SUB3_PLAF7
ID SUB3_PLAF7 Reviewed; 769 AA.
AC Q8I430;
DT 07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Subtilisin-like protease 3 {ECO:0000303|PubMed:22285468};
DE EC=3.4.21.62 {ECO:0000269|PubMed:22285468, ECO:0000269|PubMed:24080030};
DE AltName: Full=PfSUB3 {ECO:0000303|PubMed:22285468};
DE Flags: Precursor;
GN Name=SUB3 {ECO:0000303|PubMed:22285468};
GN ORFNames=PF3D7_0507200 {ECO:0000312|EMBL:CAD51437.1};
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329 {ECO:0000312|Proteomes:UP000001450};
RN [1] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368864; DOI=10.1038/nature01097;
RA Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.D.,
RA Eisen J.A., Rutherford K.M., Salzberg S.L., Craig A., Kyes S., Chan M.-S.,
RA Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.A.,
RA Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.G.;
RT "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL Nature 419:498-511(2002).
RN [2] {ECO:0000312|Proteomes:UP000001450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7 {ECO:0000312|Proteomes:UP000001450};
RX PubMed=12368867; DOI=10.1038/nature01095;
RA Hall N., Pain A., Berriman M., Churcher C.M., Harris B., Harris D.,
RA Mungall K.L., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA Christodoulou Z., Clark L., Clark R., Corton C., Cronin A., Davies R.M.,
RA Davis P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James K.D.,
RA Johnson D., Kerhornou A., Knights A., Konfortov B., Kyes S., Larke N.,
RA Lawson D., Lennard N., Line A., Maddison M., Mclean J., Mooney P.,
RA Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA Rabbinowitsch E., Rajandream M.A., Rutter S., Rutherford K.M., Sanders M.,
RA Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.R.,
RA Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL Nature 419:527-531(2002).
RN [3] {ECO:0000305}
RP CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=22285468; DOI=10.1016/j.molbiopara.2011.12.009;
RA Alam A., Bhatnagar R.K., Chauhan V.S.;
RT "Expression and characterization of catalytic domain of Plasmodium
RT falciparum subtilisin-like protease 3.";
RL Mol. Biochem. Parasitol. 183:84-89(2012).
RN [4] {ECO:0000305}
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24080030; DOI=10.1016/j.molbiopara.2013.09.006;
RA Alam A., Bhatnagar R.K., Relan U., Mukherjee P., Chauhan V.S.;
RT "Proteolytic activity of Plasmodium falciparum subtilisin-like protease 3
RT on parasite profilin, a multifunctional protein.";
RL Mol. Biochem. Parasitol. 191:58-62(2013).
CC -!- FUNCTION: Serine protease which may cleave PFN/profilin.
CC {ECO:0000269|PubMed:24080030}.
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:0000269|PubMed:22285468, ECO:0000269|PubMed:24080030};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22285468}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the parasite blood stage,
CC specifically in schizonts (at protein level).
CC {ECO:0000269|PubMed:22285468}.
CC -!- SIMILARITY: Belongs to the peptidase S8 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01240}.
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DR EMBL; AL844504; CAD51437.1; -; Genomic_DNA.
DR RefSeq; XP_001351630.1; XM_001351594.1.
DR AlphaFoldDB; Q8I430; -.
DR SMR; Q8I430; -.
DR STRING; 5833.PFE0355c; -.
DR MEROPS; S08.122; -.
DR PRIDE; Q8I430; -.
DR EnsemblProtists; CAD51437; CAD51437; PF3D7_0507200.
DR GeneID; 812882; -.
DR KEGG; pfa:PF3D7_0507200; -.
DR VEuPathDB; PlasmoDB:PF3D7_0507200; -.
DR HOGENOM; CLU_363506_0_0_1; -.
DR InParanoid; Q8I430; -.
DR OMA; ILECFNF; -.
DR PhylomeDB; Q8I430; -.
DR Proteomes; UP000001450; Chromosome 5.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0016485; P:protein processing; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:GeneDB.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..?
FT /evidence="ECO:0000305"
FT PROPEP ?..?515
FT /evidence="ECO:0000305|PubMed:22285468"
FT /id="PRO_0000450754"
FT CHAIN ?516..769
FT /note="Subtilisin-like protease 3"
FT /evidence="ECO:0000305|PubMed:22285468"
FT /id="PRO_0000450755"
FT DOMAIN 345..756
FT /note="Peptidase S8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT REGION 293..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 372
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 523
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT ACT_SITE 701
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01240"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 316
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 616
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 769 AA; 88047 MW; 6F729C31D181A88E CRC64;
MINRQYFIWY IFIFNIINKI YFENIRYVKN YEVVIRKKKN IERGIGNDFA FIRRYYKSRL
LSDVSYKNNS IKGKNRVDKE GDIKKYDNND DNKMDNSYDY KNKSIKENET KIRKEQVISL
DKRYNRNINE KEEIKKKIKD IQRKRLIIYF KQDNTILSSR NYKHIFMKVL SSCGHIEKLT
FINFYLYEFP KSINNEDMLL KICLRLLESR RINVENDNQI SHTVQMKSYN NNNNKWDNIN
SKNNCIYQIK DKIKDLPNVS PSASTFTSIS TSPYTLKLRD RNKYANDKNH IFKINHSNKH
KNNNNNNNNN DYHNNNKSNY HSHSSAKCQT QRLNKKMIGT NILDGYDIIQ MEEGLNLSHN
YELNDVNVCI IDTGIDENHI DLKDNIIEKK TFMKHSYKKY NIDGINNIES DNIDGINNIE
SDNIDGINNI ESDNIDGINN IESDNIDGIN NIESDNIDGI NNIKSSDNIK SSDNIKSSDN
INSSDNIKSS DNNNVHTMLR NKLYLKKKKE CSNYNTSNDG HGHGTFIAGI IAGNSPKGKK
GIKGISKKAK LIICKALNNN NAGYISDILE CFNFCAKKKA RIINASFAST THYPSLFQAL
KELQDKDILV ISSSGNCSSN SKCKQAFQEC NLNIQKLYPA AYSADLNNII SVSNIIQQSN
GNIVLSPDSC YSPNYVHLAA PGGNIISTFP NNKYAISSGT SFSASVITGL ASLVLSINSN
LTSQQVIELF KKSIVQTKSL ENKVKWGGFI NVYDLVRFTI DSLPKDKDE
