DTD1_MOUSE
ID DTD1_MOUSE Reviewed; 209 AA.
AC Q9DD18; A2ANA2; Q3TY44; Q9CRE8; Q9CYL0; Q9D013; Q9D1G4;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=D-aminoacyl-tRNA deacylase 1 {ECO:0000250|UniProtKB:Q8IIS0};
DE Short=DTD;
DE EC=3.1.1.96 {ECO:0000250|UniProtKB:Q8IIS0};
DE AltName: Full=DNA-unwinding element-binding protein B;
DE Short=DUE-B;
DE AltName: Full=Gly-tRNA(Ala) deacylase {ECO:0000250|UniProtKB:Q8IIS0};
GN Name=Dtd1; Synonyms=Hars2;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Embryonic stem cell, and Visual cortex;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N-3; 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).
RN [4]
RP PROTEIN SEQUENCE OF 11-25, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-205, AND IDENTIFICATION BY
RP 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-204 AND SER-205, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [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: An aminoacyl-tRNA editing enzyme that deacylates mischarged
CC D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala),
CC protecting cells against glycine mischarging by AlaRS. Acts via tRNA-
CC based rather than protein-based catalysis; rejects L-amino acids rather
CC than detecting D-amino acids in the active site. By recycling D-
CC aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme
CC counteracts the toxicity associated with the formation of D-aminoacyl-
CC tRNA entities in vivo and helps enforce protein L-homochirality.
CC {ECO:0000250|UniProtKB:Q8IIS0}.
CC -!- FUNCTION: ATPase involved in DNA replication, may facilitate loading of
CC CDC45 onto pre-replication complexes. {ECO:0000250|UniProtKB:Q8TEA8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC Evidence={ECO:0000250|UniProtKB:Q8IIS0};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC Evidence={ECO:0000250|UniProtKB:Q8IIS0};
CC -!- SUBUNIT: Homodimer. Interacts with CDC45 and TOPBP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q8TEA8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TEA8}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8IIS0}. Note=Associated with chromatin at some
CC replication origins containing functional DNA-unwinding elements (By
CC similarity). {ECO:0000250|UniProtKB:Q8TEA8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9DD18-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9DD18-2; Sequence=VSP_026130;
CC -!- DOMAIN: A Gly-cisPro motif from one monomer fits into the active site
CC of the other monomer to allow specific chiral rejection of L-amino
CC acids. {ECO:0000250|UniProtKB:Q8IIS0}.
CC -!- PTM: Preferentially phosphorylated in cells arrested early in S phase.
CC Phosphorylation in the C-terminus weakens the interaction with CDC45
CC (By similarity). {ECO:0000250|UniProtKB:Q8TEA8}.
CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB30808.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK003594; BAB22882.1; -; mRNA.
DR EMBL; AK010822; BAB27205.1; -; mRNA.
DR EMBL; AK011917; BAB27914.1; -; mRNA.
DR EMBL; AK017565; BAB30808.1; ALT_FRAME; mRNA.
DR EMBL; AK158898; BAE34719.1; -; mRNA.
DR EMBL; AL808119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL844516; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026537; AAH26537.1; -; mRNA.
DR CCDS; CCDS16824.1; -. [Q9DD18-1]
DR RefSeq; NP_079590.1; NM_025314.3. [Q9DD18-1]
DR AlphaFoldDB; Q9DD18; -.
DR SMR; Q9DD18; -.
DR BioGRID; 211173; 1.
DR IntAct; Q9DD18; 1.
DR MINT; Q9DD18; -.
DR STRING; 10090.ENSMUSP00000028917; -.
DR iPTMnet; Q9DD18; -.
DR PhosphoSitePlus; Q9DD18; -.
DR SwissPalm; Q9DD18; -.
DR EPD; Q9DD18; -.
DR jPOST; Q9DD18; -.
DR MaxQB; Q9DD18; -.
DR PaxDb; Q9DD18; -.
DR PeptideAtlas; Q9DD18; -.
DR PRIDE; Q9DD18; -.
DR ProteomicsDB; 279817; -. [Q9DD18-1]
DR ProteomicsDB; 279818; -. [Q9DD18-2]
DR Antibodypedia; 42815; 121 antibodies from 20 providers.
DR DNASU; 66044; -.
DR Ensembl; ENSMUST00000028917; ENSMUSP00000028917; ENSMUSG00000027430. [Q9DD18-1]
DR GeneID; 66044; -.
DR KEGG; mmu:66044; -.
DR UCSC; uc008mro.2; mouse. [Q9DD18-1]
DR CTD; 92675; -.
DR MGI; MGI:1913294; Dtd1.
DR VEuPathDB; HostDB:ENSMUSG00000027430; -.
DR eggNOG; KOG3323; Eukaryota.
DR GeneTree; ENSGT00940000153431; -.
DR HOGENOM; CLU_076901_0_0_1; -.
DR InParanoid; Q9DD18; -.
DR OMA; GVFQAHM; -.
DR OrthoDB; 1411453at2759; -.
DR PhylomeDB; Q9DD18; -.
DR TreeFam; TF314886; -.
DR BioGRID-ORCS; 66044; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Dtd1; mouse.
DR PRO; PR:Q9DD18; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DD18; protein.
DR Bgee; ENSMUSG00000027430; Expressed in ventromedial nucleus of hypothalamus and 267 other tissues.
DR Genevisible; Q9DD18; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006399; P:tRNA metabolic process; IBA:GO_Central.
DR CDD; cd00563; Dtyr_deacylase; 1.
DR Gene3D; 3.50.80.10; -; 1.
DR HAMAP; MF_00518; Deacylase_Dtd; 1.
DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR InterPro; IPR023509; DTD-like_sf.
DR PANTHER; PTHR10472; PTHR10472; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; SSF69500; 1.
DR TIGRFAMs; TIGR00256; TIGR00256; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing;
KW DNA replication; DNA-binding; Hydrolase; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..209
FT /note="D-aminoacyl-tRNA deacylase 1"
FT /id="PRO_0000164627"
FT REGION 142..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 139..140
FT /note="Gly-cisPro motif, important for rejection of L-amino
FT acids"
FT /evidence="ECO:0000250|UniProtKB:Q8IIS0"
FT COMPBIAS 162..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 199..209
FT /note="AEGDVSSEREP -> DRG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_026130"
FT CONFLICT 30
FT /note="L -> F (in Ref. 1; BAB27205)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="A -> T (in Ref. 1; BAB30808)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="L -> M (in Ref. 1; BAE34719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 23384 MW; B6FBB1BB090A060F CRC64;
MKAVVQRVTR ASVTVGGEQI SAIGRGICVL LGISMEDSQK ELEHMVRKIL NLRVFEDESG
KHWSKSVMDK EYEVLCVSQF TLQCVLKGNK PDFHLAMPTE QAESFYNSFL EQLRKSYRPE
LIRDGKFGAY MQVHIQNDGP VTIELESPAP GAASSDPKQL SKLEKQQQRK EKTRAKGPSE
SSKERNAPRK EDRSASSGAE GDVSSEREP
