| IED ID | IndEnz0002010147 |
| Enzyme Type ID | protease010147 |
| Protein Name |
Serine-repeat antigen protein 5 EC 3.4.22.- 111 kDa antigen Serine protease SERA5 p126 Cleaved into: p47 SER36 ; p56; p50; p18; p25n; p25c |
| Gene Name | SERA5 SERA |
| Organism | Plasmodium falciparum (isolate CDC / Honduras) |
| Taxonomic Lineage | cellular organisms Eukaryota Sar Alveolata Apicomplexa Aconoidasida Haemosporida (haemosporidians) Plasmodiidae Plasmodium Plasmodium (Laverania) Plasmodium falciparum Plasmodium falciparum (isolate CDC / Honduras) |
| Enzyme Sequence | MKSYISLFFILCVIFNKNVIKCTGESQTGNTGGGQAGNTVGDQAGSTGGSPQGSTGASQPGSSEPSNPVSSGHSVSTVSVSQTSTSSEKQDTIQVKSALLKDYMGLKVTGPCNENFIMFLVPHIYIDVDTEDTNIELRTTLKETNNAISFESNSGSLEKKKYVKLPSNGTTGEQGSSTGTVRGDTEPISDSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSESLPANGPDSPTVKPPRNLQNICETGKNFKLVVYIKENTLIIKWKVYGETKDTTENNKVDVRKYLINEKETPFTSILIHAYKEHNGTNLIESKNYALGSDIPEKCDTLASNCFLSGNFNIEKCFQCALLVEKENKNDVCYKYLSEDIVSNFKEIKAETEDDDEDDYTEYKLTESIDNILVKMFKTNENNDKSELIKLEEVDDSLKLELMNYCSLLKDVDTTGTLDNYGMGNEMDIFNNLKRLLIYHSEENINTLKNKFRNAAVCLKNVDDWIVNKRGLVLPELNYDLEYFNEHLYNDKNSPEDKDNKGKGVVHVDTTLEKEDTLSYDNSDNMFCNKEYCNRLKDENNCISNLQVEDQGNCDTSWIFASKYHLETIRCMKGYEPTKISALYVANCYKGEHKDRCDEGSSPMEFLQIIEDYGFLPAESNYPYNYVKVGEQCPKVEDHWMNLWDNGKILHNKNEPNSLDGKGYTAYESERFHDNMDAFVKIIKTEVMNKGSVIAYIKAENVMGYEFSGKKVQNLCGDDTADHAVNIVGYGNYVNSEGEKKSYWIVRNSWGPYWGDEGYFKVDMYGPTHCHFNFIHSVVIFNVDLPMNNKTTKKESKIYDYYLKASPEFYHNLYFKNFNVGKKNLFSEKEDNENNKKLGNNYIIFGQDTAGSGQSGKESNTALESAGTSNEVSERVHVYHILKHIKDGKIRMGMRKYIDTQDVNKKHSCTRSYAFNPENYEKCVNLCNVNWKTCEEKTSPGLCLSKLDTNNECYFCYV |
| Enzyme Length | 989 |
| Uniprot Accession Number | P69193 |
| Absorption | |
| Active Site | ACT_SITE 754; /evidence=ECO:0000255|PROSITE-ProRule:PRU10089; ACT_SITE 779; /evidence=ECO:0000255|PROSITE-ProRule:PRU10090 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | 3.4.22.- |
| Enzyme Function | FUNCTION: Plays an essential role during the asexual blood stage development by controlling the kinetics of merozoite egress from host erythrocytes (By similarity). Specifically, prevents premature rupture of the parasitophorous vacuole and host erythrocyte membranes (By similarity). {ECO:0000250|UniProtKB:Q9TY95}.; FUNCTION: [p47]: May prevent merozoite phagocytosis by host monocytes via interaction with host VTN at the merozoite surface (PubMed:29567995). Plays a role in parasite growth (PubMed:12244052). {ECO:0000269|PubMed:12244052, ECO:0000269|PubMed:29567995}.; FUNCTION: [p50]: Protease activity is controversial. {ECO:0000250|UniProtKB:Q9TY95}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (7); Compositional bias (1); Disulfide bond (6); Glycosylation (3); Modified residue (3); Propeptide (1); Region (5); Signal peptide (1); Site (5) |
| Keywords | Cell membrane;Disulfide bond;Glycoprotein;Hydrolase;Malaria;Membrane;Phosphoprotein;Protease;Secreted;Signal;Thiol protease;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Serine-repeat antigen protein 5]: Parasitophorous vacuole {ECO:0000269|PubMed:12244052, ECO:0000269|PubMed:12421632}. Note=Secreted in large amount into the parasitophorous vacuole. {ECO:0000250|UniProtKB:Q9TY95}.; SUBCELLULAR LOCATION: [p18]: Secreted {ECO:0000269|PubMed:12421632}. Note=Secreted during merozoite egress from erythrocytes. {ECO:0000269|PubMed:12421632}.; SUBCELLULAR LOCATION: [p25n]: Secreted. Note=Secreted during merozoite egress from erythrocytes. {ECO:0000269|PubMed:12421632}.; SUBCELLULAR LOCATION: [p25c]: Secreted {ECO:0000269|PubMed:12421632}. Note=Secreted during merozoite egress from erythrocytes. {ECO:0000269|PubMed:12421632}.; SUBCELLULAR LOCATION: [p47]: Secreted {ECO:0000269|PubMed:12421632}. Cell membrane {ECO:0000250|UniProtKB:Q9TY95}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9TY95}; Extracellular side {ECO:0000250|UniProtKB:Q9TY95}. Note=Secreted during merozoite egress from erythrocytes (PubMed:12421632). Colocalizes at the merozoite surface with human VTN (By similarity). {ECO:0000250|UniProtKB:Q9TY95, ECO:0000269|PubMed:12421632}.; SUBCELLULAR LOCATION: [p50]: Secreted {ECO:0000269|PubMed:12421632}. Note=Secreted during merozoite egress from erythrocytes. {ECO:0000269|PubMed:12421632}.; SUBCELLULAR LOCATION: [p56]: Secreted {ECO:0000250|UniProtKB:Q9TY95}. Note=Secreted during egress from host erythrocytes. {ECO:0000250|UniProtKB:Q9TY95}. |
| Modified Residue | MOD_RES 167; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9TY95; MOD_RES 541; /note=Phosphothreonine; /evidence=ECO:0000250|UniProtKB:Q9TY95; MOD_RES 858; /note=Phosphoserine; /evidence=ECO:0000250|UniProtKB:Q9TY95 |
| Post Translational Modification | PTM: [p50]: Phosphorylation by CPK1/CDPK1 increases SERA5 protease activity towards a synthetic peptide in vitro. {ECO:0000250|UniProtKB:Q9TY95}.; PTM: Just prior to merozoite egress from host erythrocytes, proteolytically cleaved into multiple fragments (PubMed:12421632). Cleaved by SUB1 into p47 and p73, p73 is further cleaved by SUB1 into p56 and p18 and p56 is further processed into p50 by an unidentified protease (By similarity). p47 remains covalently associated with p18 via disulfide bond (By similarity). p47 can be processed into p25n and p25c by SUB1 (By similarity). p25c and p25n remain associated with p18 (By similarity). Proteolytic processing is essential for merozoite egress from host erythrocytes (By similarity). The cleavage of the propeptide to produce p50 is necessary for protease activity and to promote merozoite egress (By similarity). {ECO:0000250|UniProtKB:Q9TY95, ECO:0000269|PubMed:12421632}. |
| Signal Peptide | SIGNAL 1..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 111,095 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |