SERA5_PLAF7
ID SERA5_PLAF7 Reviewed; 997 AA.
AC Q9TY95; A0A143ZWK2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Serine-repeat antigen protein 5 {ECO:0000305};
DE EC=3.4.22.- {ECO:0000269|PubMed:13679369, ECO:0000269|PubMed:24769454, ECO:0000269|PubMed:29716996};
DE AltName: Full=111 kDa antigen;
DE AltName: Full=Serine protease SERA5 {ECO:0000305};
DE AltName: Full=p126;
DE Contains:
DE RecName: Full=p47 {ECO:0000303|PubMed:25599609};
DE AltName: Full=SER36 {ECO:0000250|UniProtKB:P69193};
DE Contains:
DE RecName: Full=p56 {ECO:0000303|PubMed:25599609};
DE Contains:
DE RecName: Full=p50 {ECO:0000303|PubMed:25599609};
DE Contains:
DE RecName: Full=p18 {ECO:0000303|PubMed:25599609};
DE Contains:
DE RecName: Full=p25n {ECO:0000303|PubMed:25599609};
DE Contains:
DE RecName: Full=p25c {ECO:0000303|PubMed:25599609};
DE Flags: Precursor;
GN Name=SERA5 {ECO:0000303|PubMed:18083098}; ORFNames=PFB0340c;
OS Plasmodium falciparum (isolate 3D7).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=36329;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
RX PubMed=9804551; DOI=10.1126/science.282.5391.1126;
RA Gardner M.J., Tettelin H., Carucci D.J., Cummings L.M., Aravind L.,
RA Koonin E.V., Shallom S.J., Mason T., Yu K., Fujii C., Pederson J., Shen K.,
RA Jing J., Aston C., Lai Z., Schwartz D.C., Pertea M., Salzberg S.L.,
RA Zhou L., Sutton G.G., Clayton R., White O., Smith H.O., Fraser C.M.,
RA Adams M.D., Venter J.C., Hoffman S.L.;
RT "Chromosome 2 sequence of the human malaria parasite Plasmodium
RT falciparum.";
RL Science 282:1126-1132(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3D7;
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 [3]
RP PROTEIN SEQUENCE OF 23-27; 201-205; 391-394 AND 887-891, SUBCELLULAR
RP LOCATION, DEVELOPMENTAL STAGE, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=18083098; DOI=10.1016/j.cell.2007.10.049;
RA Yeoh S., O'Donnell R.A., Koussis K., Dluzewski A.R., Ansell K.H.,
RA Osborne S.A., Hackett F., Withers-Martinez C., Mitchell G.H.,
RA Bannister L.H., Bryans J.S., Kettleborough C.A., Blackman M.J.;
RT "Subcellular discharge of a serine protease mediates release of invasive
RT malaria parasites from host erythrocytes.";
RL Cell 131:1072-1083(2007).
RN [4]
RP PROTEIN SEQUENCE OF 391-395, FUNCTION, LACK OF CATALYTIC ACTIVITY, SUBUNIT,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PROTEOLYTIC CLEAVAGE, MASS
RP SPECTROMETRY, AND MUTAGENESIS OF 560-GLU--VAL-997 AND SER-596.
RX PubMed=25599609; DOI=10.1111/mmi.12941;
RA Stallmach R., Kavishwar M., Withers-Martinez C., Hackett F., Collins C.R.,
RA Howell S.A., Yeoh S., Knuepfer E., Atid A.J., Holder A.A., Blackman M.J.;
RT "Plasmodium falciparum SERA5 plays a non-enzymatic role in the malarial
RT asexual blood-stage lifecycle.";
RL Mol. Microbiol. 96:368-387(2015).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=13679369; DOI=10.1074/jbc.m306755200;
RA Hodder A.N., Drew D.R., Epa V.C., Delorenzi M., Bourgon R., Miller S.K.,
RA Moritz R.L., Frecklington D.F., Simpson R.J., Speed T.P., Pike R.N.,
RA Crabb B.S.;
RT "Enzymic, phylogenetic, and structural characterization of the unusual
RT papain-like protease domain of Plasmodium falciparum SERA5.";
RL J. Biol. Chem. 278:48169-48177(2003).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, PROTEOLYTIC CLEAVAGE,
RP AND MUTAGENESIS OF SER-596.
