ID   TR112_MOUSE             Reviewed;         125 AA.
AC   Q9DCG9; Q91YP8; Q9D1N6;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Multifunctional methyltransferase subunit TRM112-like protein;
DE   AltName: Full=tRNA methyltransferase 112 homolog;
GN   Name=Trmt112;
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, and Kidney;
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].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Pancreas, 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   [4]
RP   FUNCTION.
RX   PubMed=20606008; DOI=10.1128/mcb.00218-10;
RA   Liu P., Nie S., Li B., Yang Z.Q., Xu Z.M., Fei J., Lin C., Zeng R.,
RA   Xu G.L.;
RT   "Deficiency in a glutamine-specific methyltransferase for release factor
RT   causes mouse embryonic lethality.";
RL   Mol. Cell. Biol. 30:4245-4253(2010).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH N6AMT1.
RX   PubMed=26797129; DOI=10.1074/jbc.m115.711952;
RA   Kusevic D., Kudithipudi S., Jeltsch A.;
RT   "Substrate specificity of the HEMK2 protein glutamine methyltransferase and
RT   identification of novel substrates.";
RL   J. Biol. Chem. 291:6124-6133(2016).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=34669960; DOI=10.1093/nar/gkab927;
RA   Yang W.Q., Xiong Q.P., Ge J.Y., Li H., Zhu W.Y., Nie Y., Lin X., Lv D.,
RA   Li J., Lin H., Liu R.J.;
RT   "THUMPD3-TRMT112 is a m2G methyltransferase working on a broad range of
RT   tRNA substrates.";
RL   Nucleic Acids Res. 49:11900-11919(2021).
CC   -!- FUNCTION: Acts as an activator of both rRNA/tRNA and protein
CC       methyltransferases (PubMed:20606008, PubMed:26797129). Together with
CC       methyltransferase BUD23, methylates the N(7) position of a guanine in
CC       18S rRNA (By similarity). The heterodimer with HEMK2/N6AMT1 catalyzes
CC       N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as
CC       methyl donor (PubMed:20606008, PubMed:26797129). The heterodimer with
CC       ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-
CC       methylcarboxymethyl uridine at the wobble position of the anticodon
CC       loop in target tRNA species (By similarity). Together with
CC       methyltransferase THUMPD3, catalyzes the formation of N(2)-
CC       methylguanosine at position 6 in a broad range of tRNA substrates and
CC       at position 7 of tRNA(Trp) (By similarity). Involved in the pre-rRNA
CC       processing steps leading to small-subunit rRNA production (By
CC       similarity). Together with methyltransferase METTL5, specifically
CC       methylates the 6th position of adenine in position 1832 of 18S rRNA (By
CC       similarity). {ECO:0000250|UniProtKB:Q9UI30,
CC       ECO:0000269|PubMed:20606008, ECO:0000269|PubMed:26797129}.
CC   -!- SUBUNIT: Heterodimer with BUD23/WBSCR22; this heterodimerization is
CC       necessary for the metabolic stability and activity of the catalytic
CC       subunit BUD23 (By similarity). Heterodimer with N6AMT1/HEMK2; this
CC       heterodimerization is necessary for S-adenosyl-L-methionine-binding to
CC       N6AMT1/HEMK2 (PubMed:26797129). Heterodimer with ALKBH8 (By
CC       similarity). Heterodimer with METTL5; this heterodimerization is
CC       necessary for the stability of the catalytic subunit METTL5 (By
CC       similarity). Interacts with THUMPD3; the interaction is direct and is
CC       required for THUMPD3 methyltransferase activity (By similarity).
CC       Interacts with THUMPD2 (By similarity). {ECO:0000250|UniProtKB:Q9UI30,
CC       ECO:0000269|PubMed:26797129}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q9UI30}. Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q9UI30}. Note=Localizes to a polarized
CC       perinuclear structure, overlapping partially with the Golgi and
CC       lysosomes. {ECO:0000250|UniProtKB:Q9UI30}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in the testis, also expressed
CC       in the brain, heart, kidney, liver, lung, muscle and spleen.
CC       {ECO:0000269|PubMed:34669960}.
CC   -!- SIMILARITY: Belongs to the TRM112 family. {ECO:0000305}.
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DR   EMBL; AK002791; BAB22361.1; -; mRNA.
