Q9Y008 · SUB2_PLAFP
- ProteinSubtilisin-like protease 2
- GeneSUB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1337 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Serine protease which plays an essential role in the shedding of AMA1, MSP1 and MSP7 from the surface of the invading merozoite; this step is essential for productive invasion and the release of the adhesion between the erythrocyte and the merozoite. May cleave TRAMP/PTTRAMP, thereby shedding TRAMP from the merozoite surface during erythrocyte invasion.
Catalytic activity
Activity regulation
Activation may be calcium-dependent. Inhibited by the non-covalent interaction with the cleaved propeptide.
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 750 | Charge relay system | |||
Active site | 793 | Charge relay system | |||
Active site | 956 | Charge relay system | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic vesicle | |
Cellular Component | microneme membrane | |
Cellular Component | plasma membrane | |
Molecular Function | serine-type endopeptidase activity | |
Biological Process | protein processing |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSubtilisin-like protease 2
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ9Y008
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Cytoplasmic vesicle, secretory vesicle, microneme membrane ; Single-pass type I membrane protein
Note: In mature schizonts, localizes to micronemes at the merozoite apical region (PubMed:10339607).
Immediately after schizont rupture, secreted from the micronemes to the merozoite surface where it redistributes in an actin-dependent manner to accumulate at the posterior end of newly released merozoites (By similarity).
Immediately after schizont rupture, secreted from the micronemes to the merozoite surface where it redistributes in an actin-dependent manner to accumulate at the posterior end of newly released merozoites (By similarity).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Topological domain | 683-1132 | Extracellular | |||
Transmembrane | 1133-1153 | Helical | |||
Topological domain | 1154-1337 | Cytoplasmic | |||
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, propeptide, glycosylation, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-18 | ||||
Propeptide | PRO_0000450753 | 19-682 | Inhibition peptide | ||
Glycosylation | 157 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 335 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 445 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 449 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 488 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 546 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 570 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 637 | N-linked (GlcNAc...) asparagine | |||
Chain | PRO_5004337835 | 683-1337 | Subtilisin-like protease 2 | ||
Glycosylation | 724 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 816 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 852 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 888 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 946 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 1005 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 1101 | N-linked (GlcNAc...) asparagine | |||
Post-translational modification
Proteolytically cleaved at the N-terminus to generate a 74kDa intermediate which is further processed into a 72kDa form (PubMed:10339607).
The first maturation cleavage is autocatalytic, occurs in the ER and is necessary for the subsequent SUB2 trafficking to the microneme (By similarity).
The second cleavage may be mediated by PMX/plasmepsin X (By similarity).
The first maturation cleavage is autocatalytic, occurs in the ER and is necessary for the subsequent SUB2 trafficking to the microneme (By similarity).
The second cleavage may be mediated by PMX/plasmepsin X (By similarity).
Keywords
- PTM
PTM databases
Expression
Developmental stage
Expressed during the parasite blood stage, specifically in schizonts and merozoites (at protein level).
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 85-105 | Disordered | |||
Region | 135-163 | Disordered | |||
Compositional bias | 143-163 | Basic and acidic residues | |||
Region | 407-470 | Disordered | |||
Compositional bias | 418-470 | Polar residues | |||
Compositional bias | 495-514 | Basic and acidic residues | |||
Region | 495-526 | Disordered | |||
Domain | 722-1015 | Peptidase S8 | |||
Domain
The propeptide domain acts as an intramolecular chaperone for the folding of the catalytic domain (By similarity).
Also acts as an inhibitor of the catalytic domain thereby regulating SUB2 activity during secretion (By similarity).
Also acts as an inhibitor of the catalytic domain thereby regulating SUB2 activity during secretion (By similarity).
The transmembrane domain is required for SUB2 progression through the secretory pathway.
The cytoplasmic domain is required for the correct redistribution at the merozoite surface and posterior capping but is dispensable for its progression through the secretory pathway.
Sequence similarities
Belongs to the peptidase S8 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,337
- Mass (Da)154,394
- Last updated1999-11-01 v1
- Checksum42B900BE2E8FC1A4
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 143-163 | Basic and acidic residues | |||
Compositional bias | 418-470 | Polar residues | |||
Compositional bias | 495-514 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ132006 EMBL· GenBank· DDBJ | CAB43592.1 EMBL· GenBank· DDBJ | Genomic DNA |