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Protein
Submitted name:

M17 leucyl aminopeptidase

Gene

LAP

Organism
Plasmodium falciparum (isolate 3D7)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi374 – 3741Zinc 1Combined sources
Metal bindingi379 – 3791MagnesiumCombined sources
Metal bindingi379 – 3791Zinc 1Combined sources
Metal bindingi379 – 3791Zinc 2Combined sources
Metal bindingi399 – 3991Zinc 1Combined sources
Metal bindingi459 – 4591MagnesiumCombined sources
Metal bindingi459 – 4591Zinc 2Combined sources
Metal bindingi461 – 4611MagnesiumCombined sources
Metal bindingi461 – 4611Zinc 1Combined sources
Metal bindingi461 – 4611Zinc 2Combined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

AminopeptidaseImported, Hydrolase, Protease

Keywords - Ligandi

MagnesiumCombined sources, Metal-bindingCombined sources, ZincCombined sources

Enzyme and pathway databases

BRENDAi3.4.11.1. 4889.
3.4.11.20. 4889.

Protein family/group databases

MEROPSiM17.008.

Names & Taxonomyi

Protein namesi
Submitted name:
M17 leucyl aminopeptidaseImported (EC:3.4.11.1Imported)
Gene namesi
Name:LAPImported
ORF Names:PF14_0439Imported, PF3D7_1446200Imported
OrganismiPlasmodium falciparum (isolate 3D7)Imported
Taxonomic identifieri36329 [NCBI]
Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiidaePlasmodiumPlasmodium (Laverania)
Proteomesi
  • UP000001450 Componenti: Chromosome 14

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_1446200.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: GeneDB
Complete GO annotation...

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL1293313.

PTM / Processingi

Proteomic databases

PRIDEiQ8IL11.

PTM databases

SwissPalmiQ8IL11.

Interactioni

Protein-protein interaction databases

DIPiDIP-58533N.

Chemistry

BindingDBiQ8IL11.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KQXX-ray2.01A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
3KQZX-ray2.39A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
3KR4X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
3KR5X-ray2.56A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
3T8WX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
4K3NX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
4R6TX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
4R76X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
4R7MX-ray2.85A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
4X2TX-ray2.73A/B/C/D/E/F/G/H/I/J/K/L85-603[»]
ProteinModelPortaliQ8IL11.
SMRiQ8IL11. Positions 85-603.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IL11.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini457 – 4648CYTOSOL_APInterPro annotation

Phylogenomic databases

HOGENOMiHOG000243129.
InParanoidiQ8IL11.
KOiK01255.
PhylomeDBiQ8IL11.

Family and domain databases

HAMAPiMF_00181. Cytosol_peptidase_M17.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
[Graphical view]
PfamiPF00883. Peptidase_M17. 1 hit.
[Graphical view]
PRINTSiPR00481. LAMNOPPTDASE.
PROSITEiPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8IL11-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYFSSLCKFL PISEKEKIYL NIVKKRFCKS NIYYNNNNNN IINYNKRGLK
60 70 80 90 100
FYPFCNNLKK NINFVNINNK KGINFHSINK ERKMASEVPQ VVSLDPTSIP
110 120 130 140 150
IEYNTPIHDI KVQVYDIKGG CNVEEGLTIF LVNNPGKENG PVKISSKVND
160 170 180 190 200
KNVSEFLKDE NMEKFNVKLG TSKHFYMFND NKNSVAVGYV GCGSVADLSE
210 220 230 240 250
ADMKRVVLSL VTMLHDNKLS KLTVVFEINV DKNLFRFFLE TLFYEYMTDE
260 270 280 290 300
RFKSTDKNVN MEYIKHLGVY INNADTYKEE VEKARVYYFG TYYASQLIAA
310 320 330 340 350
PSNYCNPVSL SNAAVELAQK LNLEYKILGV KELEELKMGA YLSVGKGSMY
360 370 380 390 400
PNKFIHLTYK SKGDVKKKIA LVGKGITFDS GGYNLKAAPG SMIDLMKFDM
410 420 430 440 450
SGCAAVLGCA YCVGTLKPEN VEIHFLSAVC ENMVSKNSYR PGDIITASNG
460 470 480 490 500
KTIEVGNTDA EGRLTLADAL VYAEKLGVDY IVDIATLTGA MLYSLGTSYA
510 520 530 540 550
GVFGNNEELI NKILNSSKTS NEPVWWLPII NEYRATLNSK YADINNISSS
560 570 580 590 600
VKASSIVASL FLKEFVQNTA WAHIDIAGVS WNFKARKPKG FGVRLLTEFV

LNDAL
Length:605
Mass (Da):67,821
Last modified:March 1, 2003 - v1
Checksum:iCA30B9A341AB9F44
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014187 Genomic DNA. Translation: AAN37052.1.
LN999946 Genomic DNA. Translation: CZU00157.1.
RefSeqiXP_001348613.1. XM_001348577.1.

