ID RUSD3_MOUSE Reviewed; 344 AA. AC Q14AI6; Q3UZF6; Q8BVS3; Q8CHZ5; DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 07-NOV-2018, entry version 87. DE RecName: Full=Mitochondrial mRNA pseudouridine synthase Rpusd3; DE EC=5.4.99.-; DE AltName: Full=RNA pseudouridylate synthase domain-containing protein 3; DE Flags: Precursor; GN Name=Rpusd3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC STRAIN=C57BL/6J; TISSUE=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., 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=FVB/N; TISSUE=Brain, and Kidney; 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). CC -!- FUNCTION: Catalyzes uridine to pseudouridine isomerization CC (pseudouridylation) of specific mitochondrial mRNAs (mt-mRNAs), a CC post-transcriptional modification necessary for their translation. CC Acts at position 390 in COXI mt-mRNA and at position 697-699 in CC mitochondrial COXIII mt-mRNA. As a component of a functional CC protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, CC TRUB2, FASTKD2 and 16S mitochondrial ribosomal RNA (16S mt-rRNA), CC controls 16S mt-rRNA abundance and may play a role in CC mitochondrial ribosome biogenesis. {ECO:0000250|UniProtKB:Q6P087}. CC -!- CATALYTIC ACTIVITY: mRNA uridine = mRNA pseudouridine. CC {ECO:0000250|UniProtKB:Q6P087}. CC -!- SUBUNIT: Forms a regulatory protein-RNA complex, consisting of CC RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA. CC {ECO:0000250|UniProtKB:Q6P087}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000250|UniProtKB:Q6P087}. Note=Localizes to mitochondrial CC RNA granules, platforms for post-transcriptional RNA modification CC and ribosome assembly. {ECO:0000250|UniProtKB:Q6P087}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14AI6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14AI6-2; Sequence=VSP_027871; CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAE21901.1; Type=Frameshift; Positions=198, 239; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK076749; BAC36463.1; -; mRNA. DR EMBL; AK133871; BAE21901.1; ALT_FRAME; mRNA. DR EMBL; BC038081; AAH38081.1; -; mRNA. DR EMBL; BC116825; AAI16826.1; -; mRNA. DR EMBL; BC116827; AAI16828.1; -; mRNA. DR CCDS; CCDS51872.1; -. [Q14AI6-1] DR RefSeq; NP_001028376.1; NM_001033204.1. [Q14AI6-1] DR RefSeq; NP_001333440.1; NM_001346511.1. DR UniGene; Mm.31204; -. DR UniGene; Mm.473120; -. DR ProteinModelPortal; Q14AI6; -. DR SMR; Q14AI6; -. DR STRING; 10090.ENSMUSP00000108715; -. DR PhosphoSitePlus; Q14AI6; -. DR MaxQB; Q14AI6; -. DR PaxDb; Q14AI6; -. DR PRIDE; Q14AI6; -. DR Ensembl; ENSMUST00000113092; ENSMUSP00000108715; ENSMUSG00000051169. [Q14AI6-1] DR Ensembl; ENSMUST00000129047; ENSMUSP00000120380; ENSMUSG00000051169. [Q14AI6-2] DR GeneID; 101122; -. DR KEGG; mmu:101122; -. DR UCSC; uc009dfy.2; mouse. [Q14AI6-1] DR UCSC; uc009dga.1; mouse. [Q14AI6-2] DR CTD; 285367; -. DR MGI; MGI:2141440; Rpusd3. DR eggNOG; KOG1919; Eukaryota. DR eggNOG; COG0564; LUCA. DR GeneTree; ENSGT00530000063800; -. DR HOGENOM; HOG000082513; -. DR HOVERGEN; HBG098171; -. DR InParanoid; Q14AI6; -. DR KO; K22537; -. DR OMA; DWTCKQL; -. DR OrthoDB; EOG091G0LFU; -. DR PhylomeDB; Q14AI6; -. DR TreeFam; TF337899; -. DR PRO; PR:Q14AI6; -. DR Proteomes; UP000000589; Chromosome 6. DR Bgee; ENSMUSG00000051169; Expressed in 160 organ(s), highest expression level in cardiac ventricle. DR CleanEx; MM_RPUSD3; -. DR ExpressionAtlas; Q14AI6; baseline and differential. DR Genevisible; Q14AI6; MM. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. DR CDD; cd02869; PseudoU_synth_RluCD_like; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluD. DR Pfam; PF00849; PseudoU_synth_2; 1. DR SUPFAM; SSF55120; SSF55120; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Complete proteome; Isomerase; Mitochondrion; KW mRNA processing; Reference proteome; Transit peptide. FT TRANSIT 1 36 Mitochondrion. {ECO:0000255}. FT CHAIN 37 344 Mitochondrial mRNA pseudouridine synthase FT Rpusd3. FT /FTId=PRO_0000300823. FT VAR_SEQ 283 344 LDEALLRHLRLSPSQVAQMPLHLHLHRLLLPGTGSRDPPSE FT LLAPLPPYFSRTLQCLRLSQQ -> GPLSHMPALCGFGGNC FT VSQISCTFRLGGSWLGV (in isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_027871. FT CONFLICT 14 14 W -> T (in Ref. 2; AAH38081). FT {ECO:0000305}. SQ SEQUENCE 344 AA; 38076 MW; 3B3C75A2F67CB7D0 CRC64; MGALRVLRYV SMIWRPELGS CARQRDAGFG TEARRPSQPH RSSKHKDLVE DQPFPGLLRT ENLGLEELAH VLRAAVVDQK GPLVTLNKPQ GLPVTGRPGE LTLLSVLPQL SQALGLEHQE LQVVRAPGKE ASGLVLLSSC PQTASRLQKF FIHSRRAQRP TATYCAVTDG IPEPSEGTVC MPLKMEQMND VDLAVPVMSP SRKDIQEGVK RTLSRFHVMA TGRGCALVQL QPLTVFPNQL QVHMALQLCP ILGDHTYAAR VGTVLGQRFL WPAETTKPQR QVLDEALLRH LRLSPSQVAQ MPLHLHLHRL LLPGTGSRDP PSELLAPLPP YFSRTLQCLR LSQQ //