ID   CERC_SCHMA              Reviewed;         264 AA.
AC   P12546;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Cercarial protease;
DE            EC=3.4.21.-;
DE   AltName: Full=Cercarial elastase;
DE   Flags: Precursor;
OS   Schistosoma mansoni (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6183;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3166457; DOI=10.1016/s0021-9258(18)37688-9;
RA   Newport G.R., McKerrow J.H., Hedstrom R., Petitt M., McGarrigle L.,
RA   Barr P.J., Agabian N.;
RT   "Cloning of the proteinase that facilitates infection by schistosome
RT   parasites.";
RL   J. Biol. Chem. 263:13179-13184(1988).
CC   -!- FUNCTION: This protease cleaves elastin and thus facilitates
CC       penetration of schistosome parasite larvae through elastin-rich tissue
CC       of the host.
CC   -!- ACTIVITY REGULATION: Activated by an autocatalytic mechanism.
CC   -!- TISSUE SPECIFICITY: Acetabular (penetration) glands.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; J03946; AAA29864.1; -; mRNA.
DR   PIR; A28942; A28942.
DR   AlphaFoldDB; P12546; -.
DR   SMR; P12546; -.
DR   STRING; 6183.Smp_119130.1; -.
DR   MEROPS; S01.144; -.
DR   PRIDE; P12546; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   HOGENOM; CLU_1058926_0_0_1; -.
DR   Proteomes; UP000008854; Unassembled WGS sequence.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.10.10; -; 1.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Hydrolase; Protease; Reference proteome; Serine protease;
KW   Signal; Zymogen.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   PROPEP          20..27
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028440"
FT   CHAIN           28..264
FT                   /note="Cercarial protease"
FT                   /id="PRO_0000028441"
FT   DOMAIN          28..264
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        68
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        126
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        218
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        53..69
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   DISULFID        192..202
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
SQ   SEQUENCE   264 AA;  28545 MW;  E2E5129A7C5D5010 CRC64;
     MSNRWRFVVV VTLFTYCLTF ERVSTWLIRS GEPVQHPAEF PFIAFLTTER TMCTGSLVST
     RAVLTAGHCV CSPLPVIRVS FLTLRNGDQQ GIHHQPSGVK VAPGYMPSCM SARQRRPIAQ
     TLSGFDIAIV MLAQMVNLQS GIRVISLPQP SDIPPPGTGV FIVGYGRDDN DRDPSRKNGG
     ILKKGRATIM ECRHATNGNP ICVKAGQNFG QLPAPGDSGG PLLPSLQGPV LGVVSHGVTL
     PNLPDIIVEY ASVARMLDFV RSNI