Genome annotation databases

EnsemblProtistsiPF14_0439:mRNA; PF14_0439:pep; PF14_0439.
GeneDBiPF3D7_1446200.1:pep.
GeneIDi812021.
KEGGipfa:PF14_0439.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014187 Genomic DNA. Translation: AAN37052.1.
LN999946 Genomic DNA. Translation: CZU00157.1.
RefSeqiXP_001348613.1. XM_001348577.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3KQXX-ray2.01A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
3KQZX-ray2.39A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
3KR4X-ray2.00A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
3KR5X-ray2.56A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
3T8WX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
4K3NX-ray2.00A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
4R6TX-ray2.60A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
4R76X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
4R7MX-ray2.85A/B/C/D/E/F/G/H/I/J/K/L84-605[»]
4X2TX-ray2.73A/B/C/D/E/F/G/H/I/J/K/L85-603[»]
ProteinModelPortaliQ8IL11.
SMRiQ8IL11. Positions 85-603.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58533N.

Chemistry

BindingDBiQ8IL11.
ChEMBLiCHEMBL1293313.

Protein family/group databases

MEROPSiM17.008.

PTM databases

SwissPalmiQ8IL11.

Proteomic databases

PRIDEiQ8IL11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsiPF14_0439:mRNA; PF14_0439:pep; PF14_0439.
GeneDBiPF3D7_1446200.1:pep.
GeneIDi812021.
KEGGipfa:PF14_0439.

Organism-specific databases

EuPathDBiPlasmoDB:PF3D7_1446200.

Phylogenomic databases

HOGENOMiHOG000243129.
InParanoidiQ8IL11.
KOiK01255.
PhylomeDBiQ8IL11.

Enzyme and pathway databases

BRENDAi3.4.11.1. 4889.
3.4.11.20. 4889.

Miscellaneous databases

EvolutionaryTraceiQ8IL11.

Family and domain databases

HAMAPiMF_00181. Cytosol_peptidase_M17.
InterProiIPR011356. Leucine_aapep/pepB.
IPR000819. Peptidase_M17_C.
IPR023042. Peptidase_M17_leu_NH2_pept.
[Graphical view]
PfamiPF00883. Peptidase_M17. 1 hit.
[Graphical view]
PRINTSiPR00481. LAMNOPPTDASE.
PROSITEiPS00631. CYTOSOL_AP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 3D7Imported and Isolate 3D7Imported.
  2. Wen N., Song Y., Chen R., Wu D., Song Y., Zhou Q.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 3D7Imported.
  3. Briggs B.G., Marchant A.D., Perkins A.J.
    Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 3D7Imported.
  4. "Structure of the Plasmodium falciparum M17 aminopeptidase and significance for the design of drugs targeting the neutral exopeptidases."
    McGowan S., Oellig C.A., Birru W.A., Caradoc-Davies T.T., Stack C.M., Lowther J., Skinner-Adams T., Mucha A., Kafarski P., Grembecka J., Trenholme K.R., Buckle A.M., Gardiner D.L., Dalton J.P., Whisstock J.C.
    Proc. Natl. Acad. Sci. U.S.A. 107:2449-2454(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 84-605 IN COMPLEX WITH MAGNESIUM AND ZINC.
  5. "Bestatin-based chemical biology strategy reveals distinct roles for malaria M1- and M17-family aminopeptidases."
    Harbut M.B., Velmourougane G., Dalal S., Reiss G., Whisstock J.C., Onder O., Brisson D., McGowan S., Klemba M., Greenbaum D.C.
    Proc. Natl. Acad. Sci. U.S.A. 108:E526-E534(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 84-605 IN COMPLEX WITH ZINC.
  6. "Synthesis and structure-activity relationships of phosphonic arginine mimetics as inhibitors of the M1 and M17 aminopeptidases from Plasmodium falciparum."
    Kannan Sivaraman K., Paiardini A., Sienczyk M., Ruggeri C., Oellig C.A., Dalton J.P., Scammells P.J., Drag M., McGowan S.
    J. Med. Chem. 56:5213-5217(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 84-605 IN COMPLEX WITH ZINC.
  7. "Two-pronged attack: dual inhibition of Plasmodium falciparum M1 and M17 metalloaminopeptidases by a novel series of hydroxamic acid-based inhibitors."
    Mistry S.N., Drinkwater N., Ruggeri C., Sivaraman K.K., Loganathan S., Fletcher S., Drag M., Paiardini A., Avery V.M., Scammells P.J., McGowan S.
    J. Med. Chem. 57:9168-9183(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 84-605 IN COMPLEX WITH ZINC.
  8. "X-ray crystal structures of an orally available aminopeptidase inhibitor, Tosedostat, bound to anti-malarial drug targets PfA-M1 and PfA-M17."
    Drinkwater N., Bamert R.S., Sivaraman K.K., Paiardini A., McGowan S.
    Proteins 83:789-795(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.73 ANGSTROMS) OF 85-603 IN COMPLEX WITH ZINC.

Entry informationi

Entry nameiQ8IL11_PLAF7
AccessioniPrimary (citable) accession number: Q8IL11
Entry historyi
Integrated into UniProtKB/TrEMBL: March 1, 2003
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteome, Reference proteomeImported

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.