DUS4L_MOUSE
ID DUS4L_MOUSE Reviewed; 324 AA.
AC Q32M08; Q9D6P4;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]-like;
DE EC=1.3.1.90 {ECO:0000250|UniProtKB:O95620};
DE AltName: Full=tRNA-dihydrouridine synthase 4-like;
GN Name=Dus4l;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs. {ECO:0000250|UniProtKB:O95620}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20a) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53344, Rhea:RHEA-COMP:13535,
CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000250|UniProtKB:O95620};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53346;
CC Evidence={ECO:0000250|UniProtKB:O95620};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20a) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(20a) in tRNA; Xref=Rhea:RHEA:53348, Rhea:RHEA-COMP:13535,
CC Rhea:RHEA-COMP:13536, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000250|UniProtKB:O95620};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53350;
CC Evidence={ECO:0000250|UniProtKB:O95620};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20b) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(20b) in tRNA; Xref=Rhea:RHEA:53352, Rhea:RHEA-COMP:13537,
CC Rhea:RHEA-COMP:13538, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53354;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(20b) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(20b) in tRNA; Xref=Rhea:RHEA:53356, Rhea:RHEA-COMP:13537,
CC Rhea:RHEA-COMP:13538, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.90;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53358;
CC Evidence={ECO:0000250|UniProtKB:Q06063};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC -!- SIMILARITY: Belongs to the Dus family. Dus4 subfamily. {ECO:0000305}.
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DR EMBL; AK010138; BAB26724.1; -; mRNA.
DR EMBL; BC109351; AAI09352.1; -; mRNA.
DR CCDS; CCDS25865.1; -.
DR RefSeq; NP_082278.1; NM_028002.2.
DR AlphaFoldDB; Q32M08; -.
DR SMR; Q32M08; -.
DR STRING; 10090.ENSMUSP00000020977; -.
DR PhosphoSitePlus; Q32M08; -.
DR EPD; Q32M08; -.
DR MaxQB; Q32M08; -.
DR PaxDb; Q32M08; -.
DR PRIDE; Q32M08; -.
DR ProteomicsDB; 277639; -.
DR DNASU; 71916; -.
DR GeneID; 71916; -.
DR KEGG; mmu:71916; -.
DR UCSC; uc007nhr.1; mouse.
DR CTD; 11062; -.
DR MGI; MGI:1919166; Dus4l.
DR eggNOG; KOG2335; Eukaryota.
DR InParanoid; Q32M08; -.
DR OrthoDB; 1345916at2759; -.
DR PhylomeDB; Q32M08; -.
DR TreeFam; TF105618; -.
DR BioGRID-ORCS; 71916; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q32M08; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q32M08; protein.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central.
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; IPR001269; DUS_fam.
DR InterPro; IPR018517; tRNA_hU_synthase_CS.
DR Pfam; PF01207; Dus; 1.
DR PIRSF; PIRSF006621; Dus; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 2: Evidence at transcript level;
KW Flavoprotein; FMN; Oxidoreductase; Reference proteome; tRNA processing.
FT CHAIN 1..324
FT /note="tRNA-dihydrouridine(20a/20b) synthase [NAD(P)+]-
FT like"
FT /id="PRO_0000247348"
FT ACT_SITE 116
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 33..35
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 87
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 158
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 186
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 216..218
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 240..241
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT CONFLICT 245
FT /note="A -> T (in Ref. 1; BAB26724)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 324 AA; 36620 MW; 0E6FB06B8F1A3B7D CRC64;
MRSDSLPTTI CQERKKDPIE MFHSGQLVKV CAPMVRYSKL AFRTLVRKYS CDLCYTPMII
AADFVRSIKA RDSEFTTNQG DCPLIVQFAA NDARLLSDAA LLVCPYANGI DINCGCPQRW
AMADGYGACL INKPELVHDM VRQVRNRVES PRFSVSIKIR IHDDLARTID LCRKAEATGV
SWITVHGRTV EERHQPVHYD AIKMIKENVS IPIVANGDIR SLKEAENVWQ MTGTDGVMVA
RGLLANPAMF AGYEETPLKC IWDWVDISLE LGTPFMCFHQ HLMYMMEKIT SRQEKRVFNA
LSSTSAVLDY LTDHYGDESL SKSL
