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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: 4 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 – 1581 By similarity
Active sitei338 – 3381 By similarity

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-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Vacuole

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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

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.

Miscellaneous databases

EvolutionaryTraceiP46925.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase A1 family.

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

MDITVREHDF KHGFIKSNST FDGLNIDNSK NKKKIQKGFQ ILYVLLFCSV    50
MCGLFYYVYE NVWLQRDNEM NEILKNSEHL TIGFKVENAH DRILKTIKTH 100
KLKNYIKESV NFLNSGLTKT NYLGSSNDNI ELVDFQNIMF YGDAEVGDNQ 150
QPFTFILDTG SANLWVPSVK CTTAGCLTKH LYDSSKSRTY EKDGTKVEMN 200
YVSGTVSGFF SKDLVTVGNL SLPYKFIEVI DTNGFEPTYT ASTFDGILGL 250
GWKDLSIGSV DPIVVELKNQ NKIENALFTF YLPVHDKHTG FLTIGGIEER 300
FYEGPLTYEK LNHDLYWQIT LDAHVGNIML EKANCIVDSG TSAITVPTDF 350
LNKMLQNLDV IKVPFLPFYV TLCNNSKLPT FEFTSENGKY TLEPEYYLQH 400
IEDVGPGLCM LNIIGLDFPV PTFILGDPFM RKYFTVFDYD NHSVGIALAK 450
KNL 453
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.

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: September 3, 2014
This is version 87 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.

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

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