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Protein

Plasmepsin-1

Gene
N/A
Organism
Plasmodium falciparum
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

pH dependencei

Optimum pH is 4.5-5.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei157 – 1571PROSITE-ProRule annotation
Active sitei337 – 3371PROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, Hydrolase, Protease

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15375.
BRENDAi3.4.23.38. 4889.

Protein family/group databases

MEROPSiA01.022.

Names & Taxonomyi

Protein namesi
Recommended name:
Plasmepsin-1 (EC:3.4.23.38)
Alternative name(s):
Aspartic hemoglobinase I
PfAPG
OrganismiPlasmodium falciparum
Taxonomic identifieri5833 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)

Subcellular locationi

  • Vacuole

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Vacuole

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL4687.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 124Activation peptide1 PublicationPRO_0000025928
Signal peptidei1 – ?Sequence analysis
Chaini125 – 452328Plasmepsin-1PRO_0000025929Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi170 ↔ 175By similarity
Glycosylationi184 – 1841N-linked (GlcNAc...)Sequence analysis
Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence analysis
Glycosylationi326 – 3261N-linked (GlcNAc...)Sequence analysis
Disulfide bondi372 ↔ 408By similarity
Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP39898.
PRIDEiP39898.

Expressioni

Developmental stagei

Erythrocytic stages.

Interactioni

Protein-protein interaction databases

STRINGi5833.PF14_0076.

Chemistry

BindingDBiP39898.

Structurei

Secondary structure

1
452
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi127 – 1348Combined sources
Turni135 – 1373Combined sources
Beta strandi138 – 1458Combined sources
Turni146 – 1494Combined sources
Beta strandi150 – 1578Combined sources
Beta strandi162 – 1676Combined sources
Helixi175 – 1773Combined sources
Helixi183 – 1853Combined sources
Beta strandi190 – 1967Combined sources
Beta strandi205 – 21612Combined sources
Beta strandi219 – 23416Combined sources
Turni238 – 2403Combined sources
Beta strandi244 – 2485Combined sources
Helixi252 – 2543Combined sources
Helixi262 – 2687Combined sources
Beta strandi271 – 28010Combined sources
Beta strandi283 – 2875Combined sources
Beta strandi289 – 2957Combined sources
Helixi298 – 3003Combined sources
Beta strandi301 – 3099Combined sources
Turni313 – 3164Combined sources
Beta strandi317 – 3248Combined sources
Beta strandi327 – 33610Combined sources
Beta strandi341 – 3455Combined sources
Helixi347 – 3548Combined sources
Turni355 – 3584Combined sources
Beta strandi368 – 3714Combined sources
Beta strandi380 – 3834Combined sources
Beta strandi388 – 3914Combined sources
Helixi393 – 3964Combined sources
Beta strandi397 – 4015Combined sources
Beta strandi403 – 4053Combined sources
Beta strandi407 – 4148Combined sources
Beta strandi421 – 4244Combined sources
Helixi426 – 4316Combined sources
Beta strandi432 – 4376Combined sources
Turni438 – 4414Combined sources
Beta strandi442 – 4487Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LCRmodel-A78-452[»]
1LDUmodel-A73-452[»]
3QRVX-ray2.40A/B117-452[»]
3QS1X-ray3.10A/B/C/D117-452[»]
ProteinModelPortaliP39898.
SMRiP39898. Positions 78-452.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini139 – 446308Peptidase A1PROSITE-ProRule annotationAdd
BLAST

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. 1 hit.
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.

P39898-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSIKEDFS SAFAKNESAV NSSTFNNNMK TWKIQKRFQI LYVFFFLLIT
60 70 80 90 100
GALFYYLIDN VLFPKNKKIN EIMNTSKHVI IGFSIENSHD RIMKTVKQHR
110 120 130 140 150
LKNYIKESLK FFKTGLTQKP HLGNAGDSVT LNDVANVMYY GEAQIGDNKQ
160 170 180 190 200
KFAFIFDTGS ANLWVPSAQC NTIGCKTKNL YDSNKSKTYE KDGTKVEMNY
210 220 230 240 250
VSGTVSGFFS KDIVTIANLS FPYKFIEVTD TNGFEPAYTL GQFDGIVGLG
260 270 280 290 300
WKDLSIGSVD PVVVELKNQN KIEQAVFTFY LPFDDKHKGY LTIGGIEDRF
310 320 330 340 350
YEGQLTYEKL NHDLYWQVDL DLHFGNLTVE KATAIVDSGT SSITAPTEFL
360 370 380 390 400
NKFFEGLDVV KIPFLPLYIT TCNNPKLPTL EFRSATNVYT LEPEYYLQQI
410 420 430 440 450
FDFGISLCMV SIIPVDLNKN TFILGDPFMR KYFTVFDYDN HTVGFALAKK

KL
Length:452
Mass (Da):51,461
Last modified:November 1, 1995 - v2
Checksum:i8F8F8478F2F7D931
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75787 mRNA. Translation: CAA53432.1.
PIRiS41717.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75787 mRNA. Translation: CAA53432.1.
PIRiS41717.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LCRmodel-A78-452[»]
1LDUmodel-A73-452[»]
3QRVX-ray2.40A/B117-452[»]
3QS1X-ray3.10A/B/C/D117-452[»]
ProteinModelPortaliP39898.
SMRiP39898. Positions 78-452.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5833.PF14_0076.

Chemistry

BindingDBiP39898.
ChEMBLiCHEMBL4687.

Protein family/group databases

MEROPSiA01.022.

Proteomic databases

PaxDbiP39898.
PRIDEiP39898.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiKOG1339. Eukaryota.
ENOG410XNV7. LUCA.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15375.
BRENDAi3.4.23.38. 4889.

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. 1 hit.
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 nameiPLM1_PLAFA
AccessioniPrimary (citable) accession number: P39898
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 1, 1995
Last modified: April 13, 2016
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

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.