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P46925 (PLM2_PLAFA) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Plasmepsin-2

EC=3.4.23.39
Alternative name(s):
Aspartic hemoglobinase II
PFAPD
OrganismPlasmodium falciparum
Taxonomic identifier5833 [NCBI]
Taxonomic lineageEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Protein attributes

Sequence length453 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves small molecules substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO2)-Ser-Phe-Pro-Thr.

Subcellular location

Vacuole.

Developmental stage

Erythrocytic stages.

Sequence similarities

Belongs to the peptidase A1 family.

Caution

It is uncertain whether Met-1 or Met-51 is the initiator.

Sequence caution

The sequence AAA68217.1 differs from that shown. Reason: Erroneous initiation.

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_0000025930
Chain125 – 453329Plasmepsin-2
PRO_0000025931

Sites

Active site1581 By similarity
Active site3381 By similarity

Amino acid modifications

Glycosylation2191N-linked (GlcNAc...) Potential
Glycosylation3741N-linked (GlcNAc...) Potential
Glycosylation4411N-linked (GlcNAc...) Potential
Disulfide bond171 ↔ 176
Disulfide bond373 ↔ 409

Secondary structure

.................................................................................... 453
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P46925 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 0D78A8A65D0C80B5

FASTA45351,490
        10         20         30         40         50         60 
MDITVREHDF KHGFIKSNST FDGLNIDNSK NKKKIQKGFQ ILYVLLFCSV MCGLFYYVYE 

        70         80         90        100        110        120 
NVWLQRDNEM NEILKNSEHL TIGFKVENAH DRILKTIKTH KLKNYIKESV NFLNSGLTKT 

       130        140        150        160        170        180 
NYLGSSNDNI ELVDFQNIMF YGDAEVGDNQ QPFTFILDTG SANLWVPSVK CTTAGCLTKH 

       190        200        210        220        230        240 
LYDSSKSRTY EKDGTKVEMN YVSGTVSGFF SKDLVTVGNL SLPYKFIEVI DTNGFEPTYT 

       250        260        270        280        290        300 
ASTFDGILGL GWKDLSIGSV DPIVVELKNQ NKIENALFTF YLPVHDKHTG FLTIGGIEER 

       310        320        330        340        350        360 
FYEGPLTYEK LNHDLYWQIT LDAHVGNIML EKANCIVDSG TSAITVPTDF LNKMLQNLDV 

       370        380        390        400        410        420 
IKVPFLPFYV TLCNNSKLPT FEFTSENGKY TLEPEYYLQH IEDVGPGLCM LNIIGLDFPV 

       430        440        450 
PTFILGDPFM RKYFTVFDYD NHSVGIALAK KNL 

« Hide

References

[1]"Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum."
Dame J.B., Reddy G.R., Yowell C.A., Dunn B.M., Kay J., Berry C.
Mol. Biochem. Parasitol. 64:177-190(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, 3D-STRUCTURE MODELING.
Strain: HB3.
[2]"Structure and inhibition of plasmepsin II, a hemoglobin-degrading enzyme from Plasmodium falciparum."
Silva A.M., Lee A.Y., Gulnik S.V., Maier P., Collins J., Bhat T.N., Collins P.J., Cachau R.E., Luker K.E., Gluzman I.Y., Francis S.E., Oksman A., Goldberg D.E., Erickson J.W.
Proc. Natl. Acad. Sci. U.S.A. 93:10034-10039(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
[3]"Crystal structure of the novel aspartic proteinase zymogen proplasmepsin II from Plasmodium falciparum."
Bernstein N.K., Cherney M.M., Loetscher H., Ridley R.G., James M.N.
Nat. Struct. Biol. 6:32-37(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF ZYMOGEN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10740 Genomic DNA. Translation: AAA68217.1. Different initiation.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J8Jmodel-A125-453[»]
1LEEX-ray1.90A123-453[»]
1LF2X-ray1.80A123-453[»]
1LF3X-ray2.70A123-453[»]
1LF4X-ray1.90A123-453[»]
1M43X-ray2.40A/B123-453[»]
1ME6X-ray2.70A/B125-453[»]
1PFZX-ray1.85A/B/C/D77-453[»]
1SMEX-ray2.70A/B125-453[»]
1W6HX-ray2.24A/B123-453[»]
1W6IX-ray2.70A/C123-453[»]
1XDHX-ray1.70A/B123-453[»]
1XE5X-ray2.40A/B125-453[»]
1XE6X-ray2.80A/B125-453[»]
2BJUX-ray1.56A1-453[»]
2BL3model-A125-453[»]
2IGXX-ray1.70A125-453[»]
2IGYX-ray2.60A/B125-453[»]
2R9BX-ray2.80A/B125-453[»]
3F9QX-ray1.90A125-453[»]
ProteinModelPortalP46925.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP46925.
ChEMBLCHEMBL4414.

Protein family/group databases

MEROPSA01.023.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG248684.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15374.

Family and domain databases

Gene3D2.40.70.10. 2 hits.
InterProIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERPTHR13683. PTHR13683. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. SSF50630. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP46925.

Entry information

Entry namePLM2_PLAFA
AccessionPrimary (citable) accession number: P46925
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: December 11, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references