ADAT3_MOUSE
ID ADAT3_MOUSE Reviewed; 349 AA.
AC Q6PAT0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Probable inactive tRNA-specific adenosine deaminase-like protein 3;
DE AltName: Full=tRNA-specific adenosine-34 deaminase subunit ADAT3;
GN Name=Adat3;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-162.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 87-349.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC family. ADAT3 subfamily. {ECO:0000305}.
CC -!- CAUTION: Val-225 is present instead of the conserved Glu which is an
CC active site in the cytidine and deoxycytidylate deaminase family of
CC enzymes. It is suggested that this protein may act as a regulatory
CC subunit. {ECO:0000305}.
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DR EMBL; AC152058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060071; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CA325386; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK020747; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS48637.1; -.
DR RefSeq; NP_001094076.1; NM_001100606.1.
DR PDB; 7NZ7; X-ray; 2.96 A; B=1-349.
DR PDB; 7NZ8; X-ray; 2.12 A; B=1-349.
DR PDB; 7NZ9; X-ray; 1.99 A; B=1-349.
DR PDBsum; 7NZ7; -.
DR PDBsum; 7NZ8; -.
DR PDBsum; 7NZ9; -.
DR AlphaFoldDB; Q6PAT0; -.
DR SMR; Q6PAT0; -.
DR STRING; 10090.ENSMUSP00000136259; -.
DR iPTMnet; Q6PAT0; -.
DR PhosphoSitePlus; Q6PAT0; -.
DR EPD; Q6PAT0; -.
DR MaxQB; Q6PAT0; -.
DR PaxDb; Q6PAT0; -.
DR PeptideAtlas; Q6PAT0; -.
DR PRIDE; Q6PAT0; -.
DR ProteomicsDB; 285553; -.
DR Ensembl; ENSMUST00000038411; ENSMUSP00000040551; ENSMUSG00000113640.
DR Ensembl; ENSMUST00000178231; ENSMUSP00000136259; ENSMUSG00000035370.
DR Ensembl; ENSMUST00000218067; ENSMUSP00000151394; ENSMUSG00000035370.
DR GeneID; 100113398; -.
DR KEGG; mmu:100113398; -.
DR UCSC; uc007gdx.1; mouse.
DR CTD; 113179; -.
DR MGI; MGI:1924344; Adat3.
DR VEuPathDB; HostDB:ENSMUSG00000035370; -.
DR VEuPathDB; HostDB:ENSMUSG00000113640; -.
DR eggNOG; KOG2771; Eukaryota.
DR GeneTree; ENSGT00390000010706; -.
DR HOGENOM; CLU_013817_2_1_1; -.
DR InParanoid; Q6PAT0; -.
DR OMA; QHWPCKF; -.
DR OrthoDB; 1301800at2759; -.
DR PhylomeDB; Q6PAT0; -.
DR TreeFam; TF313277; -.
DR BioGRID-ORCS; 100113398; 25 hits in 76 CRISPR screens.
DR PRO; PR:Q6PAT0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6PAT0; protein.
DR Bgee; ENSMUSG00000035370; Expressed in ascending aorta and 64 other tissues.
DR ExpressionAtlas; Q6PAT0; baseline and differential.
DR Genevisible; Q6PAT0; MM.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR002125; CMP_dCMP_dom.
DR InterPro; IPR016193; Cytidine_deaminase-like.
DR Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR SUPFAM; SSF53927; SSF53927; 1.
DR PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Metal-binding; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..349
FT /note="Probable inactive tRNA-specific adenosine deaminase-
FT like protein 3"
FT /id="PRO_0000287659"
FT DOMAIN 171..334
FT /note="CMP/dCMP-type deaminase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01083"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96EY9"
FT CONFLICT 87
FT /note="A -> T (in Ref. 3; AK020747)"
FT /evidence="ECO:0000305"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:7NZ7"
FT HELIX 34..37
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:7NZ9"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 124..131
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 167..190
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:7NZ9"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:7NZ9"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 290..299
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 302..308
FT /evidence="ECO:0007829|PDB:7NZ9"
FT STRAND 325..328
FT /evidence="ECO:0007829|PDB:7NZ8"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:7NZ9"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:7NZ9"
SQ SEQUENCE 349 AA; 37517 MW; CACA04B0857AF4A8 CRC64;
MEPTSGFAEQ PGPVKAESEE QEPAQWQALP VLSEQQSGAV ELILAYAAPV LDKRQTSRLL
REVSAVYPLP AQPHLKRVRP SRSAGGAQSS DLLLCLAGPS AGPRSLAELL PRPAVDPRGL
GTPFLVPVPA RPPLTRSQFE EARAHWPTSF HEDKQVTSAL AGQLFSTQER AAMQTHMERA
VCAAQRAAAQ GLRAVGAVVV DPASDRVLAT GHDCSSVASP LLHAVMVCID LVAQGQGRGS
CDLRSHPACS FTQATATQGA RAGSVRKLDE DSLPYVCTGY DLYVTREPCV MCAMALVHAR
IQRVFYGAPS PDGALGTLFR VHARPDLNHR FQVFRGILED QCRQLDPDP
