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P39898 (PLM1_PLAFA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Plasmepsin-1
EC=3.4.23.38
Alternative name(s):
Aspartic hemoglobinase I
PfAPG
OrganismPlasmodium falciparum
Taxonomic identifier5833 [NCBI]
Taxonomic lineageEukaryota › Alveolata › Apicomplexa › Aconoidasida › Haemosporida › Plasmodium › Plasmodium (Laverania)

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Catalytic activity

Hydrolysis of the 33-Phe-|-Leu-34 bond in the alpha-chain of hemoglobin, leading to denaturation of molecule.

Subcellular location

Vacuole. Note: Could be first anchored to the membrane through its propeptide before being released.

Developmental stage

Erythrocytic stages.

Sequence similarities

Belongs to the peptidase A1 family.

Biophysicochemical properties

pH dependence:

Optimum pH is 4.5-5.

Ontologies

Keywords
   Cellular componentVacuole
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentvacuole

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – ? Potential
Propeptide? – 124Activation peptidePRO_0000025928
Chain125 – 452328Plasmepsin-1
PRO_0000025929

Sites

Active site1571 By similarity
Active site3371 By similarity

Amino acid modifications

Glycosylation1841N-linked (GlcNAc...) Potential
Glycosylation2181N-linked (GlcNAc...) Potential
Glycosylation3261N-linked (GlcNAc...) Potential
Glycosylation4401N-linked (GlcNAc...) Potential
Disulfide bond170 ↔ 175 By similarity
Disulfide bond372 ↔ 408 By similarity

Secondary structure

1 ........................................................................... 452
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39898 [UniParc].

Last modified November 1, 1995. Version 2.
Checksum: 8F8F8478F2F7D931

FASTA45251,461
        10         20         30         40         50         60 
MALSIKEDFS SAFAKNESAV NSSTFNNNMK TWKIQKRFQI LYVFFFLLIT GALFYYLIDN 

        70         80         90        100        110        120 
VLFPKNKKIN EIMNTSKHVI IGFSIENSHD RIMKTVKQHR LKNYIKESLK FFKTGLTQKP 

       130        140        150        160        170        180 
HLGNAGDSVT LNDVANVMYY GEAQIGDNKQ KFAFIFDTGS ANLWVPSAQC NTIGCKTKNL 

       190        200        210        220        230        240 
YDSNKSKTYE KDGTKVEMNY VSGTVSGFFS KDIVTIANLS FPYKFIEVTD TNGFEPAYTL 

       250        260        270        280        290        300 
GQFDGIVGLG WKDLSIGSVD PVVVELKNQN KIEQAVFTFY LPFDDKHKGY LTIGGIEDRF 

       310        320        330        340        350        360 
YEGQLTYEKL NHDLYWQVDL DLHFGNLTVE KATAIVDSGT SSITAPTEFL NKFFEGLDVV 

       370        380        390        400        410        420 
KIPFLPLYIT TCNNPKLPTL EFRSATNVYT LEPEYYLQQI FDFGISLCMV SIIPVDLNKN 

       430        440        450 
TFILGDPFMR KYFTVFDYDN HTVGFALAKK KL

« Hide

References

[1]"Molecular characterization and inhibition of a Plasmodium falciparum aspartic hemoglobinase."
Francis S.E., Gluzman I.Y., Oksman A., Knickerbocker A., Mueller R., Bryant M.L., Sherman D.R., Russell D.G., Goldberg D.E.
EMBO J. 13:306-317(1994) [PubMed: 8313875] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: FAF-2.
[2]"Hemoglobin degradation in the human malaria pathogen Plasmodium falciparum: a catabolic pathway initiated by a specific aspartic protease."
Goldberg D.E., Slater A.F.G., Beavis R., Chait B., Cerami A., Henderson G.B.
J. Exp. Med. 173:961-969(1991) [PubMed: 2007860] [Abstract]
Cited for: PROTEIN SEQUENCE OF 125-146.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X75787 mRNA. Translation: CAA53432.1.
PIRS41717.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LCRmodel-A78-452[»]
1LDUmodel-A73-452[»]
3QRVX-ray2.40A/B117-452[»]
3QS1X-ray3.10A/B/C/D117-452[»]
ProteinModelPortalP39898.
ModBaseSearch...

Protein family/group databases

MEROPSA01.022.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsPF14_0076:mRNA; PF14_0076:pep; PF14_0076.

Phylogenomic databases

eggNOGKOG1339.
PhylomeDBP39898.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15375.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. Pept_Aspartic. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP39898.

Entry information

Entry namePLM1_PLAFA
AccessionPrimary (citable) accession number: P39898
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: November 16, 2011
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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