MOD5_MOUSE
ID MOD5_MOUSE Reviewed; 467 AA.
AC Q80UN9; B1ARS6; Q9D1H5;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=tRNA dimethylallyltransferase;
DE EC=2.5.1.75 {ECO:0000250|UniProtKB:Q9H3H1};
DE AltName: Full=Isopentenyl-diphosphate:tRNA isopentenyltransferase;
DE Short=IPP transferase;
DE Short=IPPT;
DE AltName: Full=tRNA isopentenyltransferase;
DE Short=IPTase;
DE Flags: Precursor;
GN Name=Trit1; Synonyms=Ipt;
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] (ISOFORM 2).
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 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 MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II; TISSUE=Kidney, and 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 FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-32 AND ASP-55.
RX PubMed=23289710; DOI=10.1042/bj20121713;
RA Fradejas N., Carlson B.A., Rijntjes E., Becker N.P., Tobe R., Schweizer U.;
RT "Mammalian Trit1 is a tRNA([Ser]Sec)-isopentenyl transferase required for
RT full selenoprotein expression.";
RL Biochem. J. 450:427-432(2013).
CC -!- FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the
CC adenine at position 37 of both cytosolic and mitochondrial tRNAs,
CC leading to the formation of N6-(dimethylallyl)adenosine (i6A37)
CC (PubMed:23289710). Mediates modification of a limited subset of tRNAs:
CC tRNA(Ser)(AGA), tRNA(Ser)(CGA), tRNA(Ser)(UGA), as well as partial
CC modification of the selenocysteine tRNA(Ser)(UCA) (By similarity).
CC TRIT1 is therefore required for selenoprotein expression
CC (PubMed:23289710). {ECO:0000250|UniProtKB:Q9H3H1,
CC ECO:0000269|PubMed:23289710}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate =
CC diphosphate + N(6)-dimethylallyladenosine(37) in tRNA;
CC Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74415; EC=2.5.1.75;
CC Evidence={ECO:0000269|PubMed:23289710};
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000250|UniProtKB:Q9H3H1}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}. Nucleus
CC {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80UN9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80UN9-2; Sequence=VSP_010722;
CC -!- SIMILARITY: Belongs to the IPP transferase family. {ECO:0000305}.
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DR EMBL; AK003556; BAB22853.2; -; mRNA.
DR EMBL; AL606906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC019812; AAH19812.1; -; mRNA.
DR EMBL; BC051040; AAH51040.1; -; mRNA.
DR CCDS; CCDS18607.1; -. [Q80UN9-1]
DR RefSeq; NP_080149.2; NM_025873.2. [Q80UN9-1]
DR AlphaFoldDB; Q80UN9; -.
DR SMR; Q80UN9; -.
DR STRING; 10090.ENSMUSP00000099709; -.
DR iPTMnet; Q80UN9; -.
DR PhosphoSitePlus; Q80UN9; -.
DR EPD; Q80UN9; -.
DR MaxQB; Q80UN9; -.
DR PaxDb; Q80UN9; -.
DR PeptideAtlas; Q80UN9; -.
DR PRIDE; Q80UN9; -.
DR ProteomicsDB; 290092; -. [Q80UN9-1]
DR ProteomicsDB; 290093; -. [Q80UN9-2]
DR Antibodypedia; 17887; 137 antibodies from 22 providers.
DR DNASU; 66966; -.
DR Ensembl; ENSMUST00000102649; ENSMUSP00000099709; ENSMUSG00000028653. [Q80UN9-1]
DR GeneID; 66966; -.
DR KEGG; mmu:66966; -.
DR UCSC; uc008uor.1; mouse. [Q80UN9-1]
DR CTD; 54802; -.
DR MGI; MGI:1914216; Trit1.
DR VEuPathDB; HostDB:ENSMUSG00000028653; -.
DR eggNOG; KOG1384; Eukaryota.
DR GeneTree; ENSGT00390000015214; -.
DR HOGENOM; CLU_032616_2_1_1; -.
DR InParanoid; Q80UN9; -.
DR OMA; NGDAMQM; -.
DR OrthoDB; 1003231at2759; -.
DR PhylomeDB; Q80UN9; -.
DR TreeFam; TF315069; -.
DR BRENDA; 2.5.1.75; 3474.
DR BioGRID-ORCS; 66966; 15 hits in 74 CRISPR screens.
DR ChiTaRS; Trit1; mouse.
DR PRO; PR:Q80UN9; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q80UN9; protein.
DR Bgee; ENSMUSG00000028653; Expressed in saccule of membranous labyrinth and 262 other tissues.
DR Genevisible; Q80UN9; MM.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0052381; F:tRNA dimethylallyltransferase activity; IDA:UniProtKB.
DR GO; GO:0070900; P:mitochondrial tRNA modification; ISS:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00185; IPP_trans; 1.
DR InterPro; IPR039657; Dimethylallyltransferase.
DR InterPro; IPR030666; IPP_transferase_euk.
DR InterPro; IPR018022; IPT.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022755; Znf_C2H2_jaz.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR11088; PTHR11088; 1.
DR Pfam; PF12171; zf-C2H2_jaz; 1.
DR PIRSF; PIRSF039110; IPP_transferase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR TIGRFAMs; TIGR00174; miaA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Transit peptide; tRNA processing; Zinc; Zinc-finger.
FT TRANSIT 1..47
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 48..467
FT /note="tRNA dimethylallyltransferase"
FT /id="PRO_0000019024"
FT ZN_FING 395..425
FT /note="Matrin-type"
FT REGION 55..58
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 183..187
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 221..230
FT /note="Core aggregation region"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 233..255
FT /note="Interaction with isopentenylpyrophosphate
FT transferase"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 281..283
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 313..331
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT REGION 432..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 32..37
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT SITE 122
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT SITE 206
FT /note="Interaction with substrate tRNA"
FT /evidence="ECO:0000250|UniProtKB:P07884"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H1"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3H1"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010722"
FT MUTAGEN 32
FT /note="T->A: Reduced tRNA dimethylallyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:23289710"
FT MUTAGEN 55
FT /note="D->G: Reduced tRNA dimethylallyltransferase
FT activity."
FT /evidence="ECO:0000269|PubMed:23289710"
FT CONFLICT 379
FT /note="M -> T (in Ref. 3; AAH51040)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="A -> T (in Ref. 3; AAH51040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 467 AA; 52437 MW; BC0EEF50AE05FD82 CRC64;
MAAAAAARAV PVSSGFRGLR RTLPLVVILG ATGTGKSTLA LQLGQRLGGE IVSADSMQVY
EGLDIITNKV SAQEQKMCQH HMISFVDPLV TSYTVVDFRN KATALIEDIF ARDKIPIVVG
GTNYYIESLL WKVLITTKPQ EMGTGKVVDR KVELEKEDGH ELHKRLSQVD PEMAAKLHPH
DKRKVARSLQ VFEETGISHS EFLHRQHAEE GGGPLGGPLR FPNPCILWLH ADQAVLDERL
DKRVDDMLAA GLLEELRGFH RRYNLKNISE NSQDYQHGIF QSIGFKEFHE YLTTEGKCTP
ETSNQLLKKG IEALKQVTKR YARKQNRWVK NRFLSRPGPS VPPVYGLEVS DVSKWEESVL
EPALNIVQSF IQGHKPTAMP VKMAYNESEN KRSYHMCDLC DRIIIGDREW AAHLKSKSHL
HQLKKRRRLD LDAVSATGSQ SNSPDCDPER IEGESSGQHN QELKASV
