QTRT2_MOUSE
ID QTRT2_MOUSE Reviewed; 415 AA.
AC B8ZXI1; A9C446; Q5XK35;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Queuine tRNA-ribosyltransferase accessory subunit 2 {ECO:0000255|HAMAP-Rule:MF_03043};
DE AltName: Full=Queuine tRNA-ribosyltransferase domain-containing protein 1 {ECO:0000255|HAMAP-Rule:MF_03043};
GN Name=Qtrt2 {ECO:0000255|HAMAP-Rule:MF_03043};
GN Synonyms=Qtrtd1 {ECO:0000255|HAMAP-Rule:MF_03043};
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 [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH QTRT1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
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 [5] {ECO:0007744|PDB:6FV5}
RP X-RAY CRYSTALLOGRAPHY (2.18 ANGSTROMS) IN COMPLEX WITH ZINC IONS, COFACTOR,
RP 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: Non-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). {ECO:0000255|HAMAP-
CC Rule:MF_03043, ECO:0000269|PubMed:19414587}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03043,
CC ECO:0000269|PubMed:29862811};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03043,
CC ECO:0000269|PubMed:29862811};
CC -!- SUBUNIT: Heterodimer of a catalytic subunit QTRT1 and an accessory
CC subunit QTRT2. {ECO:0000255|HAMAP-Rule:MF_03043,
CC ECO:0000269|PubMed:19414587, ECO:0000269|PubMed:29862811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03043,
CC ECO:0000269|PubMed:19414587}. Mitochondrion outer membrane
CC {ECO:0000255|HAMAP-Rule:MF_03043, ECO:0000269|PubMed:19414587};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03043,
CC ECO:0000269|PubMed:19414587}; Cytoplasmic side {ECO:0000255|HAMAP-
CC Rule:MF_03043, ECO:0000269|PubMed:19414587}. Note=May associate with
CC the mitochondrion outer membrane. {ECO:0000255|HAMAP-Rule:MF_03043,
CC ECO:0000269|PubMed:19414587}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Qv1;
CC IsoId=B8ZXI1-1; Sequence=Displayed;
CC Name=2; Synonyms=Qv0;
CC IsoId=B8ZXI1-2; Sequence=VSP_038046;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung,
CC skeletal muscle, spleen and testis. {ECO:0000269|PubMed:19414587}.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform in adult tissues.
CC -!- SIMILARITY: Belongs to the queuine tRNA-ribosyltransferase family.
CC QTRT2 subfamily. {ECO:0000255|HAMAP-Rule:MF_03043}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAP19252.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAX17683.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EDK98022.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EDK98023.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; FM985972; CAX17683.1; ALT_INIT; mRNA.
DR EMBL; CT025520; CAP19252.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH466521; EDK98022.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH466521; EDK98023.1; ALT_INIT; Genomic_DNA.
DR EMBL; BC083089; AAH83089.1; -; mRNA.
DR RefSeq; NP_083404.2; NM_029128.2.
DR RefSeq; XP_006521731.1; XM_006521668.1.
DR RefSeq; XP_006521733.1; XM_006521670.3.
DR PDB; 6FV5; X-ray; 2.18 A; A/B=1-415.
DR PDB; 7B2I; X-ray; 1.65 A; A=2-415.
DR PDBsum; 6FV5; -.
DR PDBsum; 7B2I; -.
DR AlphaFoldDB; B8ZXI1; -.
DR SMR; B8ZXI1; -.
DR BioGRID; 223011; 3.
DR IntAct; B8ZXI1; 1.
DR PhosphoSitePlus; B8ZXI1; -.
DR EPD; B8ZXI1; -.
DR MaxQB; B8ZXI1; -.
DR PaxDb; B8ZXI1; -.
DR PeptideAtlas; B8ZXI1; -.
DR PRIDE; B8ZXI1; -.
DR ProteomicsDB; 300281; -. [B8ZXI1-1]
DR ProteomicsDB; 300282; -. [B8ZXI1-2]
DR DNASU; 106248; -.
DR GeneID; 106248; -.
DR KEGG; mmu:106248; -.
DR UCSC; uc007zgl.1; mouse. [B8ZXI1-1]
DR CTD; 79691; -.
DR MGI; MGI:1922194; Qtrt2.
DR eggNOG; KOG3909; Eukaryota.
DR InParanoid; B8ZXI1; -.
DR OMA; MAGSRMK; -.
DR OrthoDB; 883398at2759; -.
DR PhylomeDB; B8ZXI1; -.
DR TreeFam; TF317105; -.
DR BRENDA; 2.4.2.64; 3474.
DR BioGRID-ORCS; 106248; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Qtrtd1; mouse.
DR PRO; PR:B8ZXI1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; B8ZXI1; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:1990234; C:transferase complex; ISO:MGI.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; NAS:UniProtKB.
DR GO; GO:0101030; P:tRNA-guanine transglycosylation; IDA:UniProtKB.
DR Gene3D; 3.20.20.105; -; 1.
DR HAMAP; MF_03043; QTRT2; 1.
DR InterPro; IPR028592; QTRTD1.
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; TIGR00449; tgt_general; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Membrane; Metal-binding;
KW Mitochondrion; Mitochondrion outer membrane; Reference proteome;
KW tRNA processing; Zinc.
FT CHAIN 1..415
FT /note="Queuine tRNA-ribosyltransferase accessory subunit 2"
FT /id="PRO_0000383924"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043,
FT ECO:0000269|PubMed:29862811, ECO:0007744|PDB:6FV5"
FT BINDING 353
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043,
FT ECO:0000269|PubMed:29862811, ECO:0007744|PDB:6FV5"
FT BINDING 356
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043,
FT ECO:0000269|PubMed:29862811, ECO:0007744|PDB:6FV5"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03043,
FT ECO:0000269|PubMed:29862811, ECO:0007744|PDB:6FV5"
FT VAR_SEQ 112..182
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038046"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:7B2I"
FT TURN 21..23
FT /evidence="ECO:0007829|PDB:6FV5"
FT STRAND 26..36
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:6FV5"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 71..77
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6FV5"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:6FV5"
FT HELIX 157..179
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6FV5"
FT HELIX 230..240
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 257..264
FT /evidence="ECO:0007829|PDB:7B2I"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:7B2I"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 338..340
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 361..369
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 373..400
FT /evidence="ECO:0007829|PDB:7B2I"
FT HELIX 403..412
FT /evidence="ECO:0007829|PDB:7B2I"
SQ SEQUENCE 415 AA; 46288 MW; 4E95A4FC8FFBAB22 CRC64;
MKLSLIKVVN GCRLGKIQNL GKAGDCTVDI PGCLLYTRTG SAPHLTHQTL RNIHGVPGIA
QLTLSSLAEH HEVLAEYKKG VGSFIGMPES LFYCSLHDPV TPGPAGYVTS KSVSVWGFGG
RVEMTVSKFM AIQEALQPDW FQCLSDGEAS CAETTSIKRA RKSVDRSLLF LDSCLRLQEE
SEVLQKSVII GVIEGGDVME ERLRSARETA KRPVGGFLLD GFQGDPAVTE TRLHLLSSVT
AELPEDKPRL ICGVSRPDEV LECIERGVDL FESFFPYQVT ERGCALTFTF DCQLNPEETL
LQQNGIQEKI KGLDQAKKIE ATGCNQEMTS FEINLKEKKY QEDFDPLVRG CSCYCCKNHT
RAYIHHLLMT NELLAGVLLM MHNFEHYFGF FCSIREALKN DTLAQLKELI CRQMF
