TRUB2_MOUSE
ID TRUB2_MOUSE Reviewed; 331 AA.
AC Q91WG3; Q8BTK3;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Pseudouridylate synthase TRUB2, mitochondrial {ECO:0000305};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:O95900};
DE AltName: Full=TruB pseudouridine synthase homolog 2 {ECO:0000250|UniProtKB:O95900};
DE AltName: Full=tRNA pseudouridine 55 synthase TRUB2 {ECO:0000305};
DE Short=Psi55 synthase TRUB2 {ECO:0000305};
DE EC=5.4.99.25 {ECO:0000250|UniProtKB:O95900};
DE Flags: Precursor;
GN Name=Trub2 {ECO:0000312|MGI:MGI:2442186};
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=Amnion;
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=FVB/N; TISSUE=Kidney, and Liver;
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: Minor enzyme contributing to the isomerization of uridine to
CC pseudouridine (pseudouridylation) of specific mitochondrial mRNAs (mt-
CC mRNAs) such as COXI and COXIII mt-mRNAs. As a component of a functional
CC protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2,
CC FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S
CC mt-rRNA abundance and is required for intra-mitochondrial translation.
CC Also catalyzes pseudouridylation of some tRNAs, including synthesis of
CC pseudouridine(55) from uracil-55, in the psi GC loop of a subset of
CC tRNAs. {ECO:0000250|UniProtKB:O95900}.
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:O95900};
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:O95900};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42533;
CC Evidence={ECO:0000250|UniProtKB:O95900};
CC -!- SUBUNIT: Forms a regulatory protein-RNA complex, consisting of RCC1L,
CC NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA.
CC {ECO:0000250|UniProtKB:O95900}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:O95900}. Note=Localizes to mitochondrial RNA
CC granules, platforms for post-transcriptional RNA modification and
CC ribosome assembly. {ECO:0000250|UniProtKB:O95900}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000305}.
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DR EMBL; AK090004; BAC41040.1; -; mRNA.
DR EMBL; AK167294; BAE39399.1; -; mRNA.
DR EMBL; BC015285; AAH15285.1; -; mRNA.
DR EMBL; BC024075; AAH24075.1; -; mRNA.
DR CCDS; CCDS15856.1; -.
DR RefSeq; NP_001277425.1; NM_001290496.1.
DR RefSeq; NP_663495.3; NM_145520.5.
DR AlphaFoldDB; Q91WG3; -.
DR SMR; Q91WG3; -.
DR STRING; 10090.ENSMUSP00000041848; -.
DR PhosphoSitePlus; Q91WG3; -.
DR EPD; Q91WG3; -.
DR MaxQB; Q91WG3; -.
DR PaxDb; Q91WG3; -.
DR PeptideAtlas; Q91WG3; -.
DR PRIDE; Q91WG3; -.
DR ProteomicsDB; 258990; -.
DR Antibodypedia; 17439; 149 antibodies from 23 providers.
DR DNASU; 227682; -.
DR Ensembl; ENSMUST00000048044; ENSMUSP00000041848; ENSMUSG00000039826.
DR GeneID; 227682; -.
DR KEGG; mmu:227682; -.
DR UCSC; uc008jaa.3; mouse.
DR CTD; 26995; -.
DR MGI; MGI:2442186; Trub2.
DR VEuPathDB; HostDB:ENSMUSG00000039826; -.
DR eggNOG; KOG2559; Eukaryota.
DR GeneTree; ENSGT00940000156773; -.
DR HOGENOM; CLU_032087_1_1_1; -.
DR InParanoid; Q91WG3; -.
DR OMA; CIHFQPP; -.
DR OrthoDB; 1535798at2759; -.
DR PhylomeDB; Q91WG3; -.
DR TreeFam; TF320759; -.
DR BioGRID-ORCS; 227682; 19 hits in 73 CRISPR screens.
DR ChiTaRS; Trub2; mouse.
DR PRO; PR:Q91WG3; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91WG3; protein.
DR Bgee; ENSMUSG00000039826; Expressed in metanephric renal vesicle and 250 other tissues.
DR ExpressionAtlas; Q91WG3; baseline and differential.
DR Genevisible; Q91WG3; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISO:MGI.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; ISO:MGI.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR039048; Trub2.
DR PANTHER; PTHR13195; PTHR13195; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
PE 2: Evidence at transcript level;
KW Isomerase; Mitochondrion; mRNA processing; Reference proteome;
KW Transit peptide; tRNA processing.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..331
FT /note="Pseudouridylate synthase TRUB2, mitochondrial"
FT /id="PRO_0000252091"
FT REGION 309..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9Y606"
FT CONFLICT 266
FT /note="D -> H (in Ref. 1; BAC41040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 331 AA; 36807 MW; 918D5634828FA63A CRC64;
MGSSGLARLQ GLFAVYKPPG LKWLHLRETV ELQLLKGLNA QQPPAPDQRV RFLLGPVEGS
EEKKLTLRAT NVPSLTTHRL VRGPAFTNLK IGVGHRLDVQ ASGVLVLAVG HGRSLLTDMY
DAHLTKDYTV RGLLGKATDN FCEDGRLIEK TTYDHVTRER LDRILAVIQG SHQKALVMYS
NLDLKSQEAY EMAVQGVIRP MNKSPMLISG IRCLHFAPPE FLLEVQCMHE TQQQLRKLVH
EIGLELKTSA VCTQVRRTRD GFFGLDDALL RTQWDLHNIQ DAIQAAAPRV AAELQKNLSL
KLGHHQLPST GQPWGLKDPS STLELESCSG Q
