TGT_MOUSE
ID TGT_MOUSE Reviewed; 403 AA.
AC Q9JMA2; Q80VS3;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Queuine tRNA-ribosyltransferase catalytic subunit 1 {ECO:0000255|HAMAP-Rule:MF_03218};
DE EC=2.4.2.64 {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587, ECO:0000269|PubMed:29862811};
DE AltName: Full=Guanine insertion enzyme {ECO:0000255|HAMAP-Rule:MF_03218};
DE AltName: Full=tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_03218};
GN Name=Qtrt1 {ECO:0000255|HAMAP-Rule:MF_03218}; Synonyms=Tgt, Tgut;
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=Embryo;
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=FVB/N; 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-403.
RC TISSUE=Brain;
RA Morishita T., Hidaka T.;
RT "Another gene for tRNA-guanine transglycosylase in mammals.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH QTRT2, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=19414587; DOI=10.1074/jbc.m109.002477;
RA Boland C., Hayes P., Santa-Maria I., Nishimura S., Kelly V.P.;
RT "Queuosine formation in eukaryotic tRNA occurs via a mitochondria-localized
RT heteromeric transglycosylase.";
RL J. Biol. Chem. 284:18218-18227(2009).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=29862811; DOI=10.1021/acs.biochem.8b00294;
RA Behrens C., Biela I., Petiot-Becard S., Botzanowski T., Cianferani S.,
RA Sager C.P., Klebe G., Heine A., Reuter K.;
RT "Homodimer Architecture of QTRT2, the Noncatalytic Subunit of the
RT Eukaryotic tRNA-Guanine Transglycosylase.";
RL Biochemistry 57:3953-3965(2018).
CC -!- FUNCTION: Catalytic subunit of the queuine tRNA-ribosyltransferase
CC (TGT) that catalyzes the base-exchange of a guanine (G) residue with
CC queuine (Q) at position 34 (anticodon wobble position) in tRNAs with
CC GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the
CC hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-
CC cyclopenten-1-yl)amino)methyl)-7-deazaguanosine) (PubMed:19414587,
CC PubMed:29862811). Catalysis occurs through a double-displacement
CC mechanism. The nucleophile active site attacks the C1' of nucleotide 34
CC to detach the guanine base from the RNA, forming a covalent enzyme-RNA
CC intermediate. The proton acceptor active site deprotonates the incoming
CC queuine, allowing a nucleophilic attack on the C1' of the ribose to
CC form the product (By similarity). {ECO:0000255|HAMAP-Rule:MF_03218,
CC ECO:0000269|PubMed:19414587, ECO:0000269|PubMed:29862811}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(34) in tRNA + queuine = guanine + queuosine(34) in
CC tRNA; Xref=Rhea:RHEA:16633, Rhea:RHEA-COMP:10341, Rhea:RHEA-
CC COMP:10345, ChEBI:CHEBI:16235, ChEBI:CHEBI:74269, ChEBI:CHEBI:77674,
CC ChEBI:CHEBI:82831; EC=2.4.2.64; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03218, ECO:0000269|PubMed:19414587,
CC ECO:0000269|PubMed:29862811};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03218};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit QTRT1 and an accessory
CC subunit QTRT2. {ECO:0000255|HAMAP-Rule:MF_03218,
CC ECO:0000269|PubMed:19414587, ECO:0000269|PubMed:29862811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03218,
CC ECO:0000269|PubMed:19414587}. Mitochondrion outer membrane
CC {ECO:0000255|HAMAP-Rule:MF_03218, ECO:0000269|PubMed:19414587};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03218,
CC ECO:0000305|PubMed:19414587}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_03218, ECO:0000269|PubMed:19414587}. Nucleus
CC {ECO:0000269|PubMed:19414587}. Note=Weakly associates with
CC mitochondria, possibly via QTRT2. {ECO:0000255|HAMAP-Rule:MF_03218,
CC ECO:0000269|PubMed:19414587}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, ling,
CC skeletal muscle, spleen and testis. {ECO:0000269|PubMed:19414587}.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC {ECO:0000255|HAMAP-Rule:MF_03218}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB27717.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB27717.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK011586; BAB27717.1; ALT_SEQ; mRNA.
DR EMBL; BC044811; AAH44811.1; -; mRNA.
DR EMBL; AB034632; BAA93550.1; -; mRNA.
DR CCDS; CCDS52735.1; -.
DR RefSeq; NP_068688.2; NM_021888.2.
DR PDB; 6H62; X-ray; 2.68 A; A/B=1-403.
DR PDB; 7B2I; X-ray; 1.65 A; C=11-403.
DR PDBsum; 6H62; -.
DR PDBsum; 7B2I; -.
