ID   CYSP2_LEIPI             Reviewed;         444 AA.
AC   Q05094;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Cysteine proteinase 2;
DE            EC=3.4.22.-;
DE   AltName: Full=Amastigote cysteine proteinase A-2;
DE   Flags: Precursor;
GN   Name=CYS2;
OS   Leishmania pifanoi.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5682;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 125-159; 237-266
RP   AND 308-322.
RX   PubMed=8426606; DOI=10.1016/0166-6851(93)90248-v;
RA   Traub-Cseko Y.M., Duboise M., Boukai L.K., McMahon-Pratt D.;
RT   "Identification of two distinct cysteine proteinase genes of Leishmania
RT   pifanoi axenic amastigotes using the polymerase chain reaction.";
RL   Mol. Biochem. Parasitol. 57:101-115(1993).
CC   -!- FUNCTION: The cysteine proteinases have a potential role in host-
CC       parasite interaction and virulence.
CC   -!- SUBCELLULAR LOCATION: Lysosome. Note=Associated with megasome, a unique
CC       lysosomal organelle found in intracellular amastigotes of the
CC       L.mexicana complex.
CC   -!- DEVELOPMENTAL STAGE: Primarily expressed by the amastigote stage.
CC       Expressed 15 times more in amastigotes than in promastigotes.
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; M97695; AAA29229.1; -; Genomic_DNA.
DR   PIR; A48566; A48566.
DR   AlphaFoldDB; Q05094; -.
DR   SMR; Q05094; -.
DR   MEROPS; C01.074; -.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02248; Peptidase_C1A; 1.
DR   InterPro; IPR021981; DUF3586.
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; PF12131; DUF3586; 1.
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; Glycoprotein; Hydrolase;
KW   Lysosome; Protease; Signal; Thiol protease; Virulence; Zymogen.
FT   SIGNAL          1..19
FT                   /note="Or 27"
FT   PROPEP          20..124
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000305|PubMed:8426606"
FT                   /id="PRO_0000026386"
FT   CHAIN           125..444
FT                   /note="Cysteine proteinase 2"
FT                   /id="PRO_0000026387"
FT   ACT_SITE        150
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        228
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        147..188
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   444 AA;  47857 MW;  B85B6ED4874A8D6B CRC64;
     MATSRAALCA VAVVCVVLAA ACAPARAIHV GTPAAALFEE FKRTYGRAYE TLAEEQQRLA
     NFERNLELMR EHQARNPHAQ FGITKFFDLS EAEFAARYLN GAAYFAAAKR HAAQHYRKAR
     ADLSAVPDAV DWREKGAVTP VKDQGACGSC WAFSAVGNIE GQWYLAGHEL VSLSEQQLVS
     CDDMNDGCDG GLMLQAFDWL LQNTNGHLHT EDSYPYVSGN GYVPECSNSS EELVVGAQID
     GHVLIGSSEK AMAAWLAKNG PIAIALDASS FMSYKSGVLT ACIGKQLNHG VLLVGYDMTG
     EVPYWVIKNS WGGDWGEQGY VRVVMGVNAC LLSEYPVSAH VRESAAPGTS TSSETPAPRP
     VMVEQVICFD KNCTQGCRKT LIKANECHKN GGGGASMIKC SPQKVTMCTY SNEFCVGGGL
     CFETPDGKCA PYFLGSIMNT CHYT