RX PubMed=24769454; DOI=10.1016/j.bbagen.2014.04.013;
RA Kanodia S., Kumar G., Rizzi L., Pedretti A., Hodder A.N., Romeo S.,
RA Malhotra P.;
RT "Synthetic peptides derived from the C-terminal 6kDa region of Plasmodium
RT falciparum SERA5 inhibit the enzyme activity and malaria parasite
RT development.";
RL Biochim. Biophys. Acta 1840:2765-2775(2014).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PROTEOLYTIC CLEAVAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=28683142; DOI=10.1371/journal.ppat.1006453;
RA Collins C.R., Hackett F., Atid J., Tan M.S.Y., Blackman M.J.;
RT "The Plasmodium falciparum pseudoprotease SERA5 regulates the kinetics and
RT efficiency of malaria parasite egress from host erythrocytes.";
RL PLoS Pathog. 13:e1006453-e1006453(2017).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CPK1, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP PHOSPHORYLATION AT SER-183; THR-549 AND SER-866.
RX PubMed=29716996; DOI=10.1074/jbc.ra117.001540;
RA Iyer G.R., Singh S., Kaur I., Agarwal S., Siddiqui M.A., Bansal A.,
RA Kumar G., Saini E., Paul G., Mohmmed A., Chitnis C.E., Malhotra P.;
RT "Calcium-dependent phosphorylation of Plasmodium falciparum serine repeat
RT antigen 5 triggers merozoite egress.";
RL J. Biol. Chem. 293:9736-9746(2018).
RN [9]
RP SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX PubMed=29567995; DOI=10.1038/s41598-018-23194-9;
RA Tougan T., Edula J.R., Takashima E., Morita M., Shinohara M., Shinohara A.,
RA Tsuboi T., Horii T.;
RT "Molecular Camouflage of Plasmodium falciparum Merozoites by Binding of
RT Host Vitronectin to P47 Fragment of SERA5.";
RL Sci. Rep. 8:5052-5052(2018).
RN [10]
RP INTERACTION WITH PTKL.
RX PubMed=31148576; DOI=10.1038/s41598-019-44542-3;
RA Gnangnon B., Freville A., Cailliau K., Leroy C., De Witte C., Tulasne D.,
RA Martoriarti A., Jung V., Guerrera I.C., Marion S., Khalife J., Pierrot C.;
RT "Plasmodium pseudo-Tyrosine Kinase-like binds PP1 and SERA5 and is exported
RT to host erythrocytes.";
RL Sci. Rep. 9:8120-8120(2019).
RN [11] {ECO:0007744|PDB:2WBF, ECO:0007744|PDB:3CH2, ECO:0007744|PDB:3CH3}
RP X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS) OF 564-828, AND DISULFIDE BONDS.
RX PubMed=19591843; DOI=10.1016/j.jmb.2009.07.007;
RA Hodder A.N., Malby R.L., Clarke O.B., Fairlie W.D., Colman P.M.,
RA Crabb B.S., Smith B.J.;
RT "Structural insights into the protease-like antigen Plasmodium falciparum
RT SERA5 and its noncanonical active-site serine.";
RL J. Mol. Biol. 392:154-165(2009).
CC -!- FUNCTION: Plays an essential role during the asexual blood stage
CC development by controlling the kinetics of merozoite egress from host
CC erythrocytes (PubMed:25599609, PubMed:28683142). Specifically, prevents
CC premature rupture of the parasitophorous vacuole and host erythrocyte
CC membranes (PubMed:28683142). {ECO:0000269|PubMed:25599609,
CC ECO:0000269|PubMed:28683142}.
