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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}.
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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
 
 
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