TYW2_MOUSE
ID TYW2_MOUSE Reviewed; 446 AA.
AC Q8BG71; Q0P5W5; Q7TNQ8; Q9D2N1;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=tRNA wybutosine-synthesizing protein 2 homolog;
DE Short=tRNA-yW-synthesizing protein 2;
DE EC=2.5.1.114;
DE AltName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase;
GN Name=Trmt12; Synonyms=Tyw2;
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=Skin, Testis, and Urinary bladder;
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=Czech II, and FVB/N; TISSUE=Lung, and Salivary gland;
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).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts as a
CC component of the wybutosine biosynthesis pathway. Wybutosine is a hyper
CC modified guanosine with a tricyclic base found at the 3'-position
CC adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes
CC the transfer of the alpha-amino-alpha-carboxypropyl (acp) group from S-
CC adenosyl-L-methionine to the C-7 position of 4-demethylwyosine (imG-14)
CC to produce wybutosine-86 (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-demethylwyosine(37) in tRNA(Phe) + S-adenosyl-L-methionine =
CC 4-demethyl-7-[(3S)-3-amino-3-carboxypropyl]wyosine(37) in tRNA(Phe) +
CC H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:36355, Rhea:RHEA-
CC COMP:10164, Rhea:RHEA-COMP:10378, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17509, ChEBI:CHEBI:59789, ChEBI:CHEBI:64315,
CC ChEBI:CHEBI:73550; EC=2.5.1.114;
CC -!- PATHWAY: tRNA modification; wybutosine-tRNA(Phe) biosynthesis.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TRM5/TYW2 family. {ECO:0000255|PROSITE-ProRule:PRU01021}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52533.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB31750.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK019481; BAB31750.1; ALT_FRAME; mRNA.
DR EMBL; AK031429; BAC27399.1; -; mRNA.
DR EMBL; AK076857; BAC36508.1; -; mRNA.
DR EMBL; AK079291; BAC37597.1; -; mRNA.
DR EMBL; BC052533; AAH52533.1; ALT_FRAME; mRNA.
DR EMBL; BC055850; AAH55850.1; -; mRNA.
DR CCDS; CCDS37081.1; -.
DR RefSeq; NP_080918.2; NM_026642.2.
DR AlphaFoldDB; Q8BG71; -.
DR SMR; Q8BG71; -.
DR STRING; 10090.ENSMUSP00000047831; -.
DR iPTMnet; Q8BG71; -.
DR PhosphoSitePlus; Q8BG71; -.
DR EPD; Q8BG71; -.
DR MaxQB; Q8BG71; -.
DR PaxDb; Q8BG71; -.
DR PeptideAtlas; Q8BG71; -.
DR PRIDE; Q8BG71; -.
DR ProteomicsDB; 298051; -.
DR Antibodypedia; 13906; 102 antibodies from 19 providers.
DR DNASU; 68260; -.
DR Ensembl; ENSMUST00000036937; ENSMUSP00000047831; ENSMUSG00000037085.
DR GeneID; 68260; -.
DR KEGG; mmu:68260; -.
DR UCSC; uc007vtp.1; mouse.
DR CTD; 55039; -.
DR MGI; MGI:1915510; Trmt12.
DR VEuPathDB; HostDB:ENSMUSG00000037085; -.
DR eggNOG; KOG1227; Eukaryota.
DR GeneTree; ENSGT00940000153304; -.
DR HOGENOM; CLU_022610_1_0_1; -.
DR InParanoid; Q8BG71; -.
DR OMA; WQRHGNL; -.
DR OrthoDB; 736943at2759; -.
DR PhylomeDB; Q8BG71; -.
DR TreeFam; TF314137; -.
DR UniPathway; UPA00375; -.
DR BioGRID-ORCS; 68260; 0 hits in 72 CRISPR screens.
DR PRO; PR:Q8BG71; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BG71; protein.
DR Bgee; ENSMUSG00000037085; Expressed in superior cervical ganglion and 75 other tissues.
DR Genevisible; Q8BG71; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0102522; F:tRNA 4-demethylwyosine alpha-amino-alpha-carboxypropyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0008175; F:tRNA methyltransferase activity; IBA:GO_Central.
DR GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR030382; MeTrfase_TRM5/TYW2.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02475; Met_10; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..446
FT /note="tRNA wybutosine-synthesizing protein 2 homolog"
FT /id="PRO_0000281838"
FT BINDING 208
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT BINDING 215
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT BINDING 255
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT BINDING 283..284
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01021"
FT CONFLICT 396
FT /note="L -> F (in Ref. 2; AAH52533)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="V -> I (in Ref. 1; BAB31750)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="R -> Q (in Ref. 2; AAH52533/AAH55850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 50299 MW; BB416D36D212E44B CRC64;
MERECEESVV VAVVTEPRFT QRYRDYLEEQ KLLDRLHRVA KLRDGAVALP VLAESLSEQH
LQELRDRVAP GSTCVLTRLP DPLPSKKARV RSPAQILCLE VRRWVEDRGV TWSAELEADL
PRSWQRHGDL MLLSEDCFQA TLWKGLEPEL WETVASALGV QRLAKRGRVL PDGTRTPSVT
LLLGDHGWVE HMDNGIRYKF DVTQCMFSFG NITEKLRVAS LSCAGEVLVD LYAGIGYFTL
PFLVHAGAAF VHACEWNPHA VVALRNNLEI NGVADRCQIH FGDNRKLKLS DIADRVNLGL
IPSSKEGWPV ACQVLRKDVG GILHIHQNVE SFSGKTPQPP GSNNVEKEHW PRPQKITTDT
QGNGTTENFR GEISSANKPE WWRWAESAET QIASLLHQVH GKPWRTRILH VHPVKSYAPH
VDHIVLDLEC RPLTSSWPEG VDLLTQ
