Q7KQM4 (PLM1_PLAF7) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 49.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Plasmepsin-1 EC=3.4.23.38 Alternative name(s): Aspartic hemoglobinase I PfAPG | ||
| Gene names |
| ||
| Organism | Plasmodium falciparum (isolate 3D7) | ||
| Taxonomic identifier | 36329 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania) |
Protein attributes
| Sequence length | 452 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Participates in the digestion of the host hemoglobin. Initial cleavage at the hinge region of hemoglobin, than cleaves at other sites, leading to denaturation of the molecule and to further degradation By similarity. |
| Catalytic activity | Hydrolysis of the 33-Phe-|-Leu-34 bond in the alpha-chain of hemoglobin, leading to denaturation of molecule. |
| Subcellular location | Vacuole By similarity. Note: Could be first anchored to the membrane through its propeptide before being released By similarity. |
| Developmental stage | Erythrocytic stages. |
| Sequence similarities | Belongs to the peptidase A1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Vacuole |
| Domain | Signal |
| Molecular function | Aspartyl protease Hydrolase Protease |
| PTM | Disulfide bond Glycoprotein Zymogen |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | hemoglobin catabolic process Traceable author statement. Source: GeneDB_Pfalciparum proteolysisInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | food vacuole Traceable author statement. Source: GeneDB_Pfalciparum |
| Molecular function | aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – ? | Potential | |||||||||
| Propeptide | ? – 124 | Activation peptide By similarity | PRO_0000233400 | ||||||||
| Chain | 125 – 452 | 328 | Plasmepsin-1 | PRO_0000233401 | |||||||
Sites | |||||||||||
| Active site | 157 | 1 | By similarity | ||||||||
| Active site | 337 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 184 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 218 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 326 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 440 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 170 ↔ 175 | By similarity | |||||||||
| Disulfide bond | 372 ↔ 408 | By similarity | |||||||||
Sequences
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References
| [1] | "Genome sequence of the human malaria parasite Plasmodium falciparum." Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W., Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D., Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S. Barrell B.G.Nature 419:498-511(2002) [PubMed: 12368864] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE014187 Genomic DNA. Translation: AAN36688.1. |
| RefSeq | XP_001348249.1. XM_001348213.1. |
3D structure databases | |
| ProteinModelPortal | Q7KQM4. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblProtists | PF14_0076:mRNA; PF14_0076:pep; PF14_0076. |
| GeneID | 811658. |
| KEGG | pfa:PF14_0076. |
| NMPDR | fig|36329.1.peg.1951. |
Organism-specific databases | |
| EuPathDB | EupathDB:PF14_0076. |
Phylogenomic databases | |
| GeneTree | EPrGT00050000002995. |
| HOGENOM | HBG629136. |
| OMA | SYITGPA. |
| ProtClustDB | PTZ00147. |
Family and domain databases | |
| InterPro | IPR001461. Peptidase_A1. IPR021109. Peptidase_aspartic. IPR001969. Peptidase_aspartic_AS. IPR009007. Peptidase_aspartic_catalytic. [Graphical view] |
| Gene3D | G3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits. |
| KO | K06007. |
| PANTHER | PTHR13683. Peptidase_A1. 1 hit. |
| Pfam | PF00026. Asp. 1 hit. [Graphical view] |
| PRINTS | PR00792. PEPSIN. |
| SUPFAM | SSF50630. Pept_Aspartic. 1 hit. |
| PROSITE | PS00141. ASP_PROTEASE. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| BindingDB | Q7KQM4. |
Entry information
| Entry name | PLM1_PLAF7 | ||||||||
| Accession | Primary (citable) accession number: Q7KQM4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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