TRM61_MOUSE
ID TRM61_MOUSE Reviewed; 290 AA.
AC Q80XC2; Q8BMD4; Q8BX33;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=tRNA (adenine(58)-N(1))-methyltransferase catalytic subunit TRMT61A;
DE EC=2.1.1.220 {ECO:0000250|UniProtKB:Q96FX7};
DE AltName: Full=mRNA methyladenosine-N(1)-methyltransferase catalytic subunit TRMT61A;
DE EC=2.1.1.- {ECO:0000250|UniProtKB:Q96FX7};
DE AltName: Full=tRNA(m1A58)-methyltransferase subunit TRMT61A;
DE Short=tRNA(m1A58)MTase subunit TRMT61A;
GN Name=Trmt61a; Synonyms=Trm61;
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=Embryonic stem cell, and Wolffian duct;
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].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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, Pancreas, and 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 tRNA (adenine-N(1)-)-methyltransferase,
CC which catalyzes the formation of N(1)-methyladenine at position 58
CC (m1A58) in initiator methionyl-tRNA. Catalytic subunit of mRNA N(1)-
CC methyltransferase complex, which mediates methylation of adenosine
CC residues at the N(1) position of a small subset of mRNAs: N(1)
CC methylation takes place in tRNA T-loop-like structures of mRNAs and is
CC only present at low stoichiometries. {ECO:0000250|UniProtKB:Q96FX7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine(58) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC methyladenosine(58) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:43152, Rhea:RHEA-COMP:10365, Rhea:RHEA-COMP:10366,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491; EC=2.1.1.220;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00952};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an adenosine in mRNA + S-adenosyl-L-methionine = an N(1)-
CC methyladenosine in mRNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:55392, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12415,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74491;
CC Evidence={ECO:0000250|UniProtKB:Q96FX7};
CC -!- SUBUNIT: Heterotetramer; composed of two copies of TRMT6 and two copies
CC of TRMT61A. {ECO:0000250|UniProtKB:Q96FX7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P46959}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM61 family. {ECO:0000255|PROSITE-ProRule:PRU00952}.
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DR EMBL; AK049138; BAC33565.1; -; mRNA.
DR EMBL; AK032824; BAC28042.1; -; mRNA.
DR EMBL; BC051186; AAH51186.1; -; mRNA.
DR CCDS; CCDS26184.1; -.
DR RefSeq; NP_001093262.1; NM_001099792.1.
DR RefSeq; NP_001093263.1; NM_001099793.1.
DR RefSeq; NP_796348.2; NM_177374.4.
DR AlphaFoldDB; Q80XC2; -.
DR SMR; Q80XC2; -.
DR BioGRID; 236550; 11.
DR IntAct; Q80XC2; 1.
DR MINT; Q80XC2; -.
DR STRING; 10090.ENSMUSP00000082011; -.
DR iPTMnet; Q80XC2; -.
DR PhosphoSitePlus; Q80XC2; -.
DR EPD; Q80XC2; -.
DR MaxQB; Q80XC2; -.
DR PaxDb; Q80XC2; -.
DR PeptideAtlas; Q80XC2; -.
DR PRIDE; Q80XC2; -.
DR ProteomicsDB; 258850; -.
DR Antibodypedia; 6565; 74 antibodies from 20 providers.
DR DNASU; 328162; -.
DR Ensembl; ENSMUST00000084947; ENSMUSP00000082011; ENSMUSG00000060950.
DR Ensembl; ENSMUST00000168338; ENSMUSP00000133128; ENSMUSG00000060950.
DR GeneID; 328162; -.
DR KEGG; mmu:328162; -.
DR UCSC; uc007pdo.1; mouse.
DR CTD; 115708; -.
DR MGI; MGI:2443487; Trmt61a.
DR VEuPathDB; HostDB:ENSMUSG00000060950; -.
DR eggNOG; KOG2915; Eukaryota.
DR GeneTree; ENSGT00940000154239; -.
DR HOGENOM; CLU_025402_4_1_1; -.
DR InParanoid; Q80XC2; -.
DR OMA; VVYPKDA; -.
DR OrthoDB; 1032689at2759; -.
DR PhylomeDB; Q80XC2; -.
DR TreeFam; TF315053; -.
DR BioGRID-ORCS; 328162; 24 hits in 74 CRISPR screens.
DR ChiTaRS; Trmt61a; mouse.
DR PRO; PR:Q80XC2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q80XC2; protein.
DR Bgee; ENSMUSG00000060950; Expressed in dorsal pancreas and 207 other tissues.
DR ExpressionAtlas; Q80XC2; baseline and differential.
DR Genevisible; Q80XC2; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; ISO:MGI.
DR GO; GO:0061953; F:mRNA (adenine-N1-)-methyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro.
DR GO; GO:0080009; P:mRNA methylation; ISS:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; ISO:MGI.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR014816; tRNA_MeTrfase_Gcd14.
DR PANTHER; PTHR12133; PTHR12133; 1.
DR Pfam; PF08704; GCD14; 1.
DR PIRSF; PIRSF017269; GCD14; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51620; SAM_TRM61; 1.
PE 1: Evidence at protein level;
KW Acetylation; Methyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT CHAIN 2..290
FT /note="tRNA (adenine(58)-N(1))-methyltransferase catalytic
FT subunit TRMT61A"
FT /id="PRO_0000233095"
FT REGION 20..22
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 35..42
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 64..65
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 85..89
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 110..117
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 180..183
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT REGION 205..212
FT /note="Substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 87
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 114..116
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7,
FT ECO:0000255|PROSITE-ProRule:PRU00952"
FT BINDING 140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 163..164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7,
FT ECO:0000255|PROSITE-ProRule:PRU00952"
FT BINDING 279
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FX7"
FT CONFLICT 70
FT /note="H -> R (in Ref. 1; BAC33565)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="G -> D (in Ref. 1; BAC28042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 31639 MW; 7F9F291EE94E6FFC CRC64;
MSFVAYEELI KEGDTAILSL GHGSMVAVRV QRGAQTQTRH GVLRHSVDLI GRPFGSKVIC
SRGGWVYVLH PTPELWTVNL PHRTQILYST DIALITMMLE LRPGSVVCES GTGSGSVSHA
IIRSVAPTGH LHTVEFHQQR ADKAREEFQE HRLSQWVTVH TQDVCCSGFG VVHVADAVFL
DIPSPWEAVG HAWDALKVEG GRFCSFSPCI EQVQRTCQAL AAHGFTELST LEVLPQVYNV
RTVSLPLPDL GANNLETNMG SDASPFRSGT PMKETVGHTG YLTFATKTPG
