ID TRM1L_MOUSE Reviewed; 728 AA.
AC A2RSY6; Q0VGB9; Q3UFG1; Q3UKB0; Q8C2S4; Q8CI50; Q8R203; Q9CT68;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=TRMT1-like protein;
DE EC=2.1.1.-;
GN Name=Trmt1l;
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] (ISOFORMS 1; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Pancreas, Placenta, and Thymus;
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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 202-728 (ISOFORM 2).
RC STRAIN=FVB/N; TISSUE=Brain, Eye, 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 [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=17198746; DOI=10.1016/j.gene.2006.11.004;
RA Vauti F., Goller T., Beine R., Becker L., Klopstock T., Hoelter S.M.,
RA Wurst W., Fuchs H., Gailus-Durner V., de Angelis M.H., Arnold H.-H.;
RT "The mouse Trm1-like gene is expressed in neural tissues and plays a role
RT in motor coordination and exploratory behaviour.";
RL Gene 389:174-185(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, 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: May play a role in motor coordination and exploratory
CC behavior. {ECO:0000269|PubMed:17198746}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=A2RSY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2RSY6-2; Sequence=VSP_031047;
CC Name=3;
CC IsoId=A2RSY6-3; Sequence=VSP_031045, VSP_031046;
CC Name=4;
CC IsoId=A2RSY6-4; Sequence=VSP_031044;
CC -!- TISSUE SPECIFICITY: Expressed in various neuronal structures during
CC embryonic development, including spinal ganglia, trigeminal nerve and
CC ganglion, olfactory and nasopharyngeal epithelium, nuclei of the
CC metencephalon, thalamus and medulla oblongata. Also expressed in lung,
CC esophagus, epiglottis, ependyma, vertebral column, spinal cord and
CC brown adipose tissue. Expression persists in the adult brain with
CC dynamically changing patterns in cortex and cerebellum.
CC {ECO:0000269|PubMed:17198746}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and show no apparent anatomical
CC defects. However, they display significantly altered motor coordination
CC and aberrant exploratory behavior. {ECO:0000269|PubMed:17198746}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. Trm1 family. {ECO:0000255|PROSITE-ProRule:PRU00958}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH37478.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK004493; BAB23331.1; -; mRNA.
DR EMBL; AK088077; BAC40131.1; -; mRNA.
DR EMBL; AK146088; BAE26891.1; -; mRNA.
DR EMBL; AK148524; BAE28600.1; -; mRNA.
DR EMBL; BC022682; AAH22682.1; -; mRNA.
DR EMBL; BC037478; AAH37478.1; ALT_INIT; mRNA.
DR EMBL; BC110425; AAI10426.1; -; mRNA.
DR EMBL; BC132299; AAI32300.1; -; mRNA.
DR CCDS; CCDS15361.1; -. [A2RSY6-1]
DR RefSeq; NP_081152.2; NM_026876.3.
DR AlphaFoldDB; A2RSY6; -.
DR SMR; A2RSY6; -.
DR BioGRID; 221107; 3.
DR IntAct; A2RSY6; 1.
DR MINT; A2RSY6; -.
DR STRING; 10090.ENSMUSP00000068309; -.
DR GlyGen; A2RSY6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A2RSY6; -.
DR PhosphoSitePlus; A2RSY6; -.
DR SwissPalm; A2RSY6; -.
DR EPD; A2RSY6; -.
DR MaxQB; A2RSY6; -.
DR PaxDb; 10090-ENSMUSP00000068309; -.
DR PeptideAtlas; A2RSY6; -.
DR ProteomicsDB; 300120; -. [A2RSY6-1]
DR ProteomicsDB; 300121; -. [A2RSY6-2]
DR ProteomicsDB; 300122; -. [A2RSY6-3]
DR ProteomicsDB; 300123; -. [A2RSY6-4]
DR Pumba; A2RSY6; -.
DR DNASU; 98685; -.
DR GeneID; 98685; -.
DR KEGG; mmu:98685; -.
DR UCSC; uc007cyr.1; mouse. [A2RSY6-4]
DR UCSC; uc007cyt.1; mouse. [A2RSY6-3]
DR UCSC; uc007cyu.1; mouse. [A2RSY6-1]
DR UCSC; uc029qua.1; mouse. [A2RSY6-2]
DR AGR; MGI:1916185; -.
DR CTD; 81627; -.