CC -!- FUNCTION: [p47]: May prevent merozoite phagocytosis by host monocytes
CC via interaction with host VTN at the merozoite surface (By similarity).
CC Plays a role in parasite growth (By similarity).
CC {ECO:0000250|UniProtKB:P69193}.
CC -!- FUNCTION: [p50]: Protease activity is controversial (PubMed:25599609).
CC Has been shown in a number of studies to have protease activity towards
CC a synthetic peptide in vitro (PubMed:13679369, PubMed:24769454,
CC PubMed:29716996). Has also been shown to lack protease activity towards
CC a synthetic peptide in vitro (PubMed:25599609).
CC {ECO:0000269|PubMed:13679369, ECO:0000269|PubMed:24769454,
CC ECO:0000269|PubMed:25599609, ECO:0000269|PubMed:29716996}.
CC -!- SUBUNIT: May interact (via C-terminus) with PTKL (via SAM domain).
CC {ECO:0000269|PubMed:31148576}.
CC -!- SUBUNIT: [p47]: Interacts (via C-terminus) with human VTN (via
CC hemopexin repeat 2); may form heterotetramers of two VTN and SERA5 P47
CC heterodimers; the interaction may protect merozoites from phagocytosis
CC by host monocytes; VTN glycosylation appears to be dispensable for the
CC interaction. {ECO:0000250|UniProtKB:P69193}.
CC -!- SUBUNIT: [p50]: Monomer (PubMed:13679369, PubMed:25599609). Interacts
CC with kinase CPK1/CDPK1 at the schizont stage (PubMed:29716996).
CC {ECO:0000269|PubMed:13679369, ECO:0000269|PubMed:25599609,
CC ECO:0000269|PubMed:29716996}.
CC -!- INTERACTION:
CC Q9TY95; Q8I0V0: SUB1; NbExp=3; IntAct=EBI-826913, EBI-1568896;
CC -!- SUBCELLULAR LOCATION: [Serine-repeat antigen protein 5]:
CC Parasitophorous vacuole {ECO:0000269|PubMed:25599609,
CC ECO:0000269|PubMed:28683142, ECO:0000269|PubMed:29716996,
CC ECO:0000305|PubMed:18083098}. Note=Secreted in large amount into the
CC parasitophorous vacuole. {ECO:0000305|PubMed:18083098}.
CC -!- SUBCELLULAR LOCATION: [p18]: Secreted {ECO:0000250|UniProtKB:P69193}.
CC Note=Secreted during merozoite egress from erythrocytes.
CC {ECO:0000250|UniProtKB:P69193}.
CC -!- SUBCELLULAR LOCATION: [p25n]: Secreted. Note=Secreted during merozoite
CC egress from erythrocytes. {ECO:0000250|UniProtKB:P69193}.
CC -!- SUBCELLULAR LOCATION: [p25c]: Secreted {ECO:0000250|UniProtKB:P69193}.
CC Note=Secreted during merozoite egress from erythrocytes.
CC {ECO:0000250|UniProtKB:P69193}.
CC -!- SUBCELLULAR LOCATION: [p47]: Secreted {ECO:0000250|UniProtKB:P69193}.
CC Cell membrane {ECO:0000269|PubMed:29567995}; Peripheral membrane
CC protein {ECO:0000269|PubMed:29567995}; Extracellular side
CC {ECO:0000250|UniProtKB:P69193}. Note=Secreted during merozoite egress
CC from erythrocytes (By similarity). Colocalizes at the merozoite surface
CC with human VTN (PubMed:29567995). {ECO:0000250|UniProtKB:P69193,
CC ECO:0000269|PubMed:29567995}.
CC -!- SUBCELLULAR LOCATION: [p50]: Secreted {ECO:0000269|PubMed:18083098,
CC ECO:0000269|PubMed:25599609}. Note=Secreted during egress from host
CC erythrocytes. {ECO:0000269|PubMed:25599609}.
CC -!- SUBCELLULAR LOCATION: [p56]: Secreted {ECO:0000269|PubMed:18083098}.
