DUS3L_MOUSE
ID DUS3L_MOUSE Reviewed; 637 AA.
AC Q91XI1; Q3TZQ1; Q7TT12;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like {ECO:0000305};
DE EC=1.3.1.89 {ECO:0000250|UniProtKB:Q06053};
DE AltName: Full=mRNA-dihydrouridine synthase DUS3L {ECO:0000305};
DE EC=1.3.1.- {ECO:0000250|UniProtKB:Q06053};
DE AltName: Full=tRNA-dihydrouridine synthase 3-like;
GN Name=Dus3l {ECO:0000312|MGI:MGI:2147092};
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] (ISOFORM 1).
RC STRAIN=BALB/cJ; TISSUE=Heart;
RA Leu M., Ehler E., Perriard J.-C.;
RT "Cloning of a putative zinc finger protein.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Spleen;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-260; SER-263 AND SER-264, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC 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: Catalyzes the synthesis of dihydrouridine, a modified base,
CC in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs
CC (lncRNAs). Mainly modifies the uridine in position 47 (U47) in the D-
CC loop of most cytoplasmic tRNAs. Also able to mediate the formation of
CC dihydrouridine in some mRNAs, thereby regulating their translation.
CC {ECO:0000250|UniProtKB:Q96G46}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(47) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(47) in tRNA; Xref=Rhea:RHEA:53364, Rhea:RHEA-COMP:13539,
CC Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89;
CC Evidence={ECO:0000250|UniProtKB:Q06053};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53366;
CC Evidence={ECO:0000250|UniProtKB:Q06053};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(47) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(47) in tRNA; Xref=Rhea:RHEA:53360, Rhea:RHEA-COMP:13539,
CC Rhea:RHEA-COMP:13540, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.89;
CC Evidence={ECO:0000250|UniProtKB:Q06053};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53362;
CC Evidence={ECO:0000250|UniProtKB:Q06053};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NAD(+) = a uridine in mRNA +
CC H(+) + NADH; Xref=Rhea:RHEA:69851, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000250|UniProtKB:Q9UTH9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69853;
CC Evidence={ECO:0000250|UniProtKB:Q9UTH9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5,6-dihydrouridine in mRNA + NADP(+) = a uridine in mRNA +
CC H(+) + NADPH; Xref=Rhea:RHEA:69855, Rhea:RHEA-COMP:14658, Rhea:RHEA-
CC COMP:17789, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:65315, ChEBI:CHEBI:74443;
CC Evidence={ECO:0000250|UniProtKB:Q9UTH9};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:69857;
CC Evidence={ECO:0000250|UniProtKB:Q9UTH9};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91XI1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91XI1-2; Sequence=VSP_019973, VSP_019974;
CC -!- SIMILARITY: Belongs to the Dus family. Dus3 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY040840; AAK84684.1; -; mRNA.
DR EMBL; AK157702; BAE34157.1; -; mRNA.
DR EMBL; BC052481; AAH52481.1; -; mRNA.
DR CCDS; CCDS28914.1; -. [Q91XI1-1]
DR RefSeq; NP_659107.2; NM_144858.2.
DR AlphaFoldDB; Q91XI1; -.
DR SMR; Q91XI1; -.
DR BioGRID; 230340; 5.
DR STRING; 10090.ENSMUSP00000007747; -.
DR iPTMnet; Q91XI1; -.
DR PhosphoSitePlus; Q91XI1; -.
DR EPD; Q91XI1; -.
DR MaxQB; Q91XI1; -.
DR PaxDb; Q91XI1; -.
DR PeptideAtlas; Q91XI1; -.
DR PRIDE; Q91XI1; -.
DR ProteomicsDB; 277611; -. [Q91XI1-1]
DR ProteomicsDB; 277612; -. [Q91XI1-2]
DR DNASU; 224907; -.
DR GeneID; 224907; -.
DR KEGG; mmu:224907; -.
DR UCSC; uc008ddd.2; mouse. [Q91XI1-1]
DR CTD; 56931; -.
DR MGI; MGI:2147092; Dus3l.
DR eggNOG; KOG2333; Eukaryota.
DR InParanoid; Q91XI1; -.
DR OrthoDB; 1016307at2759; -.
DR PhylomeDB; Q91XI1; -.
DR TreeFam; TF105726; -.
DR BioGRID-ORCS; 224907; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Dus3l; mouse.
DR PRO; PR:Q91XI1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91XI1; protein.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106414; F:mRNA dihydrouridine synthase activity; ISO:MGI.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR GO; GO:0002943; P:tRNA dihydrouridine synthesis; ISS:UniProtKB.
DR CDD; cd02801; DUS_like_FMN; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR035587; DUS-like_FMN-bd.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR Pfam; PF01207; Dus; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR PROSITE; PS01136; UPF0034; 1.
DR PROSITE; PS50103; ZF_C3H1; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Flavoprotein; FMN; Isopeptide bond; Metal-binding;
KW mRNA processing; NAD; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Repeat; tRNA processing; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..637
FT /note="tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like"
FT /id="PRO_0000247343"
FT ZN_FING 107..137
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 145..175
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 383
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 298..300
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 352
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 422
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 452
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 484..486
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 507..508
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT MOD_RES 260
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 403
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96G46"
FT VAR_SEQ 392..457
FT /note="GGGCALMNRSAKFQQIVRGVNGVLDVPLTVKMRTGVQERVSLAHRLLPELRD
FT WGVALVTLHGRSRE -> VMAALPWSLGWVWPKPGTLPCWPCVSVSPSGHGAH (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019973"
FT VAR_SEQ 458..637
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019974"
FT CONFLICT 413
FT /note="G -> E (in Ref. 2; BAE34157)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 71078 MW; 759FE837CAEBC34A CRC64;
MAETAAESGG GGDSGVGACE RGVAPIKAQY RTTKERFHEY LDGDKQEGAC QEVPTGDPAE
PGAKRIRLED GQENGKTEVA IESRERQVPK RARGQNKSRP HVKPAHYDKD RLCPSFLQEP
ATPCAFGDRC RFLHDVGRYL ETKPADLGPR CVLFETFGRC PFSMTCRFAG AHLGPEGQNL
VQEEVVARCA QLPSVRNGLD RALQQQLRKR QVCFERAEQA LNRLTQSPMP TVVPETTVAM
ATPKQNSCHA QLDTVGGAGT PQSSPVPTCG PLTDEDVIRL RPCEKKRLDI SGKLYLAPLT
TCGNLPFRRI CKRFGADVTC GEMAVCTNLL QGQMSEWALL KRHPCEDIFG VQLEGAFPDT
MTKCAELLNR TIDVDFVDIN VGCPIDLVYK KGGGCALMNR SAKFQQIVRG VNGVLDVPLT
VKMRTGVQER VSLAHRLLPE LRDWGVALVT LHGRSREQRY TRLADWPYIE QCAKVASPMP
LFGNGDILSF EDANCAMQTG VAGIMVARGA LLKPWLFTEI KEQRHWDISS SERLDILRDF
THYGLEHWGS DTQGVERTRR FLLEWLSFLC RYVPVGLLER PPQRINERPP YYLGRDYLET
LMASQQAADW IRISEMLLGP VPPGFVFLPK HKANAYK
