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P46925

- PLM2_PLAFA

UniProt

P46925 - PLM2_PLAFA

Protein

Plasmepsin-2

Gene
N/A
Organism
Plasmodium falciparum
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    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 – 1581PROSITE-ProRule annotation
    Active sitei338 – 3381PROSITE-ProRule annotation

    GO - Molecular functioni

    1. aspartic-type endopeptidase activity Source: UniProtKB-KW

    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

    Keywords - Cellular componenti

    Vacuole

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46925.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase A1 family.Curated

    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: October 1, 2014
    This is version 88 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

    External Data

    Dasty 3