CPP1_ENTHI
ID CPP1_ENTHI Reviewed; 315 AA.
AC Q01957;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cysteine proteinase 1;
DE EC=3.4.22.-;
DE Flags: Precursor;
GN Name=CPP1; Synonyms=CPP;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=1518524; DOI=10.1016/0166-6851(92)90101-o;
RA Tannich E., Nickel R., Buss H., Horstmann R.D.;
RT "Mapping and partial sequencing of the genes coding for two different
RT cysteine proteinases in pathogenic Entamoeba histolytica.";
RL Mol. Biochem. Parasitol. 54:109-111(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-315.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
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 [3]
RP PROTEIN SEQUENCE OF 94-99; 101-110 AND 112-113.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=2557443; DOI=10.1111/j.1550-7408.1989.tb01092.x;
RA Schulte W., Scholze H.;
RT "Action of the major protease from Entamoeba histolytica on proteins of the
RT extracellular matrix.";
RL J. Protozool. 36:538-543(1989).
CC -!- FUNCTION: Involved in the destruction of human tissue by E.histolytica.
CC Can abolish adhesion and degrade matrix proteins such as collagen,
CC laminin and fibronectin. May play an important role in pathogenicity.
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; M94162; AAA29090.1; -; Genomic_DNA.
DR EMBL; M64712; AAA29093.1; -; mRNA.
DR PIR; A23705; A23705.
DR AlphaFoldDB; Q01957; -.
DR SMR; Q01957; -.
DR STRING; 5759.rna_EHI_074180-1; -.
DR ChEMBL; CHEMBL3774301; -.
DR MEROPS; C01.050; -.
DR VEuPathDB; AmoebaDB:EHI5A_238670; -.
DR VEuPathDB; AmoebaDB:EHI7A_106950; -.
DR VEuPathDB; AmoebaDB:EHI8A_050360; -.
DR VEuPathDB; AmoebaDB:EHI_074180; -.
DR VEuPathDB; AmoebaDB:KM1_218550; -.
DR eggNOG; KOG1543; Eukaryota.
DR BRENDA; 3.4.22.35; 2080.
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; Signal;
KW Thiol protease; Zymogen.
FT SIGNAL 1..13
FT /evidence="ECO:0000255"
FT PROPEP 14..93
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2557443"
FT /id="PRO_0000026176"
FT CHAIN 94..315
FT /note="Cysteine proteinase 1"
FT /id="PRO_0000026177"
FT ACT_SITE 118
FT /evidence="ECO:0000250"
FT ACT_SITE 259
FT /evidence="ECO:0000250"
FT ACT_SITE 279
FT /evidence="ECO:0000250"
FT DISULFID 115..161
FT /evidence="ECO:0000250"
FT DISULFID 152..193
FT /evidence="ECO:0000250"
FT CONFLICT 4
FT /note="F -> V (in Ref. 2; AAA29093)"
FT /evidence="ECO:0000305"
FT CONFLICT 269
FT /note="V -> A (in Ref. 2; AAA29093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 35056 MW; DF4E3BC795164147 CRC64;
MFTFILMFYI GYGIDFNTWV ANNNKHFTAV ESLRRRAIFN MNARIVAENN RKETFKLSVD
GPFAAMTNEE YNSLLKLKRS GEEKGEVRYL NIQAPKAVDW RKKGKVTPIR DQGNCGSCYT
FGSIAALEGR LLIEKGGDSE TLDLSEEHMV QCTREDGNNG CNGGLGSNVY NYIMENGIAK
ESDYPYTGSD STCRSDVKAF AKIKSYNRVA RNNEVELKAA ISQGLVDVSI DASSVQFQLY
KSGAYTDTQC KNNYFALNHE VCAVGYGVVD GKECWIVRNS WGTGWGEKGY INMVIEGNTC
GVATDPLYPT GVEYL
