MRPP3_MOUSE
ID MRPP3_MOUSE Reviewed; 584 AA.
AC Q8JZY4; Q6A076; Q8BSN8; Q9CTH1; Q9D7W9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=Kiaa0391, Mrpp3 {ECO:0000250|UniProtKB:O15091};
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; TISSUE=Bone marrow, Embryo, Forelimb, and Stomach;
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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary gland;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 327-584.
RC TISSUE=Splenocyte;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
CC -!- FUNCTION: Catalytic ribonuclease component of mitochondrial
CC ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and
CC PRORP, which cleaves tRNA molecules in their 5'-ends. The presence of
CC TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA molecules in
CC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB25874.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD32220.1; Type=Miscellaneous discrepancy; Note=Partial sequence.; Evidence={ECO:0000305};
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DR EMBL; AK003589; BAB22879.1; -; mRNA.
DR EMBL; AK008749; BAB25874.1; ALT_INIT; mRNA.
DR EMBL; AK031144; BAC27278.1; -; mRNA.
DR EMBL; AK151976; BAE30844.1; -; mRNA.
DR EMBL; AK152028; BAE30887.1; -; mRNA.
DR EMBL; CH466526; EDL36732.1; -; Genomic_DNA.
DR EMBL; BC034876; AAH34876.1; -; mRNA.
DR EMBL; AK172942; BAD32220.1; ALT_SEQ; mRNA.
DR CCDS; CCDS49068.1; -.
DR RefSeq; NP_079649.1; NM_025373.1.
DR AlphaFoldDB; Q8JZY4; -.
DR SMR; Q8JZY4; -.
DR BioGRID; 211239; 7.
DR STRING; 10090.ENSMUSP00000021411; -.
DR PhosphoSitePlus; Q8JZY4; -.
DR EPD; Q8JZY4; -.
DR MaxQB; Q8JZY4; -.
DR PaxDb; Q8JZY4; -.
DR PeptideAtlas; Q8JZY4; -.
DR PRIDE; Q8JZY4; -.
DR ProteomicsDB; 291415; -.
DR Ensembl; ENSMUST00000021411; ENSMUSP00000021411; ENSMUSG00000021023.
DR Ensembl; ENSMUST00000184766; ENSMUSP00000139204; ENSMUSG00000021023.
DR GeneID; 66132; -.
DR KEGG; mmu:66132; -.
DR UCSC; uc007noo.2; mouse.
DR CTD; 9692; -.
DR MGI; MGI:1913382; Prorp.
DR VEuPathDB; HostDB:ENSMUSG00000021023; -.
DR eggNOG; ENOG502QRKG; Eukaryota.
DR GeneTree; ENSGT00390000002201; -.
DR InParanoid; Q8JZY4; -.
DR OMA; TNNLSHD; -.
DR OrthoDB; 1247650at2759; -.
DR PhylomeDB; Q8JZY4; -.
DR TreeFam; TF324726; -.
DR BioGRID-ORCS; 66132; 20 hits in 74 CRISPR screens.
DR ChiTaRS; Prorp; mouse.
DR PRO; PR:Q8JZY4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8JZY4; protein.
DR Bgee; ENSMUSG00000021023; Expressed in metanephric ureteric bud and 164 other tissues.
DR ExpressionAtlas; Q8JZY4; baseline and differential.
DR Genevisible; Q8JZY4; MM.
DR GO; GO:0042645; C:mitochondrial nucleoid; IDA:MGI.
DR GO; GO:0030678; C:mitochondrial ribonuclease P complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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..43
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 44..584
FT /note="Mitochondrial ribonuclease P catalytic subunit"
FT /id="PRO_0000360397"
FT DOMAIN 339..575
FT /note="PRORP"
FT BINDING 345
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 406
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 475
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="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 496
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 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O15091"
FT CONFLICT 430
FT /note="L -> V (in Ref. 1; BAC27278)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 584 AA; 66857 MW; BB68EF585649A3BD CRC64;
MTFYLSGFRS IPKLWKSNPY FELGPATSST PFFLCAIGNQ QRWFSVKPTT PPNSKALNLL
DTKARTHRKG NDNNGQVSSD PHYFAAGAAK KRSHIGANPQ NQGHALPVRS SVQLPTKPLN
SAEWDKLKED FKGKASFEDF IISQMARNCC SVDVAKSLLA WVAAKNNGIV GYNLLVKYLY
LCVFHKQTSE VIDVYEIMKA KYKSLESGGY TLLIRGLIHS DRWRESLLLL EDIKKVMVPS
KKNYGDCIQG ALLHQDVNTA WNLYQELIGH NLIPPLETLK AFFDYGKDIN DDHYSDKLLD
ILLYLRNNQL YPGESFAHSI KTWFESIPGR QWKGQFTTIQ KSGQCSGCGR TIEPIHLSPE
EYEFLKEKIM RDVIDGGDQY KKTTPQELKR FESFVNSCPP FDIVIDGLNV AKMFPKGRES
QNLLGVVSQL AQQNLQLLVL GRKHMLRPSS QWRKEEMEQV RKQAHCFFAD NISEDDPFLL
YATLNSGNHC KFITKDLLRD HKACLPDART QRLFFKWQQG HQLAIMKGFQ KSKLTFQHIL
SYDTVVQRTG DSWHIPYDED LVQRSSCEVP TKWLCLQRKT PDPC
