DUS1L_MOUSE
ID DUS1L_MOUSE Reviewed; 475 AA.
AC Q8C2P3; Q8VCN7; Q9D124;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like;
DE EC=1.3.1.88 {ECO:0000250|UniProtKB:Q6P1R4};
DE AltName: Full=tRNA-dihydrouridine synthase 1-like;
GN Name=Dus1l;
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=NOD; TISSUE=Embryo, and Thymus;
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] OF 86-475.
RC STRAIN=FVB/N; TISSUE=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).
CC -!- FUNCTION: Catalyzes the synthesis of dihydrouridine, a modified base
CC found in the D-loop of most tRNAs. {ECO:0000250|UniProtKB:Q6P1R4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53376, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000250|UniProtKB:Q6P1R4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53378;
CC Evidence={ECO:0000250|UniProtKB:Q6P1R4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(16) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(16) in tRNA; Xref=Rhea:RHEA:53380, Rhea:RHEA-COMP:13543,
CC Rhea:RHEA-COMP:13544, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000250|UniProtKB:Q6P1R4};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53382;
CC Evidence={ECO:0000250|UniProtKB:Q6P1R4};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NAD(+) = H(+) + NADH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53372, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53374;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5,6-dihydrouridine(17) in tRNA + NADP(+) = H(+) + NADPH +
CC uridine(17) in tRNA; Xref=Rhea:RHEA:53368, Rhea:RHEA-COMP:13541,
CC Rhea:RHEA-COMP:13542, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:65315, ChEBI:CHEBI:74443; EC=1.3.1.88;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:53370;
CC Evidence={ECO:0000250|UniProtKB:P53759};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q5SMC7};
CC -!- SIMILARITY: Belongs to the Dus family. Dus1 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH19480.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB23138.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK004041; BAB23138.1; ALT_INIT; mRNA.
DR EMBL; AK088243; BAC40231.1; -; mRNA.
DR EMBL; BC019480; AAH19480.1; ALT_INIT; mRNA.
DR CCDS; CCDS49012.1; -.
DR RefSeq; NP_081100.2; NM_026824.4.
DR RefSeq; XP_006534140.1; XM_006534077.3.
DR RefSeq; XP_011247515.1; XM_011249213.2.
DR RefSeq; XP_011247516.1; XM_011249214.2.
DR AlphaFoldDB; Q8C2P3; -.
DR SMR; Q8C2P3; -.
DR STRING; 10090.ENSMUSP00000026151; -.
DR PhosphoSitePlus; Q8C2P3; -.
DR EPD; Q8C2P3; -.
DR MaxQB; Q8C2P3; -.
DR PaxDb; Q8C2P3; -.
DR PRIDE; Q8C2P3; -.
DR ProteomicsDB; 277529; -.
DR Antibodypedia; 19877; 124 antibodies from 23 providers.
DR Ensembl; ENSMUST00000167023; ENSMUSP00000132516; ENSMUSG00000025155.
DR GeneID; 68730; -.
DR KEGG; mmu:68730; -.
DR UCSC; uc007mur.1; mouse.
DR CTD; 64118; -.
DR MGI; MGI:1915980; Dus1l.
DR VEuPathDB; HostDB:ENSMUSG00000025155; -.
DR eggNOG; KOG2335; Eukaryota.
DR GeneTree; ENSGT00550000075089; -.
DR HOGENOM; CLU_013299_5_1_1; -.
DR InParanoid; Q8C2P3; -.
DR OMA; VKQYPPC; -.
DR OrthoDB; 1318230at2759; -.
DR BioGRID-ORCS; 68730; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Dus1l; mouse.
DR PRO; PR:Q8C2P3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C2P3; protein.
DR Bgee; ENSMUSG00000025155; Expressed in paneth cell and 278 other tissues.
DR ExpressionAtlas; Q8C2P3; baseline and differential.
DR Genevisible; Q8C2P3; MM.
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; IPR018517; tRNA_hU_synthase_CS.
DR Pfam; PF01207; Dus; 1.
DR PROSITE; PS01136; UPF0034; 1.
PE 2: Evidence at transcript level;
KW Flavoprotein; FMN; NAD; NADP; Oxidoreductase; Reference proteome;
KW tRNA processing.
FT CHAIN 1..475
FT /note="tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-
FT like"
FT /id="PRO_0000247227"
FT REGION 343..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 23..25
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 79
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 147
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 175
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 208..210
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT BINDING 232..233
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250|UniProtKB:Q5SMC7"
FT CONFLICT 243..244
FT /note="EG -> DD (in Ref. 1; BAB23138)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 475 AA; 53512 MW; F1CC2254238CD679 CRC64;
MPKLQGFEFW SRTLGGARHV VAPMVDQSEL AWRLLSRRHG AQLCYTPMLH AQVFVRDANY
RKENLYCDVC PEDRPLIVQF CANDPEVFVQ AALLAQDYCD AIDLNLGCPQ MIAKRGHYGA
FLQEEWDLLQ RMILLAHERL SVPVTCKIRV FPEIDKTVRY AQMLEKAGCQ LLTVHGRTKE
QKGPMAGTAS WEHIKAVRKA VGIPVFANGN IQCLQDVERC IQDTGVQGVM SAEGNLHNPA
LFEGRSPAVW ELAEEYLDIV RQHPCPLSYV RAHLFKLWHH TLQVHQQLRE ELAKVKTLEG
VAAVSQALKL RCQEDMSRQQ EGVRPADNLP AFHWICQPYI RPGPREGSKE NSGGRSKRAL
EEEEGSMEGL SKNKLKKQLR NPHKTFDPSL KPKYAKCDQC GNPKGNRCVF NLCRGCCKKR
AFRETADCPG HGLLFKTKLE KSLAWKGTQP GLQEAQQVRP VTPSGFSEVV GSALA
