ID   LMCPA_LEIME             Reviewed;         354 AA.
AC   P25775;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Cysteine proteinase A;
DE            EC=3.4.22.-;
DE   Flags: Precursor;
GN   Name=LMCPA;
OS   Leishmania mexicana.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=MNYC/BZ/62/M379;
RX   PubMed=1508041; DOI=10.1111/j.1365-2958.1992.tb01365.x;
RA   Mottram J.C., Robertson C.D., Coombs G.H., Barry J.D.;
RT   "A developmentally regulated cysteine proteinase gene of Leishmania
RT   mexicana.";
RL   Mol. Microbiol. 6:1925-1932(1992).
CC   -!- DEVELOPMENTAL STAGE: Expressed in all life-cycle stages but at higher
CC       levels in the amastigote stage in the mammal and in stationary phase
CC       promastigote cultures which contain the infective metacyclic form of
CC       the parasite.
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; X62163; CAA44094.1; -; mRNA.
DR   PIR; S25267; S25267.
DR   AlphaFoldDB; P25775; -.
DR   SMR; P25775; -.
DR   MEROPS; C01.076; -.
DR   VEuPathDB; TriTrypDB:LmxM.19.1420; -.
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..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..125
FT                   /note="Activation peptide"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000026380"
FT   CHAIN           126..354
FT                   /note="Cysteine proteinase A"
FT                   /id="PRO_0000026381"
FT   ACT_SITE        153
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        289
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        309
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        208
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        150..191
FT                   /evidence="ECO:0000250"
FT   DISULFID        184..229
FT                   /evidence="ECO:0000250"
FT   DISULFID        282..330
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   354 AA;  38745 MW;  F11EB3986D36D1C5 CRC64;
     MARRNPLLFA IVVTILFVVC YGSALIAQTP PPVDNFVASA HYGSFKKRHG KAFGGDAEEG
     HRFNAFKQNM QTAYFLNTQN PHAHYDVSGK FADLTPQEFA KLYLNPDYYA RHLKNHKEDV
     HVDDSAPSGV MSVDWRDKGA VTPVKNQGLC GSCWAFSAIG NIEGQWAASG HSLVSLSEQM
     LVSCDNIDEG CNGGLMDQAM NWIMQSHNGS VFTEASYPYT SGGGTRPPCH DEGEVGAKIT
     GFLSLPHDEE RIAEWVEKRG PVAVAVDATT WQLYFGGVVS LCLAWSLNHG VLIVGFNKNA
     KPPYWIVKNS WGSSWGEKGY IRLAMGSNQC MLKNYPVSAT VESPHTPHVP TTTA