| IED ID | IndEnz0002009399 |
| Enzyme Type ID | protease009399 |
| Protein Name |
Subtilisin-like protease 2 EC 3.4.21.62 Merozoite surface sheddase MESH PfSUB2 |
| Gene Name | SUB2 PF3D7_1136900 |
| Organism | Plasmodium falciparum (isolate 3D7) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate 3D7) |
| Enzyme Sequence | MLNIIYVVSLILIKFIFYKECNNNNNYYLSNIELYNYKLRKRNRILNNNINDRKSFLSDLEQNYKPLFDIYELSANFEKRRKELEKKTKGEENEIEKKKENDLEKKKENEIEKKKENDLEKEYNDVINLLELSLSSEYKELNADVSNNDNSGHEENNKHKLNKKNSSNYKNDKSLDELIKGAILKLKQNPNIKNKNMLDYDKIFKIIKEKLINKNLASNKIKGGDNEKLKEEKKQSDISTNVEVKKDIINDQLNKGIPTKKENKDDMINKESNKEDITNEGKSNSLNNLNTLNNDGNIITKVYDHYTIVTNSNDILNDISIDASDISKNSIGGINIPFNENDNSSFTHQRYIVLSNNGEKKYKIVLMTKNPKFMDMDGIYDEEEKKESLIELNQKVNKEENTNLYDGTGTLYYGKKSKKEKENTQQKGGNNPNVDINILNNNNNNNNNNNSNNNSNSMNDEEINYNNNNNNKESPSMFRRFINFLSFSGNENETEDTLIYHNKNDNSYKNKKEGTGKNNDNNDPNNNNNKKILLNVDKLVDQYLLNLKNNHTSKQELILVLKGELDLHSKNMKNVINNAKKNLEKYFKEHFKEFDKISYDISTPINFLCIFIPTLFDMNNMDLLKQALLILHNDLHEYVENWSFSSTYHTYEADYIKEQDSVYDRSPKKKYIKASKKLYNNKYSFLNKFLNIEPLILFAKKLNSKRSNIEKEILNFLPKELRDYSTWNLSIIRVFNAWFLAGYGNKNVKVCVVDSGADINHVDLNGNLYIPEYNEKYEMTQDFYNFMVKNPTDASGHGTHVTGIIGGVANDLGVVGVAPNITLISLRFIDGKKYGGSFHAIKALNVCILNKAPIINASWGSSHFDVNLHLAVERLKYTLNGKGSVLIAASGNKSNDNDISPLYPATFTFPHVYSVASISRNFEISPFSNYGHKSVHILAPGHHIYSTIPNNSYKIFTGTSMAAPHVCGVSALVYSVCYNQGFIPQAEEVLDILTRTSIKIISTKKRTINDSLVNAEGAVLTTLLGGLWMQMDCYFVKFNLEKGKKKHIPVVFSAYKKGVYETDIVIAIIPIDGKSKIYGEIHIPIKIVTDVNIPNFQESPRRGKNYTIDSNEAQHDEVLSYICENALYNLYEYDSHYLLASVILFFLALLSIFVGMIYMKSRKHSDKKCSKNLIKSNYIPEMDDGMEETQQLQQERRQYFRELFGENLEKNYDQHFVQDFGQDFRQDFKLGSTPDLKQYSDIDLQNKIQQPERKTVKIIINNFEDRKKETKRRLLKGLNYDGENAKKHDFTNESISNSRKNFKFSNNTEMKKNTIKSEDVKIASDDNVNKAMNQLDDMFMK |
| Enzyme Length | 1341 |
| Uniprot Accession Number | Q8IHZ5 |
| Absorption | |
| Active Site | ACT_SITE 754; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 797; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 960; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
| Activity Regulation | ACTIVITY REGULATION: Activation may be calcium-dependent (PubMed:16879884). Inhibited by the non-covalent interaction with the cleaved propeptide (PubMed:16879884, PubMed:19214190). {ECO:0000269|PubMed:16879884, ECO:0000269|PubMed:19214190}. |
| 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:0000269|PubMed:23834729, ECO:0000305|PubMed:16879884, ECO:0000305|PubMed:19214190}; |
| 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:16879884, PubMed:19214190). May cleave TRAMP/PTTRAMP, thereby shedding TRAMP from the merozoite surface during erythrocyte invasion (PubMed:16879884). {ECO:0000269|PubMed:16879884, ECO:0000269|PubMed:19214190}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (3); Domain (1); Glycosylation (14); Mutagenesis (1); Propeptide (1); Region (4); Signal peptide (1); Topological domain (2); Transmembrane (1) |
| Keywords | Autocatalytic cleavage;Cell membrane;Cytoplasmic vesicle;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Serine protease;Signal;Transmembrane;Transmembrane helix;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23834729}; Single-pass type I membrane protein {ECO:0000305|PubMed:23834729}. Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:23834729}; Single-pass type I membrane protein {ECO:0000305|PubMed:23834729}. Note=In mature schizonts, localizes to micronemes at the merozoite apical region (PubMed:23834729). 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:23834729). {ECO:0000269|PubMed:23834729}. |
| 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:23834729). The first maturation cleavage is autocatalytic, occurs in the ER and is necessary for the subsequent SUB2 trafficking to the microneme (PubMed:23834729). The second cleavage may be mediated by PMX/plasmepsin X (PubMed:32109369). {ECO:0000269|PubMed:23834729, ECO:0000269|PubMed:32109369}. |
| Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16267556; |
| Motif | |
| Gene Encoded By | |
| Mass | 154,800 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |