HGNC:25570; DNAJC11.
DR HPA; ENSG00000007923; Low tissue specificity.
DR MIM; 614827; gene.
DR neXtProt; NX_Q9NVH1; -.
DR OpenTargets; ENSG00000007923; -.
DR PharmGKB; PA134893823; -.
DR VEuPathDB; HostDB:ENSG00000007923; -.
DR eggNOG; KOG0718; Eukaryota.
DR GeneTree; ENSGT00860000133842; -.
DR HOGENOM; CLU_019611_2_0_1; -.
DR InParanoid; Q9NVH1; -.
DR OMA; SMSTQID; -.
DR OrthoDB; 532187at2759; -.
DR PhylomeDB; Q9NVH1; -.
DR TreeFam; TF105170; -.
DR PathwayCommons; Q9NVH1; -.
DR Reactome; R-HSA-8949613; Cristae formation.
DR SignaLink; Q9NVH1; -.
DR SIGNOR; Q9NVH1; -.
DR BioGRID-ORCS; 55735; 475 hits in 1092 CRISPR screens.
DR ChiTaRS; DNAJC11; human.
DR GeneWiki; DNAJC11; -.
DR GenomeRNAi; 55735; -.
DR Pharos; Q9NVH1; Tbio.
DR PRO; PR:Q9NVH1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NVH1; protein.
DR Bgee; ENSG00000007923; Expressed in metanephros cortex and 196 other tissues.
DR ExpressionAtlas; Q9NVH1; baseline and differential.
DR Genevisible; Q9NVH1; HS.
DR GO; GO:0140275; C:MIB complex; HDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IMP:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0001401; C:SAM complex; HDA:UniProtKB.
DR GO; GO:0042407; P:cristae formation; IMP:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IC:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR024586; DnaJ-like_C11_C.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF11875; DUF3395; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chaperone; Coiled coil; Membrane;
KW Mitochondrion; Mitochondrion outer membrane; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..559
FT /note="DnaJ homolog subfamily C member 11"
FT /id="PRO_0000247157"
FT DOMAIN 14..82
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT COILED 417..457
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U458"
FT VAR_SEQ 367..418
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019932"
FT VAR_SEQ 465..502
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019933"
FT VARIANT 267
FT /note="V -> M (in dbSNP:rs12137794)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_027078"
FT VARIANT 290
FT /note="T -> A (in dbSNP:rs200454)"
FT /id="VAR_027079"
FT VARIANT 290
FT /note="T -> S (in dbSNP:rs200454)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055703"
FT CONFLICT 309
FT /note="S -> I (in Ref. 1; BAA91780)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 559 AA; 63278 MW; B16D49B296362800 CRC64;
MATALSEEEL DNEDYYSLLN VRREASSEEL KAAYRRLCML YHPDKHRDPE LKSQAERLFN
LVHQAYEVLS DPQTRAIYDI YGKRGLEMEG WEVVERRRTP AEIREEFERL QREREERRLQ
QRTNPKGTIS VGVDATDLFD RYDEEYEDVS GSSFPQIEIN KMHISQSIEA PLTATDTAIL
SGSLSTQNGN GGGSINFALR RVTSAKGWGE LEFGAGDLQG PLFGLKLFRN LTPRCFVTTN
CALQFSSRGI RPGLTTVLAR NLDKNTVGYL QWRWGIQSAM NTSIVRDTKT SHFTVALQLG
IPHSFALISY QHKFQDDDQT RVKGSLKAGF FGTVVEYGAE RKISRHSVLG AAVSVGVPQG
VSLKVKLNRA SQTYFFPIHL TDQLLPSAMF YATVGPLVVY FAMHRLIIKP YLRAQKEKEL
EKQRESAATD VLQKKQEAES AVRLMQESVR RIIEAEESRM GLIIVNAWYG KFVNDKSRKS
EKVKVIDVTV PLQCLVKDSK LILTEASKAG LPGFYDPCVG EEKNLKVLYQ FRGVLHQVMV
LDSEALRIPK QSHRIDTDG
