TRM11_MOUSE
ID TRM11_MOUSE Reviewed; 460 AA.
AC Q9CWH5; Q80Y71;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=tRNA (guanine(10)-N2)-methyltransferase homolog;
DE EC=2.1.1.-;
DE AltName: Full=tRNA guanosine-2'-O-methyltransferase TRM11 homolog;
GN Name=Trmt11;
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).
RA Chen Y., Huang C.-H.;
RT "Molecular identification and conserved evolution of a novel RNA methylase
RT protein gene in higher eukaryotic organisms.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Limb;
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=Spleen;
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: Catalytic subunit of an S-adenosyl-L-methionine-dependent
CC tRNA methyltransferase complex that mediates the methylation of the
CC guanosine nucleotide at position 10 (m2G10) in tRNAs. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TRMT112. {ECO:0000250|UniProtKB:Q7Z4G4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CWH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CWH5-2; Sequence=VSP_017819, VSP_017820;
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM11 methyltransferase family. {ECO:0000255|PROSITE-
CC ProRule:PRU00959}.
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DR EMBL; AF532979; AAQ10286.1; -; mRNA.
DR EMBL; AK010722; BAB27142.1; -; mRNA.
DR EMBL; BC048703; AAH48703.1; -; mRNA.
DR CCDS; CCDS23763.1; -. [Q9CWH5-1]
DR RefSeq; XP_006512947.1; XM_006512884.3.
DR AlphaFoldDB; Q9CWH5; -.
DR SMR; Q9CWH5; -.
DR BioGRID; 216187; 25.
DR STRING; 10090.ENSMUSP00000019927; -.
DR iPTMnet; Q9CWH5; -.
DR PhosphoSitePlus; Q9CWH5; -.
DR EPD; Q9CWH5; -.
DR MaxQB; Q9CWH5; -.
DR PaxDb; Q9CWH5; -.
DR PeptideAtlas; Q9CWH5; -.
DR PRIDE; Q9CWH5; -.
DR ProteomicsDB; 298229; -. [Q9CWH5-1]
DR ProteomicsDB; 298230; -. [Q9CWH5-2]
DR DNASU; 73681; -.
DR UCSC; uc007etf.1; mouse. [Q9CWH5-2]
DR MGI; MGI:1920931; Trmt11.
DR eggNOG; KOG2671; Eukaryota.
DR InParanoid; Q9CWH5; -.
DR PhylomeDB; Q9CWH5; -.
DR BioGRID-ORCS; 73681; 6 hits in 74 CRISPR screens.
DR PRO; PR:Q9CWH5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9CWH5; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008168; F:methyltransferase activity; IBA:GO_Central.
DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR000241; RNA_methylase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016691; tRNA_mtfrase_TRM11.
DR Pfam; PF01170; UPF0020; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
DR PROSITE; PS51627; SAM_MT_TRM11; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Methyltransferase; Reference proteome;
KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing;
KW tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4G4"
FT CHAIN 2..460
FT /note="tRNA (guanine(10)-N2)-methyltransferase homolog"
FT /id="PRO_0000230289"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z4G4"
FT VAR_SEQ 1..225
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017819"
FT VAR_SEQ 226
FT /note="T -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017820"
SQ SEQUENCE 460 AA; 52904 MW; C3B66046F7B56663 CRC64;
MALPGSLNRY LLLMAQEHLE FRLPEIKSLL SVIGGQFTNS QETYGKSPFW ILNIPSEDIA
RNLMKRTVCA KSIFELWGHG KSPEELYTSL KSYPVEKMVP YLHSDSTYKI KIHTFNKTLT
QEEKVKRIDA LEFLPFQGKV NLKKPQHVFS ILEDYGLDPN SIPKDPHNIY FGRWIADGQR
ELIESYSVKK RHFIGNTSMD AGLSFIMTNH AKVKENDLVF DPFVGTGGLL IASAHFGAYV
CGTDIDYNTV HGLGKASRKN QKWRGPDENI RANLRQYGLE KFYLDVLVSD ASKPSWRKGT
YFDAIITDPP YGIRESTRRS GSQKDIPKGI EKCPESHVPV SLSYHLSDMF FDLLNFAAET
LVLGGRLVYW LPVYTPEYTE EMVPWHPCLR LISNCEQKLS SHTARRLITM EKVKEFENRD
KYSHLLSDHF LPYQGHNSFR EKYFSGVTKR IAKEEKCSHE
