RUSD4_RAT
ID RUSD4_RAT Reviewed; 377 AA.
AC Q4QQT0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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|RGD:1311268};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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; BC098023; AAH98023.1; -; mRNA.
DR RefSeq; NP_001020455.1; NM_001025284.1.
DR AlphaFoldDB; Q4QQT0; -.
DR SMR; Q4QQT0; -.
DR STRING; 10116.ENSRNOP00000015670; -.
DR PaxDb; Q4QQT0; -.
DR PRIDE; Q4QQT0; -.
DR Ensembl; ENSRNOT00000015670; ENSRNOP00000015670; ENSRNOG00000011567.
DR GeneID; 315550; -.
DR KEGG; rno:315550; -.
DR UCSC; RGD:1311268; rat.
DR CTD; 84881; -.
DR RGD; 1311268; Rpusd4.
DR eggNOG; KOG1919; Eukaryota.
DR GeneTree; ENSGT00940000158436; -.
DR HOGENOM; CLU_016902_2_1_1; -.
DR InParanoid; Q4QQT0; -.
DR OMA; RMRIAKH; -.
DR OrthoDB; 1378690at2759; -.
DR PhylomeDB; Q4QQT0; -.
DR TreeFam; TF337899; -.
DR PRO; PR:Q4QQT0; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000011567; Expressed in quadriceps femoris and 20 other tissues.
DR Genevisible; Q4QQT0; RN.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0035770; C:ribonucleoprotein granule; ISO:RGD.
DR GO; GO:1990400; F:mitochondrial ribosomal large subunit rRNA binding; ISO:RGD.
DR GO; GO:0009982; F:pseudouridine synthase activity; ISO:RGD.
DR GO; GO:0000049; F:tRNA binding; ISO:RGD.
DR GO; GO:0000455; P:enzyme-directed rRNA pseudouridine synthesis; IBA:GO_Central.
DR GO; GO:0070902; P:mitochondrial tRNA pseudouridine synthesis; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IEA:Ensembl.
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..35
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 36..377
FT /note="Pseudouridylate synthase RPUSD4, mitochondrial"
FT /id="PRO_0000300827"
FT ACT_SITE 153
FT /evidence="ECO:0000250|UniProtKB:P0AA39"
SQ SEQUENCE 377 AA; 42595 MW; BE327163AE77C30A CRC64;
MAAPLLGSPG LQVLSMSSRT GKLFTPSSRS FCSRATSSRP LNAQRLAEKL RAQKQEQKTK
EMRVPTNPVQ RRVQELVRFT QQLQRVHPNV LAKELSRRIL HQDKDLVVIN KPYGLPVHGG
PGVQLCISDV LPILAKMLHG HKAEPLHLCH RLDKETTGVM VLAWEKDMAH QVQELFRTRQ
VEKKYWAITV RVPLPSAGVV DIPIMEKEVA GQQQHHKMTL RPSYRMDNGK MVKVRASRDA
HVAVTQYQVL SSTPSSALVE LQPVTGIKHQ LRVHLAFGLD CPILGDHKYS DWNRLAPQKL
SAGTLKKLGL QQSKARYIPL HLHARQLILP ALGSRTEELL LACKLPHFFA RSLRRLGLDM
PNEDQSRSHE ARHVEAR
