O15091 · MRPP3_HUMAN
- ProteinMitochondrial ribonuclease P catalytic subunit
- GenePRORP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids583 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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, PubMed:34715011).
The presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA molecules in their 5'-ends (PubMed:25953853).
The presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA molecules in their 5'-ends (PubMed:25953853).
Catalytic activity
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Binds 2 Mg2+ or Mg2+ ions per subunit.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 348 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 351 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 409 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 478 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 479 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 499 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 557 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 578 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrial nucleoid | |
Cellular Component | mitochondrial ribonuclease P complex | |
Cellular Component | mitochondrion | |
Cellular Component | nucleoplasm | |
Molecular Function | metal ion binding | |
Molecular Function | ribonuclease P activity | |
Biological Process | mitochondrial tRNA 5'-end processing | |
Biological Process | tRNA 5'-leader removal |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMitochondrial ribonuclease P catalytic subunit
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO15091
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Combined oxidative phosphorylation deficiency 54 (COXPD54)
- Note
- DescriptionAn autosomal recessive, multisystem disorder with highly variable manifestations resulting from defective mitochondrial transcription and translation. Clinical features include early-onset sensorineural hearing loss, sometimes associated with global developmental delay or primary ovarian failure, peripheral hypertonia, seizures, muscle weakness, behavioral abnormalities, and leukoencephalopathy on brain imaging. Serum lactate may or may not be elevated.
- See alsoMIM:619737
Natural variants in COXPD54
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086903 | 412 | N>S | in COXPD54; results in decreased mitochondrial tRNA 5'-end processing as shown by assays with mitochondrial ribonuclease P complex reconstituted in vitro; dbSNP:rs148259590 | |
VAR_086904 | 421 | R>C | in COXPD54; uncertain significance; dbSNP:rs147065101 | |
VAR_086905 | 434 | A>D | in COXPD54; uncertain significance; dbSNP:rs144536804 | |
VAR_086906 | 445 | R>Q | in COXPD54; results in decreased mitochondrial tRNA 5'-end processing as shown by assays with mitochondrial ribonuclease P complex reconstituted in vitro; dbSNP:rs777185638 | |
VAR_086907 | 485 | A>V | in COXPD54; decreased protein levels in homozygous patient cells; impaired mitochondrial RNA processing in homozygous patient cells; dbSNP:rs1169927428 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 409 | Abolishes ribonuclease activity. | ||||
Sequence: D → N | ||||||
Natural variant | VAR_086903 | 412 | in COXPD54; results in decreased mitochondrial tRNA 5'-end processing as shown by assays with mitochondrial ribonuclease P complex reconstituted in vitro; dbSNP:rs148259590 | |||
Sequence: N → S | ||||||
Natural variant | VAR_086904 | 421 | in COXPD54; uncertain significance; dbSNP:rs147065101 | |||
Sequence: R → C | ||||||
Natural variant | VAR_086905 | 434 | in COXPD54; uncertain significance; dbSNP:rs144536804 | |||
Sequence: A → D | ||||||
Natural variant | VAR_054212 | 437 | in dbSNP:rs11156878 | |||
Sequence: N → S | ||||||
Natural variant | VAR_086906 | 445 | in COXPD54; results in decreased mitochondrial tRNA 5'-end processing as shown by assays with mitochondrial ribonuclease P complex reconstituted in vitro; dbSNP:rs777185638 | |||
Sequence: R → Q | ||||||
Mutagenesis | 478 | Abolishes ribonuclease activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 479 | Abolishes ribonuclease activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 480 | Does not affect ribonuclease activity. | ||||
Sequence: P → G | ||||||
Natural variant | VAR_086907 | 485 | in COXPD54; decreased protein levels in homozygous patient cells; impaired mitochondrial RNA processing in homozygous patient cells; dbSNP:rs1169927428 | |||
Sequence: A → V | ||||||
