THG1_MOUSE
ID THG1_MOUSE Reviewed; 298 AA.
AC Q9CY52; Q562D7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable tRNA(His) guanylyltransferase;
DE EC=2.7.7.79 {ECO:0000250|UniProtKB:Q9NWX6};
DE AltName: Full=tRNA-histidine guanylyltransferase;
GN Name=Thg1l;
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=Liver;
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].
RC TISSUE=Testis;
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 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).
CC -!- FUNCTION: Adds a GMP to the 5'-end of tRNA(His) after transcription and
CC RNase P cleavage. This step is essential for proper recognition of the
CC tRNA and for the fidelity of protein synthesis. Also functions as a
CC guanyl-nucleotide exchange factor/GEF for the MFN1 and MFN2 mitofusins
CC thereby regulating mitochondrial fusion. By regulating both
CC mitochondrial dynamics and bioenergetic function, it contributes to
CC cell survival following oxidative stress.
CC {ECO:0000250|UniProtKB:Q9NWX6}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end ribonucleotide-tRNA(His) + ATP + GTP + H2O = a 5'-end
CC phospho-guanosine-ribonucleotide-tRNA(His) + AMP + 2 diphosphate +
CC H(+); Xref=Rhea:RHEA:54564, Rhea:RHEA-COMP:14193, Rhea:RHEA-
CC COMP:14917, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:138282,
CC ChEBI:CHEBI:141847, ChEBI:CHEBI:456215; EC=2.7.7.79;
CC Evidence={ECO:0000250|UniProtKB:Q9NWX6};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homotetramer. Interacts with MFN1 and MFN2; functions as a
CC guanyl-nucleotide exchange factor/GEF for MFN2 and also probably MFN1.
CC {ECO:0000250|UniProtKB:Q9NWX6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9NWX6}.
CC -!- SIMILARITY: Belongs to the tRNA(His) guanylyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AK010876; BAB27240.1; -; mRNA.
DR EMBL; AL645948; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC092541; AAH92541.1; -; mRNA.
DR EMBL; BC115561; AAI15562.1; -; mRNA.
DR EMBL; BC115560; AAI15561.1; -; mRNA.
DR CCDS; CCDS36132.1; -.
DR RefSeq; NP_001074438.1; NM_001080969.3.
DR AlphaFoldDB; Q9CY52; -.
DR SMR; Q9CY52; -.
DR BioGRID; 211607; 9.
DR STRING; 10090.ENSMUSP00000011398; -.
DR iPTMnet; Q9CY52; -.
DR PhosphoSitePlus; Q9CY52; -.
DR EPD; Q9CY52; -.
DR MaxQB; Q9CY52; -.
DR PaxDb; Q9CY52; -.
DR PeptideAtlas; Q9CY52; -.
DR PRIDE; Q9CY52; -.
DR ProteomicsDB; 262809; -.
DR Antibodypedia; 28457; 92 antibodies from 23 providers.
DR Ensembl; ENSMUST00000011398; ENSMUSP00000011398; ENSMUSG00000011254.
DR GeneID; 66628; -.
DR KEGG; mmu:66628; -.
DR UCSC; uc007inv.2; mouse.
DR CTD; 54974; -.
DR MGI; MGI:1913878; Thg1l.
DR VEuPathDB; HostDB:ENSMUSG00000011254; -.
DR eggNOG; KOG2721; Eukaryota.
DR GeneTree; ENSGT00390000011705; -.
DR HOGENOM; CLU_044271_0_0_1; -.
DR InParanoid; Q9CY52; -.
DR OMA; WKQHTEI; -.
DR OrthoDB; 1152974at2759; -.
DR PhylomeDB; Q9CY52; -.
DR TreeFam; TF325119; -.
DR BioGRID-ORCS; 66628; 23 hits in 67 CRISPR screens.
DR ChiTaRS; Thg1l; mouse.
DR PRO; PR:Q9CY52; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CY52; protein.
DR Bgee; ENSMUSG00000011254; Expressed in spermatocyte and 138 other tissues.
DR ExpressionAtlas; Q9CY52; baseline and differential.
DR Genevisible; Q9CY52; MM.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:1990234; C:transferase complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0016779; F:nucleotidyltransferase activity; ISO:MGI.
DR GO; GO:0008193; F:tRNA guanylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; ISO:MGI.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR GO; GO:1990046; P:stress-induced mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; ISS:UniProtKB.
DR Gene3D; 3.30.70.3000; -; 1.
DR InterPro; IPR025845; Thg1_C_dom.
DR InterPro; IPR024956; tRNAHis_GuaTrfase_cat.
DR InterPro; IPR007537; tRNAHis_GuaTrfase_Thg1.
DR InterPro; IPR038469; tRNAHis_GuaTrfase_Thg1_sf.
DR PANTHER; PTHR12729; PTHR12729; 1.
DR Pfam; PF04446; Thg1; 1.
DR Pfam; PF14413; Thg1C; 1.
DR PIRSF; PIRSF028980; tRNAHis_guanylyltransferase; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Magnesium; Metal-binding; Mitochondrion;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase; tRNA processing.
FT CHAIN 1..298
FT /note="Probable tRNA(His) guanylyltransferase"
FT /id="PRO_0000284985"
FT BINDING 58..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 59
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 104..105
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 105
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 192
FT /note="A -> V (in Ref. 3; AAH92541)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 34971 MW; D4CA0C154E452ECA CRC64;
MWAFRTARIG SLLAATSVIL RRCLRLGVAM AKSKFEYVRN FEVQDTCLPH CWVVVRLDGR
NFHRFAEEHN FAKPNDSRAL HLMTKCAQTV MEELEDIVIA YGQSDEYSFV FRKKSNWFKR
RASKFMTLVA SQFASSYVFY WRDYFEDQPL RYPPGFDGRV VLYPSNQTLK DYLSWRQADC
HINNLYNTVF WALIQQSGLT PVQAQQRLKG TLTADKNEIL FSEFHINYNN EPHMYRKGTV
LVWQKVEEVR TQEVRLPAEM EGEKKAVART RTRVVALNCD LIGDAFWKEH PEILAEEN
