RUSD4_BOVIN
ID RUSD4_BOVIN Reviewed; 377 AA.
AC Q5E9Z1; A7YWI2; Q0V8H4; Q1JP71; Q1JPL3; Q58D36; Q58DF5; Q5E9Z6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
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:0000250|UniProtKB:Q96CM3};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46489.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAX46608.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BT020717; AAX08734.1; -; mRNA.
DR EMBL; BT020773; AAX08790.1; -; mRNA.
DR EMBL; BT020778; AAX08795.1; -; mRNA.
DR EMBL; BT021642; AAX46489.1; ALT_FRAME; mRNA.
DR EMBL; BT021761; AAX46608.1; ALT_FRAME; mRNA.
DR EMBL; BT025340; ABF57296.1; -; mRNA.
DR EMBL; BT025483; ABF57439.1; -; mRNA.
DR EMBL; BT026244; ABG67083.1; -; mRNA.
DR EMBL; BC134590; AAI34591.1; -; mRNA.
DR RefSeq; NP_001015616.1; NM_001015616.1.
DR AlphaFoldDB; Q5E9Z1; -.
DR SMR; Q5E9Z1; -.
DR STRING; 9913.ENSBTAP00000027843; -.
DR PaxDb; Q5E9Z1; -.
DR PRIDE; Q5E9Z1; -.
DR GeneID; 516934; -.
DR KEGG; bta:516934; -.
DR CTD; 84881; -.
DR eggNOG; KOG1919; Eukaryota.
DR HOGENOM; CLU_016902_2_1_1; -.
DR InParanoid; Q5E9Z1; -.
DR OrthoDB; 1378690at2759; -.
DR TreeFam; TF337899; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; 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 GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; 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..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..377
FT /note="Pseudouridylate synthase RPUSD4, mitochondrial"
FT /id="PRO_0000300824"
FT REGION 51..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /evidence="ECO:0000250|UniProtKB:P0AA39"
FT CONFLICT 8
FT /note="V -> A (in Ref. 1; AAX46489/ABF57296)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="Q -> R (in Ref. 1; AAX46489/AAX46608/ABG67083/
FT AAX08790 and 2; AAI34591)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="Q -> R (in Ref. 1; AAX08790 and 2; AAI34591)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 377 AA; 42000 MW; 03F892FF05CC737F CRC64;
MVAPGCSVPG LWVRGFGQCL GSLFTLFSKP LCSAAAAASQ PLDAQRLAER LRAQKQQQKT
KEPAPTNPVQ RRVRELVRFT EQLQRVHPNV LAKALSRGIV HQDKELVVIN KPYGLPVHGG
PGVKLCISDV LPVLAKILHG PKAKPLHLCH RLDKETTGVM VLAWEKEVAH QVQELFRTRQ
VTKKYWAITV RVPVPEAGVV DIPIVEKEAQ GQQHHHKMTL SPSYRMDDGK MVRVRSSRNA
QLAVTQYQVL SSSLSAALLE LQPITGIKHQ LRVHMSFGLD CPILGDHKYS DWNRLAPQKL
SAGILKKLGL QQSKARHLPL HLHACQLTLP ALQPQKEELT LLCRPPRYFV NSLRRLGLKM
PSRDHSADEE AAQPGAQ
