PLM9_PLAFO
ID PLM9_PLAFO Reviewed; 627 AA.
AC A0A2I0C265; W7JL89;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2018, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Plasmepsin IX {ECO:0000303|PubMed:29074774};
DE EC=3.4.23.- {ECO:0000250|UniProtKB:Q8ILG2};
DE AltName: Full=Plasmepsin 9 {ECO:0000305};
DE Flags: Precursor;
GN Name=PMIX {ECO:0000303|PubMed:29074774};
GN ORFNames=CK202_0216 {ECO:0000312|EMBL:PKC49510.1};
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:0000312|Proteomes:UP000030673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-250.
RC STRAIN=NF54 {ECO:0000312|Proteomes:UP000030673};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum NF54.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=29074774; DOI=10.1126/science.aan1478;
RA Nasamu A.S., Glushakova S., Russo I., Vaupel B., Oksman A., Kim A.S.,
RA Fremont D.H., Tolia N., Beck J.R., Meyers M.J., Niles J.C., Zimmerberg J.,
RA Goldberg D.E.;
RT "Plasmepsins IX and X are essential and druggable mediators of malaria
RT parasite egress and invasion.";
RL Science 358:518-522(2017).
CC -!- FUNCTION: During the asexual blood stage, initiates the proteolytic
CC maturation of several rhoptry proteins and thus, is required for
CC merozoite invasion of host erythrocytes and probably the subsequent
CC development of the ring-stage (PubMed:29074774). Cleaves rhoptry
CC associated protein 1 RAP1 and apical sushi protein ASP during schizont
CC maturation (PubMed:29074774). Also cleaves rhoptry protein RON3 (By
CC similarity). {ECO:0000250|UniProtKB:Q8ILG2,
CC ECO:0000269|PubMed:29074774}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle,
CC rhoptry {ECO:0000269|PubMed:29074774}. Note=In schizonts, localizes to
CC the bulb of rhoptries. {ECO:0000269|PubMed:29074774}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the asexual blood stage, in
CC schizonts and free merozoites (at protein level).
CC {ECO:0000269|PubMed:29074774}.
CC -!- PTM: Autocleaved into a p55 mature form.
CC {ECO:0000250|UniProtKB:Q8ILG2}.
CC -!- DISRUPTION PHENOTYPE: Normal asexual development in host erythrocytes;
CC however, erythrocyte invasion by newly released merozoites is severely
CC impaired (PubMed:29074774). Abnormal rhoptry morphology and impaired
CC processing of rhoptry-associated protein RAP1 (PubMed:29074774).
CC {ECO:0000269|PubMed:29074774}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
CC -!- CAUTION: It is unclear if PMIX 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; NYMT01000001; PKC49510.1; -; Genomic_DNA.
DR EMBL; KE123882; EWC85658.1; -; Genomic_DNA.
DR SMR; A0A2I0C265; -.
DR EnsemblProtists; EWC85658; EWC85658; PFNF54_05325.
DR VEuPathDB; PlasmoDB:PfNF54_140034000; -.
DR Proteomes; UP000030673; Unassembled WGS sequence.
DR Proteomes; UP000232684; Unassembled WGS sequence.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0020008; C:rhoptry; IDA:UniProtKB.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0085017; P:entry into host cell by a symbiont-containing vacuole; IMP:UniProtKB.
DR GO; GO:0016485; P:protein processing; IMP:UniProtKB.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 3.
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; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW Aspartyl protease; Cytoplasmic vesicle; Hydrolase; Membrane; Protease;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix;
KW Zymogen.
FT PROPEP 1..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000453737"
FT CHAIN ?..627
FT /note="Plasmepsin IX"
FT /id="PRO_0000453738"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 14..34
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 35..627
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT DOMAIN 228..605
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 246
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 495
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 627 AA; 74183 MW; 3F838C4676AD4280 CRC64;
MFFINFKKIK KKQFPIYLTQ HRIITVFLIF IYFINLKDCF HINNSRILSD VDKHRGLYYN
IPKCNVCHKC SICTHENGEA QNVIPMVAIP SKRKHIQDIN KEREENKYPL HIFEEKDIYN
NKDNVVKKED IYKLRKKKKQ KKNCLNFLEK DTMFLSPSHD KETFHINHMN KIKDEKYKQE
YEEEKEIYDN TNTSQEKNET NNEQNLNINL INNDKVTLPL QQLEDSQYVG YIQIGTPPQT
IRPIFDTGST NIWIVSTKCK DETCLKVHRY NHKLSSSFKY YEPHTNLDIM FGTGIIQGVI
GVETFKIGPF EIKNQSFGLV KREKASDNKS NVFERINFEG IVGLAFPEML STGKSTLYEN
LMSSYKLQHN EFSIYIGKDS KYSALIFGGV DKNFFEGDIY MFPVVKEYYW EIHFDGLYID
HQKFCCGVNS IVYDLKKKDQ ENNKLFFTRK YFRKNKFKTH LRKYLLKKIK HQKKQKHSNH
KKKKLNKKKN YLIFDSGTSF NSVPKDEIEY FFRVVPSKKC DDSNIDQVVS SYPNLTYVIN
KMPFTLTPSQ YLVRKNDMCK PAFMEIEVSS EYGHAYILGN ATFMRYYYTV YRRGNNNNSS
YVGIAKAVHT EENEKYLSSL HNKINNL
