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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)DescriptionActionsGraphical viewLength
Active sitei157PROSITE-ProRule annotation1
Active sitei337PROSITE-ProRule annotation1

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 databases

ChEMBLiCHEMBL4687.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_0000025928? – 124Activation peptide1 Publication
Signal peptidei1 – ?Sequence analysis
ChainiPRO_0000025929125 – 452Plasmepsin-1Add BLAST328

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi170 ↔ 175By similarity
Glycosylationi184N-linked (GlcNAc...)Sequence analysis1
Glycosylationi218N-linked (GlcNAc...)Sequence analysis1
Glycosylationi326N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi372 ↔ 408By similarity
Glycosylationi440N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP39898.

Expressioni

Developmental stagei

Erythrocytic stages.

Interactioni

Protein-protein interaction databases

STRINGi5833.PF14_0076.

Chemistry databases

BindingDBiP39898.

Structurei

Secondary structure

1452
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi127 – 134Combined sources8
Turni135 – 137Combined sources3
Beta strandi138 – 145Combined sources8
Turni146 – 149Combined sources4
Beta strandi150 – 157Combined sources8
Beta strandi162 – 167Combined sources6
Helixi175 – 177Combined sources3
Helixi183 – 185Combined sources3
Beta strandi190 – 196Combined sources7
Beta strandi205 – 216Combined sources12
Beta strandi219 – 234Combined sources16
Turni238 – 240Combined sources3
Beta strandi244 – 248Combined sources5
Helixi252 – 254Combined sources3
Helixi262 – 268Combined sources7
Beta strandi271 – 280Combined sources10
Beta strandi283 – 287Combined sources5
Beta strandi289 – 295Combined sources7
Helixi298 – 300Combined sources3
Beta strandi301 – 309Combined sources9
Turni313 – 316Combined sources4
Beta strandi317 – 324Combined sources8
Beta strandi327 – 336Combined sources10
Beta strandi341 – 345Combined sources5
Helixi347 – 354Combined sources8
Turni355 – 358Combined sources4
Beta strandi368 – 371Combined sources4
Beta strandi380 – 383Combined sources4
Beta strandi388 – 391Combined sources4
Helixi393 – 396Combined sources4
Beta strandi397 – 401Combined sources5
Beta strandi403 – 405Combined sources3
Beta strandi407 – 414Combined sources8
Beta strandi421 – 424Combined sources4
Helixi426 – 431Combined sources6
Beta strandi432 – 437Combined sources6
Turni438 – 441Combined sources4
Beta strandi442 – 448Combined sources7

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini139 – 446Peptidase 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. 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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LCRmodel-A78-452[»]
1LDUmodel-A73-452[»]
3QRVX-ray2.40A/B117-452[»]
3QS1X-ray3.10A/B/C/D117-452[»]
ProteinModelPortaliP39898.
SMRiP39898.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5833.PF14_0076.

Chemistry databases

BindingDBiP39898.
ChEMBLiCHEMBL4687.

Protein family/group databases

MEROPSiA01.022.

Proteomic databases

PaxDbiP39898.

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: November 2, 2016
This is version 102 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.