Q76NL8 · FCLN_PLAF7
- ProteinFalcilysin
- GeneFLN
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1193 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
In the food vacuole, acts downstream of proteases plasmepsins PMI and PMII and falcipains during the catabolism of host hemoglobin by cleaving peptide fragments of alpha and beta hemoglobin subunits generated by PMI and PMII and falcipains (PubMed:17074076).
In the apicoplast, degrades apicoplast transit peptides after their cleavage (PubMed:17074076).
Prefers bulky hydrophobic amino acids in the P1' position at both acidic and neutral pH (By similarity).
At P2', prefers hydrophobic residues at acidic pH; at neutral pH, these same residues are abundant but prefers Arg (By similarity).
At P3', prefers hydrophobic residues, especially Met, at both pH conditions. At P4' and P5', prefers acidic residues at acidic pH, however, at neutral pH, the enzyme is less selective at these positions (By similarity).
The optimal site cleavage at acidic pH is YNEHS-|-FFMEE and, at neutral pH, MKRHS-|-FRMRG (By similarity).
In the apicoplast, degrades apicoplast transit peptides after their cleavage (PubMed:17074076).
Prefers bulky hydrophobic amino acids in the P1' position at both acidic and neutral pH (By similarity).
At P2', prefers hydrophobic residues at acidic pH; at neutral pH, these same residues are abundant but prefers Arg (By similarity).
At P3', prefers hydrophobic residues, especially Met, at both pH conditions. At P4' and P5', prefers acidic residues at acidic pH, however, at neutral pH, the enzyme is less selective at these positions (By similarity).
The optimal site cleavage at acidic pH is YNEHS-|-FFMEE and, at neutral pH, MKRHS-|-FRMRG (By similarity).
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apicoplast | |
Cellular Component | food vacuole | |
Cellular Component | vacuolar membrane | |
Molecular Function | metal ion binding | |
Molecular Function | metalloendopeptidase activity | |
Biological Process | hemoglobin catabolic process | |
Biological Process | protein processing |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameFalcilysin
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ76NL8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Vacuole membrane ; Peripheral membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000454646 | 1-1193 | UniProt | Falcilysin | |||
Sequence: MNLTKLMKVIGYINIITNCVQSFTNRADKKRYNVFAKSFINTINTNLYTFKAVMSKTPEWIHEKSPKHNSYDIIEKRYNEEFKMTYTVYQHKKAKTQVISLGTNDPLDVEQAFAFYVKTLTHSGKGIPHILEHSVLSGSKNYNYKNSIGLLEKGTLHTHLNAYTFNDRTVYMAGSMNNKDFFNIMGVYMDSVFQPNVLENKYIFETEGWTYEVEKLKEDEKGKAEIPQMKDYKVSFNGIVYNEMKGALSSPLEDLYHEEMKYMFPDNVHSNNSGGDPKEITNLTYEEFKEFYYKNYNPKKVKVFFFSKNNPTELLNFVDQYLGQLDYSKYRDDAVESVEYQTYKKGPFYIKKKYGDHSEEKENLVSVAWLLNPKVDKTNNHNNNHSNNQSSENNGYSNGSHSSDLSLENPTDYFVLLIINNLLIHTPESVLYKALTDCGLGNNVIDRGLNDSLVQYIFSIGLKGIKRNNEKIKNFDKVHYEVEDVIMNALKKVVKEGFNKSAVEASINNIEFILKEANLKTSKSIDFVFEMTSKLNYNRDPLLIFEFEKYLNIVKNKIKNEPMYLEKFVEKHFINNAHRSVILLEGDENYAQEQENLEKQELKKRIENFNEQEKEQVIKNFEELSKYKNAEESPEHLNKFPIISISDLNKKTLEVPVNVYFTNINENNNIMETYNKLKTNEHMLKDNMDVFLKKYVLKNDKHNTNNNNNNNNNMDYSFTETKYEGNVPILVYEMPTTGIVYLQFVFSLDHLTVDELAYLNLFKTLILENKTNKRSSEDFVILREKNIGSMSANVALYSKDDHLNVTDKYNAQALFNLEMHVLSHKCNDALNIALEAVKESDFSNKKKVIDILKRKINGMKTTFSEKGYAILMKYVKAHLNSKHYAHNIIYGYENYLKLQEQLELAENDFKTLENILVRIRNKIFNKKNLMVSVTSDYGALKHLFVNSNESLKNLVSYFEENDKYINDMQNKVNDPTVMGWNEEIKSKKLFDEEKVKKEFFVLPTFVNSVSMSGILFKPGEYLDPSFTVIVAALKNSYLWDTVRGLNGAYGVFADIEYDGSVVFLSARDPNLEKTLATFRESAKGLRKMADTMTENDLLRYIINTIGTIDKPRRGIELSKLSFLRLISNESEQDRVEFRKRIMNTKKEDFYKFADLLESKVNEFEKNIVIITTKEKANEYIANVDGEFKKVLIE | |||||||
Modified residue (large scale data) | 633 | PTMeXchange | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 776 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Does not require processing for targeting to the food vacuole or maturation.
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed during the asexual blood stage; expression begins at the late ring, early trophozoite stage, increases in the mid-trophozoite stage, and persists throughout the schizont stage (at protein level).
Interaction
Subunit
Monomer (By similarity).
Component of the hemozoin formation complex (HFC) composed of falcipains FP2A and/or FP2B, plasmepsins PMII, PMIII/HAP and PMIV, heme detoxifying protein HDP and falcilysin FLN (PubMed:23471987).
The HFC complex is involved in hemoglobin degradation and detoxification of heme in the food vacuole during the asexual blood stage (PubMed:23471987).
Component of the hemozoin formation complex (HFC) composed of falcipains FP2A and/or FP2B, plasmepsins PMII, PMIII/HAP and PMIV, heme detoxifying protein HDP and falcilysin FLN (PubMed:23471987).
The HFC complex is involved in hemoglobin degradation and detoxification of heme in the food vacuole during the asexual blood stage (PubMed:23471987).
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 376-404 | Disordered | ||||
Sequence: DKTNNHNNNHSNNQSSENNGYSNGSHSSD | ||||||
Coiled coil | 583-619 | |||||
Sequence: LLEGDENYAQEQENLEKQELKKRIENFNEQEKEQVIK |
Sequence similarities
Belongs to the peptidase M16 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,193
- Mass (Da)138,863
- Last updated2004-07-05 v1
- ChecksumDBA1FC548ED5056A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF123458 EMBL· GenBank· DDBJ | AAF06062.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL844509 EMBL· GenBank· DDBJ | CAD52728.1 EMBL· GenBank· DDBJ | Genomic DNA |