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 02-OCT-2024, entry version 116. 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; 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=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 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 project: RT 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 post- CC transcriptional modification necessary for their translation. Acts at CC position 390 in COXI mt-mRNA and at position 697-699 in mitochondrial CC COXIII mt-mRNA. As a component of a functional protein-RNA module, CC consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S CC mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA CC abundance and may play a role in mitochondrial ribosome biogenesis. CC {ECO:0000250|UniProtKB:Q6P087}. 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:Q6P087}; 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:Q6P087}. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000250|UniProtKB:Q6P087}. Note=Localizes to mitochondrial RNA CC granules, platforms for post-transcriptional RNA modification and CC 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; 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 AlphaFoldDB; Q14AI6; -. DR SMR; Q14AI6; -. DR BioGRID; 221589; 2. DR STRING; 10090.ENSMUSP00000108715; -. DR PhosphoSitePlus; Q14AI6; -. DR PaxDb; 10090-ENSMUSP00000108715; -. DR ProteomicsDB; 256848; -. [Q14AI6-1] DR ProteomicsDB; 256849; -. [Q14AI6-2] DR Pumba; Q14AI6; -. DR Antibodypedia; 25685; 64 antibodies from 16 providers. DR Ensembl; ENSMUST00000113092.9; ENSMUSP00000108715.3; ENSMUSG00000051169.15. [Q14AI6-1] DR Ensembl; ENSMUST00000129047.8; ENSMUSP00000120380.2; ENSMUSG00000051169.15. [Q14AI6-2] DR GeneID; 101122; -. DR KEGG; mmu:101122; -. DR UCSC; uc009dfy.2; mouse. [Q14AI6-1] DR UCSC; uc009dga.1; mouse. [Q14AI6-2] DR AGR; MGI:2141440; -. DR CTD; 285367; -. DR MGI; MGI:2141440; Rpusd3. DR VEuPathDB; HostDB:ENSMUSG00000051169; -. DR eggNOG; KOG1919; Eukaryota. DR GeneTree; ENSGT00940000161059; -. DR InParanoid; Q14AI6; -. DR OMA; PTVTYWA; -. DR OrthoDB; 5400777at2759; -. DR PhylomeDB; Q14AI6; -. DR TreeFam; TF337899; -. DR BioGRID-ORCS; 101122; 3 hits in 77 CRISPR screens. DR PRO; PR:Q14AI6; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; Q14AI6; protein. DR Bgee; ENSMUSG00000051169; Expressed in right kidney and 143 other cell types or tissues. DR ExpressionAtlas; Q14AI6; baseline and differential. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0035770; C:ribonucleoprotein granule; IEA:Ensembl. 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_RluA_like; 1. DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf. DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA. DR InterPro; IPR050188; RluA_PseudoU_synthase. DR PANTHER; PTHR21600:SF49; MITOCHONDRIAL MRNA PSEUDOURIDINE SYNTHASE RPUSD3; 1. DR PANTHER; PTHR21600; MITOCHONDRIAL RNA PSEUDOURIDINE SYNTHASE; 1. DR Pfam; PF00849; PseudoU_synth_2; 1. DR SUPFAM; SSF55120; Pseudouridine synthase; 1. PE 2: Evidence at transcript level; KW Alternative splicing; Isomerase; Mitochondrion; mRNA processing; KW Reference proteome; Transit peptide. FT TRANSIT 1..36 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 37..344 FT /note="Mitochondrial mRNA pseudouridine synthase Rpusd3" FT /id="PRO_0000300823" FT REGION 25..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 283..344 FT /note="LDEALLRHLRLSPSQVAQMPLHLHLHRLLLPGTGSRDPPSELLAPLPPYFSR FT TLQCLRLSQQ -> GPLSHMPALCGFGGNCVSQISCTFRLGGSWLGV (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_027871" FT CONFLICT 14 FT /note="W -> T (in Ref. 2; AAH38081)" FT /evidence="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 //