HDGF_MOUSE
ID HDGF_MOUSE Reviewed; 237 AA.
AC P51859; Q8BPG7; Q9CYA4; Q9JK87;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Hepatoma-derived growth factor;
DE Short=HDGF;
GN Name=Hdgf; Synonyms=Tdrm1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=9299445; DOI=10.1006/bbrc.1997.7233;
RA Izumoto Y., Kuroda T., Harada H., Kishimoto T., Nakamura H.;
RT "Hepatoma-derived growth factor belongs to a gene family in mice showing
RT significant homology in the amino terminus.";
RL Biochem. Biophys. Res. Commun. 238:26-32(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Zhao Y., Chen W., Wang Y.;
RT "Cloning of novel gene related to thymus development.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Head;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Mammary gland;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Teratocarcinoma;
RX PubMed=17622165; DOI=10.1021/pr070122r;
RA Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
RT "A differential phosphoproteomic analysis of retinoic acid-treated P19
RT cells.";
RL J. Proteome Res. 6:3174-3186(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-132; SER-133 AND
RP SER-165, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132 AND SER-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18630941; DOI=10.1021/pr800223m;
RA Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
RT "Specific phosphopeptide enrichment with immobilized titanium ion affinity
RT chromatography adsorbent for phosphoproteome analysis.";
RL J. Proteome Res. 7:3957-3967(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [10]
RP SUBCELLULAR LOCATION, DOMAIN, DISULFIDE BOND, AND MUTAGENESIS OF SER-98;
RP 102-SER-SER-103; CYS-108; SER-128; SER-132; SER-133; SER-165; SER-202 AND
RP SER-206.
RX PubMed=21087088; DOI=10.1515/bc.2010.147;
RA Thakar K., Kroecher T., Savant S., Gollnast D., Kelm S., Dietz F.;
RT "Secretion of hepatoma-derived growth factor is regulated by N-terminal
RT processing.";
RL Biol. Chem. 391:1401-1410(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-128; SER-132; SER-133;
RP SER-165; SER-202 AND SER-206, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts as a transcriptional repressor (By similarity). Has
CC mitogenic activity for fibroblasts (By similarity). Heparin-binding
CC protein (By similarity). {ECO:0000250|UniProtKB:P51858}.
CC -!- SUBUNIT: Monomer, and domain-swapped homodimer (By similarity).
CC Interacts with nuclear proteins NCL and YBX1/YB1 (By similarity).
CC {ECO:0000250|UniProtKB:P51858}.
CC -!- INTERACTION:
CC P51859; Q3UMU9: Hdgfl2; NbExp=4; IntAct=EBI-2943087, EBI-7627961;
CC P51859; Q3UMU9-1; NbExp=4; IntAct=EBI-2943087, EBI-7627862;
CC P51859; Q3UMU9-3; NbExp=4; IntAct=EBI-2943087, EBI-7627932;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51858}. Cytoplasm
CC {ECO:0000250|UniProtKB:P51858}. Secreted, extracellular exosome
CC {ECO:0000269|PubMed:21087088}. Note=Secreted by exosomes and is located
CC inside the exosome (By similarity). May also be secreted as free
CC protein via an as yet unknown pathway (By similarity).
CC {ECO:0000250|UniProtKB:P51858}.
CC -!- TISSUE SPECIFICITY: Expressed predominantly in testis and skeletal
CC muscle, to intermediate extents in heart, brain, lung, liver, and
CC kidney, and to a minimal extent in spleen.
CC -!- DOMAIN: The PWWP domain harbors the heparin-binding sites and is
CC responsible for DNA-binding, while the C-terminal region is essentially
CC unstructured. {ECO:0000250|UniProtKB:P51858}.
CC -!- DOMAIN: The N-terminal region does not contain a typical signal
CC sequence but is required for secretion (PubMed:21087088). It also
CC determines exosomal location (By similarity).
CC {ECO:0000250|UniProtKB:P51858, ECO:0000269|PubMed:21087088}.
CC -!- PTM: Sumoylated with SUMO1. Sumoylation prevents binding to chromatin.
CC {ECO:0000250|UniProtKB:P51858}.
CC -!- PTM: Phosphorylation at Ser-165 is likely to be required for secretion.
CC {ECO:0000269|PubMed:21087088}.
CC -!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
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DR EMBL; D63707; BAA09838.1; -; mRNA.
DR EMBL; AF251787; AAF65469.1; -; mRNA.
DR EMBL; AK017863; BAB30979.1; -; mRNA.
DR EMBL; AK029475; BAC26466.1; -; mRNA.
DR EMBL; AK076021; BAC36126.1; -; mRNA.
DR EMBL; BC005713; AAH05713.1; -; mRNA.
DR EMBL; BC021654; AAH21654.1; -; mRNA.
DR CCDS; CCDS17457.1; -.
DR PIR; JC5660; JC5660.
DR RefSeq; NP_032257.3; NM_008231.4.
DR AlphaFoldDB; P51859; -.
DR BMRB; P51859; -.
DR SMR; P51859; -.
