RUSD3_MOUSE
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 03-AUG-2022, entry version 106.
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};
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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 EPD; Q14AI6; -.
DR MaxQB; Q14AI6; -.
DR PaxDb; Q14AI6; -.
DR PRIDE; Q14AI6; -.
DR ProteomicsDB; 256848; -. [Q14AI6-1]
DR ProteomicsDB; 256849; -. [Q14AI6-2]
DR Antibodypedia; 25685; 57 antibodies from 15 providers.
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 VEuPathDB; HostDB:ENSMUSG00000051169; -.
DR eggNOG; KOG1919; Eukaryota.
DR GeneTree; ENSGT00940000161059; -.
DR InParanoid; Q14AI6; -.
DR OMA; PTVTYWA; -.
DR OrthoDB; 1378690at2759; -.
DR PhylomeDB; Q14AI6; -.
DR TreeFam; TF337899; -.
DR BioGRID-ORCS; 101122; 3 hits in 72 CRISPR screens.
DR PRO; PR:Q14AI6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q14AI6; protein.
DR Bgee; ENSMUSG00000051169; Expressed in right kidney and 140 other tissues.
DR ExpressionAtlas; Q14AI6; baseline and differential.
DR Genevisible; Q14AI6; 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; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR SUPFAM; SSF55120; SSF55120; 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
