ADAT2_MOUSE
ID ADAT2_MOUSE Reviewed; 191 AA.
AC Q6P6J0; Q9CX14;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=tRNA-specific adenosine deaminase 2;
DE EC=3.5.4.33 {ECO:0000305};
DE AltName: Full=Deaminase domain-containing protein 1;
DE AltName: Full=tRNA-specific adenosine-34 deaminase subunit ADAT2;
GN Name=Adat2; Synonyms=Deadc1;
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=Stomach;
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].
RC STRAIN=NMRI; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, 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: Probably participates in deamination of adenosine-34 to
CC inosine in many tRNAs. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA +
CC NH4(+); Xref=Rhea:RHEA:43168, Rhea:RHEA-COMP:10373, Rhea:RHEA-
CC COMP:10374, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:82852; EC=3.5.4.33;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT2 subfamily. {ECO:0000305}.
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DR EMBL; AK021291; BAB32363.2; -; mRNA.
DR EMBL; BC062195; AAH62195.1; -; mRNA.
DR CCDS; CCDS35847.1; -.
DR RefSeq; NP_080024.3; NM_025748.4.
DR PDB; 7NZ7; X-ray; 2.96 A; A=1-191.
DR PDB; 7NZ8; X-ray; 2.12 A; A=1-191.
DR PDB; 7NZ9; X-ray; 1.99 A; A=1-191.
DR PDBsum; 7NZ7; -.
DR PDBsum; 7NZ8; -.
DR PDBsum; 7NZ9; -.
DR AlphaFoldDB; Q6P6J0; -.
DR SMR; Q6P6J0; -.
DR STRING; 10090.ENSMUSP00000019944; -.
DR PhosphoSitePlus; Q6P6J0; -.
DR EPD; Q6P6J0; -.
DR MaxQB; Q6P6J0; -.
DR PaxDb; Q6P6J0; -.
DR PeptideAtlas; Q6P6J0; -.
DR PRIDE; Q6P6J0; -.
DR ProteomicsDB; 285676; -.
DR Antibodypedia; 33139; 63 antibodies from 19 providers.
DR DNASU; 66757; -.
DR Ensembl; ENSMUST00000019944; ENSMUSP00000019944; ENSMUSG00000019808.
DR GeneID; 66757; -.
DR KEGG; mmu:66757; -.
DR UCSC; uc007ela.2; mouse.
DR CTD; 134637; -.
DR MGI; MGI:1914007; Adat2.
DR VEuPathDB; HostDB:ENSMUSG00000019808; -.
DR eggNOG; KOG1018; Eukaryota.
DR GeneTree; ENSGT00390000000280; -.
DR HOGENOM; CLU_025810_8_1_1; -.
DR InParanoid; Q6P6J0; -.
DR OMA; PCQMCAG; -.
DR OrthoDB; 1616309at2759; -.
DR PhylomeDB; Q6P6J0; -.
DR TreeFam; TF313782; -.
DR BioGRID-ORCS; 66757; 26 hits in 77 CRISPR screens.
DR PRO; PR:Q6P6J0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6P6J0; protein.
DR Bgee; ENSMUSG00000019808; Expressed in endocardial cushion and 176 other tissues.
DR Genevisible; Q6P6J0; MM.
DR GO; GO:0052717; F:tRNA-specific adenosine-34 deaminase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002100; P:tRNA wobble adenosine to inosine editing; IBA:GO_Central.
DR HAMAP; MF_00972; tRNA_aden_deaminase; 1.
DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR InterPro; IPR028883; tRNA_aden_deaminase.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..191
FT /note="tRNA-specific adenosine deaminase 2"
FT /id="PRO_0000287654"
FT DOMAIN 20..145
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT ACT_SITE 73
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 12
FT /note="D -> H (in Ref. 1; BAB32363)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="M -> T (in Ref. 1; BAB32363)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="K -> N (in Ref. 1; BAB32363)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="R -> T (in Ref. 1; BAB32363)"
FT /evidence="ECO:0000305"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 22..38
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 53..59
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:7NZ9"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:7NZ9"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 160..172
FT /evidence="ECO:0007829|PDB:7NZ9"
SQ SEQUENCE 191 AA; 21308 MW; 59DCEC6AEEA94B64 CRC64;
MEEKVESTTT PDGPCVVSVQ ETEKWMEEAM RMAKEALENI EVPVGCLMVY NNEVVGKGRN
EVNQTKNATR HAEMVAIDQV LDWCHQHGQS PSTVFEHTVL YVTVEPCIMC AAALRLMKIP
LVVYGCQNER FGGCGSVLNI ASADLPNTGR PFQCIPGYRA EEAVELLKTF YKQENPNAPK
SKVRKKDCQK S
