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P46925

- PLM2_PLAFA

UniProt

P46925 - PLM2_PLAFA

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Protein

Plasmepsin-2

Gene
N/A
Organism
Plasmodium falciparum
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei158 – 1581PROSITE-ProRule annotation
Active sitei338 – 3381PROSITE-ProRule annotation

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15374.

Protein family/group databases

MEROPSiA01.023.

Names & Taxonomyi

Protein namesi
Recommended name:
Plasmepsin-2 (EC:3.4.23.39)
Alternative name(s):
Aspartic hemoglobinase II
PFAPD
OrganismiPlasmodium falciparum
Taxonomic identifieri5833 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

Subcellular locationi

GO - Cellular componenti

  1. vacuole Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 124Activation peptidePRO_0000025930
Signal peptidei1 – ?Sequence Analysis
Chaini125 – 453329Plasmepsin-2PRO_0000025931Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi171 ↔ 176
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi373 ↔ 409
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi441 – 4411N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Expressioni

Developmental stagei

Erythrocytic stages.

Interactioni

Structurei

Secondary structure

1
453
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi80 – 878Combined sources
Helixi89 – 9911Combined sources
Helixi103 – 11311Combined sources
Turni114 – 1163Combined sources
Beta strandi118 – 1203Combined sources
Beta strandi127 – 1359Combined sources
Turni136 – 1383Combined sources
Beta strandi139 – 1468Combined sources
Turni147 – 1504Combined sources
Beta strandi151 – 1588Combined sources
Beta strandi164 – 1685Combined sources
Helixi176 – 1783Combined sources
Helixi184 – 1863Combined sources
Beta strandi191 – 20010Combined sources
Beta strandi202 – 21716Combined sources
Beta strandi220 – 23112Combined sources
Helixi233 – 2353Combined sources
Helixi238 – 2414Combined sources
Beta strandi246 – 2494Combined sources
Helixi253 – 2553Combined sources
Beta strandi256 – 2583Combined sources
Helixi263 – 2697Combined sources
Beta strandi272 – 2754Combined sources
Beta strandi277 – 2815Combined sources
Turni285 – 2873Combined sources
Beta strandi290 – 2967Combined sources
Helixi299 – 3013Combined sources
Beta strandi302 – 31312Combined sources
Turni314 – 3174Combined sources
Beta strandi318 – 3258Combined sources
Beta strandi328 – 33710Combined sources
Beta strandi343 – 3464Combined sources
Helixi348 – 3547Combined sources
Turni355 – 3573Combined sources
Beta strandi358 – 3625Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi369 – 3724Combined sources
Beta strandi381 – 3844Combined sources
Beta strandi389 – 3924Combined sources
Helixi394 – 3974Combined sources
Beta strandi398 – 4003Combined sources
Turni402 – 4043Combined sources
Beta strandi408 – 4114Combined sources
Beta strandi413 – 4153Combined sources
Beta strandi422 – 4254Combined sources
Helixi427 – 4326Combined sources
Beta strandi433 – 4386Combined sources
Turni439 – 4424Combined sources
Beta strandi443 – 4497Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4CKUX-ray1.85A/B/C/D/E/F125-453[»]
ProteinModelPortaliP46925.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46925.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG248684.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 1 hit.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46925-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDITVREHDF KHGFIKSNST FDGLNIDNSK NKKKIQKGFQ ILYVLLFCSV
60 70 80 90 100
MCGLFYYVYE NVWLQRDNEM NEILKNSEHL TIGFKVENAH DRILKTIKTH
110 120 130 140 150
KLKNYIKESV NFLNSGLTKT NYLGSSNDNI ELVDFQNIMF YGDAEVGDNQ
160 170 180 190 200
QPFTFILDTG SANLWVPSVK CTTAGCLTKH LYDSSKSRTY EKDGTKVEMN
210 220 230 240 250
YVSGTVSGFF SKDLVTVGNL SLPYKFIEVI DTNGFEPTYT ASTFDGILGL
260 270 280 290 300
GWKDLSIGSV DPIVVELKNQ NKIENALFTF YLPVHDKHTG FLTIGGIEER
310 320 330 340 350
FYEGPLTYEK LNHDLYWQIT LDAHVGNIML EKANCIVDSG TSAITVPTDF
360 370 380 390 400
LNKMLQNLDV IKVPFLPFYV TLCNNSKLPT FEFTSENGKY TLEPEYYLQH
410 420 430 440 450
IEDVGPGLCM LNIIGLDFPV PTFILGDPFM RKYFTVFDYD NHSVGIALAK

KNL
Length:453
Mass (Da):51,490
Last modified:November 1, 1995 - v1
Checksum:i0D78A8A65D0C80B5
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L10740 Genomic DNA. Translation: AAA68217.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L10740 Genomic DNA. Translation: AAA68217.1 . Different initiation.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J8J model - A 125-453 [» ]
1LEE X-ray 1.90 A 123-453 [» ]
1LF2 X-ray 1.80 A 123-453 [» ]
1LF3 X-ray 2.70 A 123-453 [» ]
1LF4 X-ray 1.90 A 123-453 [» ]
1M43 X-ray 2.40 A/B 123-453 [» ]
1ME6 X-ray 2.70 A/B 125-453 [» ]
1PFZ X-ray 1.85 A/B/C/D 77-453 [» ]
1SME X-ray 2.70 A/B 125-453 [» ]
1W6H X-ray 2.24 A/B 123-453 [» ]
1W6I X-ray 2.70 A/C 123-453 [» ]
1XDH X-ray 1.70 A/B 123-453 [» ]
1XE5 X-ray 2.40 A/B 125-453 [» ]
1XE6 X-ray 2.80 A/B 125-453 [» ]
2BJU X-ray 1.56 A 1-453 [» ]
2BL3 model - A 125-453 [» ]
2IGX X-ray 1.70 A 125-453 [» ]
2IGY X-ray 2.60 A/B 125-453 [» ]
2R9B X-ray 2.80 A/B 125-453 [» ]
3F9Q X-ray 1.90 A 125-453 [» ]
4CKU X-ray 1.85 A/B/C/D/E/F 125-453 [» ]
ProteinModelPortali P46925.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P46925.
ChEMBLi CHEMBL4414.
DrugBanki DB01218. Halofantrine.

Protein family/group databases

MEROPSi A01.023.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG248684.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-15374.

Miscellaneous databases

EvolutionaryTracei P46925.

Family and domain databases

Gene3Di 2.40.70.10. 2 hits.
InterProi IPR001461. Aspartic_peptidase.
IPR001969. Aspartic_peptidase_AS.
IPR021109. Peptidase_aspartic_dom.
[Graphical view ]
PANTHERi PTHR13683. PTHR13683. 1 hit.
Pfami PF00026. Asp. 1 hit.
[Graphical view ]
PRINTSi PR00792. PEPSIN.
SUPFAMi SSF50630. SSF50630. 1 hit.
PROSITEi PS00141. ASP_PROTEASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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. 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.

Entry informationi

Entry nameiPLM2_PLAFA
AccessioniPrimary (citable) accession number: P46925
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Caution

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

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3