PUS3_MOUSE
ID PUS3_MOUSE Reviewed; 481 AA.
AC Q9JI38; Q8BVA6; Q8K0Y3;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=tRNA pseudouridine(38/39) synthase;
DE EC=5.4.99.45 {ECO:0000269|PubMed:11027153};
DE AltName: Full=tRNA pseudouridine synthase 3;
DE AltName: Full=tRNA pseudouridylate synthase 3;
DE AltName: Full=tRNA-uridine isomerase 3;
GN Name=Pus3;
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 [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11027153; DOI=10.1021/bi001109m;
RA Chen J., Patton J.R.;
RT "Pseudouridine synthase 3 from mouse modifies the anticodon loop of tRNA.";
RL Biochemistry 39:12723-12730(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Diencephalon;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=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).
RN [4]
RP PROTEIN SEQUENCE OF 142-149, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
CC -!- FUNCTION: Formation of pseudouridine at position 39 in the anticodon
CC stem and loop of transfer RNAs. Also acts on position 38, but much less
CC efficiently. {ECO:0000269|PubMed:11027153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine(38/39) in tRNA = pseudouridine(38/39) in tRNA;
CC Xref=Rhea:RHEA:42564, Rhea:RHEA-COMP:10117, Rhea:RHEA-COMP:10118,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.45;
CC Evidence={ECO:0000269|PubMed:11027153};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC {ECO:0000305}.
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DR EMBL; AF266505; AAF91402.1; -; mRNA.
DR EMBL; AK079095; BAC37536.1; -; mRNA.
DR EMBL; BC029253; AAH29253.1; -; mRNA.
DR CCDS; CCDS22965.1; -.
DR RefSeq; NP_075781.3; NM_023292.4.
DR RefSeq; XP_011240888.1; XM_011242586.2.
DR AlphaFoldDB; Q9JI38; -.
DR SMR; Q9JI38; -.
DR BioGRID; 211902; 5.
DR STRING; 10090.ENSMUSP00000034615; -.
DR iPTMnet; Q9JI38; -.
DR PhosphoSitePlus; Q9JI38; -.
DR EPD; Q9JI38; -.
DR MaxQB; Q9JI38; -.
DR PaxDb; Q9JI38; -.
DR PeptideAtlas; Q9JI38; -.
DR PRIDE; Q9JI38; -.
DR ProteomicsDB; 301833; -.
DR Antibodypedia; 46038; 95 antibodies from 22 providers.
DR DNASU; 67049; -.
DR Ensembl; ENSMUST00000034615; ENSMUSP00000034615; ENSMUSG00000032103.
DR GeneID; 67049; -.
DR KEGG; mmu:67049; -.
DR UCSC; uc009oth.2; mouse.
DR CTD; 83480; -.
DR MGI; MGI:1914299; Pus3.
DR VEuPathDB; HostDB:ENSMUSG00000032103; -.
DR eggNOG; KOG2554; Eukaryota.
DR GeneTree; ENSGT00950000183160; -.
DR HOGENOM; CLU_014673_2_0_1; -.
DR InParanoid; Q9JI38; -.
DR OMA; NLFRCDF; -.
DR OrthoDB; 1093493at2759; -.
DR PhylomeDB; Q9JI38; -.
DR TreeFam; TF314428; -.
DR BRENDA; 4.2.1.70; 3474.
DR BRENDA; 5.4.99.12; 3474.
DR BRENDA; 5.4.99.45; 3474.
DR BioGRID-ORCS; 67049; 14 hits in 69 CRISPR screens.
DR ChiTaRS; Pus3; mouse.
DR PRO; PR:Q9JI38; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JI38; protein.
DR Bgee; ENSMUSG00000032103; Expressed in rostral migratory stream and 248 other tissues.
DR ExpressionAtlas; Q9JI38; baseline and differential.
DR Genevisible; Q9JI38; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IDA:MGI.
DR CDD; cd02569; PseudoU_synth_ScPus3; 1.
DR Gene3D; 3.30.70.580; -; 1.
DR Gene3D; 3.30.70.660; -; 1.
DR HAMAP; MF_00171; TruA; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001406; PsdUridine_synth_TruA.
DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR InterPro; IPR041707; Pus3-like.
DR InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR PANTHER; PTHR11142; PTHR11142; 1.
DR Pfam; PF01416; PseudoU_synth_1; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00071; hisT_truA; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isomerase; Nucleus;
KW Reference proteome; tRNA processing.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE2"
FT CHAIN 2..481
FT /note="tRNA pseudouridine(38/39) synthase"
FT /id="PRO_0000057521"
FT ACT_SITE 119
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZE2"
FT CONFLICT 237
FT /note="N -> D (in Ref. 1; AAF91402)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="D -> G (in Ref. 2; BAC37536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 55546 MW; 32B6B59984AF830D CRC64;
MAENTDRNQI EKLLNRVKEL EQEVERLKKK KEQANNIKDS SIRENSLGSG KAKRAFDFSA
HGRRHVALKI AYLGWGYQGF ASQENTSNTI EEKLFEALTK TRLVESRQTS NYHRCGRTDK
GVSAFGQVIS LDLRSQFPTS RDSEDSNLKH EADDLAKEIR YTHILNRVLP ADIRVLAWAP
VEPSFSARFS CLERTYRYFF PRADLDIATM NYAAQKYVGT HDFRNLCKMD VANGVINFQR
TILCAQVQLV AQSPGEERRQ EPFQLCQFEV IGQAFLYHQV RCMMAILFLI GQGMEKPEII
DELLNIQKNP QKPQYSMAVE FPLVLYDCKF ENTKWIYDHE VQEFNVTHLQ QLWANHAVKT
HMLYSMLQGL DSVMVTCAAG TKMDEATEWR NIQPPVIKHT SAFVEGVKMR TYKPLMDRPK
CQGLESRIRH FVSRGRIEHP HLLHKEEIKA RRDCADKEEN TVVENPSKRV CIIDAEINSI
A
