PLM8_PLABA
ID PLM8_PLABA Reviewed; 373 AA.
AC A0A509AWX2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Plasmepsin VIII {ECO:0000303|PubMed:28192122};
DE Short=PbPMVIII {ECO:0000303|PubMed:28192122};
DE EC=3.4.23.- {ECO:0000305};
DE AltName: Full=Plasmepsin 8 {ECO:0000305};
DE Flags: Precursor;
GN Name=PMVIII {ECO:0000303|PubMed:28192122}; Synonyms=PM8 {ECO:0000305};
GN ORFNames=PBANKA_1329100 {ECO:0000312|EMBL:VUC57677.1};
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=28192122; DOI=10.1016/j.ijpara.2016.11.009;
RA Mastan B.S., Narwal S.K., Dey S., Kumar K.A., Mishra S.;
RT "Plasmodium berghei plasmepsin VIII is essential for sporozoite gliding
RT motility.";
RL Int. J. Parasitol. 47:239-245(2017).
CC -!- FUNCTION: During the development in the mosquito vector, plays an
CC essential role in sporozoite egress from the oocyst and sporozoite
CC gliding motility, which is required for the invasion of salivary glands
CC and subsequent transmission to the host. {ECO:0000269|PubMed:28192122}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed at day 4 post-infection of the
CC mosquito midgut followed by a reduction at day 8 post-infection and in
CC midgut sporozoites (PubMed:28192122). Expression is low in salivary
CC gland sporozoites (PubMed:28192122). Not expressed during the host
CC liver stage (PubMed:28192122). {ECO:0000269|PubMed:28192122}.
CC -!- DISRUPTION PHENOTYPE: In the mosquito vector, midgut infection and
CC oocyst development are normal; however, sporozoites fail to egress from
CC oocysts and their gliding motility is impaired resulting in a failure
CC to invade the salivary glands (PubMed:28192122). Processing of
CC circumsporozoite protein CSP on the oocyst inner surface is normal
CC (PubMed:28192122). In the mouse host, sporozoite invasion of the liver
CC is impaired but the growth and development of asexual blood stages are
CC normal (PubMed:28192122). {ECO:0000269|PubMed:28192122}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000255|RuleBase:RU000454}.
CC -!- CAUTION: It is unclear if PMVIII is glycosylated as other members of
CC the same enzyme family, i.e. PMI and PMII, are not. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LK023128; VUC57677.1; -; Genomic_DNA.
DR SMR; A0A509AWX2; -.
DR STRING; 5821.PBANKA_132910; -.
DR VEuPathDB; PlasmoDB:PBANKA_1329100; -.
DR OMA; YLYILGQ; -.
DR Proteomes; UP000074855; Chromosome 13.
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; IPR001969; Aspartic_peptidase_AS.
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; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 2: Evidence at transcript level;
KW Aspartyl protease; Hydrolase; Protease; Reference proteome; Signal;
KW Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..?
FT /evidence="ECO:0000305"
FT /id="PRO_0000453698"
FT CHAIN ?..373
FT /note="Plasmepsin VIII"
FT /evidence="ECO:0000255"
FT /id="PRO_5021226517"
FT DOMAIN 50..370
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 68
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 258
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
SQ SEQUENCE 373 AA; 42148 MW; 0EDBA3F52CA5947C CRC64;
MNKFFVFPLL LILNSIVLVK SLTENLRVSR YSKPGVSTII LKGGYINRQF IGEISIGNPP
QSFKVLFDTG STNLWIPSKN CYAKACYNKK KYDYNISKNY RISSSKNPVN IFFGTGKVQI
AYATDDIHLG SIKVRNQEFG IANYMSDDPF SDMQFDGLFG LGISEDIKRK GLIYDNIPRN
SSRKNVFSIY YPKSVDDNGA ITFGGYDKKY IEPNSNIDWF VVSSRKYWTI KMTGIKINGL
FLEVCSGNIE GYCDAVIDTG TSSIAGPQND LILLTKLLNP VKSCQNKTLL KNFSFVFSDE
NGVEKEYELT SNDYIVNSFK VDPILKNPCN FAFMPINISS PNGYLYILGQ VFLQKYYAIF
EKDNMRIGLA KSI