DR   EMBL; AK003292; BAB22695.1; -; mRNA.
DR   EMBL; BC016191; AAH16191.1; -; mRNA.
DR   CCDS; CCDS29508.1; -.
DR   RefSeq; NP_001159842.1; NM_001166370.1.
DR   RefSeq; NP_080582.3; NM_026306.3.
DR   AlphaFoldDB; Q9DCG9; -.
DR   SMR; Q9DCG9; -.
DR   BioGRID; 212357; 10.
DR   STRING; 10090.ENSMUSP00000112250; -.
DR   iPTMnet; Q9DCG9; -.
DR   PhosphoSitePlus; Q9DCG9; -.
DR   SwissPalm; Q9DCG9; -.
DR   EPD; Q9DCG9; -.
DR   jPOST; Q9DCG9; -.
DR   MaxQB; Q9DCG9; -.
DR   PaxDb; Q9DCG9; -.
DR   PRIDE; Q9DCG9; -.
DR   ProteomicsDB; 259173; -.
DR   Antibodypedia; 29268; 88 antibodies from 18 providers.
DR   Ensembl; ENSMUST00000088257; ENSMUSP00000085591; ENSMUSG00000038812.
DR   Ensembl; ENSMUST00000116551; ENSMUSP00000112250; ENSMUSG00000038812.
DR   GeneID; 67674; -.
DR   KEGG; mmu:67674; -.
DR   UCSC; uc008gjd.2; mouse.
DR   CTD; 51504; -.
DR   MGI; MGI:1914924; Trmt112.
DR   VEuPathDB; HostDB:ENSMUSG00000038812; -.
DR   eggNOG; KOG1088; Eukaryota.
DR   GeneTree; ENSGT00390000009268; -.
DR   HOGENOM; CLU_086140_2_0_1; -.
DR   InParanoid; Q9DCG9; -.
DR   OMA; NMLTSKC; -.
DR   OrthoDB; 1465773at2759; -.
DR   PhylomeDB; Q9DCG9; -.
DR   TreeFam; TF313256; -.
DR   Reactome; R-MMU-156581; Methylation.
DR   Reactome; R-MMU-72764; Eukaryotic Translation Termination.
DR   BioGRID-ORCS; 67674; 25 hits in 73 CRISPR screens.
DR   ChiTaRS; Trmt112; mouse.
DR   PRO; PR:Q9DCG9; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q9DCG9; protein.
DR   Bgee; ENSMUSG00000038812; Expressed in embryonic brain and 103 other tissues.
DR   ExpressionAtlas; Q9DCG9; baseline and differential.
DR   Genevisible; Q9DCG9; MM.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR   GO; GO:0008276; F:protein methyltransferase activity; ISO:MGI.
DR   GO; GO:0034968; P:histone lysine methylation; ISS:UniProtKB.
DR   GO; GO:0018364; P:peptidyl-glutamine methylation; IDA:UniProtKB.
DR   GO; GO:2000234; P:positive regulation of rRNA processing; ISS:UniProtKB.
DR   GO; GO:0070476; P:rRNA (guanine-N7)-methylation; ISS:UniProtKB.
DR   GO; GO:0031167; P:rRNA methylation; ISS:UniProtKB.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   GO; GO:0002940; P:tRNA N2-guanine methylation; ISS:UniProtKB.
DR   InterPro; IPR039127; Trm112.
DR   InterPro; IPR005651; Trm112-like.
DR   PANTHER; PTHR12773; PTHR12773; 1.
DR   Pfam; PF03966; Trm112p; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Reference proteome.
FT   CHAIN           1..125
FT                   /note="Multifunctional methyltransferase subunit TRM112-
FT                   like protein"
FT                   /id="PRO_0000215798"
FT   DOMAIN          2..119
FT                   /note="TRM112"
FT   CONFLICT        85
FT                   /note="H -> Q (in Ref. 1; BAB22695)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        122
FT                   /note="Missing (in Ref. 2; AAH16191)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   125 AA;  14141 MW;  A749605B3982A6F6 CRC64;
     MKLLTHNLLS SHVRGVGTRG FPLRLQATEV RINPVEFNPE FVARMIPKVE WAALVQAADT
     LNLAEVPKEP TEGYEHDETF LRKMHHVLLE VDVLEGTLQC PESGRLFPIS RGIPNMLLND
     EETET