DR BioGRID; 200265; 45.
DR IntAct; P51859; 6.
DR MINT; P51859; -.
DR STRING; 10090.ENSMUSP00000005017; -.
DR iPTMnet; P51859; -.
DR PhosphoSitePlus; P51859; -.
DR SwissPalm; P51859; -.
DR EPD; P51859; -.
DR jPOST; P51859; -.
DR MaxQB; P51859; -.
DR PaxDb; P51859; -.
DR PeptideAtlas; P51859; -.
DR PRIDE; P51859; -.
DR ProteomicsDB; 269821; -.
DR TopDownProteomics; P51859; -.
DR Antibodypedia; 34226; 368 antibodies from 38 providers.
DR DNASU; 15191; -.
DR Ensembl; ENSMUST00000005017; ENSMUSP00000005017; ENSMUSG00000004897.
DR GeneID; 15191; -.
DR KEGG; mmu:15191; -.
DR UCSC; uc008ptc.2; mouse.
DR CTD; 3068; -.
DR MGI; MGI:1194494; Hdgf.
DR VEuPathDB; HostDB:ENSMUSG00000004897; -.
DR eggNOG; KOG1904; Eukaryota.
DR GeneTree; ENSGT00940000157485; -.
DR InParanoid; P51859; -.
DR OMA; RGRFVPQ; -.
DR OrthoDB; 530959at2759; -.
DR PhylomeDB; P51859; -.
DR TreeFam; TF105385; -.
DR BioGRID-ORCS; 15191; 3 hits in 76 CRISPR screens.
DR ChiTaRS; Hdgf; mouse.
DR PRO; PR:P51859; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P51859; protein.
DR Bgee; ENSMUSG00000004897; Expressed in otic placode and 278 other tissues.
DR ExpressionAtlas; P51859; baseline and differential.
DR Genevisible; P51859; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0017053; C:transcription repressor complex; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; ISO:MGI.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0098761; P:cellular response to interleukin-7; IDA:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0051781; P:positive regulation of cell division; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd05834; HDGF_related; 1.
DR InterPro; IPR035496; HDGF-rel_PWWP.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
DR PROSITE; PS50812; PWWP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Disulfide bond; DNA-binding; Growth factor;
KW Heparin-binding; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Secreted; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..237
FT /note="Hepatoma-derived growth factor"
FT /id="PRO_0000191701"
FT DOMAIN 12..69
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT REGION 69..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 75..80
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 155..170
FT /note="Bipartite nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 69..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..223
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 21
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT MOD_RES 44
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:18630941, ECO:0007744|PubMed:21183079"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VHK7"
FT MOD_RES 200
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 236
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT DISULFID 12..108
FT /evidence="ECO:0000269|PubMed:21087088"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P51858"
FT MUTAGEN 12
FT /note="C->A: Abolishes disulfide bond formation."
FT /evidence="ECO:0000269|PubMed:21087088"
FT MUTAGEN 98
FT /note="S->A: Does not affect secretion."
FT /evidence="ECO:0000269|PubMed:21087088"
FT MUTAGEN 102..103
FT /note="SS->AA: Does not affect secretion."
FT /evidence="ECO:0000269|PubMed:21087088"
FT MUTAGEN 108
FT /note="C->A: Abolishes disulfide bond formation."
FT /evidence="ECO:0000269|PubMed:21087088"
FT MUTAGEN 128
FT /note="S->A: Does not affect secretion."
FT /evidence="ECO:0000269|PubMed:21087088"
FT MUTAGEN 132
FT /note="S->A: Does not affect secretion."
FT /evidence="ECO:0000269|PubMed:21087088"
FT MUTAGEN 133
FT /note="S->A: Does not affect secretion."
FT /evidence="ECO:0000269|PubMed:21087088"
FT MUTAGEN 165
FT /note="S->A: Abolishes secretion."
FT /evidence="ECO:0000269|PubMed:21087088"
FT MUTAGEN 202
FT /note="S->A: Does not affect secretion."
FT /evidence="ECO:0000269|PubMed:21087088"
FT MUTAGEN 206
FT /note="S->A: Does not affect secretion."
FT /evidence="ECO:0000269|PubMed:21087088"
FT CONFLICT 118
FT /note="A -> D (in Ref. 3; BAB30979)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="P -> H (in Ref. 1; BAA09838)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="Q -> E (in Ref. 3; BAC36126)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="Q -> P (in Ref. 1; BAA09838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 26269 MW; AAE4CF574DA4733F CRC64;
MSRSNRQKEY KCGDLVFAKM KGYPHWPARI DEMPEAAVKS TANKYQVFFF GTHETAFLGP
KDLFPYEESK EKFGKPNKRK GFSEGLWEIE NNPTVKASGY QSSQKKSCAA EPEVEPEAHE
GDGDKKGSAE GSSDEEGKLV IDEPAKEKNE KGTLKRRAGD VLEDSPKRPK ESGDHEEEDK
EIAALEGERP LPVEVEKNST PSEPDSGQGP PAEEEEGEEE AAKEEAEAQG VRDHESL