DR AlphaFoldDB; Q9JMA2; -.
DR SMR; Q9JMA2; -.
DR BioGRID; 208581; 1.
DR IntAct; Q9JMA2; 1.
DR STRING; 10090.ENSMUSP00000002902; -.
DR iPTMnet; Q9JMA2; -.
DR PhosphoSitePlus; Q9JMA2; -.
DR EPD; Q9JMA2; -.
DR MaxQB; Q9JMA2; -.
DR PaxDb; Q9JMA2; -.
DR PeptideAtlas; Q9JMA2; -.
DR PRIDE; Q9JMA2; -.
DR ProteomicsDB; 263171; -.
DR Antibodypedia; 25490; 156 antibodies from 20 providers.
DR DNASU; 60507; -.
DR Ensembl; ENSMUST00000002902; ENSMUSP00000002902; ENSMUSG00000002825.
DR GeneID; 60507; -.
DR KEGG; mmu:60507; -.
DR UCSC; uc009oli.2; mouse.
DR CTD; 81890; -.
DR MGI; MGI:1931441; Qtrt1.
DR VEuPathDB; HostDB:ENSMUSG00000002825; -.
DR eggNOG; KOG3908; Eukaryota.
DR GeneTree; ENSGT00530000063679; -.
DR HOGENOM; CLU_022060_1_0_1; -.
DR InParanoid; Q9JMA2; -.
DR OMA; GIDLFDC; -.
DR OrthoDB; 684306at2759; -.
DR PhylomeDB; Q9JMA2; -.
DR TreeFam; TF300732; -.
DR BRENDA; 2.4.2.64; 3474.
DR BioGRID-ORCS; 60507; 3 hits in 74 CRISPR screens.
DR PRO; PR:Q9JMA2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JMA2; protein.
DR Bgee; ENSMUSG00000002825; Expressed in dorsal pancreas and 251 other tissues.
DR ExpressionAtlas; Q9JMA2; baseline and differential.
DR Genevisible; Q9JMA2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:1990234; C:transferase complex; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IDA:UniProtKB.
DR Gene3D; 3.20.20.105; -; 1.
DR HAMAP; MF_00168; Q_tRNA_Tgt; 1.
DR InterPro; IPR004803; TGT.
DR InterPro; IPR036511; TGT-like_sf.
DR InterPro; IPR002616; tRNA_ribo_trans-like.
DR Pfam; PF01702; TGT; 1.
DR SUPFAM; SSF51713; SSF51713; 1.
DR TIGRFAMs; TIGR00430; Q_tRNA_tgt; 1.
DR TIGRFAMs; TIGR00449; tgt_general; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Glycosyltransferase; Membrane;
KW Metal-binding; Mitochondrion; Mitochondrion outer membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transferase; tRNA processing; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BXR0"
FT CHAIN 2..403
FT /note="Queuine tRNA-ribosyltransferase catalytic subunit 1"
FT /id="PRO_0000135566"
FT REGION 260..266
FT /note="RNA binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT REGION 284..288
FT /note="RNA binding; important for wobble base 34
FT recognition"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT ACT_SITE 105
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT ACT_SITE 279
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 105..109
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 319
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03218"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXR0"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BXR0"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:7B2I"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 38..45
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 49..54
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 59..64
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6H62"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 140..150
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 169..188
FT /evidence="ECO:0007829|PDB:7B2I"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 207..217
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 223..227
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 231..234
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 236..249
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:6H62"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 320..324
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 327..336
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 338..365
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 369..381
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 384..386
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 389..397
FT /evidence="ECO:0007829|PDB:7B2I"
SQ SEQUENCE 403 AA; 44093 MW; DC514C9E384314AD CRC64;
MAAVGSPGSL ESAPRIMRLV AECSRSGARA GELRLPHGTV ATPVFMPVGT QATMKGITTE
QLDSLGCRIC LGNTYHLGLR PGPELIRKAQ GLHGFMNWPH NLLTDSGGFQ MVSLFSLSEV
TEEGVHFRSP YDGEETLLSP ERSVEIQNAL GSDIIMQLDH VVSSTVTGPL VEEAMHRSVR
WLDRCIAAHK HPDKQNLFAI IQGGLNADLR TTCLKEMTKR DVPGFAIGGL SGGESKAQFW
KMVALSTSML PKDKPRYLMG VGYATDLVVC VALGCDMFDC VYPTRTARFG SALVPTGNLQ
LKKKQYAKDF SPINPECPCP TCQTHSRAFL HALLHSDNTT ALHHLTVHNI AYQLQLLSAV
RSSILEQRFP DFVRNFMRTM YGDHSLCPAW AVEALASVGI MLT
