TRUB1_MOUSE
ID TRUB1_MOUSE Reviewed; 338 AA.
AC Q8C0D0; Q5EBH7; Q9D331;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Pseudouridylate synthase TRUB1 {ECO:0000305};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:Q8WWH5};
DE AltName: Full=TruB pseudouridine synthase homolog 1 {ECO:0000250|UniProtKB:Q8WWH5};
DE AltName: Full=tRNA pseudouridine 55 synthase TRUB1 {ECO:0000305};
DE Short=Psi55 synthase TRUB1 {ECO:0000305};
DE EC=5.4.99.25 {ECO:0000250|UniProtKB:Q8WWH5};
GN Name=Trub1 {ECO:0000312|MGI:MGI:1919383};
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 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Colon, Liver, and Testis;
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).
RC TISSUE=Heart;
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=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: Pseudouridine synthase that catalyzes pseudouridylation of
CC mRNAs and tRNAs. Mediates pseudouridylation of mRNAs with the consensus
CC sequence 5'-GUUCNANNC-3', harboring a stem-loop structure. Constitutes
CC the major pseudouridine synthase acting on mRNAs. Also catalyzes
CC pseudouridylation of some tRNAs, including synthesis of
CC pseudouridine(55) from uracil-55, in the psi GC loop of a subset of
CC tRNAs. Promotes the processing of pri-let-7 microRNAs (pri-miRNAs)
CC independently of its RNA pseudouridylate synthase activity. Acts by
CC binding to the stem-loop structure on pri-let-7, preventing LIN28-
CC binding (LIN28A and/or LIN28B), thereby enhancing the interaction
CC between pri-let-7 and the microprocessor DGCR8, which mediates miRNA
CC maturation. {ECO:0000250|UniProtKB:Q8WWH5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in mRNA = a pseudouridine in mRNA;
CC Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:Q8WWH5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in tRNA = a pseudouridine in tRNA;
CC Xref=Rhea:RHEA:54572, Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13934,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:Q8WWH5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC Evidence={ECO:0000250|UniProtKB:Q8WWH5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42533;
CC Evidence={ECO:0000250|UniProtKB:Q8WWH5};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8WWH5}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8WWH5}. Note=Catalyzes
CC pseudouridylation of mRNAs in the nucleus.
CC {ECO:0000250|UniProtKB:Q8WWH5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C0D0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C0D0-2; Sequence=VSP_020860, VSP_020861;
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; AK018525; BAB31254.1; -; mRNA.
DR EMBL; AK031674; BAC27506.1; -; mRNA.
DR EMBL; AK169221; BAE40991.1; -; mRNA.
DR EMBL; BC089592; AAH89592.1; -; mRNA.
DR CCDS; CCDS29926.1; -. [Q8C0D0-1]
DR CCDS; CCDS29927.1; -. [Q8C0D0-2]
DR RefSeq; NP_082391.1; NM_028115.3. [Q8C0D0-1]
DR RefSeq; NP_084115.2; NM_029839.3. [Q8C0D0-2]
DR AlphaFoldDB; Q8C0D0; -.
DR SMR; Q8C0D0; -.
DR STRING; 10090.ENSMUSP00000026073; -.
DR iPTMnet; Q8C0D0; -.
DR PhosphoSitePlus; Q8C0D0; -.
DR EPD; Q8C0D0; -.
DR MaxQB; Q8C0D0; -.
DR PaxDb; Q8C0D0; -.
DR PRIDE; Q8C0D0; -.
DR ProteomicsDB; 258988; -. [Q8C0D0-1]
DR ProteomicsDB; 258989; -. [Q8C0D0-2]
DR Antibodypedia; 31974; 126 antibodies from 22 providers.
DR DNASU; 72133; -.
DR Ensembl; ENSMUST00000026072; ENSMUSP00000026072; ENSMUSG00000025086. [Q8C0D0-2]
DR Ensembl; ENSMUST00000026073; ENSMUSP00000026073; ENSMUSG00000025086. [Q8C0D0-1]
DR GeneID; 72133; -.
DR KEGG; mmu:72133; -.
DR UCSC; uc008iae.2; mouse. [Q8C0D0-2]
DR UCSC; uc008iag.2; mouse. [Q8C0D0-1]
DR CTD; 142940; -.
DR MGI; MGI:1919383; Trub1.
DR VEuPathDB; HostDB:ENSMUSG00000025086; -.
DR eggNOG; KOG2529; Eukaryota.
DR GeneTree; ENSGT00940000158962; -.
DR HOGENOM; CLU_032087_1_0_1; -.
DR InParanoid; Q8C0D0; -.
DR OMA; ELQFIRW; -.
DR OrthoDB; 1535798at2759; -.
DR PhylomeDB; Q8C0D0; -.
DR TreeFam; TF320759; -.
DR BioGRID-ORCS; 72133; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Trub1; mouse.
DR PRO; PR:Q8C0D0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8C0D0; protein.
DR Bgee; ENSMUSG00000025086; Expressed in gastrula and 204 other tissues.
DR ExpressionAtlas; Q8C0D0; baseline and differential.
DR Genevisible; Q8C0D0; MM.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070883; F:pre-miRNA binding; ISS:UniProtKB.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; ISS:UniProtKB.
DR GO; GO:2000633; P:positive regulation of pre-miRNA processing; ISS:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; ISS:UniProtKB.
DR HAMAP; MF_01080; TruB_bact; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR PANTHER; PTHR13767; PTHR13767; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00431; TruB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Isomerase; mRNA processing;
KW Nucleus; Reference proteome; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8WWH5"
FT CHAIN 2..338
FT /note="Pseudouridylate synthase TRUB1"
FT /id="PRO_0000252088"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q8WWH5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q8WWH5"
FT VAR_SEQ 234..247
FT /note="DVECGGGFYIRSLV -> GFLCIALAVLELTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020860"
FT VAR_SEQ 248..338
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020861"
FT CONFLICT 60
FT /note="F -> L (in Ref. 1; BAB31254)"
FT /evidence="ECO:0000305"
FT CONFLICT 74
FT /note="L -> P (in Ref. 2; AAH89592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 338 AA; 36348 MW; B76CFC4381A6772A CRC64;
MAAAEAEVVS PLIVDTAPDT SGTAEASVAA SVAEAARTES QAPASKAALA AKLMSLSGVF
AVHKPKGPTS AELLNRLKEK LLAEAGMPSP EWNKRQKQTL KVGHGGTLDS AAQGVLVVGI
GRGTKMLTSM LSGSKRYITI GELGKATDTL DSTGKVTEEK PYDKITREDI EGILQKFTGN
IMQVPPLYSA LKKDGQRLST LMKKGKVVEA RPARPVTVHS ISLLKFQPPF FTLDVECGGG
FYIRSLVSDI GKELSSCASV LELTRTKQGP FTLAQHALPE DRWTIDDIEQ SLERCTSLLP
EELTFKKLKS DNSSDQVISC GYITLRDTKR EDDAVKTL
