ID   CYSP_PLAFA              Reviewed;         569 AA.
AC   P25805;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Trophozoite cysteine proteinase;
DE            Short=TCP;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
OS   Plasmodium falciparum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=5833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1565129; DOI=10.1016/0166-6851(92)90209-3;
RA   Rosenthal P.J., Nelson R.G.;
RT   "Isolation and characterization of a cysteine proteinase gene of Plasmodium
RT   falciparum.";
RL   Mol. Biochem. Parasitol. 51:143-152(1992).
CC   -!- FUNCTION: Probably degrades erythrocyte hemoglobin.
CC   -!- DEVELOPMENTAL STAGE: Trophozoite.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU10088, ECO:0000255|PROSITE-ProRule:PRU10089,
CC       ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   EMBL; M81341; AAA29578.1; -; Genomic_DNA.
DR   PIR; A45624; A45624.
DR   AlphaFoldDB; P25805; -.
DR   SMR; P25805; -.
DR   BindingDB; P25805; -.
DR   ChEMBL; CHEMBL2366471; -.
DR   MEROPS; C01.077; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1458000; -.
DR   VEuPathDB; PlasmoDB:Pf7G8-2_000531800; -.
DR   VEuPathDB; PlasmoDB:Pf7G8_140063200; -.
DR   VEuPathDB; PlasmoDB:PfCD01_140063300; -.
DR   VEuPathDB; PlasmoDB:PfDd2_140062400; -.
DR   VEuPathDB; PlasmoDB:PfGA01_140063400; -.
DR   VEuPathDB; PlasmoDB:PfGB4_140064100; -.
DR   VEuPathDB; PlasmoDB:PfGN01_140063300; -.
DR   VEuPathDB; PlasmoDB:PfHB3_140063700; -.
DR   VEuPathDB; PlasmoDB:PfIT_140064400; -.
DR   VEuPathDB; PlasmoDB:PfKE01_140062800; -.
DR   VEuPathDB; PlasmoDB:PfKH01_140063500; -.
DR   VEuPathDB; PlasmoDB:PfKH02_140063700; -.
DR   VEuPathDB; PlasmoDB:PfML01_140063600; -.
DR   VEuPathDB; PlasmoDB:PfNF135_140062100; -.
DR   VEuPathDB; PlasmoDB:PfNF166_140060900; -.
DR   VEuPathDB; PlasmoDB:PfNF54_140061700; -.
DR   VEuPathDB; PlasmoDB:PfSD01_140061300; -.
DR   VEuPathDB; PlasmoDB:PfSN01_140065200; -.
DR   VEuPathDB; PlasmoDB:PfTG01_140063300; -.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR000169; Pept_cys_AS.
DR   InterPro; IPR025660; Pept_his_AS.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR039417; Peptidase_C1A_papain-like.
DR   InterPro; IPR013201; Prot_inhib_I29.
DR   Pfam; PF08246; Inhibitor_I29; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   PRINTS; PR00705; PAPAIN.
DR   SMART; SM00848; Inhibitor_I29; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
DR   PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Protease; Signal; Thiol protease;
KW   Zymogen.
FT   SIGNAL          1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..332
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000026473"
FT   CHAIN           333..569
FT                   /note="Trophozoite cysteine proteinase"
FT                   /id="PRO_0000026474"
FT   REGION          97..118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..112
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        357
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        488
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        533
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        58
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        127
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        479
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        487
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        354..395
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   569 AA;  66880 MW;  E5E762A3637F7C60 CRC64;
     MVAIKEMKEL AFARPSLVET LNKKKKFLKK KEKRTFVLSI YAFITFIIFC IGILYFTNKS
     SAHNNNNNKN EHSLKKEEIE LLRVLLEKYK KQKDGILNES SNEEDEEKYT LNSETYNNKN
     NVSNIKNDSI KSKKEEYINL ERILLEKYKK FINENNEENR KELSNILHKL LEINKLILRE
     EKDDKKVYLI NDNYDEKGAL EIGMNEEMKY KKEDPINNIK YASKFFKFMK EHNKVYKNID
     EQMRKFEIFK INYISIKNHN KLNKNAMYKK KVNQFSDYSE EELKEYFKTL LHVPNHMIEK
     YSKPFENHLK DNILISEFYT NGKRNEKDIF SKVPEILDYR EKGIVHEPKD QGLCGSCWAF
     ASVGNIESVF AKKNKNILSF SEQEVVDCSK DNFGCDGGHP FYSFLYVLQN ELCLGDEYKY
     KAKDDMFCLN YRCKRKVSLS SIGAVKENQL ILALNEVGPL SVNVGVNNDF VAYSEGVYNG
     TCSEELNHSV LLVGYGQVEK TKLNYNNKIQ TYNTKENSNQ PDDNIIYYWI IKNSWSKKWG
     ENGFMRLSRN KNGDNVFCGI GEEVFYPIL