CC Note=Secreted during egress from host erythrocytes.
CC {ECO:0000269|PubMed:25599609}.
CC -!- DEVELOPMENTAL STAGE: [Serine-repeat antigen protein 5]: Expressed
CC during parasite asexual blood stages, specifically in late trophozoite
CC and schizont stages (at protein level). {ECO:0000269|PubMed:18083098,
CC ECO:0000269|PubMed:24769454, ECO:0000269|PubMed:25599609,
CC ECO:0000269|PubMed:28683142, ECO:0000269|PubMed:29567995,
CC ECO:0000269|PubMed:29716996}.
CC -!- DEVELOPMENTAL STAGE: [p50]: Produced during parasite asexual blood
CC stages, specifically at the merozoite stage just prior to egress (at
CC protein level). {ECO:0000269|PubMed:25599609,
CC ECO:0000269|PubMed:29716996}.
CC -!- PTM: [p50]: Phosphorylation by CPK1/CDPK1 increases SERA5 protease
CC activity towards a synthetic peptide in vitro.
CC {ECO:0000269|PubMed:29716996}.
CC -!- PTM: Just prior to merozoite egress from host erythrocytes,
CC proteolytically cleaved into multiple fragments (PubMed:18083098,
CC PubMed:25599609, PubMed:24769454). Cleaved by SUB1 into p47 and p73,
CC p73 is further cleaved by SUB1 into p56 and p18 and p56 is further
CC processed into p50 by an unidentified protease (PubMed:25599609,
CC PubMed:18083098). p47 remains covalently associated with p18 via
CC disulfide bond (PubMed:25599609). p47 can be processed into p25n and
CC p25c by SUB1 (PubMed:25599609, PubMed:18083098). p25c and p25n remain
CC associated with p18 (PubMed:25599609). Proteolytic processing is
CC essential for merozoite egress from host erythrocytes
CC (PubMed:28683142). The cleavage of the propeptide to produce p50 is
CC necessary for protease activity and to promote merozoite egress
CC (PubMed:24769454). {ECO:0000269|PubMed:18083098,
CC ECO:0000269|PubMed:24769454, ECO:0000269|PubMed:25599609,
CC ECO:0000269|PubMed:28683142}.
CC -!- MASS SPECTROMETRY: [p50]: Mass=52540.17; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:25599609};
CC -!- DISRUPTION PHENOTYPE: Conditional knockout at the merozoite stage, does
CC not cause any defect in schizont morphology, merozoite number and
CC maturation initially. During the subsequent invasive cycle in host
CC erythrocytes, merozoite replication is severely impaired due to a
CC premature rupture of the parasitophorous vacuole and erythrocyte
CC membranes resulting in an inefficient dispersal of released merozoites.
CC {ECO:0000269|PubMed:28683142}.
CC -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU10089, ECO:0000255|PROSITE-ProRule:PRU10090}.
CC -!- CAUTION: In contrast to other serine-repeat antigen proteins (SERA) of
CC the peptidase C1 family, contains a serine residue at the position of
CC the canonical catalytic cysteine and has been shown to lack protease
CC activity. However, other studies show that it has protease activity
CC towards synthetic peptides in vitro (PubMed:13679369, PubMed:24769454,
CC PubMed:29716996). {ECO:0000269|PubMed:13679369,
CC ECO:0000269|PubMed:24769454, ECO:0000269|PubMed:29716996,
CC ECO:0000305|PubMed:19591843, ECO:0000305|PubMed:25599609}.
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DR EMBL; LN999943; CZT98089.1; -; Genomic_DNA.
DR PIR; B71617; B71617.
DR RefSeq; XP_001349586.1; XM_001349550.1.
DR PDB; 2WBF; X-ray; 1.60 A; X=564-828.
DR PDB; 3CH2; X-ray; 1.80 A; X=564-828.
DR PDB; 3CH3; X-ray; 1.79 A; X=564-828.
DR PDB; 6X42; X-ray; 1.20 A; X=544-828.
