| IED ID | IndEnz0002001794 |
| Enzyme Type ID | protease001794 |
| Protein Name |
Subtilisin-like protease 2 EC 3.4.21.62 Merozoite surface sheddase MESH PfSUB2 |
| Gene Name | SUB2 |
| Organism | Plasmodium falciparum |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum |
| Enzyme Sequence | MLNIIYVVSLILIKFIFYKECNNNNNYYLSNIELYNYKLRKRNRILNNNINDRKSFLSDLEQNYKPLFDIYELSANFEKRRKELEKKTKGEENEIEKKKENDLEEKKENEIEKKKENDLEKEYNDVINLLELSLSSEYKELNADVSNNDNSGHEENNKHKLNKKNSSNYKNDKSLDELIKGAILKLKQNPNIKNKNMLDYDKIFKIIKEKLINKNLASNKIKGGDNEKLKEEKKQSDISTNVEVKKDIINDQLNKGIPTKIENKDDMINKESNKEDITNEGKSNSLNNLNTLNNDGNIITKVYDHYTIVTNSNDILNDISIDASDISKNSIGGINIPFNENDNSSFTHQRYIVLSNNGEKKYKIVLMTKNPKFMDMDGIYDEEEKKESLIELNQKVNKEENTNLYDGTGTLYYGKKSKKEKENTQQKGGNNPNVDINILNNNNNNNNNNNNNSNNNSNSMNDEEINYNNNNNKESPSMFRRFINFLSFSGNENETEDTLIYHNKNDNSYKNKKEGTGKNNDNNDPNNNNNKKILLNVDKLVDQYLLNLKNNHTSKQELILVLKGELDLHSKNMKNVINNAKKNLEKYFKEHFKEFDKISYDISTPINFLCIFIPTLFDMNNMDLLKQALLILHNDLHEYVENWSFSSTYHTYEADYIKEQDSVYDRSPKKKYIKASKKLYNNKYSFLNKFLNIEPLILFAKKLNSKRSNIEKEILNFLPKELRDYSTWNLSIIRVFNAWFLAGYGNKNVKVCVVDSGADIKHVDLNGNLYIPEYNEKYEMTQDFYNFMVKNPTDASGHGTHVTGIIGGVANDLGVVGVAPNITLISLRFIDGKKYGGSFHAIKALNVCILNKAPIINASWGSSHFDVNLHLAVERLKYTLNGKGSVLIAASGNKSNDNDISPLYPATFTFPHVYSVASISRNFEISPFSNYGHKSVHILAPGHHIYSTIPNNSYKIFTGTSMAAPHVCGVSALVYSVCYNQGFIPQAEEVLDILTRTSIKIISTKKRTINDSLVNAEGAVLTTLLGGLWMQMDCYFVKFNLEKGKKKHIPVVFSAYKKGVYETDIVIAIIPIDGKSKIYGEIHIPIKIVTDVNIPNFQESPRRGKNYTIDSNEAQHDEVLSYICENALYNLYEYDSHYLLASVILFFLALLSIFVGMIYMKSRKHSDKKCSKNLMKSNYIPEMDDGMEETQQLQQERRQYFRELFGENLEKNYDQHFVQDFGQDFRQDFKLGSTPDLKQYSDIDLQNKIQQPERKTVKIIINNFEDRKKETKRRLLKGLNYDGENAKKHDFTNESISNSRKNFKFSNNTEMKKNTIKSEDVKIASDDNVNKAMNQLDDMFMK |
| Enzyme Length | 1342 |
| Uniprot Accession Number | O97364 |
| Absorption | |
| Active Site | ACT_SITE 755; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 798; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 961; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | ACTIVITY REGULATION: Activation may be calcium-dependent (PubMed:16322767). Inhibited by the non-covalent interaction with the cleaved propeptide (PubMed:16322767). {ECO:0000269|PubMed:16322767}. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000305|PubMed:16322767}; |
| DNA Binding | |
| EC Number | 3.4.21.62 |
| Enzyme 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 (PubMed:16322767). May cleave TRAMP/PTTRAMP, thereby shedding TRAMP from the merozoite surface during erythrocyte invasion (By similarity). {ECO:0000250|UniProtKB:Q8IHZ5, ECO:0000269|PubMed:16322767}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Beta strand (4); Chain (1); Compositional bias (3); Domain (1); Glycosylation (14); Helix (2); Propeptide (1); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1); Turn (1) |
| Keywords | 3D-structure;Autocatalytic cleavage;Cell membrane;Cytoplasmic vesicle;Glycoprotein;Hydrolase;Membrane;Protease;Serine protease;Signal;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:16322767}; Single-pass type I membrane protein {ECO:0000305}. Note=In mature schizonts, localizes to micronemes at the merozoite apical region (PubMed:10551362, PubMed:16322767). 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 (PubMed:16322767). {ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}. |
| Modified Residue | |
| Post Translational Modification | PTM: Proteolytically cleaved at the N-terminus to generate a 74kDa intermediate which is further processed into a 72kDa form (PubMed:10551362, PubMed:16322767). 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). {ECO:0000250|UniProtKB:Q8IHZ5, ECO:0000269|PubMed:10551362, ECO:0000269|PubMed:16322767}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 2LU1; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 154,932 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |