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 01-MAY-2013, entry version 91.
DE RecName: Full=tRNA pseudouridine(38/39) synthase;
DE EC=5.4.99.45;
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; 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
RT 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.,
RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA 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.,
RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 142-149, AND 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
CC anticodon stem and loop of transfer RNAs. Also acts on position
CC 38, but much less efficiently.
CC -!- CATALYTIC ACTIVITY: tRNA uridine(38/39) = tRNA
CC pseudouridine(38/39).
CC -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF266505; AAF91402.1; -; mRNA.
DR EMBL; AK079095; BAC37536.1; -; mRNA.
DR EMBL; BC029253; AAH29253.1; -; mRNA.
DR IPI; IPI00331619; -.
DR RefSeq; NP_075781.3; NM_023292.4.
DR UniGene; Mm.425574; -.
DR UniGene; Mm.482285; -.
DR ProteinModelPortal; Q9JI38; -.
DR SMR; Q9JI38; 64-304.
DR STRING; 10090.ENSMUSP00000034615; -.
DR PhosphoSite; Q9JI38; -.
DR PRIDE; Q9JI38; -.
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 eggNOG; COG0101; -.
DR GeneTree; ENSGT00510000047444; -.
DR HOGENOM; HOG000199032; -.
DR HOVERGEN; HBG053769; -.
DR InParanoid; Q9JI38; -.
DR KO; K01855; -.
DR OMA; NHAVKTH; -.
DR OrthoDB; EOG4B2SXG; -.
DR BRENDA; 4.2.1.70; 3474.
DR NextBio; 323424; -.
DR ArrayExpress; Q9JI38; -.
DR Bgee; Q9JI38; -.
DR CleanEx; MM_PUS3; -.
DR Genevestigator; Q9JI38; -.
DR GermOnline; ENSMUSG00000032103; Mus musculus.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IDA:MGI.
DR Gene3D; 3.30.70.580; -; 1.
DR Gene3D; 3.30.70.660; -; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom.
DR InterPro; IPR001406; PsdUridine_synth_TruA.
DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR InterPro; IPR020094; PsdUridine_synth_TruA_N.
DR PANTHER; PTHR11142; PTHR11142; 1.
DR Pfam; PF01416; PseudoU_synth_1; 2.
DR SUPFAM; SSF55120; PsdUridine_synth_cat_dom; 1.
DR TIGRFAMs; TIGR00071; hisT_truA; 1.
PE 1: Evidence at protein level;
KW Complete proteome; Direct protein sequencing; Isomerase; Nucleus;
KW Reference proteome; tRNA processing.
FT CHAIN 1 481 tRNA pseudouridine(38/39) synthase.
FT /FTId=PRO_0000057521.
FT ACT_SITE 119 119 Nucleophile (By similarity).
FT BINDING 196 196 Substrate (By similarity).
FT CONFLICT 237 237 N -> D (in Ref. 1; AAF91402).
FT CONFLICT 384 384 D -> G (in Ref. 2; BAC37536).
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
//