DR PDB; 6X44; X-ray; 2.20 A; A/B=391-828.
DR PDBsum; 2WBF; -.
DR PDBsum; 3CH2; -.
DR PDBsum; 3CH3; -.
DR PDBsum; 6X42; -.
DR PDBsum; 6X44; -.
DR AlphaFoldDB; Q9TY95; -.
DR BMRB; Q9TY95; -.
DR SMR; Q9TY95; -.
DR BioGRID; 1207988; 24.
DR IntAct; Q9TY95; 24.
DR STRING; 5833.PFB0340c; -.
DR MEROPS; C01.984; -.
DR SwissPalm; Q9TY95; -.
DR PRIDE; Q9TY95; -.
DR EnsemblProtists; CZT98089; CZT98089; PF3D7_0207600.
DR GeneID; 812668; -.
DR KEGG; pfa:PF3D7_0207600; -.
DR VEuPathDB; PlasmoDB:PF3D7_0207600; -.
DR HOGENOM; CLU_005127_0_0_1; -.
DR InParanoid; Q9TY95; -.
DR OMA; GHENFSA; -.
DR PhylomeDB; Q9TY95; -.
DR Reactome; R-PFA-114608; Platelet degranulation.
DR EvolutionaryTrace; Q9TY95; -.
DR Proteomes; UP000001450; Chromosome 2.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020004; C:symbiont-containing vacuolar space; IDA:UniProtKB.
DR GO; GO:0020003; C:symbiont-containing vacuole; IDA:GeneDB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IDA:GeneDB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0035891; P:exit from host cell; IMP:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR GO; GO:0050776; P:regulation of immune response; TAS:GeneDB.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025661; Pept_asp_AS.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR Pfam; PF00112; Peptidase_C1; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Malaria; Membrane; Phosphoprotein; Protease;
KW Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:18083098"
FT CHAIN 23..997
FT /note="Serine-repeat antigen protein 5"
FT /id="PRO_0000026479"
FT CHAIN 23..390
FT /note="p47"
FT /evidence="ECO:0000269|PubMed:25599609"
FT /id="PRO_0000450177"
FT CHAIN 23..200
FT /note="p25n"
FT /evidence="ECO:0000269|PubMed:25599609"
FT /id="PRO_0000450178"
FT CHAIN 201..390
FT /note="p25c"
FT /evidence="ECO:0000269|PubMed:25599609"
FT /id="PRO_0000450179"
FT CHAIN 391..886
FT /note="p56"
FT /evidence="ECO:0000269|PubMed:25599609"
FT /id="PRO_0000450180"
FT CHAIN 391..842
FT /note="p50"
FT /evidence="ECO:0000269|PubMed:25599609"
FT /id="PRO_0000450181"
FT PROPEP 843..886
FT /note="Inhibition peptide"
FT /evidence="ECO:0000269|PubMed:24769454,
FT ECO:0000269|PubMed:25599609"
FT /id="PRO_0000450182"
FT CHAIN 887..997
FT /note="p18"
FT /evidence="ECO:0000269|PubMed:25599609"
FT /id="PRO_0000450183"
FT REGION 26..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..253
FT /note="Interaction with PTKL"
FT /evidence="ECO:0000269|PubMed:31148576"
FT REGION 373..390
FT /note="Interaction with host VTN"
FT /evidence="ECO:0000250|UniProtKB:P69193"
FT REGION 579..997
FT /note="Thiol-protease-like"
FT /evidence="ECO:0000305|PubMed:19591843"
FT COMPBIAS 183..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 762
