TAD1_ARATH
ID TAD1_ARATH Reviewed; 420 AA.
AC F4HU58; Q1PFZ4; Q9LQ80;
DT 25-APR-2018, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=tRNA-specific adenosine deaminase TAD1 {ECO:0000303|PubMed:23355609};
DE Short=AtTAD1 {ECO:0000303|PubMed:23355609};
DE EC=3.5.4.34 {ECO:0000269|PubMed:23355609};
DE AltName: Full=tRNA-specific adenosine-37 deaminase TAD1 {ECO:0000305};
GN Name=TAD1 {ECO:0000303|PubMed:23355609};
GN OrderedLocusNames=At1g01760 {ECO:0000312|Araport:AT1G01760};
GN ORFNames=T1N6.17 {ECO:0000312|EMBL:AAF78409.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-356.
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=23355609; DOI=10.1093/nar/gkt013;
RA Zhou W., Karcher D., Bock R.;
RT "Importance of adenosine-to-inosine editing adjacent to the anticodon in an
RT Arabidopsis alanine tRNA under environmental stress.";
RL Nucleic Acids Res. 41:3362-3372(2013).
RN [5]
RP HOMODIMERIZATION.
RX PubMed=25315605; DOI=10.1104/pp.114.250498;
RA Zhou W., Karcher D., Bock R.;
RT "Identification of enzymes for adenosine-to-inosine editing and discovery
RT of cytidine-to-uridine editing in nucleus-encoded transfer RNAs of
RT Arabidopsis.";
RL Plant Physiol. 166:1985-1997(2014).
CC -!- FUNCTION: Involved in RNA editing. Catalyzes the specific deamination
CC of adenosine-37 in the cytosolic tRNA-Ala. Generates inosine at the
CC position 3'-adjacent to the anticodon tRNA-Ala.
CC {ECO:0000269|PubMed:23355609}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in
CC tRNA(Ala) + NH4(+); Xref=Rhea:RHEA:50968, Rhea:RHEA-COMP:12855,
CC Rhea:RHEA-COMP:12856, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.34;
CC Evidence={ECO:0000269|PubMed:23355609};
CC -!- COFACTOR:
CC Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130;
CC Evidence={ECO:0000250|UniProtKB:P53065};
CC Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
CC {ECO:0000250|UniProtKB:P53065};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25315605}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23355609}.
CC -!- TISSUE SPECIFICITY: Highly expressed in siliques. Expressed at low
CC levels in roots, rosette leaves, cauline leaves, stems and flowers.
CC {ECO:0000269|PubMed:23355609}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but mutant plants exhibit reduced growth rate under cold or
CC heat stresses. {ECO:0000269|PubMed:23355609}.
CC -!- SIMILARITY: Belongs to the ADAT1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF78409.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC009273; AAF78409.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE27332.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59691.1; -; Genomic_DNA.
DR EMBL; DQ446219; ABE65592.1; -; mRNA.
DR PIR; B86149; B86149.
DR RefSeq; NP_001322031.1; NM_001331306.1.
DR RefSeq; NP_171681.3; NM_100059.3.
DR AlphaFoldDB; F4HU58; -.
DR SMR; F4HU58; -.
DR STRING; 3702.AT1G01760.1; -.
DR PaxDb; F4HU58; -.
DR PRIDE; F4HU58; -.
DR ProteomicsDB; 233002; -.
DR EnsemblPlants; AT1G01760.1; AT1G01760.1; AT1G01760.
DR EnsemblPlants; AT1G01760.4; AT1G01760.4; AT1G01760.
DR GeneID; 839252; -.
DR Gramene; AT1G01760.1; AT1G01760.1; AT1G01760.
DR Gramene; AT1G01760.4; AT1G01760.4; AT1G01760.
DR KEGG; ath:AT1G01760; -.
DR Araport; AT1G01760; -.
DR TAIR; locus:2198185; AT1G01760.
DR HOGENOM; CLU_005382_5_1_1; -.
DR InParanoid; F4HU58; -.
DR PRO; PR:F4HU58; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; F4HU58; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003726; F:double-stranded RNA adenosine deaminase activity; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; IMP:UniProtKB.
DR GO; GO:0006382; P:adenosine to inosine editing; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0006400; P:tRNA modification; IMP:UniProtKB.
DR InterPro; IPR002466; A_deamin.
DR Pfam; PF02137; A_deamin; 1.
DR SMART; SM00552; ADEAMc; 1.
DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Nucleus; Reference proteome; tRNA processing;
KW Zinc.
FT CHAIN 1..420
FT /note="tRNA-specific adenosine deaminase TAD1"
FT /id="PRO_0000443858"
FT DOMAIN 50..417
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT ACT_SITE 76
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 80
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 223
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
SQ SEQUENCE 420 AA; 46493 MW; C194E34953CA5E14 CRC64;
MEEDWGKTVS EKVISAYMSL PKKGKPQGRE VTVLSAFLVS SPSQDPKVIA LGTGTKCVSG
SLLSPRGDIV NDSHAEVVAR RALIRFFYSE IQRMQLTSGK SNEAKRQRID SETSSILESA
DSSCPGEVKY KLKSGCLLHL YISQLPCGYA STSSPLYALK KIPSTQVDDS LLVQASDICS
SRHSDVPEIG SNSNKGNGSQ VADMVQRKPG RGETTLSVSC SDKIARWNVL GVQGALLYQV
LQPVYISTIT VGQSLHSPDN FSLADHLRRS LYERILPLSD ELLTSFRLNK PLFFVAPVPP
SEFQHSETAQ ATLTCGYSLC WNYSGLHEVI LGTTGRKQGT SAKGALYPST QSSICKQRLL
ELFLKETHGH KRESSKSKKS YRELKNKATE YYLMSKIFKG KYPFNNWLRK PLNCEDFLIN