DR MGI; MGI:1916185; Trmt1l.
DR eggNOG; KOG1253; Eukaryota.
DR InParanoid; A2RSY6; -.
DR OrthoDB; 3146970at2759; -.
DR PhylomeDB; A2RSY6; -.
DR TreeFam; TF300851; -.
DR BioGRID-ORCS; 98685; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Trmt1l; mouse.
DR PRO; PR:A2RSY6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; A2RSY6; Protein.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0160102; F:tRNA (guanine(10)-N2)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0002940; P:tRNA N2-guanine methylation; IBA:GO_Central.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.30.56.70; N2,N2-dimethylguanosine tRNA methyltransferase, C-terminal domain; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR002905; Trm1.
DR InterPro; IPR042296; tRNA_met_Trm1_C.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR10631; N 2 ,N 2 -DIMETHYLGUANOSINE TRNA METHYLTRANSFERASE; 1.
DR PANTHER; PTHR10631:SF1; TRMT1-LIKE PROTEIN; 1.
DR Pfam; PF02005; TRM; 2.
DR SMART; SM00355; ZnF_C2H2; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51626; SAM_MT_TRM1; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Behavior; Isopeptide bond; Metal-binding;
KW Methyltransferase; Phosphoprotein; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..728
FT /note="TRMT1-like protein"
FT /id="PRO_0000317570"
FT DOMAIN 224..683
FT /note="Trm1 methyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00958"
FT ZN_FING 181..203
FT /note="C2H2-type"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..728
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 23
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2T5"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2T5"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2T5"
FT CROSSLNK 580
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2T5"
FT VAR_SEQ 152..728
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031044"
FT VAR_SEQ 285
FT /note="I -> K (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031045"
FT VAR_SEQ 286..728
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031046"
FT VAR_SEQ 645..728
FT /note="KLKKFLCCLSQAGFRVSRTHFDPMGIRTDAPLMQFKSILLKYSTPTYTGAQS
FT EGQMPPAAEDTVTDRVEMSVSDKAEASGCRRW -> NFLSLLQVKKIFVLSFASRLSSK
FT PNSL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031047"
FT CONFLICT 24
FT /note="P -> R (in Ref. 1; BAE26891/BAE28600 and 2;
FT AAI10426)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="H -> D (in Ref. 1; BAC40131)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="K -> Q (in Ref. 1; BAC40131)"
FT /evidence="ECO:0000305"
FT CONFLICT 436
FT /note="R -> I (in Ref. 1; BAB23331)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="L -> V (in Ref. 1; BAE26891)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 728 AA; 80861 MW; E39AE788EE72D903 CRC64;
MENMAEEELL PQEKEEAQVR VPTPAPDSAP VPAPAADTAL DSAPTPDSDP APALAPAPAP
ALSPSLASVP EEAESKRHIS IQRRLADLEK LAFGTEGDVD SASSLNSDNP GTENSQTCPL
CPKEKFRAYS SHKLRRHLQN LHWKISVEFE GYRMCICHLA CRPVKPTIVG EQISSKLGAH
YHCIICSATI TRRTDMLGHV KRHVNKGETK SRYIAASTAK SSNEILKETD TDIQVFPNYS
IPQKTDSYFN PKMKLNRQII FCTLAALAKE RKPLECLDAF GATGIMGLQW AKHLGNAVKV
TINDLNENSV TLIQKNCHLN KLKVVVDSEE KEEGDALEDD GTLGDIQVTR MDANVLMHLR
SFDFIHLDPF GTSVNYLDSA FRNVRNLGIV SVTSTDISSL YAKAQHVARR HYGCNIVRTE
YYKELAARIV VAAVARAAAR CNKGIEVLFA VALEHFVLVV VRVLRGPTSA DETAKKIQYL
IHCQWCEERI FQKDGNMVEE NPYRQLPCNC HGSMPGKTAI ELGPLWSSSL FNTGFLKRML
FESIHHGLDD IQPLIKTLIF ESECTPQSQC STHAPSNTNK QEENGVFVKT TDDTTIDIYS
AQGKRKSNEM AINLAKKQKT DASTAHPPFY YNIHRHSIKG MNMPKLKKFL CCLSQAGFRV
SRTHFDPMGI RTDAPLMQFK SILLKYSTPT YTGAQSEGQM PPAAEDTVTD RVEMSVSDKA
EASGCRRW
//