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10089"
FT ACT_SITE 787
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10090"
FT SITE 200..201
FT /note="Cleavage; by SUB1"
FT /evidence="ECO:0000269|PubMed:25599609"
FT SITE 390..391
FT /note="Cleavage; by SUB1"
FT /evidence="ECO:0000269|PubMed:25599609"
FT SITE 596
FT /note="Ancestral active site"
FT /evidence="ECO:0000305|PubMed:19591843,
FT ECO:0000305|PubMed:25599609"
FT SITE 842..843
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:25599609"
FT SITE 886..887
FT /note="Cleavage; by SUB1"
FT /evidence="ECO:0000269|PubMed:25599609"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29716996"
FT MOD_RES 549
FT /note="Phosphothreonine; by CPK1"
FT /evidence="ECO:0000269|PubMed:29716996"
FT MOD_RES 866
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:29716996"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 445..497
FT /evidence="ECO:0000269|PubMed:13679369"
FT DISULFID 567..572
FT /evidence="ECO:0000269|PubMed:13679369,
FT ECO:0000269|PubMed:19591843, ECO:0007744|PDB:2WBF,
FT ECO:0007744|PDB:3CH2, ECO:0007744|PDB:3CH3"
FT DISULFID 581..610
FT /evidence="ECO:0000269|PubMed:19591843,
FT ECO:0007744|PDB:2WBF, ECO:0007744|PDB:3CH2,
FT ECO:0007744|PDB:3CH3"
FT DISULFID 593..636
FT /evidence="ECO:0000269|PubMed:19591843,
FT ECO:0007744|PDB:2WBF, ECO:0007744|PDB:3CH2,
FT ECO:0007744|PDB:3CH3"
FT DISULFID 627..672
FT /evidence="ECO:0000269|PubMed:19591843,
FT ECO:0007744|PDB:2WBF, ECO:0007744|PDB:3CH2,
FT ECO:0007744|PDB:3CH3"
FT DISULFID 755..809
FT /evidence="ECO:0000269|PubMed:19591843,
FT ECO:0007744|PDB:2WBF, ECO:0007744|PDB:3CH2,
FT ECO:0007744|PDB:3CH3"
FT MUTAGEN 590..997
FT /note="Missing: No viable parasite."
FT /evidence="ECO:0000269|PubMed:25599609"
FT MUTAGEN 596
FT /note="S->A: Lacks protease activity. No cellular location
FT and growth defects in host red blood cells."
FT /evidence="ECO:0000269|PubMed:24769454,
FT ECO:0000269|PubMed:25599609"
FT MUTAGEN 596
FT /note="S->C: Gains protease activity."
FT /evidence="ECO:0000269|PubMed:25599609"
FT MUTAGEN 596
FT /note="S->R: No viable parasite."
FT /evidence="ECO:0000269|PubMed:25599609"
FT HELIX 394..415
FT /evidence="ECO:0007829|PDB:6X44"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:6X44"
FT HELIX 435..451
FT /evidence="ECO:0007829|PDB:6X44"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:6X44"
FT HELIX 465..477
FT /evidence="ECO:0007829|PDB:6X44"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:6X44"
FT HELIX 484..490
FT /evidence="ECO:0007829|PDB:6X44"
FT HELIX 494..497
FT /evidence="ECO:0007829|PDB:6X44"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:6X44"
FT HELIX 501..505
FT /evidence="ECO:0007829|PDB:6X44"
FT HELIX 518..521
FT /evidence="ECO:0007829|PDB:6X44"
FT TURN 564..566
FT /evidence="ECO:0007829|PDB:6X42"
FT STRAND 567..570
FT /evidence="ECO:0007829|PDB:6X42"
FT HELIX 574..576
FT /evidence="ECO:0007829|PDB:6X42"
FT HELIX 581..584
FT /evidence="ECO:0007829|PDB:6X42"
FT STRAND 592..594
FT /evidence="ECO:0007829|PDB:3CH2"
FT HELIX 596..611
FT /evidence="ECO:0007829|PDB:6X42"
FT HELIX 621..626
FT /evidence="ECO:0007829|PDB:6X42"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:6X42"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:6X42"
FT HELIX 642..652
FT /evidence="ECO:0007829|PDB:6X42"
FT HELIX 658..660
FT /evidence="ECO:0007829|PDB:6X42"
FT HELIX 665..667
FT /evidence="ECO:0007829|PDB:6X42"
FT TURN 682..685
FT /evidence="ECO:0007829|PDB:6X42"
FT STRAND 694..696
FT /evidence="ECO:0007829|PDB:6X42"
FT STRAND 697..700
FT /evidence="ECO:0007829|PDB:6X44"
FT STRAND 701..707
FT /evidence="ECO:0007829|PDB:6X42"
FT HELIX 708..711
FT /evidence="ECO:0007829|PDB:6X42"
FT HELIX 715..729
FT /evidence="ECO:0007829|PDB:6X42"
FT STRAND 732..736
FT /evidence="ECO:0007829|PDB:6X42"
FT HELIX 738..741
FT /evidence="ECO:0007829|PDB:6X42"
FT HELIX 744..746
FT /evidence="ECO:0007829|PDB:6X42"
FT STRAND 747..752
FT /evidence="ECO:0007829|PDB:6X42"
FT STRAND 762..773
FT /evidence="ECO:0007829|PDB:6X42"
FT STRAND 779..786
FT /evidence="ECO:0007829|PDB:6X42"
FT STRAND 791..793
FT /evidence="ECO:0007829|PDB:3CH3"
FT STRAND 798..804
FT /evidence="ECO:0007829|PDB:6X42"
FT STRAND 810..813
FT /evidence="ECO:0007829|PDB:3CH3"
FT STRAND 816..820
FT /evidence="ECO:0007829|PDB:6X42"
SQ SEQUENCE 997 AA; 111768 MW; CF26A8A03E512ED5 CRC64;
MKSYISLFFI LCVIFNKNVI KCTGESQTGN TGGGQAGNTG GDQAGSTGGS PQGSTGASPQ
GSTGASPQGS TGASQPGSSE PSNPVSSGHS VSTVSVSQTS TSSEKQDTIQ VKSALLKDYM
GLKVTGPCNE NFIMFLVPHI YIDVDTEDTN IELRTTLKKT NNAISFESNS GSLEKKKYVK
LPSNGTTGEQ GSSTGTVRGD TEPISDSSSS SSSSSSSSSS SSSSSSSSSS SSSESLPANG
PDSPTVKPPR NLQNICETGK NFKLVVYIKE NTLILKWKVY GETKDTTENN KVDVRKYLIN
EKETPFTNIL IHAYKEHNGT NLIESKNYAI GSDIPEKCDT LASNCFLSGN FNIEKCFQCA
LLVEKENKND VCYKYLSEDI VSKFKEIKAE TEDDDEDDYT EYKLTESIDN ILVKMFKTNE
NNDKSELIKL EEVDDSLKLE LMNYCSLLKD VDTTGTLDNY GMGNEMDIFN NLKRLLIYHS
EENINTLKNK FRNAAVCLKN VDDWIVNKRG LVLPELNYDL EYFNEHLYND KNSPEDKDNK
GKGVVHVDTT LEKEDTLSYD NSDNMFCNKE YCNRLKDENN CISNLQVEDQ GNCDTSWIFA
SKYHLETIRC MKGYEPTKIS ALYVANCYKG EHKDRCDEGS SPMEFLQIIE DYGFLPAESN
YPYNYVKVGE QCPKVEDHWM NLWDNGKILH NKNEPNSLDG KGYTAYESER FHDNMDAFVK
IIKTEVMNKG SVIAYIKAEN VMGYEFSGKK VQNLCGDDTA DHAVNIVGYG NYVNSEGEKK
SYWIVRNSWG PYWGDEGYFK VDMYGPTHCH FNFIHSVVIF NVDLPMNNKT TKKESKIYDY
YLKASPEFYH NLYFKNFNVG KKNLFSEKED NENNKKLGNN YIIFGQDTAG SGQSGKESNT
ALESAGTSNE VSERVHVYHI LKHIKDGKIR MGMRKYIDTQ DVNKKHSCTR SYAFNPENYE
KCVNLCNVNW KTCEEKTSPG LCLSKLDTNN ECYFCYV