Mutagenesis | 498 | Does not affect ribonuclease activity. | ||||
Sequence: R → D or N | ||||||
Mutagenesis | 499 | Abolishes ribonuclease activity. | ||||
Sequence: D → N | ||||||
Mutagenesis | 569 | Does not affect ribonuclease activity. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 581 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-45 | UniProt | Mitochondrion | ||||
Sequence: MTFYLFGIRSFPKLWKSPYLGLGPGHSYVSLFLADRCGIRNQQRL | |||||||
Chain | PRO_0000050749 | 46-583 | UniProt | Mitochondrial ribonuclease P catalytic subunit | |||
Sequence: FSLKTMSPQNTKATNLIAKARYLRKDEGSNKQVYSVPHFFLAGAAKERSQMNSQTEDHALAPVRNTIQLPTQPLNSEEWDKLKEDLKENTGKTSFESWIISQMAGCHSSIDVAKSLLAWVAAKNNGIVSYDLLVKYLYLCVFHMQTSEVIDVFEIMKARYKTLEPRGYSLLIRGLIHSDRWREALLLLEDIKKVITPSKKNYNDCIQGALLHQDVNTAWNLYQELLGHDIVPMLETLKAFFDFGKDIKDDNYSNKLLDILSYLRNNQLYPGESFAHSIKTWFESVPGKQWKGQFTTVRKSGQCSGCGKTIESIQLSPEEYECLKGKIMRDVIDGGDQYRKTTPQELKRFENFIKSRPPFDVVIDGLNVAKMFPKVRESQLLLNVVSQLAKRNLRLLVLGRKHMLRRSSQWSRDEMEEVQKQASCFFADDISEDDPFLLYATLHSGNHCRFITRDLMRDHKACLPDAKTQRLFFKWQQGHQLAIVNRFPGSKLTFQRILSYDTVVQTTGDSWHIPYDEDLVERCSCEVPTKWLCLHQKT | |||||||
Modified residue (large scale data) | 94 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 98 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 98 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Degraded by LONP1 following mitochondrial unfolded protein response, probably leading to inhibit translation in mitochondrion.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
Down-regulated following mitochondrial unfolded protein response.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Catalytic component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3 (PubMed:18984158).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 342-578 | PRORP | ||||
Sequence: VRKSGQCSGCGKTIESIQLSPEEYECLKGKIMRDVIDGGDQYRKTTPQELKRFENFIKSRPPFDVVIDGLNVAKMFPKVRESQLLLNVVSQLAKRNLRLLVLGRKHMLRRSSQWSRDEMEEVQKQASCFFADDISEDDPFLLYATLHSGNHCRFITRDLMRDHKACLPDAKTQRLFFKWQQGHQLAIVNRFPGSKLTFQRILSYDTVVQTTGDSWHIPYDEDLVERCSCEVPTKWLC |
Domain
Displays a distorted and non-productive active site that probably switches to a fully productive state only upon association with TRMT10C/MRPP1, HSD17B10/MRPP2 and pre-tRNA substrate.
Sequence similarities
Belongs to the PPR family. P subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 4 isoforms produced by Alternative splicing.
O15091-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length583
- Mass (Da)67,315
- Last updated2009-01-20 v2
- Checksum6AB17E7E8820D818
O15091-2
- Name2
- Differences from canonical
- 329-344: Missing
O15091-3
- Name3
- Differences from canonical
- 1-372: Missing
O15091-4
- Name4
- Differences from canonical
- 1-95: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A0MTQ0 | A0A0A0MTQ0_HUMAN | PRORP | 185 | ||
S4R3S1 | S4R3S1_HUMAN | PRORP | 19 | ||
S4R416 | S4R416_HUMAN | PRORP | 34 | ||
S4R3T4 | S4R3T4_HUMAN | PRORP | 23 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_036202 | 1-95 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_036201 | 1-372 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 315 | in Ref. 3; BAG63351 | ||||
Sequence: P → L | ||||||
Alternative sequence | VSP_036203 | 329-344 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 453 | in Ref. 3; BAG64540 | ||||
Sequence: S → F |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB002389 EMBL· GenBank· DDBJ | BAA20845.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BX161394 EMBL· GenBank· DDBJ | CAD61881.1 EMBL· GenBank· DDBJ | mRNA | ||
BX161487 EMBL· GenBank· DDBJ | CAD61937.1 EMBL· GenBank· DDBJ | mRNA | ||
AK301931 EMBL· GenBank· DDBJ | BAG63351.1 EMBL· GenBank· DDBJ | mRNA | ||
AK303508 EMBL· GenBank· DDBJ | BAG64540.1 EMBL· GenBank· DDBJ | mRNA | ||
AK304066 EMBL· GenBank· DDBJ | BAG64973.1 EMBL· GenBank· DDBJ | mRNA | ||
AL121594 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471078 EMBL· GenBank· DDBJ | EAW65878.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW65882.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW65879.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW65880.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW65881.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW65883.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471078 EMBL· GenBank· DDBJ | EAW65884.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC032221 EMBL· GenBank· DDBJ | AAH32221.1 EMBL· GenBank· DDBJ | mRNA | ||
BC044580 EMBL· GenBank· DDBJ | AAH44580.1 EMBL· GenBank· DDBJ | mRNA |