UniProtKB - O15091 (MRPP3_HUMAN)
Mitochondrial ribonuclease P catalytic subunit
PRORP
Functioni
Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends (PubMed:18984158, PubMed:25953853).
The presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA molecules in their 5'-ends (PubMed:25953853).
2 PublicationsCatalytic activityi
- Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.1 Publication EC:3.1.26.5
Cofactori
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 348 | ZincCombined sources1 Publication | 1 | |
Metal bindingi | 351 | ZincCombined sources1 Publication | 1 | |
Metal bindingi | 409 | Magnesium 1; catalytic1 Publication | 1 | |
Metal bindingi | 478 | Magnesium 1; catalytic1 Publication | 1 | |
Metal bindingi | 479 | Magnesium 2; catalytic1 Publication | 1 | |
Metal bindingi | 499 | Magnesium 2; catalytic1 Publication | 1 | |
Metal bindingi | 557 | Zinc; via tele nitrogenCombined sources1 Publication | 1 | |
Metal bindingi | 578 | ZincCombined sources1 Publication | 1 |
GO - Molecular functioni
- metal ion binding Source: UniProtKB-KW
- ribonuclease P activity Source: UniProtKB
GO - Biological processi
- mitochondrial tRNA 5'-end processing Source: UniProtKB
- tRNA 5'-leader removal Source: GO_Central
Keywordsi
Molecular function | Hydrolase, Nuclease |
Biological process | tRNA processing |
Ligand | Magnesium, Manganese, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.1.26.5, 2681 |
PathwayCommonsi | O15091 |
Reactomei | R-HSA-6785470, tRNA processing in the mitochondrion R-HSA-6787450, tRNA modification in the mitochondrion R-HSA-8868766, rRNA processing in the mitochondrion |
SignaLinki | O15091 |
Names & Taxonomyi
Protein namesi | Recommended name: Mitochondrial ribonuclease P catalytic subunit (EC:3.1.26.51 Publication)Alternative name(s): Mitochondrial ribonuclease P protein 31 Publication Short name: Mitochondrial RNase P protein 31 Publication Protein only RNase P catalytic subunitImported |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:19958, PRORP |
MIMi | 609947, gene |
neXtProti | NX_O15091 |
VEuPathDBi | HostDB:ENSG00000100890 |
Subcellular locationi
Mitochondrion
- Mitochondrion 1 Publication
Mitochondrion
- mitochondrial matrix Source: Reactome
- mitochondrial ribonuclease P complex Source: UniProtKB
- mitochondrion Source: HPA
Nucleus
- nucleoplasm Source: HPA
Keywords - Cellular componenti
MitochondrionPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 409 | D → N: Abolishes ribonuclease activity. 1 Publication | 1 | |
Mutagenesisi | 478 | D → N: Abolishes ribonuclease activity. 1 Publication | 1 | |
Mutagenesisi | 479 | D → N: Abolishes ribonuclease activity. 1 Publication | 1 | |
Mutagenesisi | 480 | P → G: Does not affect ribonuclease activity. 1 Publication | 1 | |
Mutagenesisi | 498 | R → D or N: Does not affect ribonuclease activity. 1 Publication | 1 | |
Mutagenesisi | 499 | D → N: Abolishes ribonuclease activity. 1 Publication | 1 | |
Mutagenesisi | 569 | S → A: Does not affect ribonuclease activity. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 9692 |
OpenTargetsi | ENSG00000100890 |
PharmGKBi | PA134879499 |
Miscellaneous databases
Pharosi | O15091, Tbio |
Genetic variation databases
BioMutai | KIAA0391 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Transit peptidei | 1 – 45 | MitochondrionSequence analysisAdd BLAST | 45 | |
ChainiPRO_0000050749 | 46 – 583 | Mitochondrial ribonuclease P catalytic subunitAdd BLAST | 538 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 98 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
PhosphoproteinProteomic databases
EPDi | O15091 |
jPOSTi | O15091 |
MassIVEi | O15091 |
MaxQBi | O15091 |
PaxDbi | O15091 |
PeptideAtlasi | O15091 |
PRIDEi | O15091 |
ProteomicsDBi | 48444 [O15091-1] 48445 [O15091-2] 48446 [O15091-3] 48447 [O15091-4] |
PTM databases
iPTMneti | O15091 |
PhosphoSitePlusi | O15091 |
Expressioni
Inductioni
Gene expression databases
Bgeei | ENSG00000100890, Expressed in tonsil and 132 other tissues |
ExpressionAtlasi | O15091, baseline and differential |
Genevisiblei | O15091, HS |
Organism-specific databases
HPAi | ENSG00000100890, Low tissue specificity |
Interactioni
Subunit structurei
Catalytic component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3 (PubMed:18984158).
1 PublicationProtein-protein interaction databases
BioGRIDi | 115044, 160 interactors |
ComplexPortali | CPX-6155, Mitochondrial ribonuclease P complex |
CORUMi | O15091 |
IntActi | O15091, 22 interactors |
MINTi | O15091 |
STRINGi | 9606.ENSP00000440915 |
Miscellaneous databases
RNActi | O15091, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | O15091 |
SMRi | O15091 |
ModBasei | Search... |
PDBe-KBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 342 – 578 | PRORPAdd BLAST | 237 |
Domaini
Sequence similaritiesi
Keywords - Domaini
Transit peptidePhylogenomic databases
eggNOGi | ENOG502QRKG, Eukaryota |
GeneTreei | ENSGT00390000002201 |
HOGENOMi | CLU_033070_1_0_1 |
InParanoidi | O15091 |
OMAi | TNNLSHD |
OrthoDBi | 1247650at2759 |
PhylomeDBi | O15091 |
TreeFami | TF324726 |
Family and domain databases
Gene3Di | 1.25.40.10, 1 hit |
InterProi | View protein in InterPro IPR033495, MRPP3 IPR031595, PRORP_C IPR011990, TPR-like_helical_dom_sf |
PANTHERi | PTHR13547:SF1, PTHR13547:SF1, 1 hit |
Pfami | View protein in Pfam PF16953, PRORP, 1 hit |
s (4+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 4 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 4 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MTFYLFGIRS FPKLWKSPYL GLGPGHSYVS LFLADRCGIR NQQRLFSLKT
60 70 80 90 100
MSPQNTKATN LIAKARYLRK DEGSNKQVYS VPHFFLAGAA KERSQMNSQT
110 120 130 140 150
EDHALAPVRN TIQLPTQPLN SEEWDKLKED LKENTGKTSF ESWIISQMAG
160 170 180 190 200
CHSSIDVAKS LLAWVAAKNN GIVSYDLLVK YLYLCVFHMQ TSEVIDVFEI
210 220 230 240 250
MKARYKTLEP RGYSLLIRGL IHSDRWREAL LLLEDIKKVI TPSKKNYNDC
260 270 280 290 300
IQGALLHQDV NTAWNLYQEL LGHDIVPMLE TLKAFFDFGK DIKDDNYSNK
310 320 330 340 350
LLDILSYLRN NQLYPGESFA HSIKTWFESV PGKQWKGQFT TVRKSGQCSG
360 370 380 390 400
CGKTIESIQL SPEEYECLKG KIMRDVIDGG DQYRKTTPQE LKRFENFIKS
410 420 430 440 450
RPPFDVVIDG LNVAKMFPKV RESQLLLNVV SQLAKRNLRL LVLGRKHMLR
460 470 480 490 500
RSSQWSRDEM EEVQKQASCF FADDISEDDP FLLYATLHSG NHCRFITRDL
510 520 530 540 550
MRDHKACLPD AKTQRLFFKW QQGHQLAIVN RFPGSKLTFQ RILSYDTVVQ
560 570 580
TTGDSWHIPY DEDLVERCSC EVPTKWLCLH QKT
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A0A0MTQ0 | A0A0A0MTQ0_HUMAN | Mitochondrial ribonuclease P cataly... | PRORP | 185 | Annotation score: | ||
S4R3S1 | S4R3S1_HUMAN | Mitochondrial ribonuclease P cataly... | PRORP | 19 | Annotation score: | ||
S4R416 | S4R416_HUMAN | Mitochondrial ribonuclease P cataly... | PRORP | 34 | Annotation score: | ||
S4R3T4 | S4R3T4_HUMAN | Mitochondrial ribonuclease P cataly... | PRORP | 23 | Annotation score: |
Sequence cautioni
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 315 | P → L in BAG63351 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 453 | S → F in BAG64540 (PubMed:14702039).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_054212 | 437 | N → S2 PublicationsCorresponds to variant dbSNP:rs11156878Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_036201 | 1 – 372 | Missing in isoform 3. 2 PublicationsAdd BLAST | 372 | |
Alternative sequenceiVSP_036202 | 1 – 95 | Missing in isoform 4. 1 PublicationAdd BLAST | 95 | |
Alternative sequenceiVSP_036203 | 329 – 344 | Missing in isoform 2. 2 PublicationsAdd BLAST | 16 |
Sequence databases
Genome annotation databases
Ensembli | ENST00000250377.11; ENSP00000250377.8; ENSG00000100890.16 [O15091-2] ENST00000321130.14; ENSP00000324697.9; ENSG00000100890.16 [O15091-3] ENST00000534898.9; ENSP00000440915.2; ENSG00000100890.16 ENST00000603544.5; ENSP00000473856.1; ENSG00000100890.16 [O15091-2] ENST00000604948.5; ENSP00000474620.1; ENSG00000100890.16 [O15091-4] ENST00000605870.5; ENSP00000474299.1; ENSG00000100890.16 [O15091-3] |
GeneIDi | 9692 |
KEGGi | hsa:9692 |
MANE-Selecti | ENST00000534898.9; ENSP00000440915.2; NM_014672.4; NP_055487.2 |
UCSCi | uc001wsy.3, human [O15091-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
4ROU | X-ray | 2.71 | A/B | 274-583 | [»] | |
4XGL | X-ray | 1.80 | A | 207-583 | [»] | |
4XGM | X-ray | 1.98 | A | 207-583 | [»] | |
7ONU | electron microscopy | 3.00 | E | 46-583 | [»] | |
AlphaFoldDBi | O15091 | |||||
SMRi | O15091 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 115044, 160 interactors |
ComplexPortali | CPX-6155, Mitochondrial ribonuclease P complex |
CORUMi | O15091 |
IntActi | O15091, 22 interactors |
MINTi | O15091 |
STRINGi | 9606.ENSP00000440915 |
PTM databases
iPTMneti | O15091 |
PhosphoSitePlusi | O15091 |
Genetic variation databases
BioMutai | KIAA0391 |
Proteomic databases
EPDi | O15091 |
jPOSTi | O15091 |
MassIVEi | O15091 |
MaxQBi | O15091 |
PaxDbi | O15091 |
PeptideAtlasi | O15091 |
PRIDEi | O15091 |
ProteomicsDBi | 48444 [O15091-1] 48445 [O15091-2] 48446 [O15091-3] 48447 [O15091-4] |
Protocols and materials databases
Antibodypediai | 23191, 131 antibodies from 23 providers |
DNASUi | 9692 |
Genome annotation databases
Organism-specific databases
CTDi | 9692 |
DisGeNETi | 9692 |
GeneCardsi | PRORP |
HGNCi | HGNC:19958, PRORP |
HPAi | ENSG00000100890, Low tissue specificity |
MIMi | 609947, gene |
neXtProti | NX_O15091 |
OpenTargetsi | ENSG00000100890 |
PharmGKBi | PA134879499 |
VEuPathDBi | HostDB:ENSG00000100890 |
HUGEi | Search... |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | ENOG502QRKG, Eukaryota |
GeneTreei | ENSGT00390000002201 |
HOGENOMi | CLU_033070_1_0_1 |
InParanoidi | O15091 |
OMAi | TNNLSHD |
OrthoDBi | 1247650at2759 |
PhylomeDBi | O15091 |
TreeFami | TF324726 |
Enzyme and pathway databases
BRENDAi | 3.1.26.5, 2681 |
PathwayCommonsi | O15091 |
Reactomei | R-HSA-6785470, tRNA processing in the mitochondrion R-HSA-6787450, tRNA modification in the mitochondrion R-HSA-8868766, rRNA processing in the mitochondrion |
SignaLinki | O15091 |
Miscellaneous databases
BioGRID-ORCSi | 9692, 318 hits in 1081 CRISPR screens |
ChiTaRSi | KIAA0391, human |
GenomeRNAii | 9692 |
Pharosi | O15091, Tbio |
PROi | PR:O15091 |
RNActi | O15091, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000100890, Expressed in tonsil and 132 other tissues |
ExpressionAtlasi | O15091, baseline and differential |
Genevisiblei | O15091, HS |
Family and domain databases
Gene3Di | 1.25.40.10, 1 hit |
InterProi | View protein in InterPro IPR033495, MRPP3 IPR031595, PRORP_C IPR011990, TPR-like_helical_dom_sf |
PANTHERi | PTHR13547:SF1, PTHR13547:SF1, 1 hit |
Pfami | View protein in Pfam PF16953, PRORP, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | MRPP3_HUMAN | |
Accessioni | O15091Primary (citable) accession number: O15091 Secondary accession number(s): B4DXD9 Q8N5L5 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 15, 1998 |
Last sequence update: | January 20, 2009 | |
Last modified: | May 25, 2022 | |
This is version 159 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families