ID   CPP3_ENTHI              Reviewed;         308 AA.
AC   Q06964;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Cysteine proteinase 3;
DE            EC=3.4.22.-;
DE   AltName: Full=Cysteine proteinase ACP3;
DE   Flags: Precursor; Fragment;
GN   Name=CPNP;
OS   Entamoeba histolytica.
OC   Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC   Entamoeba.
OX   NCBI_TaxID=5759;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=SAW 1734;
RX   PubMed=1705935; DOI=10.1016/s0021-9258(19)67719-7;
RA   Tannich E., Scholze H., Nicke R., Horstmann R.D.;
RT   "Homologous cysteine proteinases of pathogenic and nonpathogenic Entamoeba
RT   histolytica. Differences in structure and expression.";
RL   J. Biol. Chem. 266:4798-4803(1991).
RN   [2]
RP   PARTIAL NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 87-94.
RC   STRAIN=ATCC 30459 / HM-1:IMSS;
RX   PubMed=8473498; DOI=10.1172/jci116359;
RA   Reed S., Bouvier J., Pollack A.S., Engel J.C., Brown M., Hirata K., Que X.,
RA   Eakin A., Hagblom P., Gillin F., McKerrow J.H.;
RT   "Cloning of a virulence factor of Entamoeba histolytica. Pathogenic strains
RT   possess a unique cysteine proteinase gene.";
RL   J. Clin. Invest. 91:1532-1540(1993).
CC   -!- FUNCTION: Can abolish adhesion and degrade matrix proteins such as
CC       collagen, laminin and fibronectin.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space.
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; M64721; AAA29092.1; -; mRNA.
DR   AlphaFoldDB; Q06964; -.
DR   SMR; Q06964; -.
DR   MEROPS; C01.050; -.
DR   VEuPathDB; AmoebaDB:EHI5A_081530; -.
DR   VEuPathDB; AmoebaDB:EHI7A_106950; -.
DR   VEuPathDB; AmoebaDB:EHI8A_050360; -.
DR   VEuPathDB; AmoebaDB:EHI_033710; -.
DR   VEuPathDB; AmoebaDB:KM1_098010; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Protease; Secreted;
KW   Signal; Thiol protease; Zymogen.
FT   SIGNAL          <1..?
FT                   /evidence="ECO:0000255"
FT   PROPEP          ?..86
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000269|PubMed:8473498"
FT                   /id="PRO_0000026180"
FT   CHAIN           87..308
FT                   /note="Cysteine proteinase 3"
FT                   /id="PRO_0000026181"
FT   ACT_SITE        111
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        252
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        272
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..154
FT                   /evidence="ECO:0000250"
FT   DISULFID        145..186
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   308 AA;  33680 MW;  C4C862F55CB9B11E CRC64;
     LAIANAIDFN TWAANNNKHF TAVEALRRRA IFNMNARFVA EFNKKGSFKL SVDGPFAAMT
     NEEYRTLLKS KRTVEENGKV TYLNIQAPES VDWRAQGKVT PIRDQAQCGS CYTFGSLAAL
     EGRLLIEKGG NANTLDLSEE HLVQCTRDNG NNGCNGGLGS NVYDYIIQNG VAKESDYPYT
     GTDSTCKTNV KAFAKITGYN KVPRNNEAEL KAALSQGLVD VSIDASSAKF QLYKSGAYSD
     TKCKNNFFAL NHEVCAVGYG VVDGKECWIV RNSWGTGWGD KGYINMVIEG NTCGVATDPL
     YPTGVQYL