IED ID | IndEnz0002001670 |
Enzyme Type ID | protease001670 |
Protein Name |
Serine-repeat antigen protein 6 EC 3.4.22.- Cysteine protease SERA6 |
Gene Name | SERA6 PF3D7_0207500 |
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 | MICPIFFLYIINVLFTQYFIKCEGNKVTVISHNNGHNDNLDVNKNGVISQENVFDTSESLNLPSNKKVGSDDLNTTTISFTVPDNLENEVKVVSSSESGKGATVSHTKVTSEGLSDTQPNVTQSVSSSTHTPGSLDSTMSTEQHSSVSQSSLPTESSSETLNKATVPEIPIQINSGLLKNYNGVKVTGSCGSYFRVYLVPHILIYALTKYSVIQLESLFNDNARIDVEHKGELQNKCSEGYHFKLVVYITHNVLNLKWKTYKPNEESKSEDSDVRKYRIPKLERPFTSIQVYTANSKAGVIETKNYNIRTDIPDTCDAIATDCFLNGNVNIEKCFQCTLLVQKKDKSHECFKYVSSEMKKKMNEIKVKAQDDFNPNEYKLIESIDNILSKIYKKANKPFEISKDLINLEDLDYQFKNELLEYCKLLKKVDTSGTLEEYELGNAEDIYNNLTRLLKSHSDENIVTLQGKLRNTAICIKNVDEWILNKRGLTLPSESPSESSSKSDSYLNTFNDKDKNEDKDDMSKNSKEEFKNDDKENSDDQNNNDSNKKDDENNINNGDTNYVYDFDDDDYDNNSYEKDMYESPIKENKNGVIDLEKYGNQIKLKSPYFKNSKYCNYEYCNRWRDKTSCISQIEVEEQGNCGLCWIFASKLHFETIRCMRGYGHFRSSALYVANCSKRKPIDRCEEGSNPLEFLRILDEKKFLPLESNYPYSYTSAGNSCPKLPNSWTNLWGDTKLLFNKKVHRYIGNKGFISHETSYFKNNMDLFIDMVKREVQNKGSVIIYIKTQDVIGYDFNGKGVHSMCGDRTPDHAANIIGYGNYINKKGEKRSYWLIRNSWSYYWGDEGNFRVDMLGPKNCLYNFIHTVVFFKLDLGTIHVPKKKSWKKNVYFLRHNPDFMYSLYYNNYEPETSQDFESENDYDNAFVHGQSNESDETNKEGKNVHNSVEKKIQILHILKHIKDSQIKRGLVKYDNINETKDEHTCSRVNSQDAEKYEECKKFCLTKWNECKDHYSPGYCLTDLYKGEDCNFCYV |
Enzyme Length | 1031 |
Uniprot Accession Number | Q9TY96 |
Absorption | |
Active Site | ACT_SITE 644; /evidence=ECO:0000255|PROSITE-ProRule:PRU10088; ACT_SITE 810; /evidence=ECO:0000250|UniProtKB:O60911; ACT_SITE 835; /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. May cleave host SPTB/beta spectrin and ANK1/ankyrin-1 which disrupts host erythrocyte actin cytoskeleton and leads to host erythrocyte cell membrane rupture. {ECO:0000250|UniProtKB:Q26015}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Compositional bias (2); Glycosylation (8); Region (2); Signal peptide (1); Site (3) |
Keywords | Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Signal;Thiol protease;Zymogen |
Interact With | Q8I0V0 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Parasitophorous vacuole lumen {ECO:0000269|PubMed:22984267}. Parasitophorous vacuole membrane {ECO:0000269|PubMed:22984267}; 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:0000269|PubMed:18083098, ECO:0000269|PubMed:22984267}. |
Signal Peptide | SIGNAL 1..24; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | 16267556; |
Motif | |
Gene Encoded By | |
Mass | 118,836 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |