PIMM2_PLABA
ID PIMM2_PLABA Reviewed; 836 AA.
AC A0A509AKI1;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2019, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Subtilisin-like protease PIMMS2 {ECO:0000305};
DE EC=3.4.21.62 {ECO:0000250|UniProtKB:Q8I0V0};
DE AltName: Full=Midgut invasion ookinete protein 2 {ECO:0000303|PubMed:28559405};
GN Name=PIMMS2 {ECO:0000303|PubMed:28559405};
GN ORFNames=PBANKA_1106900 {ECO:0000312|EMBL:VUC56492.1};
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, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TOPOLOGY, AND
RP MUTAGENESIS OF ASP-155; HIS-222 AND SER-414.
RX PubMed=28559405; DOI=10.1128/iai.00139-17;
RA Ukegbu C.V., Akinosoglou K.A., Christophides G.K., Vlachou D.;
RT "Plasmodium berghei PIMMS2 Promotes Ookinete Invasion of the Anopheles
RT gambiae Mosquito Midgut.";
RL Infect. Immun. 85:0-0(2017).
RN [3] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29873127; DOI=10.1111/mmi.13993;
RA Armistead J.S., Jennison C., O'Neill M.T., Lopaticki S., Liehl P.,
RA Hanson K.K., Annoura T., Rajasekaran P., Erickson S.M., Tonkin C.J.,
RA Khan S.M., Mota M.M., Boddey J.A.;
RT "Plasmodium falciparum subtilisin-like ookinete protein SOPT plays an
RT important and conserved role during ookinete infection of the Anopheles
RT stephensi midgut.";
RL Mol. Microbiol. 109:458-473(2018).
CC -!- FUNCTION: Probable serine protease which plays a role in ookinete
CC traversal of the mosquito host midgut epithelium.
CC {ECO:0000269|PubMed:28559405, ECO:0000269|PubMed:29873127}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity for peptide
CC bonds, and a preference for a large uncharged residue in P1.
CC Hydrolyzes peptide amides.; EC=3.4.21.62;
CC Evidence={ECO:0000250|UniProtKB:Q8I0V0};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28559405}.
CC Note=It is not clear how the protein localizes at the cell membrane.
CC There is a predicted transmembrane domain encompassing the end of the
CC catalytic domain which appears to be intracellular suggesting a single-
CC pass type II membrane topology. {ECO:0000305|PubMed:28559405}.
CC -!- DEVELOPMENTAL STAGE: Expression is restricted to mosquito host midgut
CC stages (at protein level) (PubMed:28559405). Specifically, expression
CC begins after gametocyte activation and peaks in mature ookinetes (at
CC protein level) (PubMed:28559405). Not expressed in the oocyst
CC (PubMed:28559405). {ECO:0000269|PubMed:28559405}.
CC -!- DISRUPTION PHENOTYPE: Ookinetes fail to traverse the midgut epithelium
CC resulting in a reduced number of oocysts in the gut epithelium of the
CC mosquito host, A.gambiae or A.stephensi (PubMed:28559405,
CC PubMed:29873127). Gametogenesis, and ookinete development and motility
CC are normal (PubMed:28559405). The capacity to infect the mouse host by
CC the few sporozoites made in the mosquito host is not affected
CC (PubMed:28559405). {ECO:0000269|PubMed:28559405,
CC ECO:0000269|PubMed:29873127}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000305}.
CC -!- CAUTION: The three residues, Asp, His and Ser forming the catalytic
CC triad are conserved (PubMed:28559405). However, the conserved motifs
CC HGT and GTS, which encompass His and Ser residues of subtilases,
CC respectively, are not present in PIMMS2, suggesting that the catalytic
CC triad may be non-functional (PubMed:28559405).
CC {ECO:0000303|PubMed:28559405}.
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DR EMBL; LK023126; VUC56492.1; -; Genomic_DNA.
DR RefSeq; XP_679128.1; XM_674036.1.
DR AlphaFoldDB; A0A509AKI1; -.
DR SMR; A0A509AKI1; -.
DR STRING; 5823.A0A509AKI1; -.
DR VEuPathDB; PlasmoDB:PBANKA_1106900; -.
DR OMA; KNCKEST; -.
DR BRENDA; 3.4.21.62; 4887.
DR Proteomes; UP000074855; Chromosome 11.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Hydrolase; Membrane; Protease; Reference proteome;
KW Serine protease.
FT CHAIN 1..836
FT /note="Subtilisin-like protease PIMMS2"
FT /id="PRO_0000451407"
FT REGION 802..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 155
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10080"
FT ACT_SITE 222
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00782"
FT ACT_SITE 414
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P00782"
FT MUTAGEN 155
FT /note="D->A: Reduced number of oocysts in the gut
FT epithelium of the mosquito host; when associated with A-222
FT and A-414."
FT /evidence="ECO:0000269|PubMed:28559405"
FT MUTAGEN 222
FT /note="H->A: Reduced number of oocysts in the gut
FT epithelium of the mosquito host; when associated with A-155
FT and A-414."
FT /evidence="ECO:0000269|PubMed:28559405"
FT MUTAGEN 414
FT /note="S->A: Reduced number of oocysts in the gut
FT epithelium of the mosquito host; when associated with A-155
FT and A-222."
FT /evidence="ECO:0000269|PubMed:28559405"
SQ SEQUENCE 836 AA; 99420 MW; 1FB8FD683632D093 CRC64;
MVLLNGKLKY IAVVAIFYNL IILLVKEKFP YICTKKKFHA ISNRILYEYL NNFVSKDIFR
REDITLKNLN FVQTNLKSDK DAEIKENRDT QSVDDNMFQR VYKFILNFFY GNKKNRINKS
MNYGKYDNFN KINDIFEFMR NNGLPINITS VCLIDTGLNI KDALINYFLN HDISTYNSYT
YHSVNINYKK PDSFNFGINS ENCDEDNYSE CESTFLENHN GHGKYEDKST IQGDSLKLIE
KKYDKNVDLQ RSGIDVEICK AFNNSKEKKN SLNIIPVIKC LEYCKTKNVK IIHMDYNINE
QNEQLIQIMD DLKNSEIFVI LPSEKLFNEK PYEDNSVIYP SSFFEKFENV FFIGSLDYSD
MSSDDADIAS NFQIQKNEYL KYRKNNVFLL DSINSSLKKR DDHDILYYEI KYSSAFFINI
ITIILNIYPN MSIKELRNIL SYSIPSKETA QLKTENIFEG NFDINKFIHI LLNRGINSSG
FVRKYKDVTP NESTNKIFLL EDQKDADIEP QKDSSIDIYC DEGGSDEDIV STSNGLDVYS
EYSHSNNKSD QLLNDEKGLK YETYKDLYSV KENDIYVFES NNPTNSSFMQ MNYDDKIKSK
YLDNLEEANY QNHRTQFEIN RNDNRYPIIS EDNLRDRQNM HNIQMLNDGI NYSENANNIE
ELYDNDFEDY RGKDLNPEYN KIRDNNNNKN INKEFGILNT WRKNNEGLYL SDSEEESQPF
KWMDMHVDDI YQDRKKRLKG NNYDNRNGRV RRIYEDNKRG RYIKNRNMQK KKNFDRNLKN
KRYLNRRTKR HINEKNKRIM REKKNKYNNS VLKRNEMKSH NNSQKTPKII PRKYSR
