PLM7_PLAFO
ID PLM7_PLAFO Reviewed; 450 AA.
AC A0A2I0BRF1;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Plasmepsin VII {ECO:0000312|EMBL:PKC43661.1};
DE Short=PfPMVII {ECO:0000303|PubMed:26911483};
DE EC=3.4.23.- {ECO:0000305};
DE AltName: Full=Plasmepsin 7 {ECO:0000305};
DE Flags: Precursor;
GN Name=PMVII {ECO:0000303|PubMed:26911483};
GN ORFNames=CK202_4891 {ECO:0000312|EMBL:PKC43661.1};
OS Plasmodium falciparum (isolate NF54).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5843 {ECO:0000312|Proteomes:UP000232684};
RN [1] {ECO:0000312|Proteomes:UP000232684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NF54 {ECO:0000312|Proteomes:UP000232684};
RA Bryant J.M., Baumgarten S., Scheidig-Benatar C., Scherf A.;
RT "Plasmodium falciparum NF54 genome assembly.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND BIOTECHNOLOGY.
RX PubMed=26911483; DOI=10.1186/s12936-016-1161-5;
RA Li F., Bounkeua V., Pettersen K., Vinetz J.M.;
RT "Plasmodium falciparum ookinete expression of plasmepsin VII and plasmepsin
RT X.";
RL Malar. J. 15:111-111(2016).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26911483}.
CC -!- DEVELOPMENTAL STAGE: Expressed in zygote and ookinete (at protein
CC level) (PubMed:26911483). Expressed in gametocytes, zygote and ookinete
CC (PubMed:26911483). {ECO:0000269|PubMed:26911483}.
CC -!- BIOTECHNOLOGY: High doses of antibodies against PMVII partially reduce
CC infectivity in A.stephensi mosquito. {ECO:0000269|PubMed:26911483}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC -!- CAUTION: It is unclear if PMVII is glycosylated as other members of the
CC same enzyme family, i.e. PMI and PMII, are not. {ECO:0000305}.
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DR EMBL; NYMT01000016; PKC43661.1; -; Genomic_DNA.
DR SMR; A0A2I0BRF1; -.
DR Proteomes; UP000232684; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cytoplasm; Hydrolase; Protease; Signal; Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000453697"
FT CHAIN ?..450
FT /note="Plasmepsin VII"
FT /evidence="ECO:0000255"
FT /id="PRO_5014198737"
FT DOMAIN 92..441
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 111
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 324
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 450 AA; 52328 MW; 77567CCE7BD6AD44 CRC64;
MNKNIIQIYL FVFILLLKQH IVILKNEEFT NPYSIRKKDI KAIVNVNNKL KSINIHKLDN
INKKDLLGSY NENYILIKLK KQDIFSKKLS TYYGEVQIGE QSENNMNVLF DTGSSQVWIL
NDTCKNSLCN NIHSKYKRTK SFVYKYDKKG LPSVIEIFYL SGKIVAFEGY DTIYLGKKLK
IPHTNISFAT KVDIPILEEF KWDGIIGLGF QNGDSIKRGI KPFLDILKDD KILTNKNYKN
QFGYYLSDKE GYITLGGIDN RLKNTPDEEI IWTPVSTEMG YWTIQIMGIR KEYVNNHFEE
NKEEEEVIVK YEAFHDGGKN SIIDTGTYLI YAPKNTMENY LKDLKINNCD EKYNLPHLIF
QIKSDEIKTI KGSAIIEIVL TPNDYVIEYV DKKNNTKECI LGIQPDEQSE EDNVDGWTLG
QVFLKAYYTI FDKDNLKIGF VRSKRNVTLR
