O75439 · MPPB_HUMAN
- ProteinMitochondrial-processing peptidase subunit beta
- GenePMPCB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids489 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalytic subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins (Probable) (PubMed:29576218).
Preferentially, cleaves after an arginine at position P2 (By similarity).
Required for PINK1 turnover by coupling PINK1 mitochondrial import and cleavage, which results in subsequent PINK1 proteolysis (PubMed:22354088).
Preferentially, cleaves after an arginine at position P2 (By similarity).
Required for PINK1 turnover by coupling PINK1 mitochondrial import and cleavage, which results in subsequent PINK1 proteolysis (PubMed:22354088).
Catalytic activity
Cofactor
Note: Binds 1 zinc ion per subunit.
Activity regulation
Binding to PMPCA is required for catalytic activity.
Features
Showing features for binding site, active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 101 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 104 | Proton acceptor | ||||
Sequence: E | ||||||
Binding site | 105 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 181 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Site | 191 | Required for the specific determination of the substrate cleavage site | ||||
Sequence: E | ||||||
Site | 195 | Required for the specific determination of the substrate cleavage site | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrial matrix | |
Cellular Component | mitochondrial processing peptidase complex | |
Cellular Component | mitochondrion | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Biological Process | mitochondrial calcium ion transmembrane transport | |
Biological Process | protein processing involved in protein targeting to mitochondrion |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMitochondrial-processing peptidase subunit beta
- 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 accessionO75439
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Multiple mitochondrial dysfunctions syndrome 6 (MMDS6)
- Note
- DescriptionAn autosomal recessive, neurodegenerative disorder characterized by basal ganglia lesions, cerebellar atrophy, and neurologic regression in the first year of life. Common features include truncal hypotonia, lack of independent ambulation, poor speech, intellectual disability, and motor abnormalities, such as ataxia, dystonia, and spasticity.
- See alsoMIM:617954
Natural variants in MMDS6
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_080804 | 175 | R>C | in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast; dbSNP:rs145596167 | |
VAR_080805 | 175 | R>H | in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast; dbSNP:rs200188353 | |
VAR_080806 | 177 | V>G | in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast; dbSNP:rs1436866272 | |
VAR_080807 | 201 | A>P | in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast; dbSNP:rs146343535 | |
VAR_080808 | 422 | I>T | in MMDS6; small decrease in protein level; impaired frataxin/FXN processing, leading to the accumulation of an intermediate form, called iFXN; dbSNP:rs1461200360 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_080804 | 175 | in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast; dbSNP:rs145596167 | |||
Sequence: R → C | ||||||
Natural variant | VAR_080805 | 175 | in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast; dbSNP:rs200188353 | |||
Sequence: R → H | ||||||
Natural variant | VAR_080806 | 177 | in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast; dbSNP:rs1436866272 | |||
Sequence: V → G | ||||||
Natural variant | VAR_080807 | 201 | in MMDS6; exhibits temperature-sensitive defect in presequence processing activity, when tested in yeast; dbSNP:rs146343535 | |||
Sequence: A → P | ||||||
Natural variant | VAR_051572 | 396 | in dbSNP:rs3087615 | |||
Sequence: E → D | ||||||
Natural variant | VAR_080808 | 422 | in MMDS6; small decrease in protein level; impaired frataxin/FXN processing, leading to the accumulation of an intermediate form, called iFXN; dbSNP:rs1461200360 | |||
Sequence: I → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 550 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, modified residue (large scale data), chain.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-43 | UniProt | Mitochondrion | ||||
Sequence: MAAAAARVVLSSAARRRLWGFSESLLIRGAAGRSLYFGENRLR | |||||||
Modified residue (large scale data) | 44 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Chain | PRO_0000026777 | 44-489 | UniProt | Mitochondrial-processing peptidase subunit beta | |||
Sequence: STQAATQVVLNVPETRVTCLESGLRVASEDSGLSTCTVGLWIDAGSRYENEKNNGTAHFLEHMAFKGTKKRSQLDLELEIENMGAHLNAYTSREQTVYYAKAFSKDLPRAVEILADIIQNSTLGEAEIERERGVILREMQEVETNLQEVVFDYLHATAYQNTALGRTILGPTENIKSISRKDLVDYITTHYKGPRIVLAAAGGVSHDELLDLAKFHFGDSLCTHKGEIPALPPCKFTGSEIRVRDDKMPLAHLAIAVEAVGWAHPDTICLMVANTLIGNWDRSFGGGMNLSSKLAQLTCHGNLCHSFQSFNTSYTDTGLWGLYMVCESSTVADMLHVVQKEWMRLCTSVTESEVARARNLLKTNMLLQLDGSTPICEDIGRQMLCYNRRIPIPELEARIDAVNAETIREVCTKYIYNRSPAIAAVGPIKQLPDFKQIRSNMCWLRD | |||||||
Modified residue (large scale data) | 45 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Heterodimer of PMPCA (alpha) and PMPCB (beta) subunits, forming the mitochondrial processing protease (MPP) in which PMPCA is involved in substrate recognition and binding and PMPCB is the catalytic subunit.
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length489
- Mass (Da)54,366
- Last updated2003-04-11 v2
- Checksum79250D016E60CFEE
Computationally mapped potential isoform sequences
There are 16 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8WEA6 | F8WEA6_HUMAN | PMPCB | 119 | ||
F8WEC8 | F8WEC8_HUMAN | PMPCB | 122 | ||
F8WAZ6 | F8WAZ6_HUMAN | PMPCB | 202 | ||
F8WBE1 | F8WBE1_HUMAN | PMPCB | 122 | ||
G3V0E4 | G3V0E4_HUMAN | PMPCB | 490 | ||
A0A9L9PY03 | A0A9L9PY03_HUMAN | PMPCB | 482 | ||
A0A9L9PXH0 | A0A9L9PXH0_HUMAN | PMPCB | 506 | ||
A0A9L9PXH7 | A0A9L9PXH7_HUMAN | PMPCB | 390 | ||
A0A9L9PXI7 | A0A9L9PXI7_HUMAN | PMPCB | 508 | ||
A0A9L9PXG6 | A0A9L9PXG6_HUMAN | PMPCB | 250 | ||
A0A9L9PXH4 | A0A9L9PXH4_HUMAN | PMPCB | 66 | ||
A0A9L9PWW3 | A0A9L9PWW3_HUMAN | PMPCB | 502 | ||
A0A9L9PWX2 | A0A9L9PWX2_HUMAN | PMPCB | 157 | ||
A0A9L9PX50 | A0A9L9PX50_HUMAN | PMPCB | 221 | ||
A0A9L9PX59 | A0A9L9PX59_HUMAN | PMPCB | 382 | ||
A0A9L9PX42 | A0A9L9PX42_HUMAN | PMPCB | 475 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 16-17 | in Ref. 1; AAC39915 | ||||
Sequence: RR → GG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF054182 EMBL· GenBank· DDBJ | AAC39915.1 EMBL· GenBank· DDBJ | mRNA | ||
AC004668 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |