RUSD4_MOUSE
ID RUSD4_MOUSE Reviewed; 377 AA.
AC Q9CWX4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Pseudouridylate synthase RPUSD4, mitochondrial {ECO:0000305};
DE EC=5.4.99.- {ECO:0000250|UniProtKB:Q96CM3};
DE AltName: Full=RNA pseudouridylate synthase domain-containing protein 4 {ECO:0000305};
DE Flags: Precursor;
GN Name=Rpusd4 {ECO:0000312|MGI:MGI:1919239};
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spleen;
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].
RC TISSUE=Pituitary;
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 different mitochondrial RNA substrates. Acts on
CC position 1397 in 16S mitochondrial ribosomal RNA (16S mt-rRNA). This
CC modification is required for the assembly of 16S mt-rRNA into a
CC functional mitochondrial ribosome. As a component of a functional
CC protein-RNA module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2,
CC FASTKD2 and 16S mt-rRNA, controls 16S mt-rRNA abundance and is required
CC for intra-mitochondrial translation. Acts on position 39 in
CC mitochondrial tRNA(Phe). Also catalyzes pseudouridylation of mRNAs in
CC nucleus: acts as a regulator of pre-mRNA splicing by mediating
CC pseudouridylation of pre-mRNAs at locations associated with
CC alternatively spliced regions. Pseudouridylation of pre-mRNAs near
CC splice sites directly regulates mRNA splicing and mRNA 3'-end
CC processing. {ECO:0000250|UniProtKB:Q96CM3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=uridine in 5S rRNA = pseudouridine in 5S rRNA;
CC Xref=Rhea:RHEA:47036, Rhea:RHEA-COMP:11730, Rhea:RHEA-COMP:11731,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:Q96CM3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in tRNA = a pseudouridine in tRNA;
CC Xref=Rhea:RHEA:54572, Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13934,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000250|UniProtKB:Q96CM3};
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:Q96CM3};
CC -!- SUBUNIT: Interacts with 16S mt-rRNA, mt-tRNA(Phe) and mt-tRNA(Met).
CC Forms a regulatory protein-RNA complex, consisting of RCC1L, NGRN,
CC RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA.
CC {ECO:0000250|UniProtKB:Q96CM3}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000250|UniProtKB:Q96CM3}. Nucleus {ECO:0000250|UniProtKB:Q96CM3}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q96CM3}. Note=Mainly localizes to
CC mitochondrion. Localizes to mitochondrial RNA granules, platforms for
CC post-transcriptional RNA modification and ribosome assembly. Also found
CC in nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q96CM3}.
CC -!- SIMILARITY: Belongs to the pseudouridine synthase RluA family.
CC {ECO:0000305}.
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DR EMBL; AK010322; BAB26852.1; -; mRNA.
DR EMBL; AK156574; BAE33761.1; -; mRNA.
DR EMBL; BC061256; AAH61256.1; -; mRNA.
DR CCDS; CCDS22962.1; -.
DR RefSeq; NP_082316.1; NM_028040.2.
DR AlphaFoldDB; Q9CWX4; -.
DR SMR; Q9CWX4; -.
DR BioGRID; 215077; 5.
DR STRING; 10090.ENSMUSP00000034543; -.
DR iPTMnet; Q9CWX4; -.
DR PhosphoSitePlus; Q9CWX4; -.
DR EPD; Q9CWX4; -.
DR MaxQB; Q9CWX4; -.
DR PaxDb; Q9CWX4; -.
DR PeptideAtlas; Q9CWX4; -.
DR PRIDE; Q9CWX4; -.
DR ProteomicsDB; 257057; -.
DR Antibodypedia; 50828; 49 antibodies from 13 providers.
DR DNASU; 71989; -.
DR Ensembl; ENSMUST00000034543; ENSMUSP00000034543; ENSMUSG00000032044.
DR GeneID; 71989; -.
DR KEGG; mmu:71989; -.
DR UCSC; uc009otc.1; mouse.
DR CTD; 84881; -.
DR MGI; MGI:1919239; Rpusd4.
DR VEuPathDB; HostDB:ENSMUSG00000032044; -.
DR eggNOG; KOG1919; Eukaryota.
DR GeneTree; ENSGT00940000158436; -.
DR HOGENOM; CLU_016902_2_1_1; -.
DR InParanoid; Q9CWX4; -.
DR OMA; RMRIAKH; -.
DR OrthoDB; 1378690at2759; -.
DR PhylomeDB; Q9CWX4; -.
DR TreeFam; TF337899; -.
DR BioGRID-ORCS; 71989; 25 hits in 75 CRISPR screens.
DR PRO; PR:Q9CWX4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9CWX4; protein.
DR Bgee; ENSMUSG00000032044; Expressed in secondary oocyte and 270 other tissues.
DR ExpressionAtlas; Q9CWX4; baseline and differential.
DR Genevisible; Q9CWX4; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISO:MGI.
DR GO; GO:1990400; F:mitochondrial ribosomal large subunit rRNA binding; ISO:MGI.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISO:MGI.
DR GO; GO:0000049; F:tRNA binding; ISO:MGI.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0070902; P:mitochondrial tRNA pseudouridine synthesis; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; ISO:MGI.
DR GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd02869; PseudoU_synth_RluA_like; 1.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR006224; PsdUridine_synth_RluC/D_CS.
DR InterPro; IPR006145; PsdUridine_synth_RsuA/RluA.
DR Pfam; PF00849; PseudoU_synth_2; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR PROSITE; PS01129; PSI_RLU; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Isomerase; Mitochondrion; mRNA processing; mRNA splicing;
KW Nucleus; Reference proteome; rRNA processing; Transit peptide;
KW tRNA processing.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..377
FT /note="Pseudouridylate synthase RPUSD4, mitochondrial"
FT /id="PRO_0000300826"
FT ACT_SITE 153
FT /evidence="ECO:0000250|UniProtKB:P0AA39"
SQ SEQUENCE 377 AA; 42407 MW; 4E2234F7457DCC24 CRC64;
MAAPCLRTPG VQLLSMSSRP GRLFTPGSWS FCSSATSSRP LNAQRLAEKL RAQKQEQKAK
EVRVPTNPVQ RRVQELVRFT QQLQRVHPNV LAKELSRRIL HQDNDLVVIN KPYGLPVHGG
PGVQLCISDV LPILAKMLHG HKAEPLHLCH RLDKETTGVM VLAWEKDMAH QVQELFRTRQ
VEKKYWAITV RVPLPSAGVV DIPIKEKEVQ GPQQHHKMTL SPSYRLDNGK MVKVRASRDA
HVAVTQYQVL SSASSSALVE LQPVTGIKHQ LRVHLSFGLD CPILGDHKYS DWTRLAPQKL
SAGTLKKLGL QQSKARYIPL HLHARQLILP ALGSRTEELL LTCKLPHFFA RSLLRLGLDM
PNQDQSRGNK ARHVEAR
