ADAT1_MOUSE
ID ADAT1_MOUSE Reviewed; 499 AA.
AC Q9JHI2; Q3TU04; Q8CBP0; Q8VE23;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=tRNA-specific adenosine deaminase 1;
DE Short=mADAT1;
DE EC=3.5.4.34;
DE AltName: Full=tRNA-specific adenosine-37 deaminase;
GN Name=Adat1;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), FUNCTION, AND ENZYME
RP ACTIVITY.
RC STRAIN=129/Sv;
RX PubMed=10675613; DOI=10.1016/s0378-1119(99)00562-4;
RA Maas S., Kim Y.-G., Rich A.;
RT "Sequence, genomic organization and functional expression of the murine
RT tRNA-specific adenosine deaminase ADAT1.";
RL Gene 243:59-66(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Skin, Spinal cord, and Urinary bladder;
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 STRAIN=FVB/N; TISSUE=Mammary tumor;
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 SER-191, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, and Pancreas;
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: Specifically deaminates adenosine-37 to inosine in tRNA-Ala.
CC {ECO:0000269|PubMed:10675613}.
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:10675613};
CC -!- COFACTOR:
CC Name=1D-myo-inositol hexakisphosphate; Xref=ChEBI:CHEBI:58130;
CC Evidence={ECO:0000250};
CC Note=Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
CC {ECO:0000250};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9JHI2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JHI2-2; Sequence=VSP_025581;
CC Name=3;
CC IsoId=Q9JHI2-3; Sequence=VSP_025580, VSP_025581;
CC -!- SIMILARITY: Belongs to the ADAT1 family. {ECO:0000305}.
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DR EMBL; AF192375; AAF36820.1; -; mRNA.
DR EMBL; AF192374; AAF36821.1; -; Genomic_DNA.
DR EMBL; AF192367; AAF36821.1; JOINED; Genomic_DNA.
DR EMBL; AF192368; AAF36821.1; JOINED; Genomic_DNA.
DR EMBL; AF192369; AAF36821.1; JOINED; Genomic_DNA.
DR EMBL; AF192370; AAF36821.1; JOINED; Genomic_DNA.
DR EMBL; AF192371; AAF36821.1; JOINED; Genomic_DNA.
DR EMBL; AF192372; AAF36821.1; JOINED; Genomic_DNA.
DR EMBL; AF192373; AAF36821.1; JOINED; Genomic_DNA.
DR EMBL; AK035614; BAC29125.1; -; mRNA.
DR EMBL; AK039699; BAC30422.1; -; mRNA.
DR EMBL; AK082399; BAC38487.1; -; mRNA.
DR EMBL; AK161044; BAE36167.1; -; mRNA.
DR EMBL; BC019976; AAH19976.1; -; mRNA.
DR CCDS; CCDS22684.1; -. [Q9JHI2-1]
DR CCDS; CCDS90464.1; -. [Q9JHI2-2]
DR RefSeq; NP_038953.1; NM_013925.4. [Q9JHI2-1]
DR AlphaFoldDB; Q9JHI2; -.
DR SMR; Q9JHI2; -.
DR STRING; 10090.ENSMUSP00000034427; -.
DR iPTMnet; Q9JHI2; -.
DR PhosphoSitePlus; Q9JHI2; -.
DR EPD; Q9JHI2; -.
DR MaxQB; Q9JHI2; -.
DR PaxDb; Q9JHI2; -.
DR PeptideAtlas; Q9JHI2; -.
DR PRIDE; Q9JHI2; -.
DR ProteomicsDB; 296062; -. [Q9JHI2-1]
DR ProteomicsDB; 296063; -. [Q9JHI2-2]
DR ProteomicsDB; 296064; -. [Q9JHI2-3]
DR Antibodypedia; 16832; 168 antibodies from 22 providers.
DR DNASU; 30947; -.
DR Ensembl; ENSMUST00000034427; ENSMUSP00000034427; ENSMUSG00000031949. [Q9JHI2-1]
DR Ensembl; ENSMUST00000139820; ENSMUSP00000117279; ENSMUSG00000031949. [Q9JHI2-2]
DR GeneID; 30947; -.
DR KEGG; mmu:30947; -.
DR UCSC; uc009nnc.1; mouse. [Q9JHI2-1]
DR UCSC; uc012gkz.1; mouse. [Q9JHI2-3]
DR CTD; 23536; -.
DR MGI; MGI:1353631; Adat1.
DR VEuPathDB; HostDB:ENSMUSG00000031949; -.
DR eggNOG; KOG2777; Eukaryota.
DR GeneTree; ENSGT00940000157942; -.
DR HOGENOM; CLU_005382_5_2_1; -.
DR InParanoid; Q9JHI2; -.
DR OMA; IGRCQNV; -.
DR OrthoDB; 947117at2759; -.
DR PhylomeDB; Q9JHI2; -.
DR TreeFam; TF315806; -.
DR BioGRID-ORCS; 30947; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Adat1; mouse.
DR PRO; PR:Q9JHI2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9JHI2; protein.
DR Bgee; ENSMUSG00000031949; Expressed in floor plate of midbrain and 137 other tissues.
DR ExpressionAtlas; Q9JHI2; baseline and differential.
DR Genevisible; Q9JHI2; MM.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0008251; F:tRNA-specific adenosine deaminase activity; ISS:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; ISS: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 Alternative splicing; Hydrolase; Metal-binding; Phosphoprotein;
KW Reference proteome; tRNA processing; Zinc.
FT CHAIN 1..499
FT /note="tRNA-specific adenosine deaminase 1"
FT /id="PRO_0000287648"
FT DOMAIN 63..498
FT /note="A to I editase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT REGION 170..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 89
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 93
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00240"
FT BINDING 297
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 300
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 430
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT BINDING 466
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 343..424
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_025580"
FT VAR_SEQ 455..499
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025581"
FT CONFLICT 201
FT /note="T -> A (in Ref. 2; BAE36167)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 499 AA; 55355 MW; 8080BD40C1EE5E71 CRC64;
MWTADEIAQL CYAHYNVRLP KQGKPEPNRE WTLLAAVVKI QASANQACDI PEKEVQVTKE
VVSMGTGTKC IGQSKMRESG DILNDSHAEI IARRSFQRYL LHQLHLAAVL KEDSIFVPGT
QRGLWRLRPD LSFVFFSSHT PCGDASIIPM LEFEEQPCCP VIRSWANNSP VQETENLEDS
KDKRNCEDPA SPVAKKMRLG TPARSLSNCV AHHGTQESGP VKPDVSSSDL TKEEPDAANG
IASGSFRVVD VYRTGAKCVP GETGDLREPG AAYHQVGLLR VKPGRGDRTC SMSCSDKMAR
WNVLGCQGAL LMHFLEKPIY LSAVVIGKCP YSQEAMRRAL TGRCEETLVL PRGFGVQELE
IQQSGLLFEQ SRCAVHRKRG DSPGRLVPCG AAISWSAVPQ QPLDVTANGF PQGTTKKEIG
SPRARSRISK VELFRSFQKL LSSIADDEQP DSIRVTKKLD TYQEYKDAAS AYQEAWGALR
RIQPFASWIR NPPDYHQFK
