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Protein

Plasmepsin-2

Gene
N/A
Organism
Plasmodium falciparum
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Active sitei158PROSITE-ProRule annotation1
Active sitei338PROSITE-ProRule annotation1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15374.
BRENDAi3.4.23.39. 4889.

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 lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL4414.
DrugBankiDB01218. Halofantrine.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_0000025930? – 124Activation peptide
Signal peptidei1 – ?Sequence analysis
ChainiPRO_0000025931125 – 453Plasmepsin-2Add BLAST329

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi171 ↔ 176
Glycosylationi219N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi373 ↔ 409
Glycosylationi374N-linked (GlcNAc...)Sequence analysis1
Glycosylationi441N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP46925.

Expressioni

Developmental stagei

Erythrocytic stages.

Interactioni

Protein-protein interaction databases

STRINGi5833.PF14_0077.

Chemistry databases

BindingDBiP46925.

Structurei

Secondary structure

1453
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi80 – 87Combined sources8
Helixi89 – 99Combined sources11
Helixi103 – 113Combined sources11
Turni114 – 116Combined sources3
Beta strandi118 – 120Combined sources3
Beta strandi127 – 135Combined sources9
Turni136 – 138Combined sources3
Beta strandi139 – 146Combined sources8
Turni147 – 150Combined sources4
Beta strandi151 – 158Combined sources8
Beta strandi164 – 168Combined sources5
Helixi176 – 178Combined sources3
Helixi184 – 186Combined sources3
Beta strandi191 – 200Combined sources10
Beta strandi202 – 217Combined sources16
Beta strandi220 – 231Combined sources12
Helixi233 – 235Combined sources3
Helixi238 – 241Combined sources4
Beta strandi246 – 249Combined sources4
Helixi253 – 255Combined sources3
Beta strandi256 – 258Combined sources3
Helixi263 – 269Combined sources7
Beta strandi272 – 275Combined sources4
Beta strandi277 – 281Combined sources5
Turni285 – 287Combined sources3
Beta strandi290 – 296Combined sources7
Helixi299 – 301Combined sources3
Beta strandi302 – 313Combined sources12
Turni314 – 317Combined sources4
Beta strandi318 – 325Combined sources8
Beta strandi328 – 337Combined sources10
Beta strandi343 – 346Combined sources4
Helixi348 – 354Combined sources7
Turni355 – 357Combined sources3
Beta strandi358 – 362Combined sources5
Beta strandi364 – 366Combined sources3
Beta strandi369 – 372Combined sources4
Beta strandi381 – 384Combined sources4
Beta strandi389 – 392Combined sources4
Helixi394 – 397Combined sources4
Beta strandi398 – 400Combined sources3
Turni402 – 404Combined sources3
Beta strandi408 – 411Combined sources4
Beta strandi413 – 415Combined sources3
Beta strandi422 – 425Combined sources4
Helixi427 – 432Combined sources6
Beta strandi433 – 438Combined sources6
Turni439 – 442Combined sources4
Beta strandi443 – 449Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4Y6MX-ray2.27A/B/C125-453[»]
4YA8X-ray3.30A/B/C/D125-453[»]
4Z22X-ray2.62A/B125-453[»]
5BWYX-ray2.64A78-453[»]
ProteinModelPortaliP46925.
SMRiP46925.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46925.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini140 – 447Peptidase A1PROSITE-ProRule annotationAdd BLAST308

Sequence similaritiesi

Belongs to the peptidase A1 family.Curated
Contains 1 peptidase A1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 2 hits.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[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 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10740 Genomic DNA. Translation: AAA68217.1. Different initiation.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10740 Genomic DNA. Translation: AAA68217.1. Different initiation.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4Y6MX-ray2.27A/B/C125-453[»]
4YA8X-ray3.30A/B/C/D125-453[»]
4Z22X-ray2.62A/B125-453[»]
5BWYX-ray2.64A78-453[»]
ProteinModelPortaliP46925.
SMRiP46925.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5833.PF14_0077.

Chemistry databases

BindingDBiP46925.
ChEMBLiCHEMBL4414.
DrugBankiDB01218. Halofantrine.

Protein family/group databases

MEROPSiA01.023.

Proteomic databases

PaxDbiP46925.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15374.
BRENDAi3.4.23.39. 4889.

Miscellaneous databases

EvolutionaryTraceiP46925.

Family and domain databases

Gene3Di2.40.70.10. 2 hits.
InterProiIPR001461. Aspartic_peptidase_A1.
IPR001969. Aspartic_peptidase_AS.
IPR033121. PEPTIDASE_A1.
IPR021109. Peptidase_aspartic_dom.
[Graphical view]
PANTHERiPTHR13683. PTHR13683. 2 hits.
PfamiPF00026. Asp. 1 hit.
[Graphical view]
PRINTSiPR00792. PEPSIN.
SUPFAMiSSF50630. SSF50630. 1 hit.
PROSITEiPS00141. ASP_PROTEASE. 2 hits.
PS51767. PEPTIDASE_A1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 99 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.