ID   PLM6_PLABA              Reviewed;         441 AA.
AC   A0A509AI82;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   18-SEP-2019, sequence version 1.
DT   03-AUG-2022, entry version 12.
DE   RecName: Full=Plasmepsin VI {ECO:0000305};
DE            EC=3.4.23.- {ECO:0000305};
DE   AltName: Full=Plasmepsin 6 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=PMVI {ECO:0000305}; Synonyms=ASP {ECO:0000303|PubMed:18761621};
GN   ORFNames=PBANKA_0409700 {ECO:0000312|EMBL:VUC54321.1};
OS   Plasmodium berghei (strain Anka).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Vinckeia).
OX   NCBI_TaxID=5823 {ECO:0000312|Proteomes:UP000074855};
RN   [1] {ECO:0000312|Proteomes:UP000074855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANKA {ECO:0000312|Proteomes:UP000074855};
RX   PubMed=25359557; DOI=10.1186/s12915-014-0086-0;
RA   Otto T.D., Bohme U., Jackson A.P., Hunt M., Franke-Fayard B.,
RA   Hoeijmakers W.A., Religa A.A., Robertson L., Sanders M., Ogun S.A.,
RA   Cunningham D., Erhart A., Billker O., Khan S.M., Stunnenberg H.G.,
RA   Langhorne J., Holder A.A., Waters A.P., Newbold C.I., Pain A., Berriman M.,
RA   Janse C.J.;
RT   "A comprehensive evaluation of rodent malaria parasite genomes and gene
RT   expression.";
RL   BMC Biol. 12:86-86(2014).
RN   [2] {ECO:0000305}
RP   FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX   PubMed=18761621; DOI=10.1111/j.1365-2958.2008.06407.x;
RA   Ecker A., Bushell E.S., Tewari R., Sinden R.E.;
RT   "Reverse genetics screen identifies six proteins important for malaria
RT   development in the mosquito.";
RL   Mol. Microbiol. 70:209-220(2008).
CC   -!- FUNCTION: During the development in the mosquito midgut, plays a role
CC       in sporozoite egress from oocysts. {ECO:0000269|PubMed:18761621}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type II
CC       membrane protein {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: In the mosquito vector, expressed at the ookinete
CC       stage. {ECO:0000269|PubMed:18761621}.
CC   -!- DISRUPTION PHENOTYPE: In the mosquito midgut, number of oocysts is
CC       normal (PubMed:18761621). However, oocyst appears immature, enlarged,
CC       degenerated or vacuolated, and fails to sporulate resulting in a lack
CC       of sporozoites (PubMed:18761621). {ECO:0000269|PubMed:18761621}.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000255|RuleBase:RU000454}.
CC   -!- CAUTION: It is unclear if PMVI 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; LK023119; VUC54321.1; -; Genomic_DNA.
DR   STRING; 5823.A0A509AI82; -.
DR   VEuPathDB; PlasmoDB:PBANKA_0409700; -.
DR   OMA; SWQITMK; -.
DR   Proteomes; UP000074855; Chromosome 4.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.70.10; -; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
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; PS00141; ASP_PROTEASE; 2.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease; Hydrolase; Membrane; Protease; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Zymogen.
FT   PROPEP          1..?
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000454299"
FT   CHAIN           ?..441
FT                   /note="Plasmepsin VI"
FT                   /id="PRO_0000454300"
FT   TOPO_DOM        1..7
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        8..28
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        29..441
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          109..435
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT   ACT_SITE        324
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ   SEQUENCE   441 AA;  50319 MW;  9CDE69F5DE70B59C CRC64;
     MTNFCIKSYL FLYLSFLLFF DIITIFHVSS IRISTVLKND KKKKNFNTSL VEENKKYLFN
     EIKLNNRFKN DIKGYIQNIN NFHSIIESKI PNSLLYVHED LINFHNSQFI GDIEIGNPPQ
     SFKVVFDTGS SNFAIPSTKC VKGGCTLHNK FDAKKSRTFM SNLKNKKESI YTYVQYGTGK
     SILEHGYDDV YMKGLKINKQ CIGLIIEESM HPFSDLPFDG IVGLGFSDPD NSFQTKYSKS
     LIETIKEQNL LQQNIFSFYV PKELEKSGAI TFGRANSKYA IEGEKIEWFP VISMYFWEIN
     LLGILLPDKN FEICSNKKCR AAVDTGSSLI TGPSSLMQPL IENINLEKDC SNISSLPIIS
     FVLKNVEGKT VILDFTPDDY ILQENSEEDN SSQCVIGLMS LDIPPPRGPI FIFGNVFIRK
     YYTIFDNDHK LVGVVKSNHN F