Q9Y006 · PLM3_PLAFX
- ProteinPlasmepsin III
- GenePMIII
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids451 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
During the asexual blood stage, catalyzes the cleavage of denatured host hemoglobin (Hb) or globins (PubMed:11782538).
Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable)
Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable)
Catalytic activity
Activity regulation
Dimerization causes loss of catalytic activity (By similarity).
Inhibited by pepstatin A (PubMed:11782538).
Inhibited by pepstatin A (PubMed:11782538).
pH Dependence
Optimum pH is 5.7.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 337 | |||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | food vacuole | |
Cellular Component | membrane | |
Cellular Component | vacuolar lumen | |
Molecular Function | aspartic-type endopeptidase activity | |
Biological Process | acquisition of nutrients from host | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePlasmepsin III
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ9Y006
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Single-pass type II membrane protein
Note: In trophozoites, localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-37 | Cytoplasmic | ||||
Sequence: MNLTIKEEDFTNTFMKNEESFNTFRVTKVKRWNAKRL | ||||||
Transmembrane | 38-58 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: FKILFVTVFIVLAGGFSYYIF | ||||||
Topological domain | 59-451 | Lumenal | ||||
Sequence: ENFVFQKNRKINHIIKTSKYSTVGFNIENSYDRLMKTIKEHKLKNYIKESVKLFNKGLTKKSYLGSEFDNVELKDLANVLSFGEAKLGDNGQKFNFLFHTASSNVWVPSIKCTSESCESKNHYDSSKSKTYEKDDTPVKLTSKAGTISGIFSKDLVTIGKLSVPYKFIEMTEIVGFEPFYSESDVDGVFGLGWKDLSIGSIDPYIVELKTQNKIEQAVYSIYLPPENKNKGYLTIGGIEERFFDGPLNYEKLNHDLMWQVDLDVHFGNVSSKKANVILDSATSVITVPTEFFNQFVESASVFKVPFLSLYVTTCGNTKLPTLEYRSPNKVYTLEPKQYLEPLENIFSALCMLNIVPIDLEKNTFVLGDPFMRKYFTVYDYDNHTVGFALAKNL |
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000453380 | 1-123 | ||||
Sequence: MNLTIKEEDFTNTFMKNEESFNTFRVTKVKRWNAKRLFKILFVTVFIVLAGGFSYYIFENFVFQKNRKINHIIKTSKYSTVGFNIENSYDRLMKTIKEHKLKNYIKESVKLFNKGLTKKSYLG | ||||||
Chain | PRO_0000453381 | 124-451 | Plasmepsin III | |||
Sequence: SEFDNVELKDLANVLSFGEAKLGDNGQKFNFLFHTASSNVWVPSIKCTSESCESKNHYDSSKSKTYEKDDTPVKLTSKAGTISGIFSKDLVTIGKLSVPYKFIEMTEIVGFEPFYSESDVDGVFGLGWKDLSIGSIDPYIVELKTQNKIEQAVYSIYLPPENKNKGYLTIGGIEERFFDGPLNYEKLNHDLMWQVDLDVHFGNVSSKKANVILDSATSVITVPTEFFNQFVESASVFKVPFLSLYVTTCGNTKLPTLEYRSPNKVYTLEPKQYLEPLENIFSALCMLNIVPIDLEKNTFVLGDPFMRKYFTVYDYDNHTVGFALAKNL | ||||||
Disulfide bond | 170↔175 | |||||
Sequence: CTSESC | ||||||
Disulfide bond | 372↔408 | |||||
Sequence: CGNTKLPTLEYRSPNKVYTLEPKQYLEPLENIFSALC |
Post-translational modification
Proteolytically cleaved into the soluble active mature form by cysteine proteases in the digestive vacuole of trophozoites (PubMed:12850260).
Proteolysis requires an acidic environment (By similarity).
Transprocessing may serve as an alternate activation system (Probable)
Proteolysis requires an acidic environment (By similarity).
Transprocessing may serve as an alternate activation system (Probable)
Keywords
- PTM
Expression
Developmental stage
Expressed during the asexual blood stage; expression begins in trophozoites and continues in schizonts (at protein level).
Interaction
Subunit
Probable homodimer; in the zymogen form (PubMed:32385863).
Monomer; in the active form (PubMed:11782538, PubMed:32385863).
Acidification disrupts homodimerization (PubMed:32385863).
Component of the hemozoin formation complex (HFC) composed of falcipains FP2A and/or FP2B, plasmepsins PMII, PMIII/HAP and PMIV, heme detoxifying protein HDP and falcilysin FLN (By similarity).
The HFC complex is involved in hemoglobin degradation and detoxification of heme in the food vacuole during the asexual blood stage (By similarity).
Monomer; in the active form (PubMed:11782538, PubMed:32385863).
Acidification disrupts homodimerization (PubMed:32385863).
Component of the hemozoin formation complex (HFC) composed of falcipains FP2A and/or FP2B, plasmepsins PMII, PMIII/HAP and PMIV, heme detoxifying protein HDP and falcilysin FLN (By similarity).
The HFC complex is involved in hemoglobin degradation and detoxification of heme in the food vacuole during the asexual blood stage (By similarity).
Chemistry
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 139-446 | Peptidase A1 | ||||
Sequence: SFGEAKLGDNGQKFNFLFHTASSNVWVPSIKCTSESCESKNHYDSSKSKTYEKDDTPVKLTSKAGTISGIFSKDLVTIGKLSVPYKFIEMTEIVGFEPFYSESDVDGVFGLGWKDLSIGSIDPYIVELKTQNKIEQAVYSIYLPPENKNKGYLTIGGIEERFFDGPLNYEKLNHDLMWQVDLDVHFGNVSSKKANVILDSATSVITVPTEFFNQFVESASVFKVPFLSLYVTTCGNTKLPTLEYRSPNKVYTLEPKQYLEPLENIFSALCMLNIVPIDLEKNTFVLGDPFMRKYFTVYDYDNHTVGFA |
Sequence similarities
Belongs to the peptidase A1 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length451
- Mass (Da)51,693
- Last updated1999-11-01 v1
- ChecksumD9ED8C4A066B2154
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 451 | in Ref. 3; KOB58718 | ||||
Sequence: L → F |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY878730 EMBL· GenBank· DDBJ | AAW71454.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY878731 EMBL· GenBank· DDBJ | AAW71455.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY878732 EMBL· GenBank· DDBJ | AAW71456.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY878733 EMBL· GenBank· DDBJ | AAW71457.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY878734 EMBL· GenBank· DDBJ | AAW71458.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ009990 EMBL· GenBank· DDBJ | CAB40630.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH671923 EMBL· GenBank· DDBJ | KOB58718.1 EMBL· GenBank· DDBJ | Genomic DNA |