MRPP3_MACFA
ID MRPP3_MACFA Reviewed; 581 AA.
AC Q4R366; G7PA31;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 2.
DT 03-AUG-2022, entry version 51.
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; ORFNames=QtsA-19281 {ECO:0000303|Ref.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4;
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q4R366-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q4R366-2; Sequence=VSP_059277, VSP_059278;
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; AB179401; BAE02452.1; -; mRNA.
DR EMBL; CM001282; EHH63556.1; -; Genomic_DNA.
DR RefSeq; XP_005561126.1; XM_005561069.2. [Q4R366-1]
DR RefSeq; XP_005561127.1; XM_005561070.2. [Q4R366-1]
DR RefSeq; XP_005561128.1; XM_005561071.2. [Q4R366-1]
DR RefSeq; XP_015309193.1; XM_015453707.1. [Q4R366-1]
DR AlphaFoldDB; Q4R366; -.
DR SMR; Q4R366; -.
DR STRING; 9541.XP_005561126.1; -.
DR GeneID; 101925777; -.
DR KEGG; mcf:101925777; -.
DR CTD; 9692; -.
DR VEuPathDB; HostDB:ENSMFAG00000001453; -.
DR eggNOG; ENOG502QRKG; Eukaryota.
DR OMA; TNNLSHD; -.
DR OrthoDB; 1247650at2759; -.
DR Proteomes; UP000009130; Chromosome 7.
DR Proteomes; UP000233100; Chromosome 7.
DR GO; GO:0030678; C:mitochondrial ribonuclease P complex; ISS:UniProtKB.
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 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 Alternative splicing; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Mitochondrion; Nuclease; Reference proteome; Transit peptide;
KW tRNA processing; Zinc.
FT TRANSIT 1..46
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 47..581
FT /note="Mitochondrial ribonuclease P catalytic subunit"
FT /id="PRO_0000360396"
FT DOMAIN 340..576
FT /note="PRORP"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 346
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 349
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 407
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 476
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 477
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 497
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 555
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 576
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT VAR_SEQ 473
FT /note="I -> M (in isoform 2)"
FT /id="VSP_059277"
FT VAR_SEQ 474..581
FT /note="Missing (in isoform 2)"
FT /id="VSP_059278"
FT CONFLICT 369
FT /note="R -> G (in Ref. 1; BAE02452)"
SQ SEQUENCE 581 AA; 66785 MW; 1904E543B16CBB1D CRC64;
MTFYLFGIRS FPKLWKSNPY LGLGPGHSYV SLFLSDSCGI RSQQRLFSLK TMSPQNTKAT
NLIAKARYLR KEEGSNKQVS SVPHFFSAGA AKKRSQMNPQ SKDHALPSVR NTIQLPTQPL
NSEEWDKLKA DFKGKTSFER FIISQMAHSH SSVDVAKSLL AWVAAKNNGI VSYDLLVGYL
YLCVFHMQTS EVIDVFEIMK TRYKTLEPGG YSLLIQGLIH SDRWRESLLL LEDIKKVITP
SKKNYNDCIQ GALLHQDINT AWNLYQELLG HDFVPMLETL KAFFDFGKDI KDDNYSNKLL
DILSYLRNNQ LYPGESFAHS IKTWFESVPG KQWKGQFTTV QKSGQCLGCG KTIESIQLSP
EEYEFLKGRI MRDVIDGGDQ YKKTTPQELK RFENFVKSCP PFDIVIDGLN VAKMFPKARE
SQVLLNVVSQ LAKQNLRLLV LGRKHMLRQS FQWRKDEMAE VQKQASCFFA DNISKDDPFL
LYATLHSGNH CRFITKDLMR DHKACLPDAK TQRLFFKWQQ GHQLAIINGF PGSKLTFQHI
LSYDTVVQTT GDSWHIPYDE DVVERYSYEV PTKWLCLHQK T
