| IED ID | IndEnz0002009389 |
| Enzyme Type ID | protease009389 |
| Protein Name |
Serine-repeat antigen protein 6 EC 3.4.22.- Cysteine protease SERA6 SERP H |
| Gene Name | SERA6 |
| Organism | Plasmodium falciparum |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum |
| Enzyme Sequence | MIFFNFKLNRMICPIFFLYIINVLFTQYFIKCEGNKVTVISHNNGHNDNLDVNKNGVISQENVFDTSESLNLPSNKKVGSDDLNTTTISFTVPDNLENEVKVVSSSESGKGATVSHTKVTSEGLSDTQPNVTQSVSSSTHTPGSLDSTMSTEQHSSVSQSSLPTESSSETLNKATVPEIPIQINSGLLKNYNGVKVTGSCGSYFRVYLVPHILIYALTKYSVIQLESLFNDNARIDVEHKGELQNKCSEGYHFKLVVYITHNVLNLKWKTYKPNEESKSEDSDVRKYRIPKLERPFTSIQVYTANSKAGVIETKNYNIRTDIPDTCDAIATDCFLNGNVNIEKCFQCTLLVQKKDKSHECFKYVSSEMKKKMNEIKVKAQDDFNPNEYKLIESIDNILSKIYKKANKPFEISKDLINLEDLDYQFKNELLEYCKLLKKVDTSGTLEEYELGNAEDIYNNLTRLLKSHSDENIVTLQGKLRNTAICIKNVDEWILNKRGLTLPSESPSESSSKSDSYLNTFNDKDKNEDKDDMSKNSKEEFKNDDKENSDDQNNNDSNKKDDENNINNGDTNYVYDFDDDDYDNNSYEKDMYESPIKENKNGVIDLEKYGNQIKLKSPYFKNSKYCNYEYCNRWRDKTSCISQIEVEEQGNCGLCWIFASKLHFETIRCMRGYGHFRSSALYVANCSKRKPIDRCEEGSNPLEFLRILDEKKFLPLESNYPYSYTSAGNSCPKLPNSWTNLWGDTKLLFNKKVHRYIGNKGFISHETSYFKNNMDLFIDMVKREVQNKGSVIIYIKTQDVIGYDFNGKGVHSMCGDRTPDHAANIIGYGNYINKKGEKRSYWLIRNSWSYYWGDEGNFRVDMLGPKNCLYNFIHTVVFFKLDLGTIHVPKKKSWKKNVYFLRHNTDFMYSLYYNNYEPETSQDFESENDYDNAFVHGQSDESDETNKEGKNVHNSVEKKIQILHILKHIKDSQIKRGLVKYDNINETKDEHTCSRVNSQDAEKYEECKKFCLTKWNECKDHYSPGYCLTDLYKGEDCNFCYV |
| Enzyme Length | 1041 |
| Uniprot Accession Number | Q26015 |
| Absorption | |
| Active Site | ACT_SITE 654; /evidence=ECO:0000255|PROSITE-ProRule:PRU10088; ACT_SITE 820; /evidence=ECO:0000250|UniProtKB:O60911; ACT_SITE 845; /evidence=ECO:0000250|UniProtKB:O60911 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Cysteine protease which plays an essential role in merozoite egress from host erythrocytes (PubMed:22984267, PubMed:29459732). May cleave host SPTB/beta spectrin and ANK1/ankyrin-1 which disrupts host erythrocyte actin cytoskeleton and leads to host erythrocyte cell membrane rupture (PubMed:29459732). {ECO:0000269|PubMed:22984267, ECO:0000269|PubMed:29459732}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (2); Glycosylation (7); Mutagenesis (2); Region (2); Signal peptide (1); Site (3) |
| Keywords | Glycoprotein;Hydrolase;Membrane;Protease;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Parasitophorous vacuole lumen {ECO:0000250|UniProtKB:Q9TY96}. Parasitophorous vacuole membrane {ECO:0000250|UniProtKB:Q9TY96}; Peripheral membrane protein {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Just prior to merozoite egress from host erythrocytes, proteolytically cleaved by SUB1 to generate the active 75kDa form. {ECO:0000250|UniProtKB:Q9TY96}. |
| Signal Peptide | SIGNAL 1..34; /evidence=ECO:0000305 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 120,152 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |