MRPP3_RAT
ID MRPP3_RAT Reviewed; 587 AA.
AC B5DF07;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Mitochondrial ribonuclease P catalytic subunit {ECO:0000250|UniProtKB:O15091};
DE EC=3.1.26.5 {ECO:0000250|UniProtKB:O15091};
DE AltName: Full=Mitochondrial ribonuclease P protein 3 {ECO:0000250|UniProtKB:O15091};
DE Short=Mitochondrial RNase P protein 3 {ECO:0000250|UniProtKB:O15091};
DE Flags: Precursor;
GN Name=Prorp; Synonyms=Mrpp3;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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: Catalytic ribonuclease component of mitochondrial
CC ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and
CC PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends. The
CC presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA
CC molecules in their 5'-ends. {ECO:0000250|UniProtKB:O15091}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of RNA, removing 5'-extranucleotides
CC from tRNA precursor.; EC=3.1.26.5;
CC Evidence={ECO:0000250|UniProtKB:O15091};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O15091};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:O15091};
CC Note=Binds 2 Mg(2+) or Mg(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:O15091};
CC -!- SUBUNIT: Catalytic component of mitochondrial ribonuclease P, a complex
CC composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3.
CC {ECO:0000250|UniProtKB:O15091}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:O15091}.
CC -!- DOMAIN: Displays a distorted and non-productive active site that
CC probably switches to a fully productive state only upon association
CC with TRMT10C/MRPP1, HSD17B10/MRPP2 and pre-tRNA substrate.
CC {ECO:0000250|UniProtKB:O15091}.
CC -!- PTM: Degraded by LONP1 following mitochondrial unfolded protein
CC response, probably leading to inhibit translation in mitochondrion.
CC {ECO:0000250|UniProtKB:O15091}.
CC -!- SIMILARITY: Belongs to the PPR family. P subfamily. {ECO:0000305}.
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DR EMBL; CH473947; EDM03424.1; -; Genomic_DNA.
DR EMBL; BC168878; AAI68878.1; -; mRNA.
DR RefSeq; NP_001100200.1; NM_001106730.2.
DR AlphaFoldDB; B5DF07; -.
DR SMR; B5DF07; -.
DR STRING; 10116.ENSRNOP00000009306; -.
DR PaxDb; B5DF07; -.
DR PeptideAtlas; B5DF07; -.
DR PRIDE; B5DF07; -.
DR Ensembl; ENSRNOT00000009304; ENSRNOP00000009306; ENSRNOG00000007043.
DR GeneID; 299050; -.
DR KEGG; rno:299050; -.
DR UCSC; RGD:1305089; rat.
DR CTD; 9692; -.
DR RGD; 1305089; RGD1305089.
DR eggNOG; ENOG502QRKG; Eukaryota.
DR GeneTree; ENSGT00390000002201; -.
DR HOGENOM; CLU_033070_1_0_1; -.
DR InParanoid; B5DF07; -.
DR OMA; TNNLSHD; -.
DR OrthoDB; 1247650at2759; -.
DR PhylomeDB; B5DF07; -.
DR TreeFam; TF324726; -.
DR PRO; PR:B5DF07; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000007043; Expressed in testis and 20 other tissues.
DR Genevisible; B5DF07; RN.
DR GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR GO; GO:0030678; C:mitochondrial ribonuclease P complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004526; F:ribonuclease P activity; ISS:UniProtKB.
DR GO; GO:0097745; P:mitochondrial tRNA 5'-end processing; ISS:UniProtKB.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IBA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR033495; MRPP3.
DR InterPro; IPR031595; PRORP_C.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13547:SF1; PTHR13547:SF1; 1.
DR Pfam; PF16953; PRORP; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Manganese; Metal-binding; Mitochondrion; Nuclease;
KW Reference proteome; Transit peptide; tRNA processing; Zinc.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..587
FT /note="Mitochondrial ribonuclease P catalytic subunit"
FT /id="PRO_0000360398"
FT DOMAIN 342..578
FT /note="PRORP"
FT REGION 94..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 351
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 409
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 479
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 578
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
SQ SEQUENCE 587 AA; 67008 MW; F065F7875751BC08 CRC64;
MTFYLSGFRS FLKLWKSNPY FELGPATSSA SFFLGVHCVI GNQQRWFSVK PTTPPNSKIL
NLLVTKARTL KKGNDSNKQA SSGPHYFAAG EAKKRSHLSG NPQNQGHTLP VKSTVQLPTK
PLNSEEWDKL KEDFKGKASF EDFVISQMTR SCSSVDVAKS LLAWVAAKNN GIVGYNLLVK
YLYLCVFHKQ TSEVIDVYEI MKAKYKSLES GGYTLLIRGL IHSDRWREAL LLLEDIKKVM
VPSKKNYGDC IQGALLHQDV NVAWSLYQEL VGHNLIPLLE TLKAFFDHGK DMNDDQYSNQ
LLDILLYLRN NQLYPGESFA HSIKTWFESI PGRQWKGQFT TIQKSGQCSS CGRAIESIHL
SPEEYEFLKE TIMRDVIDGG DQYKKTTPQE LKRFERFVKS CPPFDIVIDG LNVAKMFPKG
RESQNLLGIV SQLAQQNLQL LVLGRKHMLR PSSQWRKDEM EQVRKQAHCF FADNISEDDP
FLLYATLNSG SHCKFITKDL LRDHKACLPD ARAQRLFFKW QQGHQLAITK GFLKSKLTFQ
HILSYDTVVQ TTGDTWHIPY DEDLVPRSSC EVPTKWLCLQ RKTPAPC
